Note: Descriptions are shown in the official language in which they were submitted.
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DETERGENT COMPOSITIONS COMPRISING AN ENZYME SYSTEM
10
Field of the Invention
The present invention relates to detergent compositions comprising an
enzymatic
system comprising a mannanase, a xyloglucanase and a pectate iyase.
Background of the invention
Performance of a detergent product is judged by a number of factors, including
the ability to remove soils, and the ability to prevent the redeposition of
the
2~ soils, or the breakdown products of the soils on the articles in the wash.
Therefore, detergent compositions include nowadays a complex combination of
active ingredients which full certain specific needs. In particular, current
detergent formulations generally include surfactants and detergent enzymes
providing cleaning and fabric care benefits.
Removal of stains stemming from plants, wood, mould-clay based soil, muddy
soils, and fruits is one of today's toughest cleaning tasks; especially with
the
trend toward low wash temperatures. These stains typically contain complex
mixtures of fibrous material based mainly on carbohydrates and their
derivatives
fibres and cell wall components. Plant based soils are additionally
accompanied
with amylose, sugars and their derivatives. Food soils are often difficult to
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remove effectively from a soiled substrate. Highly coloured or "dried-on"
soils
derived from fruit and/or vegetable juices are particularly challenging to
remove.
Specific examples of such soils would include orange juice, tomato juice,
banana, mango or broccoli soils. Indeed, pectin polymers are important
constituents of plant cell walls. Pectin is a hetero-polysaccharide with a
backbone
composed of alternating homogalacturonan (smooth regions) and
rhamnogalacturonan (hairy regions). The smooth regions are linear polymers of
1,4-linked alpha-D-galacturonic acid. The galacturonic acid residues can be
methyl-esterified on the carboxyl group to a varying degree, usually in a non-
random fashion with blocks of polygalacturonic acid being completely methyl-
esterified. The substrates on which pectin containing stains are commonly
found
can be fabrics, dishware or hard surfaces.
In addition, the complex nature of everyday "body" soils typically found on
pillow
~s cases, T-shirts, collars and socks, provides a continuous thorough cleaning
challenge for detergents. These soils are difficult to remove completely due
in
part to their interaction with the pectin components in the primary cell walls
of
cotton fibers comprising cotton containing fabrics, and often residues build
up on
such fabric leading to dinginess and yellowing. Moreover, body fluid stains,
such
2o as blood and menstrual fluids, are often difficult to remove effectively
from a
soiled item, especially when the stains have been aged. Everyday body soils
are
also found on sanitary and kitchen surfaces such as bathtubs, toilet bowls and
dishware.
2s The use of enzymes in detergents is well-known in the art. For example,
amylase
enzymes have long been recognised in detergent compositions to provide the
removal of starchy food residues or starchy films from dishware or hard
surfaces
or to provide cleaning performance on starchy soils as well as other soils
typically
encountered in laundry applications. Protease enzymes have long been
3o recognised in detergent compositions to provide the removal of
proteinaceous
food residues from dishware, hard surfaces or to provide cleaning performance
on proteinaceous soils as well as other soils typically encountered in laundry
applications. Additionally, the use of cellulase is also well-known in the
art. This
activity in particular on fabrics provides a cleaning, rejuvenation, softening
and
35 generally improved handfeel characteristics to the fabric structure. The
inclusion
of lipolytic enzyme (e.g. lipase) in detergent compositions for improved
cleaning
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performance is known, e.g. enhancement of removal of triglycerides containing
soils and stains from fabrics.
Pectin degrading enzymes are known to provide soil/stain removal benefits when
used in washing and cleaning operations, specifically to provide the removal
of a
broad range of plant and fruit based stains and enhance the realistic item
cleaning profile of the detergent compositions. Indeed, removal of stains
stemming from plants, wood, mould-clay based soil and fruits is one of today's
toughest cleaning task; in particular with the trends to move to low wash
~o temperatures. Food soils are often difficult to remove effectively from a
soiled
substrate. Highly coloured or "dried-on" soils derived from fruit and/or
vegetable
juices are particularly challenging to remove. Specific examples of such soils
would include orange juice, tomato juice, banana, mango or broccoli soils.
15 Xyloglucan specific endoglucanases having a high xyloglucan-degrading
activity
may be of particular use for degradations of cell wall material having a high
xyloglucan content, for instance in the wine and fruit industries, for pectin -
extraction and for removal of hemicelluloses from textile fibers. Furthermore,
it
has been recognised that such specific xyloglucan enzymes removes the
2o xyloglucan without altering the cellulose. The use of such xyloglucan
specific
endoglucanases in detergent compositions has only been recently discovered as
described in W098/50513.
Another class of enzymes that have been recently applied in the detergent
2s industry is mannanase. Mannanase enzymes are known for their hydrolytic
activity on mannans-containing stains/soils such as food and/or cosmetic
stains/soils. Food and cosmetic stains/soils represent an imporatnt part of
consumer relevant stains/soils and often comprise additives such as thickener
/
stabiliser agents. Indeed, hydrocolloids gums and emulsifiers are commonly
used
so additives.
There is a continuous effort in the detergent industry to formulate detergent
compositions which provide superior cleaning performance. This objective has
been met by formulating detergent compositions comprising a specific enzyme
35 system comprising a mannanase, a pectate lyase and/or a xyloglucanase.
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It has been surprisingly found that the combined use of the following three
specific enzymes : a mannanase, a pectate lyase and a xyloglucanase, provides
superior cleaning due to the synergistic effect of the mixed enzyme system,
i.e.
superior stain removal, dingy cleaning and whiteness maintenance.
Specifically,
it has been found that the combined use of said enzymes provides outstanding
stain removal on key stains, even at very low wash temperature and/or low
detergent level, in laundry, dishwashing and hard surface.cleaning
applications.
It has been further found that the performance of the.detergent compositions
of
1o the present invention is enhanced by the addition of selected surfactants,
a
builder, another enzyme and/or a bleach system.
Mannanases have been identified in several Bacillus organisms. For example,
Talbot et al., Appl. Environ. Microbiol., vol. 56, No. 11, pp. 3505-3510
(1990)
~ 5 describes a ~i-mannanase derived from Bacillus stearothermophilus in dimer
form
having a MW of 162 kDa and an optimum pH of 5.5-7.5. Mendoza et al., World J.
Micobio. Boitech., vol. 10, no. 5, pp. 551-555 (1994) describes a ~3-mannanase
derived from Bacillus subtilises having a MW of 38 kDa, an optimum activity at
pH
5.0 / 55°C and a pl of 4.8. J0304706 discloses a ~i-mannanase derived
from
2o Bacillus sp. having a MW of 37+/- 3kDa measured by gel filtration, an
optimum
pH of 8-10 and a pl of 5.3-5.4. J63056289 describes the production of an
alkaline, thermostable (i-mannase, which hydrolyses ~3-1,4-D-mannopyranoside
bonds of e.g. mannans and produces manno:oligo:saccharides. J63036774
relates to a Bacillus micro-organism FERM P-8856 which produces ~3-
25 mannanase and ~i-mannosidase, at an alkaline pH. A purified mannanase from
Bacillus amyloliquefaciens and its method of preparation useful in the
bleaching
of pulp and paper, is disclosed in W097/11164. W091i18974 describes an
hemicellulase such as a glucanase, xylanase or mannanase, active at extreme
pH and temperature and the production thereof. W094/25576 describes an
3o enzyme exhibiting a mannanase activity derived from Aspergillus aculeatus
CBS
101.43, that might be used for various purposes for which degradation or
modification of plant or algae cell wall material is desired. W093i24622
discloses
a mannanase isolated from Trichoderma reesie for bleaching lignocellulosic
pulps.
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Pectin degrading enzymes as detergent enzymes are described in EP-A-751
990, W098/06805, W098/06806, W098/06807, W098/06808, and
W098/06809. W095/35362 discloses cleaning compositions containing plant
cell wall degrading enzymes having a pectinase and/or hemicellulase and
5 optionally cellulase activity for the removal of stains from vegetable
origin.
Xyloglucan specific endoglucanases have been identified in various plants, see
for example, the disclosure of Fry et al., Biochem. J. (1992), Vol. 282, pp
821-
828, Nishitani and Tominaga, The Journal of Biol. Chemistry (1992). Vol. 267,
~ o No. 29, pp. 21058-21064, Hayashi et al., Plant Physiol., (1984), Vol. 75,
pp. 605-
610, McDougall and Fry, J. Plant Physiol., (1991 ), Vol. 137, pp. 332-336, and
WO 93/17101. All of these enzymes have been found to have transferase
activity (as defined e.g. by Fry et al., 1992 and Nishitani et al., 1992) and
are
therefore said not to be classified as a real endoglucanase. Further, a
xyloglucan specific endoglucanases in microorganisms is described in WO
94/14953. Therein, it is generally stated that "endoglucanases having a high
xyloglucan-degrading activity may be of particular use for degradations of
cell
wall material having a high xyloglucan content, for instance in the wine and
fruit
industry, for pectin-extraction and for removal of hemicelluloses from textile
2o fibres". Specifically referred to for this last property is the use of
these enzymes
to manufacture textile fibers: "The hemicellulose like xyloglucan has to be
removed from plant fibers like cotton, flax, hemp and jute before these can be
used for textiles. For this purpose endoglucanase of type II [i.e., the
xyloglucan-
specific enzymes] has the advantage that it specifically removes the
xyloglucan
without damaging the cellulose." "Furthermore, the endoglucanases of the
invention and analogous thereof may be used to treat cellulose fibres or
cellulose-fibre rich material. The endoglucanases may e.g. be used in the
paper
industry to improve the drainage of pulp, and to treat fabrics such as cotton
fabrics, to give a more smooth fabric."
However, the synergistic combination of a mannanase, a pectate lyase and a
xyloglucanase, for superior cleaning performance in a detergent composition,
i.e.
superior stain removal, dingy cleaning and whiteness maintenance, has never
been previously recognised.
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Summary of the invention
The present invention relates to detergent compositions, including laundry,
dishwashing, hard surface cleaner compositions, comprising a mannanase, a
pectate lyase and a xyloglucanase, for superior cleaning performance, i.e.
superior stain removal, dingy cleaning and whiteness maintenance.
Detailed description of the invention
The detergent compositions of the present invention comprise as essential
elements : a mannanase, a pectate lyase and a xyloglucanase. It has been
surprisingly found that such compositions provide superior cleaning
performance,
i.e. superior stain removal, dingy cleaning and whiteness maintenance.
Not wishing to be bound by theory it is believed that the combination of all
three
enzymes, Mannanase, Pectate Lyase and Xyloglucanase, is more effective at
breaking down complex carbohydrate soils/stains than the individual enzymes
alone. Many vegetable and fruit-based stains contain intact plant cell wall
2o material which is comprised of pecti~s and xyloglucans. In addition,
hydrocolloid
gums, such as guar gum, are commonly used stabilizers and theology modifiers
in prepared foods. Thus, it is expected that in vegetable and/or fruit-based
food
soils/stains, pectin, xyloglucan and mannan substrates are to be found. The
polymeric, branched nature of these substrates is believed to attract and hold
stain/soil components to fabric, dish, and/or hard surfaces. Attacking these
substrates with said specific mixture of enzymes provides overall superior
removal of soils/stains, especially food-based soils and stains, than is
otherwise
obtained with the individual enzyme alone. In addition, it is known that
cotton
fibers retain some portion of the primary cell wall. The pectins and
xyloglucans
so present in this residual primary cell wall layer present a preferred
binding site for
the hydrocolloid gums found in a number of prepared foods and personal and
beauty care products such as shampoos, body lotions, and make-up. When
such materials contact cotton fabrics they are difficult to remove with
standard
detergents. It is proposed that the enzyme mixture contemplated in this
invention
s5 is effective at removing such stains because the Pectate Lyase and
Xyloglucanase aid in removal of the residual primary cell wall components of
the
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cotton garment while the Mannanase serves to break down the hydrocolloid
gums found in the soils/stains themselves.
The Mannanase Enzyme
The first essential element of the detergent compositions of the present
invention
is a mannanase enzyme.
Encompassed in the present invention are the following three mannans-
o degrading enzymes : EC 3.2.1.25 : ~3-mannosidase, EC 3.2.1.78 : Endo-1,4-~3-
mannosidase, referred therein after as "mannanase" and EC 3.2.1.100 : 1,4-~i-
mannobiosidase (IUPAC Classification- Enzyme nomenclature, 1992 ISBN 0-12-
227165-3 Academic Press).
More preferably, the detergent compositions of the present invention comprise
a
~ 5 ~i-1,4-Mannosidase (E.C. 3.2.1.78) referred to as Mannanase. The term
"mannanase" or "galactomannanase" denotes a mannanase enzyme defined
according to the art as officially being named mannan endo-1,4-beta
mannosidase and having the alternative names beta-mannanase and endo-1,4
mannanase and catalysing the reaction: random hydrolysis of 1,4-beta-D
2o mannosidic linkages in mannaris, galactomannans, glucomannans, and
galactoglucomannans.
In particular, Mannanases (EC 3.2.1.78) constitute a group of polysaccharases
which degrade mannans and denote enzymes which are capable of cleaving
polyose chains contaning mannose units, i.e. are capable of cleaving
glycosidic
25 bonds in mannans, glucomannans, galactomannans and galactogluco-mannans.
Mannans are polysaccharides having a backbone composed of ~3-1,4- linked
mannose; glucomannans are polysaccharides having a backbone or more or less
regularly alternating (i-1,4 linked mannose and glucose; galactomannans and
galactoglucomannans are mannans and glucomannans with a-1,6 linked
3o galactose sidebranches. These compounds may be acetylated.
The degradation of galactomannans and galactoglucomannans is facilitated by
full or partial removal of the galactose sidebranches. Further the degradation
of
the acetylated mannans, glucomannans, galactomannans and galactogluco-
mannans is facilitated by full or partial deacetylation. Acetyl groups can be
35 removed by alkali or by mannan acetylesterases. The oligomers which are
released from the mannanases or by a combination of mannanases and a-
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galactosidase and/or mannan acetyl esterases can be further degraded tc
release free maltose by (3-mannosidase and/or ~-glucosidase.
Mannanases have been identified in several Bacillus organisms. For example,
Talbot et al., Appl. Environ. Microbiol., Vo1.56, No. 11, pp. 3505-3510 (1990)
s describes a beta-mannanase derived from Bacillus stearothermophilus in dimer
form having molecular weight of 162 kDa and an optimum pH of 5.5-7.5.
Mendoza et al., World J. Microbiol. Biotech., Vol. 10, No. 5, pp. 551-555
(1994)
describes a beta-mannanase derived from Bacillus subtilis having a molecular
weight of 38 kDa, an optimum activity at pH 5.0 and 55C and a pl of 4.8. JP-
~ 0 03047076 discloses a beta-mannanase derived from Bacillus sp., having a
molecular weight of 373 kDa measured by gel filtration, an optimum pH of 8-10
and a pl of 5.3-5.4. JP-63056289 describes the production of an alkaline,
thermostable beta-mannanase which hydrolyses beta-1,4-D-mannopyranoside
bonds of e.g. mannans and produces manno-oligosaccharides. JP-63036774
~s relates to the Bacillus microorganism FERM P-8856 which produces beta-
mannanase and beta-mannosidase at an alkaline pH. JP-08051975 discloses
alkaline beta-mannanases from alkalophilic Bacillus sp. AM-001. A purified
mannanase from Bacillus amyloliquefaciens useful in the bleaching of pulp and
paper and a method of preparation thereof is disclosed in WO 97/11164. WO
20 91/18974 describes a hemicellulase such as a glucanase, xylanase or
mannanase active at an extreme pH and temperature. WO 94/25576 discloses
an enzyme from Aspergillus aculeatus, CBS 101.43, exhibiting mannanase
activity which may be useful for degradation or modification of plant or algae
cell
wall material. WO 93/24622 discloses a mannanase isolated from Trichoderma
25 reseei useful for bleaching lignocellulosic pulps. An hemicellulase capable
of
degrading mannan-containing hemicellulose is described in W091/18974 and a
purified mannanase from Bacillus amyloliquefaciens is described in
W097/11164.
3o Preferably, the mannanase enzyme will be an alkaline mannanase as defined
below, more preferably, a mannanase originating from a bacterial source. The
terms "alkaline mannanase enzyme" is meant to encompass an enzyme having
an enzymatic activity of at least 10%, preferably at least 25%, more
preferably at
least 40% of its maximum activity at a given pH ranging from 7 to 12,
preferably
35 7.5 to 10.5.
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Especially, the laundry detergent composition of the present invention will
comprise an alkaline mannanase selected from the strain Bacillus
agaradhaerens NICMB 40482; the mannanase from Bacillus subtilis strain 168,
gene yght; the mannanase from Bacillus sp. 1633 and/or the mannanase from
Bacillus sp. AA112. Most preferred mannanase for the inclusion in the
detergent
compositions of the present invention is the mannanase enzyme originating from
Bacillus sp. 1633 as described in the co-pending Danish patent application No.
PA 1998 01340; filed internationally in PCT/DK99/00314 on June 10, 1999.
1o The alkaline mannanase from Bacillus agaradhaerens NICMB 40482 is
described in the co-pending U.S. patent application serial No. 09/111,256;
filed
internationally in PCT/DK99/00314 on June 10, 1999. More specifically, this
mannanase is:
i) a polypeptide produced by Bacillus agaradhaerens, NCIMB 40482; or
~5 ii) a polypeptide comprising an amino acid sequence as shown in positions
32-343 of SEQ ID N0:2 as shown in U.S. patent application serial No.
09/111,256; or
iii) an analogue of the polypeptide defined in i) or ii) which is at least 70%
homologous with said polypeptide, or is derived from said polypeptide by
2o substitution, deletion or addition ~ of one or several amino acids, or is
immunologically reactive with a polyclonal antibody raised against said
polypeptide in purified form.
Also encompassed is the corresponding isolated polypeptide having mannanase
activity selected from the group consisting of:
25 (a) polynucleotide molecules encoding a polypeptide having mannanase
activity and comprising a sequence of nucleotides as shown in SEQ ID NO: 1
from nucleotide 97 to nucleotide 1029 as shown in U.S. patent application
serial
No. 09/111,256;
(b) species homologs of (a);
30 (c) polynucleotide molecules that encode a polypeptide having mannanase
activity that is at least 70% identical to the amino acid sequence of SEQ ID
NO: 2
from amino acid residue 32 to amino acid residue 343 as shown in U.S. patent
application serial No. 09/111,256;
(d) molecules complementary to (a), (b) or (c); and
35 (e) degenerate nucleotide sequences of (a), (b), (c) or (d).
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The plasmid pSJ1678 comprising the polynucleotide molecule (the DNA
sequence) encoding said mannanase has been transformed into a strain of the
Escherichia coli which was deposited by the inventors according to the
Budapest
Treaty on the International Recognition of the Deposit of Microorganisms for
the
5 Purposes of Patent Procedure at the Deutsche Sammlung von Mikroorganismen
and Zellkulturen GmbH, Mascheroder Weg 1 b, D-38124 Braunschweig, Federal
Republic of Germany, on 18 May 1998 under the deposition number DSM
12180.
1 o A second more preferred enzyme is the mannanase from the Bacillus subtilis
strain 168, which is described in the co-pending U.S. patent application
serial No.
09/095,163; filed internationally in PCT/DK99/00314 on June 10, 1999. More
specifically, this mannanase is:
i) is encoded by the coding part of the DNA sequence shown in SED ID No.
5 shown in the U.S. patent application serial No. 09/095,163 or an analogue of
said sequence; and/or
ii) a polypeptide comprising an amino acid sequence as shown SEQ ID N0:6
shown in the U.S. patent application serial No. 09/095,163; or
iii) an analogue of the polypeptide defined in ii) which is at least 70%
2o homologous with said polypeptide, or is derived from said polypeptide by
substitution, deletion or addition of one or several amino acids, or is
immunologically reactive with a polyclonal antibody raised against said
polypeptide in purified form.
Also encompassed in the corresponding isolated polypeptide having mannanase
activity selected from the group consisting of:
(a) polynucleotide molecules encoding a polypeptide having mannanase
activity and comprising a sequence of nucleotides as shown in SEQ ID N0:5 as
shown in the U.S. patent application serial No. 09/095,163
(b) species homologs of (a);
(c) polynucleotide molecules that encode a polypeptide having mannanase
activity that is at least 70% identical to the amino acid sequence of SEQ ID
NO: 6
as shown in the U.S. patent application serial No. 09/095,163;
(d) molecules complementary to (a), (b) or (c); and
(e) degenerate nucleotide sequences of (a), (b), (c) or (d).
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A third more preferred mannanase is described in the co-pending Danish patent
application No. PA 1998 01340; filed internationally in PCT/DK99/00314 on June
10, 1999. More specifically, this mannanase is:
i) a polypeptide produced by Bacillus sp. 1633;
ii) a polypeptide comprising an amino acid sequence as shown in positions
33-340 of SEQ ID N0:2 as shown in the Danish application No. PA 1998 01340;
or
iii) an analogue of the polypeptide defined in i) or ii) which is at least 65%
homologous with said polypeptide, is derived from said polypeptide by
1o substitution, deletion or addition of one or several amino acids, or is
immunologically reactive with a polyclonal antibody raised against said
polypeptide in purified form.
Also encompassed is the corresponding isolated polynucleotide molecule
selected from the group consisting of:
(a) polynucleotide molecules encoding a polypeptide having mannanase activity
and comprising a sequence of nucleotides as shown in SEQ ID NO: 1 from
nucleotide 317 to nucleotide 1243 the Danish application No. PA 1998 01340;
(b) species homologs of (a);
(c) polynucleotide molecules that encode a polypeptide having mannanase
2o activity that is at least 65% identical to the amino acid sequence of SEQ
ID NO: 2
from amino acid residue 33 to amino acid residue 340 the Danish application
No.
PA 1998 01340;
(d) molecules complementary to (a), (b) or (c); and
(e) degenerate nucleotide sequences of (a), (b), (c) or (d).
The plasmid pBXM3 comprising the polynucleotide molecule (the DNA
sequence) encoding a mannanase of the present invention has been
transformed into a strain of the Escherichia coli which was deposited by the
inventors according to the Budapest Treaty on the International Recognition of
the Deposit of Microorganisms for the Purposes of Patent Procedure at the
3o Deutsche Sammlung von Mikroorganismen and Zellkulturen GmbH,
Mascheroder Weg 1 b, D-38124 Braunschweig, Federal Republic of Germany, on
29 May 1998 under the deposition number DSM 12197.
A fourth more preferred mannanase is described in the Danish co-pending patent
s5 application No. PA 1998 01341; filed internationally in PCT/DK99/00314 on
June
10, 1999. More specifically, this mannanase is:
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12
i) a polypeptide produced by Bacillus sp. AAI 12;
ii) a polypeptide comprising an amino acid sequence as shown in positions 25-
362 of SEQ ID N0:2 as shown in the Danish application No. PA 1998 01341; or
iii) an analogue of the polypeptide defined in i) or ii) which is at least 65%
homologous with said polypeptide, is derived from said polypeptide by
substitution, deletion or addition of one or several amino acids, or is
immunologically reactive with a polyclonal antibody raised against said
polypeptide in purified form.
Also encompassed is the corresponding isolated polynucleotide molecule
1o selected from the group consisting of
(a) polynucleotide molecules encoding a polypeptide having mannanase activity
and comprising a sequence of nucleotides as shown in SEQ ID NO: 1 from
nucleotide 225 to nucleotide 1236 as shown in the Danish application No. PA
1998 01341;
15 (b) species homologs of (a);
(c) polynucleotide molecules that encode a polypeptide having mannanase
activity that is at least 65% identical to the amino acid sequence of SEQ ID
NO: 2
from amino acid residue 25 to amino acid residue 362 as shown in the Danish
application No. PA 1998 01341;
20 (d) molecules complementary to (a),- (b) or (c); and
(e) degenerate nucleotide sequences of (a), (b), (c) or (d).
The plasmid pBXM1 comprising the polynucleotide molecule (the DNA
sequence) encoding a mannanase of the present invention has been
transformed into a strain of the Escherichia coli which was deposited by the
25 inventors according to the Budapest Treaty on the International Recognition
of
the Deposit of Microorganisms for the Purposes of Patent Procedure at the
Deutsche Sammlung von Mikroorganismen and Zellkulturen GmbH,
Mascheroder Weg 1 b, D-38124 Braunschweig, Federal Republic of Germany, on
7 October 1998 under the deposition number DSM 12433.
so The mannanase is incorporated into the detergent compositions of the
invention
preferably at a level of from 0.0001 % to 2%, more preferably from 0.0005% to
0.1 %, most preferred from 0.001 % to 0.02% pure enzyme by weight of the
composition.
35 The Pectate lyase enzyme
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The second essential element of the detergent compositions of the present
invention is a pectate lyase enzyme.
Pectate lyase is classified within the classification of enzymes provided by
the
Enzyme Nomenclature (1992) as EC 4.2.2.2. Said enzyme is known to split the
a-1,4,glucoside bond of galacturonic acid found in pectin substances, creating
a
double bond between C4 and C5 and is subtantially free for other pectin
degrading activities, i.e having less than 25%, preferably less than 15%, more
preferably less than 5% by weight of the enzyme compound of other pectin
1 o degrading enzyme activities.
Pectate lyases have been cloned from different bacterial genera such as
Erwinia,
Pseudomonas, Klebsiella and Xanthomonas, Strepfomyces, Penicillium,
Baceriodes, Thermomonospora, Fusarium, and Aspergillus. Also from Bacillus
1s subtilis (Nasser et al. (1993) FEBS 335:319-326) and Bacillus sp. YA-14
(Kim et
al. (1994) Biosci. Biotech. Biochem. 58:947-949) cloning of a pectate lyase
has
been described. Purification of pectate lyases with maximum activity in the pH
range of 8-10 produced by Bacillus pumilus (Dave and Vaughn (1971 ) J.
Bacteriol. 108:166-174), B, polymyxa (Nagel and Vaughn (1961 ) Arch. Biochem.
2o Biophys. 93:344-352), B. stearothermophilus (Karbassi and Vaughn (1980)
Can.
J. Microbiol. 26:377-384), Bacillus sp. (Hasegawa and Nagel (1966) J. Food
Sci.
31:838-845) and Bacillus sp. RK9 (Kelly and Fogarty (1978) Can. J. Microbiol.
24:1164-1172) has been reported. WO 98/45393 discloses detergent
compositions containing protopectinase with remarkable detergency against
2s muddy soils.
Further suitable pectate lyases for use in the present invention are the
protopectinases having an optimum reaction pH of 7.0 or higher when
polygalacturonic acid is used as a substrate such as described in W098/45393
3o and the pectic acid lyase having the amino acid sequence SEQ no 1 of EP 870
843 or having such amino acid sequence with one or more amino acid being
deleted, added or substituted.
Preferred are the pectate lyase enzymes described in the international co-
pending application PCT/DK98/00515, filed internationally on November 24,
1998 and published under W099/27084:
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WO 00/42157 PCT/US00/00839
14
- A pectate lyase comprising a first amino acid sequence consisting of seven
(7)
amino acid residues having the following sequence: Asn Leu Asn Ser Arg Val
Pro (NLNSRVP);
- A pectate lyase which is
i) a polypeptide produced by Bacillus agaradhaerens, NCIMB 40482 or
DSM 8721, or by a Bacillus species having a 16S rDNA sequence
homology to Bacillus agaradhaerens, DSM 8721, of at least 99%, or
ii) a polypeptide comprising an amino acid sequence as shown in positions
27-359 of SEQ ID N0:2 of PCTlDK98/00515, or
iii) an analogue of the polypeptide defined in i) or ii) which is at least 45%
homologous with said polypeptide, or
iv) is derived from said polypeptide b_y substitution, deletion or addition of
0 one or several amino acids, provided that the arginine in position 240, and
optionally also the arginine in position 245, is conserved and the derived
polypeptide is at least 42% homologous with said polypeptide, or
v) is immunologically reactive with a polyclonal antibody raised against
said polypeptide in purified form;
- A pectate lyase which is
i) a polypeptide produced by Bacillus licheniformis, ATCC 14580, or by a
Bacillus species having a 16S rDNA sequence homology to Bacillus
licheniformis, ATCC 14580, of at least 99%, or
ii) a polypeptide comprising an amino acid sequence as shown in positions
28-341 of SEQ ID N0:4 of PCT/DK98/00515, or
iii) an analogue of the polypeptide defined in i) or ii) which is at least 45%
homologous with said polypeptide, or
iv) is derived from said polypeptide by substitution, deletion or addition of
one or several amino acids, provided that the arginine in position 233, and
optionally also the arginine in position 238, is conserved and the derived
polypeptide is at least 42% homologous with said polypeptide, or
v) is immunologically reactive with a polyclonal antibody raised against
said polypeptide in purified form;
- A pectate lyase which is
3o i) a polypeptide produced by a Bacillus species having the 16S rDNA
sequence of SEQ ID N0:14 of PCT/DK98/00515or by a Bacillus species
having a 16S rDNA sequence homology to SEQ ID N0:14 of
PCT/DK98/00515 higher than 97.3%; or
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WO 00/42157 PCT/US00/00839
ii) a polypeptide comprising an amino acid sequence as shown in positions
181-509 of SEQ ID N0:6 of PCT/DK98/00515, or
iii) an analogue of the polypeptide defined in i) which is at least 50%
homologous with said polypeptide, or
5 iv) is derived from said polypeptide by substitution, deletion or addition
of
one or several amino acids, provided that the arginine in position 390, and
optionally also the arginine in position 395, is conserved and the derived
polypeptide is at least 44% homologous with said polypeptide, or
v) is immunologically reactive with a polyclonal antibody raised against
1o said polypeptide in purified form,
- A pectate lyase which is
i) a polypeptide produced by the species Bacillus halodurans, or
ii) a polypeptide comprising an amino acid sequence as shown in positions
42-348 of SEQ ID N0:8 of PCT/DK98/00515, or
15 iii) an analogue of the polypeptide defined in i) or ii) which is at least
45%
homologous with said polypeptide, or
iv) is derived from said polypeptide by substitution, deletion or addition of
one or several amino acids, provided that the arginine in position 240, and
optionally also the arginine in position 245, is conserved and the derived
2o polypeptide is at least 40% homologous with said polypeptide, or
v) is immunologically reactive with a polyclonal antibody raised against
said polypeptide in purified form,
- A pectate lyase which is
i) a polypeptide produced by a Bacillus species having the 16S rDNA
sequence of SEQ ID N0:13 of PCT/DK98/00515or by a Bacillus species
having a 16S rDNA sequence homology to SEQ ID N0:13 of
PCT/DK98/00515 higher than 98.1 %; or
ii) a polypeptide comprising an amino acid sequence as shown in positions
25-335 of SEQ ID N0:10 of PCT/DK98/00515, or
3o iii) an analogue of the polypeptide defined in i) or which is at least 45%
homologous with said polypeptide, or
iv) is derived from said polypeptide by substitution, deletion or addition of
one or several amino acids, provided that the arginine in position 227, and
optionally also the arginine in position 232, is conserved and the derived
polypeptide is at least 41 % homologous with said polypeptide, or
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WO 00/42157 PCT/US00/00839
16
v) is immunologically reactive with a polyclonal antibody raised against
said polypeptide in purified form.
Similarly preferred is the pectate lyase enzyme described in the international
co-
y pending application PCT/DK98/00514, filed internationally on November 24,
1998 and published under W099/27083 and which is
> a polypeptide produced by Bacillus licheniformis, ATCC 14580, or
W a polypeptide comprising an amino acid sequence as shown in positions 28-
221 of SEQ ID N0:4 of PCT/DK98/00514, or
~~~> an analogue of the polypeptide defined in i) or ii) which is at least 60%
homologous with said polypeptide, or
~V> is derived from said polypeptide by substitution, deletion or addition of
one or
several amino acids, provided that the lysines in positions 133 and 155 and
the
arginine in position 158 are conserved and the derived polypeptide is at least
66% homologous with positions 60-158 of SEQ ID N0:4 of PCT/DK98/00514, or
V> is immunologically reactive with a polyclonal antibody raised against said
polypeptide in purified form.
More preferred pectate lyases for the purpose of the present invention are
those
2o having opimum activity at pH's >7~.0 and derived from Streptomyces fradiae,
Streptomyces nitrosporeus, Erwinia carotovora, Bacillus spheroides,
Thermomonospora fusca, Pseudomonas solanacearum, Bacteroides
thetaiotaomicron, Fusarium solani, Xanthomonas campestris, Bacillus
agaradhaerens, and/or Bacillus licheniformis.
Most preferred pectate lyase for the purpose of the present invention is the
Pectate lyase from Bacillus agaradhaerens, NCIMB 40482 or DSM 8721.
The pectate lyase is incorporated into the compositions of the invention
3o preferably at a level of from 0.0001 % to 2%, more preferably from 0.0005%
to
0.1 %, most preferably from 0.001 % to 0.02% pure enzyme by weight of the
composition.
The Xyloglucanase enzyme
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17
The third essential element of the present invention is a xyloglucanase enzyme
such as described in the co-pending international patent application
PCT/US98/09126, internationally filed by Procter and Gamble on May 5, 1998,
published under W098/50513.
Suitable for the purpose of the present invention are these enzymes exhibiting
endoglucanase activity specific for xyloglucan such that the catalytic
turnover rate
Kcat at the optimum conditions for the enzyme, is at least 5 times higher on
xyloglucan than on carboxymethylcellulose.
As used herein, the term "endoglucanase activity" means the capability of the
enzyme to hydrolyze 1,4-~i-D-glycosidic linkages present in any xyloglucan
material versus cellulose. The endoglucanase activity may be determined in
accordance with methods known in the art, examples of which are described in
WO 94/14953 and hereinafter. One unit of endoglucanase activity (e.g. CMCU,
AVIU, XGU or BGU) is defined as the production of 1 ~mol reducing sugar/min
from a glucan substrate, the glucan substrate being, e.g., CMC (CMCU), acid
swollen Avicell (AVIU), xyloglucan (XGU) or cereal ~3-glucan (BGU). The
reducing sugars are determined as described in WO 94/14953 and hereinafter.
2o The specific activity of an endoglucanase towards a substrate is defined as
units/mg of protein.
Suitable are enzymes exhibiting high activity XGU endoglucanase activity
(hereinafter "specific for xyloglucan"), which enzyme:
i) is encoded by a DNA sequence comprising or included in at least one of
the following partial sequences
(a) ATTCATTTGT GGACAGTGGA C (SEQ ID No: 1 )
(b) GTTGATCGCA CATTGAACCA (SEQ ID NO: 2)
(c) ACCCCAGCCG ACCGATTGTC (SEQ ID NO: 3)
(d) CTTCCTTACC TCACCATCAT (SEQ ID NO: 4)
(e) TTAACATCTT TTCACCATGA (SEQ ID NO: 5)
(f) AGCTTTCCCT TCTCTCCCTT (SEQ ID NO: 6)
(g) GCCACCCTGG CTTCCGCTGC CAGCCTCC (SEQ ID NO: 7)
(h) GACAGTAGCA ATCCAGCATT (SEQ ID NO: 8)
(i) AGCATCAGCC GCTTTGTACA (SEQ ID NO: 9)
(j) CCATGAAGTT CACCGTATTG (SEQ ID NO: 10)
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WO 00/42157 PCT/US00/00839
18
(k) GCACTGCTTC TCTCCCAGGT (SEQ ID NO: 11 )
(I) GTGGGCGGCC CCTCAGGCAA (SEQ ID NO: 12)
(m) ACGCTCCTCC AATTTTCTCT (SEQ ID NO: 13)
(n) GGCTGGTAG TAATGAGTCT (SEQ ID NO: 14)
s (o) GGCGCAGAGT TTGGCCAGGC (SEQ ID NO: 15)
(p) CAACATCCCC GGTGTTCTGG G (SEQ ID NO: 16)
(q) AAAGATTCAT TTGTGGACAG TGGACGTTGA TCGCACATTG
AACCAACCCC AGCCGACCGA
TTGTCCTTCC TTACCTCACC ATCATTTAAC ATCTTTTCAC CATGAAGCTT
1o TCCCTTCTCT
CCCTTGCCAC CCTGGCTTCC GCTGCCAGCC TCCAGCGCCG
CACACTTCTG CGGTCAGTGG
GATACCGCCA CCGCCGGTGA CTTCACCCTG TACAACGACC
TTTGGGGCGA GACGGCCGGC
15 ACCGGCTCCC AGTGCACTGG AGTCGACTCC TACAGCGGCG
ACACCATCGC TTGTCACACC
AGCAGGTCCT GGTCGGAGTA GCAGCAGCGT CAAGAGCTAT GCCAACG
(SEQ ID N0:17) or
(r) CAGCATCTCC ATTGAGTAAT CACGTTGGTG TTCGGTGGCC
2o CGCCGTGTTG CGTGGCGGAG
GCTGCCGGGA GACGGGTGGG GATGGTGGTG GGAGAGAATG
TAGGGCGCCG TGTTTCAGTC
CCTAGGCAGG ATACCGGAAA ACCGTGTGGT AGGAGGTTTA
TAGGTTTCCA GGAGACGCTG
25 TATAGGGGAT AAATGAGATT GAATGGTGGC CACACTCAAA CCAACCAGGT
CCTGTACATA
CAATGCATAT ACCAATTATA CCTACCAAAA AAAAAAAAAA AA
AAAA (SEQ ID N0:18)
or a sequence homologous thereto encoding a polypeptide specific for
so xyloglucan with endoglucanase activity,
ii) is immunologically reactive with an antibody raised against a highly
purified endoglucanase encoded by the DNA sequence defined in i) and derived
from Aspergillus aculeatus, CBS 101.43, and is specific for xyloglucan.
3s More specifically, as used herein the term "specific for xyloglucan" means
that
the endoglucanase' enzyme exhibits its highest endoglucanase activity on a
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WO 00/42157 PCT/US00/00839
19
xyloglucan substrate, and preferably less than 75% activity, more preferably
less
than 50% activity, most preferably less than about 20% activity, on other
cellulose-containing substrates such as carboxymethyl cellulose, cellulose, or
other glucans.
Preferably, the specificity of an endoglucanase towards xyloglucan is further
defined as a relative activity determined as the release of reducing sugars at
optimal conditions obtained by incubation of the enzyme with xyloglucan and
the
other substrate to be tested, respectively. For instance, the specificity may
be
1o defined as the xyloglucan to ~i-glucan activity (XGU/BGU), xyloglucan to
carboxy
methyl cellulose activity (XGU/CMCU), or xyloglucan to acid swollen Avicell
activity (XGU/AVIU), which is preferably greater than about 50, such as 75, 90
or
100.
The term "derived from" as used herein refers not only to an endoglucanase
produced by strain CBS 101.43, but also an endoglucanase encoded by a DNA
sequence isolated from strain CBS 101.43 and produced in a host organism
transformed with said DNA sequence. The term "homologue" as used herein
indicates a polypeptide encoded by DNA which hybridizes to the same probe as
2o the DNA coding for an endoglucanase enzyme specific for xyloglucan under
certain specified conditions (such as presoaking in SxSSC and prehybridizing
for
1 h at -40°C in a solution of 5xSSC, 5xDenhardt's solution, and 50 ~g
of
denatured sonicated calf thymus DNA, followed by hybridization in the same
solution supplemented with 50 wCi 32-P-dCTP labelled probe for 18 h at -
40°C
and washing three times in 2xSSC, 0.2% SDS at 40°C for 30 minutes).
More
specifically, the term is intended to refer to a DNA sequence which is at
least
70% homologous to any of the sequences shown above encoding an
endoglucanase specific for xyloglucan, including at least 75%, at least 80%,
at
least 85%, at least 90% or even at least 95% with any of the sequences shown
3o above. The term is intended to include modifications of any of the DNA
sequences shown above, such as nucleotide substitutions which do not give rise
to another amino acid sequence of the polypeptide encoded by the sequence,
but which correspond to the codon usage of the host organism into which a DNA
construct comprising any of the DNA sequences is introduced or nucleotide
s5 substitutions which do give rise to a different amino acid sequence and
therefore,
possibly, a different amino acid sequence and therefore, possibly, a different
CA 02357801 2001-06-29
WO 00/42157 PCT/US00/00839
protein structure which might give rise to an endoglucanase mutant with
different
properties than the native enzyme. Other examples of possible modifications
are
insertion of one or more nucleotides into the sequence, addition of one or
more
nucleotides at either end of the sequence, or deletion of one or more
nucleotides
5 at either end or within the sequence.
Endoglucanase specific for xyloglucan useful in the present invention
preferably
is one which has a XGU/BGU, XGU/CMU and/or XGU/AVIU ratio (as defined
above) of more than 50, such as 75, 90 or 100.
Furthermore, the endoglucanase specific for xyloglucan is preferably
substantially devoid of activity towards ~-glucan and/or exhibits at the most
25%
such as at the most 10% or about 5%, activity towards carboxymethyl cellulose
and/or Avicell when the activity towards xyloglucan is 100%. In addition,
1s endoglucanase specific for xyloglucan of the invention is preferably
substantially
devoid of transferase activity, an activity which has been observed for most
endoglucanases specific for xyloglucan of plant origin.
Endoglucanase specific for xyloglucan may be obtained from the fungal species
2o A. aculeatus, as described in WO 94/14953. Microbial endoglucanases
specific
for xyloglucan has also been described in WO 94/14953. Endoglucanases
specific for xyloglucan from plants have been described, but these enzymes
have
transferase activity and therefore must be considered inferior to microbial
endoglucanses specific for xyloglucan whenever extensive degradation of
25 xyloglucan is desirable. An additional advantage of a microbial enzyme is
that it,
in general, may be produced in higher amounts in a microbial host, than
enzymes of other origins.
The xyloglucanase of the invention may be isolated by a general method
3o involving:
- cloning, in suitable vectors, a DNA library from Aspergillus spp.,
- transforming suitable yeast host cells with said vectors,
- culturing the host cells under suitable conditions to express any enzyme of
interest encoded by a clone in the DNA library, and
3s - screening for positive clones by determining any endoglucanase activity
of the
enzyme produced by such clones.
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21
A more detailed description of this screening method is given in WO 94/14953.
The DNA sequence coding for the enzyme may for instance be isolated by
screening a cDNA library of Aspergillus aculeatus, e.g. strain CBS 101.43,
publicly available from Centraalbureau voor Schimmelcultures, and selecting
for
clones expressing enzymes having the ability to hydrolyze ~3-1,3 and/or ~-1,4
bonds between two glucose molecules in polymers containing glucose (e.g.
cellulose, cereal ~3-glucans or xyloglucans). The appropriate DNA sequence may
then be isolated from the clone by standard procedures, e.g. as described in
WO
94/14953, Example 1. It is expected that a DNA sequence coding for a
1o homologous enzyme may be derived by similarly screening a cDNA library of
another microorganism, in particular a fungus, such as a strain of
Aspergillus, in
particular A. aculeatus or A. niger, a strain of Trichoderma, in particular T.
harianun, T. reesie, a strain of Fusarium, in particular F. oxysporum or a
strain of
Humicola.
15 Alternatively, the DNA coding for an endoglucanase of the invention may, in
accordance with well-known procedures, conveniently be isolated from DNA from
any of the above mentioned organisms by use of oligonucleotide probes, such as
20mer probes, prepared on the basis of a DNA sequence disclosed herein. For
instance, a suitable oligonucleotide probe may, e.g., be prepared on the basis
of
2o any of the partial nucleotide sequences a)-p) listed in WO 94/14953.
The DNA sequence may subsequently be inserted into a recombinant expression
vector. This may be any vector which may conveniently be subjected to
recombinant DNA procedures, and the choice of vector will often depend on the
host cell into which it is to be introduced. Thus, the vector may be an
25 autonomously replicating vector, i.e. a vector which exists as an
extrachromosomal entity, the replication of which is independent of
chromosomal
replication, e.g. a plasmid. Alternatively, the vector may be one which, when
introduced into a host cell, is integrated into the host cell genome and
replicated
together with the chromosomes) into which it has been integrated.
so In the vector, the DNA sequence encoding the endoglucanase specific for
xyloglucan should be operably connected to a suitable promoter and terminator
sequence. The promoter may be any DNA sequence which shows
transcriptional activity in the host cell of choice and may be derived from
genes
encoding proteins either homologous or heterologous to the host cell. The
35 procedures used to ligate the DNA sequences coding for the endoglucanase,
the
promoter and the terminator, respectively, and to insert them into suitable
vectors
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WO 00/42157 PCT/US00/00839
22
are well known to persons skilled in the art (cf., for instance, Sambrook et
al.,
Molecular Cloning. A Laboratory Manual, Cold Spring Harbor, NY 1989).
The host cell which is transformed with the DNA sequence encoding the enzyme
useful for the present invention compositions is preferably a eukaryotic cell,
in
particular a fungal cell such as a yeast or filamentous fungal cell. In
particular,
the cell may belong to a species of Aspergillus, most preferably Aspergillus
oryzae or Aspergillus niger. Fungal cells may be transformed by a process
involving protoplast formation and transformation of the protoplasts followed
by
regeneration of the cell wall in a manner known in the art. The use of
Aspergillus
~o as a host microorganism is described in EP 238,023 (of Novo Nordisk A/S).
The
host cell may also be a yeast cell, e.g. a strain of Saccharomyces, in
particular
Saccharomyces cerevisiae.
The medium used to culture the transformed host cells may be any conventional
medium suitable for growing the host cells in question. The expressed
~ s endoglucanase specific for xyloglucan may conveniently be secreted into
the
culture medium and may be recovered therefrom by well-known procedures
including separating the cells from the medium by centrifugation or
filtration,
precipitating proteinaceous components of the medium by means of a salt such
as ammonium sulphate, followed by chromatographic procedures such as ion
2o exchange chromatography, affinity chromatography, or the like.
The thus purified endoglucanase may be employed for immunization of animals
for the production of antibodies. More specifically, antiserum against the
endoglucanase specific for xyloglucan may be raised by immunizing rabbits (or
other rodents) according to the procedure described by N. Axelsen et al. in: A
25 Manual of Quantitative Immunoelectrophoresis Blackwell Scientific
Publications,
1973, Chapter 23, or A. Johnstone and R. Thorpe, Immunochemistry in Practice,
Blackwell Scientific Publications, 1982 (more specifically pp. 27-31 ).
Purified
immunoglobulins may be obtained from the antisera, for example by salt
precipitation ((NH4)2S04), followed by dialysis and ion exchange
3o chromatography, e.g. on DEAE-Sephadex. Immunochemical characterization of
proteins may be done either by Outcherlony double-diffusion analysis (O.
Ouchterlony in: Handbook of Experimental Immunology (D.M. Weir, Ed.),
Blackwell Scientific Publications, 1967, pp. 655-706), by crossed
immunoelectrophoresis (N. Axelsen et al., su ra, Chapters 3 and 4), or by
rocket
35 immunoelectrophoresis (N. Axelsen et al., Chapter 2).
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23
The endoglucanases specific for xyloglucan useful in the present invention
compositions may be produced essentially free from other plant cell wall
degrading enzymes.
The enzyme preparation useful in the present invention compositions may be
prepared in accordance with methods known in the art and may be in the form of
a liquid or a dry preparation. For instance, the enzyme preparation may be in
the
form of a granulate or a microgranulate. The enzyme to be included in the
preparation may also be stabilized in accordance with methods known in the
art.
~o Test Methods:
Standard incubations: For characterization of enzymes, incubations are carried
out in Eppendorf tubes comprising 1 ml of substrate (AZCL-xyloglucan
substrates
or pure polysaccharides from MegaZyme, Australia). 0.5m1 0.4% AZCL-
substrate suspension is mixed with 0.5m1 0.1 M citrate/phosphate buffer of
optimal pH and 10 ~I of a suitably diluted enzyme solution is added.
Incubations
are carried out in Eppendorf Theromixers for 15 minutes at 30°C (if not
otherwise
specified) before heat-inactivation for 20 minutes at 95°C. Enzyme
incubations
are carried out in triplicate. A blank is produced in which enzyme is added
but
inactivated immediately. After centrifugation the absorbance of the
supernatant
2o is measured in microtiter plates at 620nm and the blank is subtracted.
The activities of the enzymes are measured on different pure polysaccharides:
xyloglucan and ~3-glucan from MegaZyme (AZCL-xyloglucan and AZCL-HE
cellulose), CMC (Blanose from Aqualon) and Avicell (microcrystaline cellulose
from Merck). Before use, Avicell is swelled in 85% orthophosphoric acid for 1
2s hour at room temperature and washed with acetone and water. 0.5%
solutions/suspensions of the different substrates are made in 0.1 M acetate
buffer
(if not otherwise specified) of the optimal pH, 10p,1 enzyme solutions are
added to
1 ml of substrate, incubations are carried at 30°C for 15 minutes
before heat-
inactivation as above. Reducing sugars are determined by reaction, in
microtiter
3o plates, with a PHBAH reagent comprising 0.15 g of para hydroxy benzoic acid
hydrazide (Sigma H-9882), 0.50 g of potassium-sodium tartrate (Merck 8087)
and 2% NaOH solution up to 10.0 ml. Results of blanks are subtracted. Glucose
is used as a standard.
pH optimum is measured on substrates from MegaZyme (for the enzymes
35 described hereinafter: EG II on AZCL-xylogulcan, EG III on pure ~3-glucan,
and
EG IV on AZCL-~3-glucan). 0.5m1 of 0.4% substrate is mixed with 0.5m1 0.1 M
CA 02357801 2001-06-29
WO 00/42157 PCT/US00/00839
24
citrate/phosphate buffer of varying pH and 10 ~I of a suitably diluted enzyme
solution is added. Incubations are carried out as described above. While
enzymes useful herein may have optimum pH at any pH as desired to match the
pH of the composition or cleaning method in which it will be used, preferably
the
s enzymes useful herein are active within the pH range of from about pH 6-11,
preferably 7-11, and more preferably within from about 8 to about 10.5.
The specificity of the different enzymes on the different AZCL-substrates is
tested as above at optimal pH in 0.1 M acetate buffer.
pH stability is measured by leaving the enzyme for 1 hour in 0.1 M citric
acid/tri
sodium phosphate buffers of varying pH before the enzyme is used for
incubation of AZCL-~3-glucan at the optimal pH.
Temperature optimum is measured by incubating the enzyme with AZCL-~3-
glucan substrate at varying temperatures for 15 minutes at the optimal pH.
Temperature stability is measured by leaving the enzyme, diluted in water, at
~s various temperatures for 1 hour before incubation at 30°C with the
relevant
substrate.
Km and specific activity are measured by carrying out incubations at substrate
concentrations (S) ranging from 0.025 to 1.5% (hereinafter: xyloglucan for EG
II
and (i-glucan for EG IV), measure the reaction rate (v), picture S/v as a
function
20 of S, carry out linear regression analysis, finding the slope (=1/Vmax) and
the
intercept (Km/Vmax) and calculating Km and the specific activity (=Vmax/E),
where E is the amount of enzyme added.
For gel filtration chromatography, 1 % solutions/suspensions of the above
mentioned pure polysaccharides are made. A suitable amount of enzyme is
25 added and incubations are carried out for 0, 1, 2, 4 and 24 hours before
heat
inactivation. 25p1 of sample is injected into three TSK-columns in a row (PW
64000, PW 63000, PW 62500) and saccharides are eluted with 0.4M acetate
buffer pH 3.0 at 0.8m1/min. Eluting saccharides are determined by a Shimadzu
RI detector and data are collected and processed by Dionex software. Dextrans
30 (from Sersa) are used as molecular weight standards.
Substrate specificity
The relative activity determined as the release of reducing sugar of different
enzymes from different polysaccharides compared to the optimal substrate
35 (100%) is provided in WO 94/14953 and reproduced in the table below.
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WO 00/42157 PCT/US00/00839
Enzyme EG II EG III EG IV
Avicell 1 % 0% 3%
CMC 1 % 2% 11
~i-glucan 0% 100% 100%
xyloglucan 100% 31 % 0%
From these results the specificities of the different endoglucanases are
presented as:
Enzyme EG II EG III EG IV
XGU/BGU o0 0.31 0
XGU/CMC 104 18 0
XG U/AVI U 114 0o p
B G U/XG U 0 3. 2 00
BGU/CMC 0 58 9.4
BGU/AVIU 0 ao 25
5 The results of termined on
substrate specificity AZCL-substrates
de is also
provided in WO
94/14953, and
reproduced in
the following
table:
Enzyme EG II EG III EG IV
HE-cellulose 1 % 100% 100%
~i-glucan 0% 36% 56%
Xyloglucan 100% 33% 1
Curdlan 0% 2% 4%
From the specificity results it is seen that compared to EG III and EG IV, EG
II is
specific for xyloglucan, as defined herein for use in the present invention
o compositions whereas the other two endoglucanases are not. EG III is active
towards all types of substrates, but does not have its highest activity for
xyloglucan, whereas EG IV cannot degrade xyloglucan and is very specific for
~3-
glucans. (There are some differences in the results obtained with reducing
sugars and AZCL-substrates. An explanation for this is that some AZCL-
~5 substrates are more sensitive than others. In this case AZCL-HE-cellulose
seems to be more sensitive than AZCL-~i-glucan).
The Km and specific activity for EG II and EG III are provided in WO 94/14953.
The standard deviations on 1Nmax and Km/Vmax obtained from the linear
CA 02357801 2001-06-29
WO 00/42157 PCT/US00/00839
26
regression analysis were used therein to calculate the intervals for the
enzymes
apparent from the following table:
Enzyme Substrate Km Spec. act r~2
Substrate units/mg
EG II xyloglucan 0.242-0.306 106-119 0.98
EG III ~3-glucan 0.136-0.207 165-186 0.98
Temperature optimum and temperature/pH stability - EG II and EG III have
similar temperature optimums (optimal activity between 30°C and
60°C) and
temperature stability (stable for 1 h up to 60°C) but EG II I is more
stable at
alkaline pH than EG II.
The aelfiltration chromatograms, which verify the substrate specificities,
show
that EG II degrades xyloglucan completely into oligomers of approximately 7-9
residues which are the known repeating subunits of xyloglucans (Fry, 1989). EG
III degrades xyloglucan to a much lesser extent and EG IV does not degrade
xyloglucan at all. EG III degrades ~-glucan to a large extent into DP 3-4 and
higher oligomers. This is in accordance with (i-glucans being composed of 3-4
~3-
1, 4-linked glucose units in a row interrupted by single ~3-1, 3-linkages.
The xyloglucanase is incorporated into the detergent compositions of the
invention preferably at a level of from 0.0001 % to 2%, more preferably from
0.0005% to 0.1 %, most preferably from 0.001 % to 0.02% pure enzyme by weight
of the composition.
Preferably, the detergent compositions of the present invention will comprise
the
three enzymes at the specific weight ratio of pure enzyme of mannanase to
pectate lyase to xyloglucananse of from 10:1:1 to 1:10:1 to 1:1:10. More
preferably such ratio wil range from 5:1:1 to 1:5:1 to 1:1:5 and most
preferably
will be a 1:1:1 ratio.
The mannanase, pectate lyase and/or xyloglucanase enxcompassed in the
so detergent compositions of the present invention, in addition to the enzyme
core
comprising the catalytically domain, may also comprise a cellulose binding
domain (CBD), the cellulose binding domain and enzyme core (the catalytically
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27
active domain) of the enzyme being operably linked. The cellulose binding
domain (CBD) may exist as an integral part of the encoded enzyme, or a CBD
from another origin may be introduced into the enzyme thus creating an enzyme
hybrid. In this context, the term "cellulose-binding domain" is intended to be
understood as defined by Peter Tomme et al. "Cellulose-Binding Domains:
Classification and Properties" in "Enzymatic Degradation of Insoluble
Carbohydrates", John N. Saddler and Michael H. Penner (Eds.), ACS
Symposium Series, No. 618, 1996. This definition classifies more than 120
cellulose- binding domains into 10 families (I-X), and demonstrates that CBDs
~o are found in various enzymes such as cellulases, xylanases, mannanases,
arabinofuranosidases, acetyl esterases and chitinases. CBDs have also been
found in algae, e.g. the red alga Porphyra purpurea as a non-hydrolytic
polysaccharide-binding protein, see Tomme et al., op.cit. However, most of the
CBDs are from cellulases and xylanases, CBDs are found at the N and C termini
5 of proteins or are internal. Enzyme hybrids are known in the art, see e.g.
WO
90/00609 and WO 95/16782, and may be prepared by transforming into a host
cell a DNA construct comprising at least a fragment of DNA encoding the
cellulose- binding domain ligated, with or without a linker, to a DNA sequence
encoding the mannanase and/or pectate lyase and/or xyloglucanase enzyme and
2o growing the host cell to express 'the fused gene. Enzyme hybrids may be
described by the following formula:
CBD-MR-X
wherein CBD is the N-terminal or the C-terminal region of an amino acid
sequence corresponding to at least the cellulose binding domain; MR is the
25 middle region (the linker), and may be a bond, or a short linking group
preferably
of from about 2 to about 100 carbon atoms, more preferably of from 2 to 40
carbon atoms; or is preferably from about 2 to to about 100 amino acids, more
preferably of from 2 to 40 amino acids; and X is an N-terminal or C-terminal
region of the mannanase, pectate lyase and/or xyloglucanase of the invention.
The above-mentioned enzymes may be of any suitable origin, such as vegetable,
animal, bacterial, fungal and yeast origin. Origin can further be mesophilic
or
extremophilic (psychrophilic, psychrotrophic, thermophilic, barophilic,
alkalophilic,
acidophilic, halophilic, etc.). Purified or non-purified forms of these
enzymes may
3s be used. Nowadays, it is common practice to modify wild-type enzymes via
protein / genetic engineering techniques in order to optimise their
performance
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28
efficiency in the detergent compositions of the invention. For example, the
variants may be designed such that the compatibility of the enzyme to commonly
encountered ingredients of such compositions is increased. Alternatively, the
variant may be designed such that the optimal pH, bleach or chelant stability,
catalytic activity and the like, of the enzyme variant is tailored to suit the
particular
cleaning application.
15
In particular, attention should be focused on amino acids sensitive to
oxidation in
the case of bleach stability and on surface charges for the surfactant
compatibility. The isoelectric point of such enzymes may be modified by the
substitution of some charged amino acids, e.g. an increase in isoelectric
point
may help to improve compatibility with anionic surfactants. The stability of
the
enzymes.may be further enhanced by the creation of e.g. additional salt
bridges
and enforcing metal binding sites to increase chelant stability.
Detergent components
The detergent compositions of the invention must contain at least one
additional
2o detergent component. The precise nature of these additional component, and
levels of incorporation thereof will depend on the physical form of the
composition, and the nature of the cleaning operation for which it is to be
used.
It has been further found that the performance of the detergent compositions
of
25 the present invention is enhanced by the addition of selected surfactants,
a
builder, another enzyme and/or a bleach system.
The detergent compositions according to the invention can be liquid, paste,
gels,
bars, tablets, spray, foam, powder or granular. Granular compositions can also
so be in "compact" form and the liquid compositions can also be in a
"concentrated"
form. Tablet compositions can be in single phase or multiple phase form.
It has been surprisingly found that the cleaning benefits of pectate lyase,
mannanase and xyloglucanase enzymes can be optimised and maximised with a
time controlled release technology. In particular, the time controlled
technology is
35 a tablet wherein the enzymes are separated from the inhibiting /
deactivating
other detergent ingredients in a different product phase having a different
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29
solubility in the wash. It has been surprisingly found that optimal
performance
efficiency of the enzymes can be achieved when said enzyme is incorporated
into a tablet and such system delivers significant soil and stain cleaning
benefits.
It has further been found that such time controlled release technology allows
a
broader range of enzymes to be used, including those that show a high degree
of
instability in standard detergent matrices. Indeed, the pectate lyase and
buffer
materials can preferably be incorporated into the rapid dissolving portion of
the
tablet. Without wishing to be bound by theory, it is believed that the enzymes
of
the present invention are released earlier than the inhibiting / deactivating
other
~o detergent ingredients and that optimum enzyme activity is obtained at the
beginning of the wash under buffered conditions, allowing the formulation in
detergent of pectate lyases, mannanases and xyloglucanases in the full range
of
available pectate lyases, mannanases and xyloglucanases.
~s Suitable tablets are detergent tablets which are not only sufficiently
robust to
withstand handling and transportation, but also at least a portion of which
dissolves rapidly in the wash water providing rapid delivery of the pectate
lyase
enzyme. It is preferred that at least one phase of the tablet dissolves in the
wash
water within the first ten minutes, preferably five minutes, more preferably
four
2o minutes of the wash cycle of an automatic dishwashing or laundry washing
machine. Preferably the washing machine is either an automatic dishwashing or
laundry washing machine. The time within which the multi-phase tablet or a
phase thereof or a detergent active component dissolves is determined
according to DIN 44990 using a dishwashing machine available from Bosch on
2s the normal 65°C washing program with water hardness at 18°H
using a minimum
of six replicates or a sufficient number to ensure reproducibility.
In a first embodiment, the present invention relates to a laundry detergent
and/or
fabric care compositions comprising a mannanase, a pectate lyase and a
so xyloglucanase (Examples 1- 15). In a second embodiment, the present
invention
relates to dishwashing or household detergent compositions (Examples 16-25).
The compositions of the invention may for example, be formulated as hand
dishwashing compositions, hand and machine laundry detergent compositions
35 including laundry additive compositions and compositions suitable for use
in the
soaking and/or pretreatment of stained fabrics and compositions for use in
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general household hard surface cleaning operations. When formulated as
compositions for use in manual dishwashing methods the compositions of the
invention preferably contain a surfactant and preferably other detergent
compounds selected from organic polymeric compounds, suds enhancing
agents, group II metal ions, solvents, hydrotropes and additional enzymes.
When formulated as compositions suitable for use in a laundry machine washing
method, the compositions of the invention preferably contain both a surfactant
and a builder compound and additionally one or more detergent components
~o preferably selected from organic polymeric compounds, bleaching agents,
additional enzymes, suds suppressors, dispersants, lime=soap dispersants, soil
suspension and anti-redeposition agents and corrosion inhibitors. Laundry
compositions can also contain softening agents, as additional detergent
components. Such compositions containing a pectate lyase, a mannanase and a
5 xyloglucanase can provide fabric cleaning, stain removal, and color
appearance
when formulated as laundry detergent compositions.
When formulated as compositions suitable for use in a machine dish wash
method, the compositions of the invention preferably contain a low foaming
2o nonionic surfactant, a builder system, and one or more components
preferably
selected from organic polymeric compounds, bleaching agents, additional
enzymes, suds suppressors, dispersants, lime-soap dispersants, soil suspension
and anti-redeposition agents and corrosion inhibitors.
2s The compositions of the invention can also be used as detergent additive
products in solid or liquid form. Such additive products are intended to
supplement or boost the performance of conventional detergent compositions
and can be added at any stage of the cleaning process.
3o If needed the density of the laundry detergent compositions herein ranges
from
400 to 1200 g/litre, preferably 500 to 950 g/litre of composition measured at
20°C.
The "compact" form of the compositions herein is best reflected by density
and,
in terms of composition, by the amount of inorganic filler salt; inorganic
filler salts
are conventional ingredients of detergent compositions in powder form; in
conventional detergent compositions, the filler salts are present in
substantial
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31
amounts, typically 17-35% by weight of the total composition. In the compact
compositions, the filler salt is present in amounts not exceeding 15% of the
total
composition, preferably not exceeding 10%, most preferably not exceeding 5%
by weight of the composition. The inorganic filler salts, such as meant in the
present compositions are selected from the alkali and alkaline-earth-metal
salts
of sulphates and chlorides. A preferred filler salt is sodium sulphate.
Liquid detergent compositions according to the present invention can also be
in a
"concentrated form", in such case, the liquid detergent compositions according
the present invention will contain a lower amount of water, compared to
1o conventional liquid detergents. Typically the water content of the
concentrated
liquid detergent is preferably less than 40%, more preferably less than 30%,
most
preferably less than 20% by weight of the detergent composition.
Suitable detergent compounds for use herein are selected from the group
consisting of the below described compounds.
Surfactant system
The detergent compositions according to the present invention generally
2o comprise a surfactant system wherein the surfactant can be selected from
nonionic and/or anionic and/or cationic and/or ampholytic and/or zwitterionic
and/or semi-polar surfactants. Preferably, the detergent compositions of the
present invention will comprise a nonionic, an anionic and/or a cationic
surfactant. Indeed, it has been surprisingly found that the detergent
compositions
of the present invention further comprising a nonionic, an anionic and/or a
cationic surfactant, provide enhanced cleaning, i.e. superior stain removal,
dingy
cleaning and whiteness maintenance. Without wishing to be bound by theory, it
is
believed that the enzymatic hydrolysis of the combined three enzymes of the
present invention, results in smaller particles being more easily removed by
3o nonionic surfactants known to focus on particulate soiling. Preferred
nonionic
surfactants are alkyl ethoxylated AE3 to AE7. It is also believed that the
combination of the fabric substantive cationic surfactant with the enzymatic
hydrolysis of the pectate lyase, mannanase and xyloglucanase provide improved
performances.
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32
The surfactant is typically present at a level of from 0.1 % to 60% by weight.
More
preferred levels of incorporation are 1 % to 35% by weight, most preferably
from
1 % to 30% by weight of detergent compositions in accord with the invention.
The surfactant is preferably formulated to be compatible with enzyme
components present in the composition. In liquid or gel compositions the
surfactant is most preferably formulated such that it promotes, or at least
does
not degrade, the stability of any enzyme in these compositions.
Preferred surfactant systems to be used according to the present invention
comprise as a surfactant one or more of the nonionic and/or anionic
surfactants
described herein.
Polyethylene, polypropylene, and polybutylene oxide condensates of alkyl
15 phenols are suitable for use as the nonionic surfactant of the surfactant
systems
of the present invention, with the polyethylene oxide condensates being
preferred. These compounds include the condensation products of alkyl phenols
having an alkyl group containing from about 6 to about 14 carbon atoms,
preferably from about 8 to about 14 carbon atoms, in either a straight-chain
or
2o branched-chain configuration with the alkylene oxide. In a preferred
embodiment,
the ethylene oxide is present in an amount equal to from about 2 to about 25
moles, more preferably from about 3 to about 15 moles, of ethylene oxide per
mole of alkyl phenol. Commercially available nonionic surfactants of this type
include IgepaITM CO-630, marketed by the GAF Corporation; and TritonTM X-
25 45, X-114, X-100 and X-102, all marketed by the Rohm & Haas Company. These
surfactants are commonly referred to as alkylphenol alkoxylates (e.g., alkyl
phenol ethoxylates).
The condensation products of primary and secondary aliphatic alcohols with
from
3o about 1 to about 25 moles of ethylene oxide are suitable for use as the
nonionic
surfactant of the nonionic surfactant systems of the present invention. The
alkyl
chain of the aliphatic alcohol can either be straight or branched, primary or
secondary, and generally contains from about 8 to about 22 carbon atoms.
Preferred are the condensation products of alcohols having an alkyl group
3s containing from about 8 to about 20 carbon atoms, more preferably from
about
to about 18 carbon atoms, with from about 2 to about 10 moles of ethylene
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33
oxide per mole of alcohol. About 2 to about 7 moles of ethylene oxide and most
preferably from 2 to 5 moles of ethylene oxide per mole of alcohol are present
in
said condensation products. Examples of commercially available nonionic
surfactants of this type include TergitoITM 15-S-9 (the condensation product
of
s C11-C15 linear alcohol with 9 moles ethylene oxide), TergitoITM 24-L-6 NMW
(the condensation product of C12-C14 primary alcohol with 6 moles ethylene
oxide with a narrow molecular weight distribution), both marketed by Union
Carbide Corporation; NeodoITM 45-9 (the condensation product of C14-C15
linear alcohol with 9 moles of ethylene oxide), NeodoITM 23-3 (the
condensation
~o product of C12-C13 linear alcohol with 3.0 moles of ethylene oxide),
NeodoITM
45-7 (the condensation product of C14-C15 linear alcohol with 7 moles of
ethylene oxide), NeodoITM 45-5 (the condensation product of Clq.-C15 linear
alcohol with 5 moles of ethylene oxide) marketed by Shell Chemical Company,
KyroTM EOB (the condensation product of C13-C15 alcohol with 9 moles
~s ethylene oxide), marketed by The Procter & Gamble Company, and Genapol LA
030 or 050 (the condensation product of C12-C14 alcohol with 3 or 5 moles of
ethylene oxide) marketed by Hoechst. Preferred range of HLB in these products
is from 8-11 and most preferred from 8-10.
2o Also useful as the nonionic surfactant of the surfactant systems of the
present
invention are the alkylpolysaccharides disclosed in U.S. Patent 4,565,647,
Llenado, issued January 21, 1986, having a hydrophobic group containing from
about 6 to about 30 carbon atoms, preferably from about 10 to about 16 carbon
atoms and a polysaccharide, e.g. a polyglycoside, hydrophilic group containing
2s from about 1.3 to about 10, preferably from about 1.3 to about 3, most
preferably
from about 1.3 to about 2.7 saccharide units. Any reducing saccharide
containing
or 6 carbon atoms can be used, e.g., glucose, galactose and galactosyl
moieties can be substituted for the glucosyl moieties (optionally the
hydrophobic
group is attached at the 2-, 3-, 4-, etc. positions thus giving a glucose or
3o galactose as opposed to a glucoside or galactoside). The intersaccharide
bonds
can be, e.g., between the one position of the additional saccharide units and
the
2-, 3-, 4-, and/or 6- positions on the preceding saccharide units.
The preferred alkylpolyglycosides have the formula
35 R20(CnH2n0)t(glYcosyl)x
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34
wherein R2 is selected from the group consisting of alkyl, alkylphenyl,
hydroxyalkyl, hydroxyalkylphenyl, and mixtures thereof in which the alkyl
groups
contain from about 10 to about 18, preferably from about 12 to about 14,
carbon
atoms; n is 2 or 3, preferably 2; t is from 0 to about 10, preferably 0; and x
is from
about 1.3 to about 10, preferably from about 1.3 to about 3, most preferably
from
about 1.3 to about 2.7. The glycosyl is preferably derived from glucose. To
prepare these compounds, the alcohol or alkylpolyethoxy alcohol is formed
first
and then reacted with glucose, or a source of glucose, to form the glucoside
(attachment at the 1-position). The additional glycosyl units can then be
attached
between their 1-position and the preceding glycosyl units 2-, 3-, 4- and/or 6-
position, preferably predominately the 2-position.
The condensation products of ethylene oxide with a hydrophobic base formed by
the condensation of propylene oxide with propylene glycol are also suitable
for
~5 use as the additional nonionic surfactant systems of the present invention.
The
hydrophobic portion of these compounds will preferably have a molecular weight
of from about 1500 to about 1800 and will exhibit water insolubility. The
addition
of polyoxyethylene moieties to this hydrophobic portion tends to increase the
water solubility of the molecule as a whole, and the liquid character of the
2o product is retained up to the point where the polyoxyethylene content is
about
50% of the total weight of the condensation product, which corresponds to
condensation with up to about 40 moles of ethylene oxide. Examples of
compounds of this type include certain of the commercially-available
PlurafacTM
LF404 and PluronicTM surfactants, marketed by BASF.
Also suitable for use as the nonionic surfactant of the nonionic surfactant
system
of the present invention, are the condensation products of ethylene oxide with
the product resulting from the reaction of propylene oxide and
ethylenediamine.
The hydrophobic moiety of these products consists of the reaction product of
3o ethylenediamine and excess propylene oxide, and generally has a molecular
weight of from about 2500 to about 3000. This hydrophobic moiety is condensed
with ethylene oxide to the extent that the condensation product contains from
about 40% to about 80% by weight of polyoxyethylene and has a molecular
weight of from about 5,000 to about 11,000. Examples of this type of nonionic
surfactant include certain of the commercially available TetronicTM compounds,
marketed by BASF.
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Preferred for use as the nonionic surfactant of the surfactant systems of the
present invention are polyethylene oxide condensates of alkyl phenols,
condensation products of primary and secondary aliphatic alcohols with from
5 about 1 to about 25 moles of ethylene oxide, alkylpolysaccharides, and
mixtures
thereof. Most preferred are Cg-C14 alkyl phenol ethoxylates having from 3 to
15
ethoxy groups and Cg-C1g alcohol ethoxylates (preferably C10 avg.) having from
2 to 10 ethoxy groups, and mixtures thereof.
1o Highly preferred nonionic surfactants are polyhydroxy fatty acid amide
surfactants of the formula.
R2-C-N-Z,
~5 O R1
wherein R1 is H, or R1 is C1~ hydrocarbyl, 2-hydroxy ethyl, 2-hydroxy propyl
or
a mixture thereof, R2 is C5-31 hydrocarbyl, and Z is a polyhydroxyhydrocarbyl
having a linear hydrocarbyl chain with at least 3 hydroxyls directly connected
to
2o the chain, or an alkoxylated derivative thereof. Preferably, R1 is methyl,
R2 is a
straight C11-15 alkyl or C16-18 alkyl or alkenyl chain such as coconut alkyl
or
mixtures thereof, and Z is derived from a reducing sugar such as glucose,
fructose, maltose, lactose, in a reductive amination reaction.
25 Suitable anionic surfactants to be used are linear alkyl benzene sulfonate,
alkyl
ester sulfonate surfactants including linear esters of Cg-C2p carboxylic acids
(i.e., fatty acids) which are sulfonated with gaseous S03 according to "The
Journal of the American Oil Chemists Society", 52 (1975), pp. 323-329.
Suitable
starting materials would include natural fatty substances as derived from
tallow,
3o palm oil, etc.
The preferred alkyl ester sulfonate surfactant, especially for laundry
applications,
comprise alkyl ester sulfonate surfactants of the structural formula
O
35 R3 _ CH _ C _ OR4
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36
S03M
wherein R3 is a Cg-C20 hydrocarbyl, preferably an alkyl, or combination
thereof,
R4 is a C1-C6 hydrocarbyl, preferably an alkyl, or combination thereof, and M
is
a cation which forms a water soluble salt with the alkyl ester sulfonate.
Suitable
salt-forming cations include metals such as sodium, potassium, and lithium,
and
substituted or unsubstituted ammonium cations, such as monoethanolamine,
diethanolamine, and triethanolamine. Preferably, R3 is C10-C16 alkyl, and R4
is
methyl, ethyl or isopropyl. Especially preferred are the methyl ester
sulfonates
wherein R3 is C10-C16 alkyl.
Other suitable anionic surfactants include the alkyl sulfate surfactants which
are
water soluble salts or acids of the formula ROS03M wherein R preferably is a
C10-C24 hYdrocarbyl, preferably an alkyl or hydroxyalkyl having a C10-C20
alkyl
~s component, more preferably a C12-C1g alkyl or hydroxyalkyl, and M is H or a
cation, e.g., an alkali metal cation (e.g. sodium, potassium, lithium), or
ammonium or substituted ammonium (e.g. methyl-, dimethyl-, and trimethyl
ammonium cations and quaternary ammonium cations such as tetramethyl-
ammonium and dimethyl piperdinium cations and quaternary ammonium cations
2o derived from alkylamines such as ethylamine, diethylamine, triethylamine,
and
mixtures thereof, and the like). Typically, alkyl chains of C12-C16 are
preferred
for lower wash temperatures (e.g. below about 50°C) and C16-18 alkyl
chains
are preferred for higher wash temperatures (e.g, above about 50°C).
2s Other anionic surfactants useful for detersive purposes can also be
included in
the detergent compositions of the present invention. These can include salts
(including, for example, sodium, potassium, ammonium, and substituted
ammonium salts such as mono-, di- and triethanolamine salts) of soap, Cg-C22
primary of secondary alkanesulfonates, Cg-C24 olefinsulfonates, sulfonated
3o polycarboxylic acids prepared by sulfonation of the pyrolyzed product of
alkaline
earth metal citrates, e.g., as described in British patent specification No.
1,082,179, Cg-C24 alkylpolyglycolethersulfates (containing up to 10 moles of
ethylene oxide); alkyl glycerol sulfonates, fatty acyl glycerol sulfonates,
fatty oleyl
glycerol sulfates, alkyl phenol ethylene oxide ether sulfates, paraffin
sulfonates,
35 alkyl phosphates, isethionates such as the acyl isethionates, N-acyl
taurates,
alkyl succinamates and sulfosuccinates, monoesters of sulfosuccinates
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37
(especially saturated and unsaturated C12-C1g monoesters) and diesters of
sulfosuccinates (especially saturated and unsaturated C6-C12 diesters), acyl
sarcosinates, sulfates of alkylpolysaccharides such as the sulfates of
alkylpolyglucoside (the nonionic nonsulfated compounds being described below),
s branched primary alkyl sulfates, and alkyl polyethoxy carboxylates such as
those
of the formula RO(CH2CH20)k-CH2C00-M+ wherein R is a Cg-C22 alkyl, k is
an integer from 1 to 10, and M is a soluble salt-forming cation. Resin acids
and
hydrogenated resin acids are also suitable, such as rosin, hydrogenated rosin,
and resin acids and hydrogenated resin acids present in or derived from tall
oil.
Further examples are described in "Surface Active Agents and Detergents" (Vol.
I and II by Schwartz, Perry and Berch). A variety of such surfactants are also
generally disclosed in U.S. Patent 3,929,678, issued December 30, 1975 to
Laughlin, et al. at Column 23, line 58 through Column 29, line 23 (herein
incorporated by reference).
When included therein, the laundry detergent compositions of the present
invention typically comprise from about 1 % to about 40%, preferably from
about
3% to about 20% by weight of such anionic surfactants.
2o Highly preferred anionic surfactants' include alkyl alkoxylated sulfate
surfactants
hereof are water soluble salts or acids of the formula RO(A)mS03M wherein R is
an unsubstituted C1p-C24 alkyl or hydroxyalkyl group having a C10-C24 alkyl
component, preferably a C12-C20 alkyl or hydroxyalkyl, more preferably C12-
C1g alkyl or hydroxyalkyl, A is an ethoxy or propoxy unit, m is greater than
zero,
typically between about 0.5 and about 6, more preferably between about 0.5 and
about 3, and M is H or a cation which can be, for example, a metal cation
(e.g.,
sodium, potassium, lithium, calcium, magnesium, etc.), ammonium or
substituted-ammonium cation. Alkyl ethoxylated sulfates as well as alkyl
propoxylated sulfates are contemplated herein. Specific examples of
substituted
so ammonium cations include methyl-, dimethyl, trimethyl-ammonium cations and
quaternary ammonium cations such as tetramethyl-ammonium and dimethyl
piperdinium cations and those derived from alkylamines such as ethylamine,
diethylamine, triethylamine, mixtures thereof, and the like. Exemplary
surfactants
are C12-C1g alkyl polyethoxylate (1.0) sulfate (C12-C18E(1.0)M), C12-C1g alkyl
polyethoxylate (2.25) sulfate (C12-C18E(2.25)M), C12-C1g alkyl polyethoxylate
(3.0) sulfate (C12-C18E(3.0)M), and C12-C1g alkyl polyethoxylate (4.0) sulfate
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38
(C12-C18E(4.0)M), wherein M is conveniently selected from sodium and
potassium.
The detergent compositions of the present invention may also contain cationic,
ampholytic, zwitterionic, and semi-polar surfactants, as well as the nonionic
and/or anionic surfactants other than those already described herein.
Cationic detersive surfactants suitable for use in the detergent compositions
of
the present invention are those having one long-chain hydrocarbyl group.
~o Examples of such cationic surfactants include the ammonium surfactants such
as alkyltrimethylammonium halogenides, and those surfactants having the
formula
[R2(OR3)yl[R4(OR3)yl2R5N+X_
~ 5 wherein R2 is an alkyl or alkyl benzyl group having from about 8 to about
18
carbon atoms in the alkyl chain, each R3 is selected from the group consisting
of
-CH2CH2-, -CH2CH(CH3)-, -CH2CH(CH20H)-, -CH2CH2CH2-, and mixtures
thereof; each R4 is selected from the group consisting of C1-C4 alkyl, C1-C4
hydroxyalkyl, benzyl ring structures formed by joining the two R4 groups, -
2o CH2CHOH-CHOHCOR6CHOHCH20H wherein R6 is any hexose or hexose
polymer having a molecular weight less than about 1000, and hydrogen when y
is not 0; R5 is the same as R4 or is an alkyl chain wherein the total number
of
carbon atoms of R2 plus R5 is not more than about 18; each y is from 0 to
about
and the sum of the y values is from 0 to about 15; and X is any compatible
25 anion.
Quaternary ammonium surfactant suitable for the present invention has the
formula (I):
pp ~3',,.,,Ra
30 )(-
Formula I
whereby R1 is a short chainlength alkyl (C6-C10) or alkylamidoalkyl of the
formula (II)
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39
C6-C.~ N
~CH~
O
Formula II
y is 2-4, preferably 3.
s whereby R2 is H or a C1-C3 alkyl,
whereby x is 0-4, preferably 0-2, most preferably 0,
whereby R3, R4 and R5 are either the same or different and can be either a
short chain alkyl (C1-C3) or alkoxylated alkyl of the formula III,
~o whereby X- is a counterion, preferably a halide, e.g. chloride or
methylsulfate.
Rs
~H
O')z
Formula III
R6 is C1-C4 and z is 1 or 2.
~ 5 Preferred quat ammonium surfactants are those as defined in formula I
whereby
R1 is Cg, C10 or mixtures thereof, x=o,
Rg, R4 = CH3 and R5 = CH2CH20H.
Highly preferred cationic surfactants are the water-soluble quaternary
ammonium
2o compounds useful in the present composition having the formula
R1 R2R3R4N+X- (i)
wherein R1 is Cg-C1g alkyl, each of R2, R3 and R4 is independently C1-Cq.
alkyl,
C1-Cq, hydroxy alkyl, benzyl, and -(C2H40)xH where x has a value from 2 to 5,
25 and X is an anion. Not more than one of R2, Rg or R4 should be benzyl.
The preferred alkyl chain length for R1 is C12-C15 particularly where the
alkyl
group is a mixture of chain lengths derived from coconut or palm kernel fat or
is
derived synthetically by olefin build up or OXO alcohols synthesis. Preferred
groups for R2R3 and R4 are methyl and hydroxyethyl groups and the anion X
3o may be selected from halide, methosulphate, acetate and phosphate ions.
Examples of suitable quaternary ammonium compounds of formulae (i) for use
herein are
coconut trimethyl ammonium chloride or bromide;
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coconut methyl dihydroxyethyl ammonium chloride or bromide;
decyl triethyl ammonium chloride;
decyl dimethyl hydroxyethyl ammonium chloride or bromide;
C12-15 dimethyl hydroxyethyl ammonium chloride or bromide;
5 coconut dimethyl hydroxyethyl ammonium chloride or bromide;
myristyl trimethyl ammonium methyl sulphate;
lauryl dimethyl benzyl ammonium chloride or bromide;
lauryl dimethyl (ethenoxy)4 ammonium chlor;de or bromide;
choline esters (compounds of formula (i) wherein R1 is
CH2-CH2-O-C-C12_14 alkyl and R2R3R4 are methyl).
O
di-alkyl imidazolines [compounds of formula (i)).
~5 Other cationic surfactants useful herein are also described in U.S. Patent
4,228,044, Cambre, issued October 14, 1980 and in European Patent
Application EP 000,224.
Typical cationic fabric softening components include the water-insoluble
2o quaternary-ammonium fabric softeiling actives or thei corresponding amine
precursor, the most commonly used having been di-long alkyl chain ammonium
chloride or methyl sulfate.
Preferred cationic softeners among these include the following:
'i) ditallow dimethylammonium chloride (DTDMAC);
25 2) dehydrogenated tallow dimethylammonium chloride;
3) dehydrogenated tallow dimethylammonium methylsulfate;
4) distearyl dimethylammonium chloride;
5) dioleyl dimethylammonium chloride;
6) dipalmityl hydroxyethyl methylammonium chloride;
30 7) stearyl benzyl dimethylammonium chloride;
8) tallow trimethylammonium chloride;
9) hydrogenated tallow trimethylammonium chloride;
10) 012-14 alkyl hydroxyethyl dimethylammonium chloride;
11 ) 012-18 alkyl dihydroxyethyl methylammonium chloride;
35 12) di(stearoyloxyethyl) dimethylammonium chloride (DSOEDMAC);
13) di(tallow-oxy-ethyl) dimethylammonium chloride;
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41
14) ditallow imidazolinium methylsulfate;
15) 1-(2-tallowylamidoethyl)-2-tallowyl imidazolinium methylsulfate.
Biodegradable quaternary ammonium compounds have been presented as
alternatives to the traditionally used di-long alkyl chain ammonium chlorides
and
methyl sulfates. Such quaternary ammonium compounds contain long chain
alk(en)yl groups interrupted by functional groups such as carboxy groups. Said
materials and fabric softening compositions containing them are disclosed in
numerous publications such as EP-A-0,040,562, and EP-A-0,239,910.
The quaternary ammonium compounds and amine precursors herein have the
formula (I) or (II), below
R3 R2
+ ~~~~~ ~ 1 X_ + N-(CHZ)n-CH -CHz X
R1 T~ T2
or
wherein Q is selected from -O-C(O)-, -C(O)-O-, -O-C(O)-O-, -NR4-C(O)-, -C(O)-
N R4-;
2o R1 is (CH2)n-Q-T2 or T3;
R2 is (CH2)m-Q-T4 or T5 or R3;
R3 is C1-C4 alkyl or C1-C4 hydroxyalkyl or H;
R4 is H or C1-C4 alkyl or C1-C4 hydroxyalkyl;
T1, T2, T3, T4, T5 are independently C11-C22 alkyl or alkenyl;
n and m are integers from 1 to 4; and
X- is a softener-compatible anion. Non-limiting examples of softener-
compatible
anions include chloride or methyl sulfate.
The alkyl, or alkenyl, chain T1, T2, T3, T4, T5 must contain at least 11
carbon
3o atoms, preferably at least 16 carbon atoms. The chain may be straight or
branched. Tallow is a convenient and inexpensive source of long chain alkyl
and
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42
alkenyl material. The compounds wherein T1, T2, T3, T4, T5 represents the
mixture of long chain materials typical for tallow are particularly preferred.
Specific examples of quaternary ammonium compounds suitable for use in the
aqueous fabric softening compositions herein include
1 ) N,N-di(tallowyl-oxy-ethyl)-N,N-dimethyl ammonium chloride;
2) N,N-di(tallowyl-oxy-ethyl)-N-methyl, N-(2-hydroxyethyl) ammonium methyl
sulfate;
3) N,N-di(2-tallowyl-oxy-2-oxo-ethyl)-N,N-dimethyl ammonium chloride;
4) N,N-di(2-tallowyl-oxy-ethylcarbonyl-oxy-ethyl)-N,N-dimethyl ammonium
chloride;
5) N-(2-tallowyl-oxy-2-ethyl)-N-(2-tallowyl-oxy-2-oxo-ethyl)-N,N-dimethyl
ammonium
chloride;
15 6) N,N,N-tri(tallowyl-oxy-ethyl)-N-methyl ammonium chloride;
7) N-(2-tallowyl-oxy-2-oxo-ethyl)-N-(tallowyl-N,N-dimethyl-ammonium chloride;
and
8) 1,2-ditallowyl-oxy-3-trimethylammoniopropane chloride;
and mixtures of any of the above materials.
When included therein, the detergent compositions of the present invention
typically comprise from 0.2% to about 25%, preferably from about 1 % to about
8% by weight of such cationic surfactants.
2s Ampholytic surfactants are also suitable for use in the detergent
compositions of
the present invention. These surfactants can be broadly described as aliphatic
derivatives of secondary or tertiary amines, or aliphatic derivatives of
heterocyclic
secondary and tertiary amines in which the aliphatic radical can be straight-
or
branched-chain. One of the aliphatic substituents contains at least about 8
so carbon atoms, typically from about 8 to about 18 carbon atoms, and at least
one
contains an anionic water-solubilizing group, e.g. carboxy, sulfonate,
sulfate. See
U.S. Patent No. 3,929,678 to Laughlin et al., issued December 30, 1975 at
column 19, lines 18-35, for examples of ampholytic surfactants.
When included therein, the detergent compositions of the present invention
s5 typically comprise from 0.2% to about 15%, preferably from about 1 % to
about
10% by weight of such ampholytic surfactants.
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43
Zwitterionic surfactants are also suitable for use in cleaning compositions.
These
surfactants can be broadly described as derivatives of secondary and tertiary
amines, derivatives of heterocyclic secondary and tertiary amines, or
derivatives
s of quaternary ammonium, quaternary phosphonium or tertiary sulfonium
compounds. See U.S. Patent No. 3,929,678 to Laughlin et al., issued December
30, 1975 at column 19, line 38 through column 22, line 48, for examples of
zwitterionic surfactants.
When included therein, the detergent compositions of the present invention
~o typically comprise from 0.2% to about 15%, preferably from about 1% to
about
10% by weight of such zwitterionic surfactants.
Semi-polar nonionic surfactants are a special category of nonionic surfactants
which include water-soluble amine oxides containing one alkyl moiety of from
s about 10 to about 18 carbon atoms and 2 moieties selected from the group
consisting of alkyl groups and hydroxyalkyl groups containing from about 1 to
about 3 carbon atoms; water-soluble phosphine oxides containing one alkyl
moiety of from about 10 to about 18 carbon atoms and 2 moieties selected from
the group consisting of alkyl groups and hydroxyalkyl groups containing from
2o about 1 to about 3 carbon atoms; and water-soluble sulfoxides containing
one
alkyl moiety of from about 10 to about 18 carbon atoms and a moiety selected
from the group consisting of alkyl and hydroxyalkyl moieties of from about 1
to
about 3 carbon atoms.
Semi-polar nonionic detergent surfactants include the amine oxide surfactants
25 having the formula
0
T
R3(OR4)xN(R5)2
wherein R3 is an alkyl, hydroxyalkyl, or alkyl phenyl group or mixtures therof
3o containing from about 8 to about 22 carbon atoms; R4 is an alkylene or
hydroxyalkylene group containing from about 2 to about 3 carbon atoms or
mixtures thereof; x is from 0 to about 3; and each R5 is an alkyl or
hydroxyalkyl
group containing from about 1 to about 3 carbon atoms or a polyethylene oxide
group containing from about 1 to about 3 ethylene oxide groups. The R5 groups
3s can be attached to each other, e.g., through an oxygen or nitrogen atom, to
form
a ring structure.
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44
These amine oxide surfactants in particular include C10-C1g alkyl dimethyl
amine oxides and Cg-C12 alkoxy ethyl dihydroxy ethyl amine oxides.
When included therein, the cleaning compositions of the present invention
typically comprise from 0.2% to about 15%, preferably from about 1 % to about
10% by weight of such semi-polar nonionic surfactants.
The detergent composition of the present invention may further comprise a
cosurfactant selected from the group of primary or tertiary amines.
Suitable primary amines for use herein include amines according to the formula
R1 NH2 wherein R1 is a Cg-C12, preferably Cg-C10 alkyl chain or R4X(CH2)n, X
is -O-,-C(O)NH- or -NH-, R4 is a Cg-C12 alkyl chain n is between 1 to 5,
preferably 3. R1 alkyl chains may be straight or branched and may be
interrupted with up to 12, preferably less than 5 ethylene oxide moieties.
Preferred amines according to the formula herein above are n-alkyl amines.
Suitable amines for use herein may be selected from 1-hexylamine, 1-
octylamine, 1-decylamine and laurylamine. Other preferred primary amines
include C8-C10 oxypropylamine, octyloxypropylamine, 2-ethylhexyl-
oxypropylamine, lauryl amido propylamine and amido propylamine.
2o Suitable tertiary amines for use herein include tertiary amines having the
formula
R1 R2R3N wherein R1 and R2 are C1-Cg alkylchains or
Rs
-C CHZ-CH-O ~H
R3 is either a Cg-C12, preferably Cg-C10 alkyl chain, or R3 is R4X(CH2)n,
whereby X is -O-, -C(O)NH- or -NH-,R4 is a Cq.-C12, n is between 1 to 5,
preferably 2-3. R5 is H or C1-C2 alkyl and x is between 1 to 6 .
Rg and Rq, may be linear or branched ; R3 alkyl chains may be interrupted with
up to 12, preferably less than 5, ethylene oxide moieties.
Preferred tertiary amines are R1 R2RgN where R1 is a C6-C12 alkyl chain, R2
and R3 are C1-C3 alkyl or
Rs
I
-C CHz-CH-O ~H
where R5 is H or CH3 and x = 1-2.
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Also preferred are the amidoamines of the formula:
0
R1-C-NH-( CH2 )-N-( R2 )
n 2
wherein R1 is C6-C12 alkyl; n is 2-4,
preferably n is 3; R2 and R3 is C1-C4
5
Most preferred amines of the present invention include 1-octylamine, 1-
hexylamine, 1-decylamine, 1-dodecylamine,CB-10oxypropylamine, N coco 1-
3diaminopropane, coconutalkyldimethylamine, lauryldimethylamine, lauryl
bis(hydroxyethyl)amine, coco bis(hydroxyehtyl)amine, lauryl amine 2 moles
~o propoxylated, octyl amine 2 moles propoxylated, lauryl
amidopropyldimethylamine, C8-10 amidopropyldimethylamine and C10
amidopropyldimethylamine.
The most preferred amines for use in the compositions herein are 1-hexylamine,
1-octylamine, 1-decylamine, 1-dodecylamine. Especially desirable are n
15 dodecyldimethylamine and bishydroxyethylcoconutalkylamine and oleylamine 7
times ethoxylated, lauryl amido propylamine and cocoamido propylamine.
Conventional detergent enzymes
2o Preferably, the detergent compositions can in addition to the mannanase,
pectate lyase and xyloglucanase further comprise one or more enzymes which
provide cleaning performance, fabric care and/or sanitisation benefits,
preferably
a pectin lyase, protease, lipase, cellulase and/or amylase.
25 Said enzymes include enzymes selected from cellulases, hemicellulases,
peroxidases, proteases, gluco-amylases, amylases, xylanases, lipases,
phospholipases, esterases, cutinases, other pectinases, keratanases,
reductases, oxidases, phenoloxidases, lipoxygenases, ligninases, pullulanases,
tannases, pentosanases, malanases, f3-glucanases, arabinosidases,
3o hyaluronidase, chondroitinase, laccase or mixtures thereof.
Each type of pectin degrading enzyme has a unique profile of substrate
specificity, activity and stability under different hardness, pH, temperature,
surfactant and other detergent ingredient matrix conditions. Pectin degrading
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46
enzymes are specifically directed to degrade pectin substances and in
particular
plant cell walls. In particular, pectate lyase enzymes are specifically
directed to
pectic acid chains of plant cell walls such as low methoxy pectins while
pectin
lyase is more specifically directed towards esterified pectin chains such as
high
methoxyl pectins. Moreover, it has been found that pectate lyases are metal
and
especially calcium sensitive, whereas pectin lyases do not require metals for
stabilisation and optimum enzymatic activity. It has been surprisingly found
that a
wide range of range of substrate specificity and a high flexibility toward a
variety
of wash conditions can be achieved with combining further the pectate lyase of
o the present invention with a pectin lyase. This results in synergistic
cleaning and
especially plant-based soil / stains and body soil removal.
Pectin lyase enzyme is classified under the EC classification EC 4.2.2.10, is
preferably substantially free of other pectic enzymes, and acts on the pectic
acids
~5 to bring about non-hydrolytic cleavage of alpha-1-4 glycosidic linkages to
give
oligosaccharides with terminal 4-deoxy-6-a-D-galacto-enuronosyl groups. The
pectin lyase of the present invention is substantially free of other pectic
enzymes.
By "substantially free of other pectic enzymes", it is meant pectin lyase
enzyme-
containing compositions which contain less than 25% of pectic enzymes which
2o are not pectin lyase enzymes, preferably less than 15%, more preferably
less
than 5%. The enzymatic activity can be measured according to the "Assay of
trans-eliminase activities toward pectin and pectic acid" described by K.
Horikoshi in Agr. Biol. Chem, Vol 36(2), 286.
Preferred pectin lyase for the purpose of the present invention is the pectin
lyase
25 described in the co-pending international patent application
PCT/DK98/00514,
internationally filed on November 24, 1998 and published under W099/27083
and which is
i) a polypeptide produced by Bacillus licheniformis, ATCC 14580, or
ii) a polypeptide comprising an amino acid sequence as shown in positions 31-
so 494 of SEQ ID N0:2 of PCT/DK98/00514, or
iii) an analogue of the polypeptide defined in i) or ii) which is at least 60%
homologous with said polypeptide, or
iv) is derived from said polypeptide by substitution, deletion or addition of
one or
several amino acids, provided that the arginins in positions 377 and 383
relative
35 to SEQ ID N0:2 of PCT/DK98/00514 are conserved and that the derived
polypeptide is at least 60% homologous with said polypeptide, or
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47
is immunologically reactive with a polyclonal antibody raised against said
polypeptide in purified form.
The cellulases usable in the present invention include both bacterial or
fungal
cellulases. Preferably, they will have a pH optimum of between 5 and 12 and a
specific activity above 50 CEVU/mg (Cellulose Viscosity Unit). Suitable
cellulases
are disclosed in U.S. Patent 4,435,307, Barbesgoard et al, J61078384 and
W096/02653 which discloses fungal cellulase produced respectively from
Humicola insolens, Trichoderma, Thielavia and Sporotrichum. EP 739 982
1o describes cellulases isolated from novel Bacillus species. Suitable
cellulases are
also disclosed in GB-A-2.075.028; GB-A-2.095.275; DE-OS-2.247.832 and
W095/26398.
Examples of such cellulases are cellulases produced by a strain of Humicola
insolens (Humicola grisea var. thermoidea), particularly the Humicola strain
DSM
1800.
Other suitable cellulases are cellulases originated from Humicola insolens
having
a molecular weight of about 50KDa, an isoelectric point of 5.5 and containing
415
amino acids; and a "43kD endoglucanase derived from Humicola insolens, DSM
1800, exhibiting cellulase activity; a preferred endoglucanase component has
the
2o amino acid sequence disclosed in PCT Patent Application No. WO 91/17243.
Also suitable cellulases are the EGIII cellulases from Trichoderma
longibrachiatum described in W094/21801, Genencor, published September 29,
1994. Especially suitable cellulases are the cellulases having color care
benefits.
Examples of such cellulases are cellulases described in European patent
application No. 91202879.2, filed November 6, 1991 (Novo). Carezyme and
Celluzyme (Novo Nordisk A/S) are especially useful. See also W091/17244 and
W091/21801. Other suitable cellulases for fabric care and/or cleaning
properties
are described in W096/34092, W096/17994 and W095/24471.
Said cellulases are normally incorporated in the detergent composition at
levels
3o from 0.0001 % to 2% of pure enzyme by weight of the detergent composition.
Peroxidase enzymes are used in combination with oxygen sources, e.g.
percarbonate, perborate, persulfate, hydrogen peroxide, etc and with a
phenolic
substrate as bleach enhancing molecule. They are used for "solution
bleaching",
i.e. to prevent transfer of dyes or pigments removed from substrates during
wash
operations to other substrates in the wash solution. Peroxidase enzymes are
CA 02357801 2001-06-29
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48
known in the art, and include, for example, horseradish peroxidase, ligninase
and
haloperoxidase such as chloro- and bromo-peroxidase. Peroxidase-containing
detergent compositions are disclosed, for example, in PCT International
Application WO 89/099813, W089/09813 and in European Patent application EP
No. 91202882.6, filed on November 6, 1991 and EP No. 96870013.8, filed
February 20, 1996. Also suitable is the laccase enzyme.
Enhancers are generally comprised at a level of from 0.1 % to 5% by weight of
total composition. Preferred enhancers are substitued phenthiazine and
phenoxasine 10-Phenothiazinepropionicacid (PPT), 10-ethylphenothiazine-4-
carboxylic acid (EPC), 10-phenoxazinepropionic acid (POP) and 10-
methylphenoxazine (described in WO 94/12621 ) and substitued syringates (C3-
C5 substitued alkyl syringates) and phenols. Sodium percarbonate or perborate
are preferred sources of hydrogen peroxide.
Said peroxidases are normally incorporated in the detergent composition at
15 levels from 0.0001 % to 2% of pure enzyme by weight of the detergent
composition.
Other preferred enzymes that can be included in the detergent compositions of
the present invention include lipases. Suitable lipase enzymes for detergent
2o usage include those produced by microorganisms of the Pseudomonas group,
such as Pseudomonas stutzeri ATCC 19.154, as disclosed in British Patent
1,372,034. Suitable lipases include those which show a positive immunological
cross-reaction with the antibody of the lipase, produced by the microorganism
Pseudomonas fluorescent IAM 1057. This lipase is available from Amano
2s Pharmaceutical Co. Ltd., Nagoya, Japan, under the trade name Lipase P
"Amano," hereinafter referred to as "Amano-P". Other suitable commercial
lipases include Amano-CES, lipases ex Chromobacter viscosum, e.g.
Chromobacter viscosum var. lipolyticum NRRLB 3673 from Toyo Jozo Co.,
Tagata, Japan; Chromobacter viscosum lipases from U.S. Biochemical Corp.,
3o U.S.A. and Disoynth Co., The Netherlands, and lipases ex Pseudomonas
gladioli. Especially suitable lipases are lipases such as M1 LipaseR and
LipomaxR (Gist-Brocades) and LipolaseR and Lipolase UItraR(Novo) which have
found to be very effective when used in combination with the compositions of
the
present invention. Also suitables are the lipolytic enzymes described in EP
258
35 068, WO 92/05249 and WO 95/22615 by Novo Nordisk and in WO 94/03578,
WO 95/35381 and WO 96/00292 by Unilever.
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49
Also suitable are cutinases [EC 3.1.1.50] which can be considered as a special
kind of lipase, namely lipases which do not require interfacial activation.
Addition
of cutinases to detergent compositions have been described in e.g. WO-A
88/09367 (Genencor); WO 90/09446 (Plant Genetic System) and WO 94/14963
and WO 94/14964 (Unilever).
The lipases and/or cutinases are normally incorporated in the detergent
composition at levels from 0.0001 % to 2% of pure enzyme by weight of the
detergent composition.
o Suitable proteases are the subtilisins which are obtained from particular
strains of
B. subtilis and B. licheniformis (subtilisin BPN and BPN'). One suitable
protease
is obtained from a strain of Bacillus, having maximum activity throughout the
pH
range of 8-12, developed and sold as ESPERASE~ by Novo Industries A/S of
Denmark, hereinafter "Novo". The preparation of this enzyme and analogous
~ s enzymes is described in GB 1,243,784 to Novo. Other suitable proteases
include ALCALASE~, DURAZYM~ and SAVINASE~ from Novo and
MAXATASE~, MAXACAL~, PROPERASE~ and MAXAPEM~ (protein
engineered Maxacal) from Gist-Brocades. Proteolytic enzymes also encompass
modified bacterial serine proteases, such as those described in European
Patent
2o Application Serial Number 87 303761.8, filed April 28, 1987 (particularly
pages
17, 24 and 98), and which is called herein "Protease B", and in European
Patent
Application 199,404, Venegas, published October 29, 1986, which refers to a
modified bacterial serine protealytic enzyme which is called "Protease A"
herein.
Suitable is the protease called herein "Protease C", which is a variant of an
25 alkaline serine protease from Bacillus in which lysine replaced arginine at
position 27, tyrosine replaced valine at position 104, serine replaced
asparagine
at position 123, and alanine replaced threonine at position 274. Protease C is
described in EP 90915958:4, corresponding to WO 91/06637, Published May 16,
1991. Genetically modified variants, particularly of Protease C, are also
included
3o herein.
A preferred protease referred to as "Protease D" is a carbonyl hydrolase
variant
having an amino acid sequence not found in nature, which is derived from a
precursor carbonyl hydrolase by substituting a different amino acid for a
plurality
of amino acid residues at a position in said carbonyl hydrolase equivalent to
35 position +76, preferably also in combination with one or more amino acid
residue
positions equivalent' to those selected from the group consisting of +99,
+101,
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WO 00/42157 PCT/iJS00/00839
+103, +104, +107, +123, +27, +105, +109, +126, +128, +135, +156, +166, +195,
+197, +204, +206, +210, +216, +217, +218, +222, +260, +265, and/or +274
according to the numbering of Bacillus amyloliquefaciens subtilisin, as
described
in W095/10591 and in the patent application of C. Ghosh, et al, "Bleaching
5 Compositions Comprising Protease Enzymes" having US Serial No. 08/322,677,
filed October 13, 1994. Also suitable is a carbonyl hydrolase variant of the
protease described in W095/10591, having an amino acid sequence derived by
replacement of a plurality of amino acid residues replaced in the precursor
enzyme corresponding to position +210 in combination with one or more of the
o following residues : +33, +62, +67, +76, +100, +101, +103, +104, +107, +128,
+129, +130, +132, +135, +156, +158, +164, +166, +167, +170, +209, +215,
+217, +218, and +222, where the numbered position corresponds to naturally-
occurring subtilisin from Bacillus amyloliquefaciens or to equivalent amino
acid
residues in other carbonyl hydrolases or subtilisins, such as Bacillus lentus
~5 subtilisin (co-pending patent application US Serial No. 60/048,550, filed
June 04,
1997).
Also suitable for the present invention are proteases described in patent
applications EP 251 446 and WO 91/06637, protease BLAP~ described in
W091/02792 and their variants described in WO 95/23221.
2o See also a high pH protease from Bacillus sp. NCIMB 40338 described in WO
93/18140 A to Novo. Enzymatic detergents comprising protease, one or more
other enzymes, and a reversible protease inhibitor are described in WO
92/03529 A to Novo. When desired, a protease having decreased adsorption
and increased hydrolysis is available as described in WO 95/07791 to Procter &
25 Gamble. A recombinant trypsin-like protease for detergents suitable herein
is
described in WO 94/25583 to Novo. Other suitable proteases are described in
EP 516 200 by Unilever.
The proteolytic enzymes are incorporated in the detergent compositions of the
present invention a level of from 0.0001 % to 2%, preferably from 0.001 % to
30 0.2%, more preferably from 0.005% to 0.1 % pure enzyme by weight of the
composition.
Amylases (a and/or f3) can be included for removal of carbohydrate-based
stains.
W094/02597, Novo Nordisk A/S published February 03, 1994, describes
35 cleaning compositions which incorporate mutant amylases. See also
W095/10603, Novo Nordisk A/S, published April 20, 1995. Other amylases
CA 02357801 2001-06-29
WO 00/42157 PCT/US00/00839
51
known for use in cleaning compositions include both a- and ~-amylases. a-
Amylases are known in the art and include those disclosed in US Pat. no.
5,003,257; EP 252,666; WO/91/00353; FR 2,676,456; EP 285,123; EP 525,610;
EP 368,341; and British Patent specification no. 1,296,839 (Novo). Other
suitable
amylases are stability-enhanced amylases described in W094/18314, published
August 18, 1994 and W096/05295, Genencor, published February 22, 1996 and
amylase variants having additional modification in the immediate parent
available
from Novo Nordisk A/S, disclosed in WO 95/10603, published April 95. Also
suitable are amylases described in EP 277 216, W095/26397 and W096/23873
(all by Novo Nordisk).
Examples of commercial a-amylases products are Purafect Ox Am~ from
Genencor and Termamyl~, Ban~ ,Fungamyl~ and Duramyl~, all available from
Novo Nordisk A/S Denmark. W095/26397 describes other suitable amylases : a-
amylases characterised by having a specific activity at least 25% higher than
the
specific activity of Termamyl~ at a temperature range of 25°C to
55°C and at a
pH value in the range of 8 to 10, measured by the Phadebas~ a-amylase activity
assay. Suitable are variants of the above enzymes, described in W096/23873
(Novo Nordisk). Other amylolytic enzymes with improved properties with respect
to the activity level and the combination of thermostability and a higher
activity
level are described in W095/35382.
The amylolytic enzymes are incorporated in the detergent compositions of the
present invention a level of from 0.0001 % to 2%, preferably from 0.00018% to
0.06%, more preferably from 0.00024% to 0.048% pure enzyme by weight of the
composition.
The above-mentioned enzymes may be of any suitable origin, such as vegetable,
animal, bacterial, fungal and yeast origin. Origin can further be mesophilic
or
extremophilic (psychrophilic, psychrotrophic, thermophilic, barophilic,
alkalophilic,
acidophilic, halophilic, etc.). Purified or non-purified forms of these
enzymes may
so be used. Nowadays, it is common practice to modify wild-type enzymes via
protein / genetic engineering techniques in order to optimise their
performance
efficiency in the detergent compositions of the invention. For example, the
variants may be designed such that the compatibility of the enzyme to commonly
encountered ingredients of such compositions is increased. Alternatively, the
s5 variant may be designed such that the optimal pH, bleach or chelant
stability,
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52
catalytic activity and the like, of the enzyme variant is tailored to suit the
particular
cleaning application.
In particular, attention should be focused on amino acids sensitive to
oxidation in
the case of bleach stability and on surface charges for the surfactant
compatibility. The isoelectric point of such enzymes may be modified by the
substitution of some charged amino acids, e.g. an increase in isoelectric
point
may help to improve compatibility with anionic surfactants. The stability of
the
enzymes may be further enhanced by the creation of e.g. additional salt
bridges
and enforcing calcium binding sites to increase chelant stability. Special
attention
must be paid to the cellulases as most of the cellulases have separate binding
domains (CBD). Properties of such enzymes can be altered by modifications in
these domains.
Said enzymes are normally incorporated in the detergent composition at levels
from 0.0001 % to 2% of pure enzyme by weight of the detergent composition. The
enzymes can be added as separate single ingredients (prills, granulates,
stabilized liquids, etc... containing one enzyme ) or as mixtures of two or
more
enzymes ( e.g. cogranulates ).
Other suitable detergent ingredients that can be added are enzyme oxidation
scavengers which are described in Copending European Patent application
92870018.6 filed on January 31, 1992. Examples of such enzyme oxidation
scavengers are ethoxylated tetraethylene polyamines.
A range of enzyme materials and means for their incorporation into synthetic
detergent compositions is also disclosed in WO 9307263 A and WO 9307260 A
to Genencor International, WO 8908694 A to Novo, and U.S. 3,553,139, January
5, 1971 to McCarty et al. Enzymes are further disclosed in U.S. 4,101,457,
Place
3o et al, July 18, 1978, and in U.S. 4,507,219, Hughes, March 26, 1985. Enzyme
materials useful for liquid detergent formulations, and their incorporation
into
such formulations, are disclosed in U.S. 4,261,868, Hora et al, April 14,
1981.
Enzymes for use in detergents can be stabilised by various techniques. Enzyme
stabilisation techniques are disclosed and exemplified in U.S. 3,600,319,
August
17, 1971, Gedge et al, EP 199,405 and EP 200,586, October 29, 1986, Venegas.
Enzyme stabilisation systems are also described, for example, in U.S.
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3,519,570. A useful Bacillus, sp. AC13 giving proteases, xylanases and
cellulases, is described in WO 9401532 A to Novo.
Colour care and fabric care benefits
Technologies which provide a type of colour care benefit can also be included.
Examples of these technologies are metallo catalysts for colour maintenance.
Such metallo catalysts are described in copending European Patent Application
No. 92870181.2. Dye fixing agents, polyolefin dispersion for anti-wrinkles and
improved water absorbency, perfume and amino-functional polymer
(PCT/US97/16546) for colour care treatment and perfume substantivity are
further examples of colour care / fabric care technologies and are described
in
the co-pending Patent Application No. 96870140.9, filed November 07, 1996.
~ 5 Fabric softening agents can also be incorporated into detergent
compositions in
accordance with the present invention. These agents may be inorganic or
organic in type. Inorganic softening agents are exemplified by the smectite
clays
disclosed in GB-A-1 400 898 and in USP 5,019,292. Organic fabric softening
agents include the water insoluble tertiary amines as disclosed in GB-A1 514
276
2o and EP-BO 011 340 and their combination with mono C12-C14 quaternary
ammonium salts are disclosed in EP-B-0 026 527 and EP-B-0 026 528 and di-
long-chain amides as disclosed in EP-B-0 242 919. Other useful organic
ingredients of fabric softening systems include high molecular weight
polyethylene oxide materials as disclosed in EP-A-0 299 575 and 0 313 146.
Levels of smectite clay are normally in the range from 2% to 20%, more
preferably from 5% to 15% by weight, with the material being added as a dry
mixed component to the remainder of the formulation. Organic fabric softening
agents such as the water-insoluble tertiary amines or dilong chain amide
3o materials are incorporated at levels of from 0.5% to 5% by weight, normally
from
1 % to 3% by weight whilst the high molecular weight polyethylene oxide
materials
and the water soluble cationic materials are added at levels of from 0.1 % to
2%,
normally from 0.15% to 1.5% by weight. These materials are normally added to
the spray dried portion of the composition, although in some instances it may
be
more convenient to add them as a dry mixed particulate, or spray them as
molten
liquid on to other solid components of the composition.
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Bleaching agent
It has been surprisingly found that the detergent compositions of the present
invention further comprising a bleaching agent, especially a bleach activator
bleaching system, provide enhanced food stain removal and whiteness
maintenance. Whithout wishing to be bound by theory, it is believed the
smaller
chromophoric particles resulting from the combined hydrolysis action of the
pectate lyase, mannanase and xyloglucanase, are more easily attacked by the
1o bleach activated system, especially at low temperature.
Preferred detergent ingredients that can be included in the detergent
compositions of the present invention include bleaching agents such as
hydrogen
peroxide, PB1, PB4 and percarbonate with a particle size of 400-800 microns.
~ 5 These bleaching agent components can include one or more oxygen bleaching
agents and, depending upon the bleaching agent chosen, one or more bleach
activators. When present oxygen bleaching compounds will typically be present
at levels of from about 1 % to about 25%.
2o The bleaching agent component for use herein can be any of the bleaching
agents useful for detergent compositions including oxygen bleaches as well as
others known in the art. The bleaching agent suitable for the present
invention
can be an activated or non-activated bleaching agent.
25 One category of oxygen bleaching agent that can be used encompasses
percarboxylic acid bleaching agents and salts thereof. Suitable examples of
this
class of agents include magnesium monoperoxyphthalate hexahydrate, the
magnesium salt of meta-chloro perbenzoic acid, 4-nonylamino-4-
oxoperoxybutyric acid and diperoxydodecanedioic acid. Such bleaching agents
so are disclosed in U.S. Patent 4,483,781, U.S. Patent Application 740,446,
European Patent Application 0,133,354 and U.S. Patent 4,412,934. Highly
preferred bleaching agents also include 6-nonylamino-6-oxoperoxycaproic acid
as described in U.S. Patent 4,634,551.
Another category of bleaching agents that can be used encompasses the
35 halogen bleaching agents. Examples of hypohalite bleaching agents, for
example, include t~richloro isocyanuric acid and the sodium and potassium
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dichloroisocyanurates and N-chloro and N-bromo alkane sulphonamides. Such
materials are normally added at 0.5-10% by weight of the finished product,
preferably 1-5% by weight.
5 The hydrogen peroxide releasing agents can be used in combination with
bleach
activators such as tetraacetylethylenediamine (TAED), nonanoyloxybenzene-
sulfonate (NOBS, described in US 4,412,934), 3,5,-
trimethylhexanoloxybenzenesulfonate (ISONOBS, described in EP 120,591 ) or
pentaacetylglucose (PAG)or Phenolsulfonate ester of N-nonanoyl-6-
aminocaproic acid (NACA-OBS, described in W094/28106), which are
perhydrolyzed to form a peracid as the active bleaching species, leading to
improved bleaching effect. Also suitable activators are acylated citrate
esters
such as disclosed in co-pending European Patent Application No. 91870207.7
and unsymetrical acyclic imide bleach activator of the following formula as
15 disclosed in the Procter & Gamble co-pending patent applications US serial
No.
60/022,786 (filed July 30, 1996) and No. 60/028,122 (filed October 15, 1996)
O O
R' '
1 N R3
R2
wherein R1 is a C7-C13 linear or branched chain saturated or unsaturated alkyl
group, R2 is a C1-Cg, linear or branched chain saturated or unsaturated alkyl
2o group and R3 is a C1-C4 linear or branched chain saturated or unsaturated
alkyl
group.
Useful bleaching agents, including peroxyacids and bleaching systems
comprising bleach activators and peroxygen bleaching compounds for use in
25 detergent compositions according to the invention are described in our co-
pending applications USSN 08/136,626, PCT/US95/07823, W095/27772,
W095/27773, W095/27774 and W095/27775.
The hydrogen peroxide may also be present by adding an enzymatic system (i.e.
so an enzyme and a substrate therefore) which is capable of generating
hydrogen
peroxide at the beginning or during the washing and/or rinsing process. Such
enzymatic systems are disclosed in EP Patent Application 91202655.6 filed
October 9, 1991.
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Metal-containing catalysts for use in bleach compositions, include cobalt-
containing catalysts such as Pentaamine acetate cobalt(III) salts and
manganese-containing catalysts such as those described in EPA 549 271; EPA
549 272; EPA 458 397; US 5,246,621; EPA 458 398; US 5,194,416 and US
5,114,611. Bleaching composition comprising a peroxy compound, a
manganese-containing bleach catalyst and a chelating agent is described in the
patent application No 94870206.3.
Bleaching agents other than oxygen bleaching agents are also known in the art
and can be utilized herein. One type of non-oxygen bleaching agent of
particular
interest includes photoactivated bleaching agents such as the sulfonated zinc
and/or aluminum phthalocyanines. These materials can be deposited upon the
substrate during the washing process. Upon irradiation with light, in the
presence
~ 5 of oxygen, such as by hanging clothes out to dry in the daylight, the
sulfonated
zinc phthalocyanine is activated and, consequently, the substrate is bleached.
Preferred zinc phthalocyanine and a photoactivated bleaching process are
described in U.S. Patent 4,033,718. Typically, detergent compositions will
contain about 0.025% to about 1.25%, by weight, of sulfonated zinc
2o phthalocyanine.
Builder system
The detergent compositions according to the present invention will preferably
25 further comprise a builder system, more preferably an inorganic builder,
most
preferably Zeolite A, sodium layered silica and/or sodium tripolyphosphate. It
has
been surprisingly found that the detergent compositions of the present
invention
further comprising such builder, provide enhanced cleaning. Without wishing to
be bound by theory, it is believed that the calcium deposit on pectin-and
3o hydrocolloid gums containing stains/soil. Therefore, the use of the builder
is
believed to remove the entrapped calcium and favour the enzymatic action of
the
pectate lyase, mannanase and xyloglucanase.
Any conventional builder system is suitable for use herein including
35 aluminosilicate materials, silicates, polycarboxylates, alkyl- or alkenyl-
succinic
acid and fatty acids, materials such as ethylenediamine tetraacetate,
diethylene
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57
triamine pentamethyleneacetate, metal ion sequestrants such as
aminopolyphosphonates, particularly ethylenediamine tetramethylene
phosphonic acid and diethylene triamine pentamethylenephosphonic acid.
Phosphate builders can also be used herein.
Suitable builders can be an inorganic ion exchange material, commonly an
inorganic hydrated aluminosilicate material, more particularly a hydrated
synthetic zeolite such as hydrated zeolite A, X, B, HS or MAP.
Another suitable inorganic builder material is layered silicate, e.g. SKS-6
~o (Hoechst). SKS-6 is a crystalline layered silicate consisting of sodium
silicate
(Na2Si205).
Suitable polycarboxylates containing one carboxy group include lactic acid,
glycolic acid and ether derivatives thereof as disclosed in Belgian Patent
Nos.
831,368, 821,369 and 821,370. Polycarboxylates containing two carboxy groups
include the water-soluble salts of succinic acid, malonic acid,
(ethylenedioxy)
diacetic acid, malefic acid, diglycollic acid, tartaric acid, tartronic acid
and fumaric
acid, as well as the ether carboxylates described in German Offenlegenschrift
2,446,686, and 2,446,687 and U.S. Patent No. 3,935,257 and the sulfinyl
carboxylates described in Belgian Patent No. 840,623. Polycarboxylates
2o containing three carboxy groups include, in particular, water-soluble
citrates,
aconitrates and citraconates as well as succinate derivatives such as the
carboxymethyloxysuccinates described in British Patent No. 1,379,241,
lactoxysuccinates described in Netherlands Application 7205873, and the
oxypolycarboxylate materials such as 2-oxa-1,1,3-propane tricarboxylates
described in British Patent No. 1,387,447.
Polycarboxylates containing four carboxy groups include oxydisuccinates
disclosed in British Patent No. 1,261,829, 1,1,2,2-ethane tetracarboxylates,
1,1,3,3-propane tetracarboxylates and 1,1,2,3-propane tetracarboxylates.
3o Polycarboxylates containing sulfo substituents include the sulfosuccinate
derivatives disclosed in British Patent Nos. 1,398,421 and 1,398,422 and in
U.S.
Patent No. 3,936,448, and the sulfonated pyrolysed citrates described in
British
Patent No. 1,082,179, while polycarboxylates containing phosphone substituents
are disclosed in British Patent No. 1,439,000.
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Alicyclic and heterocyclic polycarboxylates include cyclopentane-cis,cis,cis-
tetracarboxylates, cyclopentadienide pentacarboxylates, 2,3,4,5-tetrahydro-
furan
cis, cis, cis-tetracarboxylates, 2,5-tetrahydro-furan -cis - dicarboxylates,
2,2,5,5
tetrahydrofuran - tetracarboxylates, 1,2,3,4,5,6-hexane -hexacar-boxylates and
and carboxymethyl derivatives of polyhydric alcohols such as sorbitol,
mannitol
and xylitol. Aromatic poly-carboxylates include mellitic acid, pyromellitic
acid and
the phthalic acid derivatives disclosed in British Patent No. 1,425,343.
Of the above, the preferred polycarboxylates are hydroxycarboxylates
containing
up to three carboxy groups per molecule, more particularly citrates.
Preferred builder systems for use in the present compositions include a
mixture
of a water-insoluble aluminosilicate builder such as zeolite A or of a layered
silicate (SKS-6), and a water-soluble carboxylate chelating agent such as
citric
acid. Other preferred builder systems include a mixture of a water-insoluble
~5 aluminosilicate builder such as zeolite A, and a watersoluble carboxylate
chelating agent such as citric acid. Preferred builder systems for use in
liquid
detergent compositions of the present invention are soaps and
polycarboxylates.
Other builder materials that can form part of the builder system for use in
2o granular compositions include inorganic materials such as alkali metal
carbonates, bicarbonates, silicates, and organic materials such as the organic
phosphonates, amino polyalkylene phosphonates and amino polycarboxylates.
Other suitable water-soluble organic salts are the homo- or co-polymeric acids
or
their salts, in which the polycarboxylic acid comprises at least two carboxyl
25 radicals separated from each other by not more than two carbon atoms.
Polymers of this type are disclosed in GB-A-1,596,756. Examples of such salts
are polyacrylates of MW 2000-5000 and their copolymers with malefic anhydride,
such copolymers having a molecular weight of from 20,000 to 70,000, especially
about 40,000.
Detergency builder salts are normally included in amounts of from 5% to 80% by
weight of the composition preferably from 10% to 70% and most usually from
30% to 60% by weight.
Chelating Agents
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The detergent compositions herein may also optionally contain one or more iron
and/or manganese chelating agents. Such chelating agents can be selected
from the group consisting of amino carboxylates, amino phosphonates,
polyfunctionally-substituted aromatic chelating agents and mixtures therein,
all as
hereinafter defined. Without intending to be bound by theory, it is believed
that
the benefit of these materials is due in part to their exceptional ability to
remove
iron and manganese ions from washing solutions by formation of soluble
chelates.
Amino carboxylates useful as optional chelating agents include
ethylenediaminetetracetates, N-hydroxyethylethylenediaminetriacetates,
nitrilotriacetates, ethylenediamine tetraproprionates, triethylenetetraamine-
hexacetates, diethylenetriaminepentaacetates, and ethanoldiglycines, alkali
metal, ammonium, and substituted ammonium salts therein and mixtures therein.
~ 5 Amino phosphonates are also suitable for use as chelating agents in the
compositions of the invention when at lease low levels of total phosphorus are
permitted in detergent compositions, and include ethylenediaminetetrakis
(methylenephosphonates) as DEQUEST. Preferred, these amino phosphonates
to not contain alkyl or alkenyl groups with more than about 6 carbon atoms.
Polyfunctionally-substituted aromatic chelating agents are also useful in the
compositions herein. See U.S. Patent 3,812,044, issued May 21, 1974, to
Connor et al. Preferred compounds of this type in acid form are
dihydroxydisulfobenzenes such as 1,2-dihydroxy-3,5-disulfobenzene.
A preferred biodegradable chelator for use herein is ethylenediamine
disuccinate
("EDDS"), especially the [S,S] isomer as described in U.S. Patent 4,704,233,
November 3, 1987, to Hartman and Perkins.
3o The compositions herein may also contain water-soluble methyl glycine
diacetic
acid (MGDA) salts (or acid form) as a chelant or co-builder useful with, for
example, insoluble builders such as zeolites, layered silicates and the like.
If utilized, these chelating agents will generally comprise from about 0.1 %
to
about 15% by weight of the detergent compositions herein. More preferably, if
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utilized, the chelating agents will comprise from about 0.1 % to about 3.0% by
weight of such compositions.
Suds suppressor
5
Another optional ingredient is a suds suppressor, exemplified by silicones,
and
silica-silicone mixtures. Silicones can be generally represented by alkylated
polysiloxane materials while silica is normally used in finely divided forms
exemplified by silica aerogels and xerogels and hydrophobic silicas of various
types. These materials can be incorporated as particulates in which the suds
suppressor is advantageously releasably incorporated in a water-soluble or
water-dispersible, substantially non-surface-active detergent impermeable
carrier. Alternatively the suds suppressor can be dissolved or dispersed in a
liquid carrier and applied by spraying on to one or more of the other
components.
15 A preferred silicone suds controlling agent is disclosed in Bartollota et
al. U.S.
Patent 3 933 672. Other particularly useful suds suppressors are the self-
emulsifying silicone suds suppressors, described in German Patent Application
DTOS 2 646 126 published April 28, 1977. An example of such a compound is
DC-544, commercially available from Dow Corning, which is a siloxane-glycol
2o copolymer. Especially preferred suds controlling agent are the suds
suppressor
system comprising a mixture of silicone oils and 2-alkyl-alcanols. Suitable 2-
alkyl-
alkanols are 2-butyl-octanol which are commercially available under the trade
name Isofol 12 R.
Such suds suppressor system are described in Copending European Patent
25 application N 92870174.7 filed 10 November, 1992.
Especially preferred silicone suds controlling agents are described in
Copending
European Patent application N°92201649.8. Said compositions can
comprise a
silicone/silica mixture in combination with fumed nonporous silica such as
AerosilR.
The suds suppressors described above are normally employed at levels of from
0.001 % to 2% by weight of the composition, preferably from 0.01 % to 1 % by
weight.
Others
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Other components used in detergent compositions may be employed, such as
soil-suspending agents, soil-release agents, optical brighteners, abrasives,
bactericides, tarnish inhibitors, coloring agents, and/or encapsulated or non-
encapsulated perfumes.
Especially suitable encapsulating materials are water soluble capsules which
consist of a matrix of polysaccharide and polyhydroxy compounds such as
described in GB 1,464,616. Other suitable wafer soluble encapsulating
materials
comprise dextrins derived from ungelatinized starch acid-esters of substituted
1o dicarboxylic acids such as described in US 3,455,838. These acid-ester
dextrins
are,preferably, prepared from such starches as waxy maize, waxy sorghum,
sago, tapioca and potato. Suitable examples of said encapsulating materials
include N-Lok manufactured by National Starch. The N-Lok encapsulating
material consists of a modified maize starch and glucose. The starch is
modified
by adding monofunctional substituted groups such as octenyl succinic acid
anhydride.
Antiredeposition and soil suspension agents suitable herein include cellulose
derivatives such as methylcellulose, carboxymethylcellulose and
2o hydroxyethylcellulose, and homo- or co-polymeric polycarboxylic acids or
their
salts. Polymers of this type include the polyacrylates and malefic anhydride-
acrylic acid copolymers previously mentioned as builders, as well as
copolymers
of malefic anhydride with ethylene, methylvinyl ether or methacrylic acid, the
malefic anhydride constituting at least 20 mole percent of the copolymer.
These
2s materials are normally used at levels of from 0.5% to 10% by weight, more
preferably from 0.75% to 8%, most preferably from 1 % to 6% by weight of the
composition.
Preferred optical brighteners are anionic in character, examples of which are
3o disodium 4,4'-bis-(2-diethanolamino-4-anilino -s- triazin-6-
ylamino)stilbene-2:2'
disulphonate, disodium 4, - 4'-bis-(2-morpholino-4-anilino-s-triazin-6-ylamino-
stilbene-2:2' - disulphonate, disodium 4,4' - bis-(2,4-dianilino-s-triazin-6-
ylamino)stilbene-2:2' - disulphonate, monosodium 4',4" -bis-(2,4-dianilino-s-
tri-
azin-6 ylamino)stilbene-2-sulphonate, disodium 4,4' -bis-(2-anilino-4-(N-
methyl-N-
35 2-hydroxyethylamino)-s-triazin-6-ylamino)stilbene-2,2' - disulphonate, di-
sodium
4,4' -bis-(4-phenyl-2,1,3-triazol-2-yl)-stilbene-2,2' disulphonate, di-so-dium
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4,4'bis(2-anilino-4-(1-methyl-2-hydroxyethylamino)-s-triazin-6- ylami-
no)stilbene-
2,2'disulphonate, sodium 2(stilbyl-4"-(naphtho-1',2':4,5)-1,2,3 - triazole-2"-
sulphonate and 4,4'-bis(2-sulphostyryl)biphenyl. Highly preferred brighteners
are
the specific brighteners disclosed in EP 753 567.
Other useful polymeric materials are the polyethylene glycols, particularly
those
of molecular weight 1000-10000, more particularly 2000 to 8000 and most
preferably about 4000. These are used at levels of from 0.20% to 5% more
preferably from 0.25% to 2.5% by weight. These polymers and the previously
~o mentioned homo- or co-polymeric polycarboxylate salts are valuable for
improving whiteness maintenance, fabric ash deposition, and cleaning
performance on clay, proteinaceous and oxidizable soils in the presence of
transition metal impurities.
Soil release agents useful in compositions of the present invention are
conventionally copolymers or terpolymers of terephthalic acid with ethylene
glycol
and/or propylene glycol units in various arrangements. Examples of such
polymers are disclosed in the commonly assigned US Patent Nos. 4116885 and
4711730 and European Published Patent Application No. 0 272 033. A particular
2o preferred polymer in accordance with EP-A-0 272 033 has the formula
(CH3(PEG)43)0.75(POH)0.25~-PO)2.8(T-PEG)0.4~T(PO
H)0.25((PEG)43CH3)0.75
2s where PEG is -(OC2H4)O-,PO is (OC3Hg0) and T is (pcOCgH4C0).
Also very useful are modified polyesters as random copolymers of dimethyl
terephthalate, dimethyl sulfoisophthalate, ethylene glycol and 1-2 propane
diol,
the end groups consisting primarily of sulphobenzoate and secondarily of mono
3o esters of ethylene glycol and/or propane-diol. The target is to obtain a
polymer
capped at both end by sulphobenzoate groups, "primarily", in the present
context
most of said copolymers herein will be end-capped by sulphobenzoate groups.
However, some copolymers will be less than fully capped, and therefore their
end
groups may consist of monoester of ethylene glycol and/or propane 1-2 diol,
35 thereof consist "secondarily" of such species.
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63
The selected polyesters herein contain about 46% by weight of dimethyl
terephthalic acid, about 16% by weight of propane -1.2 diol, about 10% by
weight
ethylene glycol about 13% by weight of dimethyl sulfobenzoic acid and about
15% by weight of sulfoisophthalic acid, and have a molecular weight of about
3.000. The polyesters and their method of preparation are described in detail
in
EPA 311 342.
It is well known in the art that free chlorine in tap water rapidly
deactivates the
enzymes comprised in detergent compositions. Therefore, using chlorine
1o scavenger such as perborate, ammonium sulfate, sodium sulphite or
polyethyleneimine at a level above 0.1 % by weight of total composition, in
the
formulas will provide improved through the wash stability of the detergent
enzymes. Compositions comprising chlorine scavenger are described in the
European patent application 92870018.6 filed January 31, 1992.
Alkoxylated polycarboxylates such as those prepared from polyacrylates are
useful herein to provide additional grease removal performance. Such materials
are described in WO 91/08281 and PCT 90/01815 at p. 4 et seq., incorporated
herein by reference. Chemically, these materials comprise polyacrylates having
one ethoxy side-chain per every 7-8 acrylate units. The side-chains are of the
formula -(CH2CH20)m(CH2)nCH3 wherein m is 2-3 and n is 6-12. The side-
chains are ester-linked to the polyacrylate "backbone" to provide a "comb"
polymer type structure. The molecular weight can vary, but is typically in the
range of about 2000 to about 50,000. Such alkoxylated polycarboxylates can
comprise from about 0.05% to about 10%, by weight, of the compositions herein.
Dispersants
The detergent composition of the present invention can also contain
dispersants
: Suitable water-soluble organic salts are the homo- or co-polymeric acids or
their
salts, in which the polycarboxylic acid comprises at least two carboxyl
radicals
separated from each other by not more than two carbon atoms. Polymers of this
type are disclosed in GB-A-1,596,756. Examples of such salts are polyacrylates
of MW 2000-5000 and their copolymers with malefic anhydride, such copolymers
having a molecular weight of from 1,000 to 100,000.
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Especially, copolymer of acrylate and methylacrylate such as the 480N having a
molecular weight of 4000, at a level from 0.5-20% by weight of composition can
be added in the detergent compositions of the present invention.
s The compositions of the invention may contain a lime soap peptiser compound,
which has preferably a lime soap dispersing power (LSDP), as defined
hereinafter of no more than 8, preferably no more than 7, most preferably no
more than 6. The lime soap peptiser compound is preferably present at a level
from 0% to 20% by weight.
A numerical measure of the effectiveness of a lime soap peptiser is given by
the
lime soap dispersant power (LSDP) which is determined using the lime soap
dispersant test as described in an article by H.C. Borghetty and C.A. Bergman,
J.
Am. Oil. Chem. Soc., volume 27, pages 88-90, (1950). This lime soap dispersion
test method is widely used by practitioners in this art field being referred
to, for
example, in the following review articles; W.N. Linfield, Surfactant science
Series,
Volume 7, page 3; W.N. Linfield, Tenside surf. det., volume 27, pages 159-163,
(1990); and M.K. Nagarajan, W.F. Masler, Cosmetics and Toiletries, volume 104,
pages 71-73, (1989). The LSDP is the % weight ratio of dispersing agent to
2o sodium oleate required to disperse the lime soap deposits formed by 0.025g
of
sodium oleate in 30m1 of water of 333ppm CaCo3 (Ca:Mg=3:2) equivalent
hardness.
Surfactants having good lime soap peptiser capability will include certain
amine
2s oxides, betaines, sulfobetaines, alkyl ethoxysulfates and ethoxylated
alcohols.
Exemplary surfactants having a LSDP of no more than 8 for use in accord with
the present invention include C16-C1g dimethyl amine oxide, C12-C1g alkyl
ethoxysulfates with an average degree of ethoxylation of from 1-5,
particularly
3o C12-C15 alkyl ethoxysulfate surfactant with a degree of ethoxylation of
amount 3
(LSDP=4), and the C14-C15 ethoxylated alcohols with an average degree of
ethoxylation of either 12 (LSDP=6) or 30, sold under the tradenames Lutensol
A012 and Lutensol A030 respectively, by BASF GmbH.
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Polymeric lime soap peptisers suitable for use herein are described in the
article
by M.K. Nagarajan, W.F. Masler, to be found in Cosmetics and Toiletries,
volume
104, pages 71-73, (1989).
5 Hydrophobic bleaches such as 4-[N-octanoyl-6-aminohexanoyl]benzene
sulfonate, 4-[N-nonanoyl-6-aminohexanoyl]benzene sulfonate, 4-[N-decanoyl-6-
aminohexanoyl]benzene sulfonate and mixtures thereof; and nonanoyloxy
benzene sulfonate together with hydrophilic / hydrophobic bleach formulations
can also be used as lime soap peptisers compounds.
Dye transfer inhibition
The detergent compositions of the present invention can also include compounds
for inhibiting dye transfer from one fabric to another of solubilized and
suspended
dyes encountered during fabric laundering operations involving colored
fabrics.
Polymeric dye transfer inhibiting agents
The detergent compositions according to the present invention can also
comprise
from 0.001 % to 10 %, preferably from 0.01 % to 2%, more preferably from 0.05%
2o to 1 % by weight of polymeric dye transfer inhibiting agents. Said
polymeric dye
transfer inhibiting agents are normally incorporated into detergent
compositions
in order to inhibit the transfer of dyes from colored fabrics onto fabrics
washed
therewith. These polymers have the ability to complex or adsorb the fugitive
dyes
washed out of dyed fabrics before the dyes have the opportunity to become
attached to other articles in the wash.
Especially suitable polymeric dye transfer inhibiting agents are polyamine N-
oxide polymers, copolymers of N-vinylpyrrolidone and N-vinylimidazole,
polyvinylpyrrolidone polymers, polyvinyloxazolidones and polyvinylimidazoles
or
mixtures thereof.
so Addition of such polymers also enhances the performance of the enzymes
according the invention.
a) Polyamine N-oxide polymers
The polyamine N-oxide polymers suitable for use contain units having the
following structure formula
P
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I
(I) Ax
I
R
wherein P is a polymerisable unit, whereto the R-N-O group can be attached to
or wherein the R-N-O group forms part of the polymerisable unit or a
combination
of both.
O O O
A is NC, CO, C, -O-,-S-, -N- ; x is O or 1;
R are aliphatic, ethoxylated aliphatics, aromatic, heterocyclic or alicyclic
groups
or any combination thereof whereto the nitrogen of the N-O group can be
attached or wherein the nitrogen of the N-O group is part of these groups.
The N-O group can be represented by the following general structures
O O
I
(R1 )x -N- (R2)y =N= (R1 )x
I
(R3)z
wherein R1, R2, and R3 are aliphatic groups, aromatic, heterocyclic or
alicyclic
groups or combinations thereof, x or/and y or/and z is 0 or 1 and wherein the
nitrogen of the N-O group can be attached or wherein the nitrogen of the N-O
group forms part of these groups.
The N-O group can be part of the polymerisable unit (P) or can be attached to
the polymeric backbone or a combination of both.
Suitable polyamine N-oxides wherein the N-O group forms part of the
polymerisable unit comprise polyamine N-oxides wherein R is selected from
aliphatic, aromatic, alicyclic or heterocyclic groups.
One class of said polyamine N-oxides comprises the group of polyamine N
oxides wherein the nitrogen of the N-O group forms part of the R-group.
Preferred polyamine N-oxides are those wherein R is a heterocyclic group such
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as pyrridine, pyrrole, imidazole, pyrrolidine, piperidine, quinoline, acridine
and
derivatives thereof.
Another class of said polyamine N-oxides comprises the group of polyamine N-
oxides wherein the nitrogen of the N-O group is attached to the R-group.
Other suitable polyamine N-oxides are the polyamine oxides whereto the N-O
group is attached to the polymerisable unit.
Preferred class of these polyamine N-oxides are the polyamine N-oxides having
the general formula (I) wherein R is an aromatic, heterocyclic or alicyclic
groups
~o wherein the nitrogen of the N-0 functional group is part of said R group.
Examples of these classes are polyamine oxides wherein R is a heterocyclic
compound such as pyrridine, pyrrole, imidazole and derivatives thereof.
Another preferred class of polyamine N-oxides are the polyamine oxides having
the general formula (I) wherein R are aromatic, heterocyclic or alicyclic
groups
~5 wherein the nitrogen of the N-0 functional group is attached to said R
groups.
Examples of these classes are polyamine oxides wherein R groups can be
aromatic such as phenyl.
Any polymer backbone can be used as long as the amine oxide polymer formed
2o is water-soluble and has dye transfer inhibiting properties. Examples of
suitable
polymeric backbones are polyvinyls, polyalkylenes, polyesters, polyethers,
polyamide, polyimides, polyacrylates and mixtures thereof.
The amine N-oxide polymers of the present invention typically have a ratio of
25 amine to the amine N-oxide of 10:1 to 1:1000000. However the amount of
amine
oxide groups present in the polyamine oxide polymer can be varied by
appropriate copolymerization or by appropriate degree of N-oxidation.
Preferably,
the ratio of amine to amine N-oxide is from 2:3 to 1:1000000. More preferably
from 1:4 to 1:1000000, most preferably from 1:7 to 1:1000000. The polymers of
3o the present invention actually encompass random or block copolymers where
one monomer type is an amine N-oxide and the other monomer type is either an
amine N-oxide or not. The amine oxide unit of the polyamine N-oxides has a PKa
< 10, preferably PKa < 7, more preferred PKa < 6.
The polyamine oxides can be obtained in almost any degree of polymerisation.
35 The degree of polymerisation is not critical provided the material has the
desired
water-solubility and dye-suspending power.
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Typically, the average molecular weight is within the range of 500 to
1000,000;
preferably from 1,000 to 50,000, more preferably from 2,000 to 30,000, most
preferably from 3,000 to 20,000.
b) Copolymers of N-vinylpyrrolidone and N-vinylimidazole
The N-vinylimidazole N-vinylpyrrolidone polymers used in the present invention
have an average molecular weight range from 5,000-1,000,000, preferably from
5,000-200,000.
Highly preferred polymers for use in detergent compositions according to the
o present invention comprise a polymer selected from N-vinylimidazole N
vinylpyrrolidone copolymers wherein said polymer has an average molecular
weight range from 5,000 to 50,000 more preferably from 8,000 to 30,000, most
preferably from 10,000 to 20,000.
The average molecular weight range was determined by light scattering as
~s described in Barth H.G. and Mays J.W. Chemical Analysis Vol 113,"Modern
Methods of Polymer Characterization".
Highly preferred N-vinylimidazole N-vinylpyrrolidone copolymers have an
average
molecular weight range from 5,000 to 50,000; more preferably from 8,000 to
30,000; most preferably from 10,000 to 20,000.
The N-vinylimidazole N-vinylpyrrolidone copolymers characterized by having
said
average molecular weight range provide excellent dye transfer inhibiting
properties while not adversely affecting the cleaning performance of detergent
compositions formulated therewith.
The N-vinylimidazole N-vinylpyrrolidone copolymer of the present invention has
a
molar ratio of N-vinylimidazole to N-vinylpyrrolidone from 1 to 0.2, more
preferably from 0.8 to 0.3, most preferably from 0.6 to 0.4 .
c) Polyvinylpyrrolidone
3o The detergent compositions of the present invention may also utilize
polyvinylpyrrolidone ("PVP") having an average molecular weight of from about
2,500 to about 400,000, preferably from about 5,000 to about 200,000, more
preferably from about 5,000 to about 50,000, and most preferably from about
5,000 to about 15,000. Suitable polyvinylpyrrolidones are commercially
vailable
from ISP Corporation, New York, NY and Montreal, Canada under the product
names PVP K-15 (viscosity molecular weight of 10,000), PVP K-30 (average
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molecular weight of 40,000), PVP K-60 (average molecular weight of 160,000),
and PVP K-90 (average molecular weight of 360,000). Other suitable
polyvinylpyrrolidones which are commercially available from BASF Cooperation
include Sokalan HP 165 and Sokalan HP 12; polyvinylpyrrolidones known to
persons skilled in the detergent field (see for example EP-A-262,897 and EP-A-
256,696).
d) Polyvinyloxazolidone
The detergent compositions of the present invention may also utilize
1o polyvinyloxazolidone as a polymeric dye transfer inhibiting agent. Said
polyvinyloxazolidones have an average molecular weight of from about 2,500 to
about 400,000, preferably from about 5,000 to about 200,000, more preferably
from about 5,000 to about 50,000, and most preferably from about 5,000 to
about 15,000.
e) Polyvinylimidazole
The detergent compositions of the present invention may also utilize
polyvinylimidazole as polymeric dye transfer inhibiting agent. Said
polyvinylimidazoles have an average about 2,500 to about 400,000, preferably
2o from about 5,000 to about 200,000, more preferably from about 5,000 to
about
50,000, and most preferably from about 5,000 to about 15,000.
f) Cross-linked polymers
Cross-linked polymers are polymers whose backbone are interconnected to a
certain degree; these links can be of chemical or physical nature, possibly
with
active groups n the backbone or on branches; cross-linked polymers have been
described in the Journal of Polymer Science, volume 22, pages 1035-1039.
In one embodiment, the cross-linked polymers are made in such a way that they
form a three-dimensional rigid structure, which can entrap dyes in the pores
3o formed by the three-dimensional structure. In another embodiment, the cross
linked polymers entrap the dyes by swelling. Such cross-linked polymers are
described in the co-pending patent application 94870213.9
Method of washing
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The compositions of the invention may be used in essentially any washing or
cleaning methods, including soaking methods, pretreatment methods and
methods with rinsing steps for which a separate rinse aid composition may be
added.
s
The process described herein comprises contacting fabrics, dishware or any
other hard surface with a cleaning solution in the usual manner and
exemplified
hereunder. A conventional laundry method comprises treating soiled fabric with
an aqueous liquid having dissolved or dispensed therein an effective amount of
the laundry detergent and/or fabric care composition. A preferred machine
dishwashing method comprises treating soiled articles with an aqueous liquid
having dissolved or dispensed therein an effective amount of the machine
diswashing or rinsing composition. A conventional effective amount of the
machine dishwashing composition means from 8-60 g of product dissolved or
dispersed in a wash volume from 3-10 litres. According to a manual dishwashing
method, soiled dishes are contacted with an effective amount of the diswashing
composition, typically from 0.5-20g (per 25 dishes being treated). Preferred
manual dishwashing methods include the application of a concentrated solution
to the surfaces of the dishes or the soaking in large volume of dilute
solution of
2o the detergent composition. A coriventional hard surface method comprises
treating soiled hard items/surfaces with e.g. a sponge, brush, clothe, etc.
with an
aqueous liquid having dissolved or dispensed therein an effective amount of
the
hard surface cleaner and/or with such composition undiluted. It also
encompasses the soaking of a hard item in a concentrated solution or in a
large
2s volume of dilute solution of the detergent composition.
The method of cleaning is preferably carried out at 5°C to
95°C, especially
between 10°C and 60°C. The pH of the treatment solution is
preferably from 7 to
12.
The following examples are meant to exemplify compositions of the present
invention, but are not necessarily meant to limit or otherwise define the
scope of
the invention.
In the detergent compositions, the enzymes levels are expressed by pure
enzyme by weight of the total composition and unless otherwise specified, the
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71
detergent ingredients are expressed by weight of the total compositions. The
abbreviated component identifications therein have the following meanings:
LAS : Sodium linear C11-13 alkyl benzene sulphonate.
TAS : Sodium tallow alkyl sulphate.
CxyAS : Sodium C1x- C1y alkyl sulfate.
CxySAS : Sodium C1x - C1y secondary (2,3) alkyl sulfate.
MBAS : Mid-branched alkyl sulfate.
CxyEz : C1x - C1y predominantly linear primary alcohol
condensed with an average of z moles of ethylene
oxide.
CxyEzS : C1x - C1y sodium alkyl sulfate condensed with
an
average of z moles of ethylene oxide.
CxEOy : Cy alcohol with an average of ethoxylation
of y.
Nonionic : Mixed ethoxylated/propoxylated fatty alcohol
e.g.
Plurafac LF404 being an alcohol with an average
degree
of ethoxylation of 3.8 and an average degree
of
propoxylation of 4.5.
QAS : R2.N+(CH3)2(C2H4OH) with R2 = C12'C14~
SADS : Sodium C14-22 alkyl Bisulfate of the formula
2-R.C4H7.-
1,4-(S04-)2 where R = C10-18.
MES : x-sulpho methyl ester of C18 fatty acid.
APA : Cg_10 amido propyl dimethyl ar~iine.
Soap : Sodium linear alkyl carboxylate derived from
a 80/20
mixture of tallow and coconut fatty acids.
Neodol xy-z : C1x-C1y linear primary alcohol z ethoxylate.
CFAA : C12-C14 alkyl N-methyl glucamide.
TFAA : C1g-C1g alkyl N-methyl glucamide.
TPKFA : C12-C14 topped whole cut fatty acids.
DEQA : Di-(tallow-oxy-ethyl) dimethyl ammonium chloride.
DEQA (2) : Di-(soft-tallowyloxyethyl) hydroxyethyl methyl ammonium
methylsulfate.
DTDMAMS : Ditallow dimethyl ammonium methylsulfate.
SDASA : 1:2 ratio of stearyldimethyl amineariple-pressed stearic
acid.
Silicate : Amorphous Sodium Silicate (Si02:Na20 ratio = 1.6-
3.2:1 ).
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Metasilicate : Sodium metasilicate (Si02:Na20 ratio = 1.0).
Zeolite A : Hydrated Sodium Aluminosilicate of formula
Nal2(A102Si02)12. 27H20 having a primary particle
size in the range from 0.1 to 10 micrometers (Weight
expressed on an anhydrous basis).
(Na-)SKS-6 : Crystalline layered silicate of formula 8-Na2Si205.
Citrate : Tri-sodium citrate dihydrate.
Citric : Anhydrous citric acid.
Borate : Sodium borate
Carbonate : Anhydrous sodium carbonate.
Bicarbonate : Sodium hydrogen carbonate.
Sulphate : Anhydrous sodium sulphate.
STPP : Sodium tripolyphosphate.
TSPP : Tetrasodium pyrophosphate.
MA/AA : Random copolymer of 4:1 acrylate/maleate,
average
molecular weight about 70,000-80,000.
MA/AA 1 : Random copolymer of 6:4 acrylate/maleate,
average
molecular weight about 10,000.
AA : Sodium polyacrylate polymer of average molecular
weight 4,500.
Polycarboxylate: Copolymer comprising mixture of carboxylated
monomers such as acrylate, maleate and methyacrylate
with a MW ranging between 2,000-80,000 such
as
Sokolan commercially available from BASF, being
a
copolymer of acrylic acid, MW4,500.
PB1 : Anhydrous sodium perborate monohydrate.
PB4 : Sodium perborate tetrahydrate of nominal
formula
NaB03.4H20.
Percarbonate : Anhydrous sodium percarbonate of nominal
formula 2.74
Na2C03.3H202 .
NaDCC : Sodium dichloroisocyanurate.
TAED : Tetraacetyl ethylene diamine.
NOES : Nonanoyloxybenzene sulfonate in the form
of the sodium
salt.
NACA-OBS : (6-nonamidocaproyl) oxybenzene sulfonate.
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DOBS : Decanoyl oxybenzene sulfonate in the form of the
sodium salt.
DTPA : Diethylene triamine pentaacetic acid.
HEDP : 1,1-hydroxyethane diphosphonic acid.
DETPMP : Diethyltriamine penta (methylene) phosphonate,
marketed by Monsanto under the Trade name bequest
2060.
EDDS : Ethylenediamine-N,N'-disuccinic acid, (S,S)
isomer in the
form of its sodium salt
Chelant : Chelant selected from EEDS, HEDP, DTPA, DETPMP
and/or mixtures thereof.
MnTACN : Manganese 1,4,7-trimethyl-1,4,7-triazacyclononane.
Photoactivated: Sulfonated zinc phtalocyanine encapsulated
in dextrin
Bleach soluble polymer.
Photoactivated: Sulfonated alumino phtalocyanine encapsulated
in
Bleach 1 dextrin soluble polymer.
PAAC : Pentaamine acetate cobalt(III) salt.
Paraffin : Paraffin oil sold under the tradename Winog
70 by
Wintershall.
NaBz : Sodium benzoate.
Pectate lyase : Pectate lyase from Bacillus agaradhaerens,
NCIMB
404482 or DSM 8721
Xyloglucanase : An endoglucanase specific for xyloglucan as
described
in W098/50513 and in WO 94/14953 as EG II.
Mannanase : Mannanase from Bacillus agardhaerens, NCIMB
40482
Protease : Proteolytic enzyme sold under the tradename
Savinase ,
Alcalase, Durazym by Novo Nordisk A/S, Maxacal,
Maxapem sold by Gist-Brocades and proteases
described in patents W091/06637 and/or W095/10591
and/or EP 251 446.
Amylase : Amylolytic enzyme sold under the tradename Purafact
Ox AmR described in WO 94/18314, W096/05295 sold
by Genencor; Termamyl~, Fungamyl~ and Duramyl~,
all available from Novo Nordisk A/S and those described
in W095/26397 (sold under the tradename Natalase By
Novo Nordisk).
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Lipase : Lipolytic enzyme sold under the tradename
Lipolase
Lipolase Ultra by Novo Nordisk A/S and Lipomax
by Gist-
Brocades.
Cellulase : Cellulytic enzyme sold under the tradename
Carezyme,
Celluzyme and/or Endolase by Novo Nordisk
AIS.
Pectin lyase : Pectin lyase produced by Bacillus licheniformis,
ATCC
14580.
CMC : Sodium carboxymethyl cellulose.
PVNO : Polyvinylpyridine-N-Oxide, with an average
molecular
weight of 50,000.
PVPVI : Copolymer of vinylimidazole and vinylpyrrolidone,
with an
average molecular weight of 20,000.
Brightener 1 : Disodium 4,4'-bis(2-sulphostyryl)biphenyl.
Brightener 2 : Disodium 4,4'-bis(4-anilino-6-morpholino-1.3.5-triazin-2-
yl) stilbene-2:2'-disulfonate.
Silicone antifoam: Polydimethylsiloxane foam controller with
siloxane-
oxyalkylene copolymer as dispersing agent
with a ratio of
said foam controller to said dispersing agent
of 10:1 to
100:1.
Suds Suppressor : 12% Silicorie/silica, 18% stearyl alcoho1,70% starch in
granular form.
Opacifier : Water based monostyrene latex mixture, sold
by BASF
Aktiengesellschaft under the tradename Lytron
621.
Thickener : High molecular weight crosslinked polyacrylates
such as
Carbopol offered by B.F. Goodrich Chemical Company
and Polygel.
SRP 1 : Anionically end capped poly esters.
SRP 2 : Diethoxylated poly (1,2 propylene terephtalate)
short
block polymer.
QEA : bis((C2H50)(C2H40)n)(CH3) -N+-C6H12-N+-(CH3)
bis((C2H50)-(C2H40))n, wherein n = from 20 to
30.
SCS : Sodium cumene sulphonate.
HMWPEO : High molecular weight polyethylene oxide.
PEGX : Polyethylene glycol,of a molecular weight
of x.
PEO : Polyethylene oxide, with an average molecular
weight of
5,000.
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TEPAE : Tetreaethylenepentaamine ethoxylate.
BTA : Benzotriazole.
pH : Measured as a 1 % solution in distilled water at 20°C.
Example 1
The following undry
high density detergent
and bleach-containing compositions
la
5 were prepared
according to
the present invention:
I II III
Blown Powder
Zeolite A 12.0 - 15.0
Sulfate - 5.0 -
LAS 3.0 - 3.0
C45AS 3.0 2.0 4.0
QAS - - 1.5
DETPMP 0.4 0.4 0.4
CMC 0.4 0.4 0.4
MA/AA 1.0 2.0 2.0
Agglomerates
QAS 1.0 - -
LAS - 11.0 7.0
TAS 2.0 2.0 1.0
Silicate 3.0 - 4.0
Zeolite A 8.0 8.0 8.0
Carbonate 8.0 8.0 4.0
Agglomerate
NaSKS-6 15.0 12.0 5.0
LAS 8.0 7.0 4.0
Spray On
Perfume 0.3 0.3 0.3
C25E3 2.0 - 2.0
Dry additives
QEA 1.0 0.5 0.5
Citric/Citrate5.0 - 2.0
Bicarbonate - 3.0 -
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I II III
Carbonate 8.0 15.0 10.0
TAED and/ or NACA-OBS 6.0 - 5.0
NOBS - 2.0 -
Percarbonate/ PB1 14.0 7.0 10.0
Polyethylene oxide of MW - - 0.2
5,000,000
Bentonite clay - - 10.0
Citric acid 4.0 - 1.5
Pectate lyase 0.001 0.02 0.001
Pectin Lyase - - 0.001
Mannanase 0.005 0.002 0.001
Xyloglucanase 0.001 0.002 0.001
Protease 0.033 0.033 0.033
Lipase 0.008 0.008 0.008
Amylase 0.001 0.001 0.001
Cellulase 0.0014 0.0014 0.0014
Silicone antifoam 5.0 5.0 5.0
S a Ifate - 3.0 -
Density (g/litre) 850 850 850
Moisture and miscellaneous Up to 100%
Example 2
s The following laundry compositions, which may be in the form of granules or
tablet, were prepared according to the present invention.
I II III IV V
Base Product
C45 AS/TAS 8.0 5.0 3.0 3.0 3.0
LAS 8.0 - 8.0 - 7.0
C25AE3S 0.5 2.0 1.0 - -
C25AE5/AE3 2.0 - 5.0 2.0 2.0
QAS - - - 1.0 1.0
Zeolite A 20.0 18.0 11.0 - 10.0
SKS-6 (I) (dry add) - - 9.0 - -
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I II III IV V
MA/AA 2.0 2.0 2.0 - -
A,o~ _ _ _ - 4.0
Citrate - 2.0 - - -
Citric 2.0 - 1.5 2.0 -
DTPA 0.2 0.2 - - -
EDDS - - 0.5 0.1 -
HEDP - - 0.2 0.1 -
PB 1 3.0 5.0 10.0 - 4.0
Percarbonate - - - 18.0 -
NOBS 3.0 4.0 - - 4.0
NACA OBS - - 2.0 - -
TAED - - 2.0 5.0
Carbonate 15.0 18.0 8.0 15.0 15.0
Sulphate 5.0 12.0 2.0 17.0 3.0
Silicate - 1.0 - - 8.0
Protease 0.004 0.004 0.008 0.007 0.01
Lipase 0.006 0.003 0.005 0.003 0.008
Amylase 0.003 0.015 0.007 0.006 0.010
Cellulase 0.001 0.0015 0.001 0.0014 0.003
Pectate lyase 0.001 0.005 0.001 0.05 0.005
Pectin Lyase - 0.001 - - -
Mannanase 0.005 0.001 0.001 0.005 0.005
Xyloglucanase 0.001 0.001 0.005 0.005 0.005
Minors 0.5 0.5 0.5 0.5 0.5
Perfume 0.2 0.3 0.5 0.2 0.1
Moisture and miscellaneous Up
to
100%
Minors include Brightener otobleach 4 / PVPVI/
/ SRP1 / CMC / Ph / Suds
Mg50
suppressor /PEG.
Example 3
The following high density laundry detergent compositions were prepared
according to the present invention:
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Agglomerate
QAS 2.0 - 2.0
MES - 2.0 -
LAS 6.0 - -
TAS - 2.0 -
C45AS 6.0 4.0 2.0
M BAS 16.5, 1.9 4.0 - -
Zeolite A 15.0 6.0 -
Carbonate 4.0 8.0 4.0
MA/AA 4.0 2.0
CMC 0.5 0.5 -
DETPMP 0.4 0.4 -
Spray On
C25E3 1.0 1.0 -
Perfume 0.5 0.5 0.5
Agglomerate
SKS-6 7.0 15.0 20.0
LAS 5.8 9.0 15.0
Zeolite - 0.9 -
Water 0.08 0.1 -
Dry Adds
EDDS/HEDP 0.5 0.3 0.5
NaSKS 6 (I) 5.0 6.0 4.0
Citrate - 1.0 -
Citric 2.0 - 2.0
NACA-OBS 4.1 - 5.0
TAED 0.8 2.0
Percarbonate 20.0 20.0 15.0
SRP 1 0.3 0.3 -
Pectate lyase 0.002 0.001 0.03
Pectin Lyase - 0.001 -
Mannanase 0.002 0.010 0.003
Xyloglucananse 0.020 0.001 0.003
Protease 0.046 0.046 0.033
Lipase 0.008 0.008 0.006
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I 11 III
Amylase 0.001 0.001 -
QEA 1.0 - 1.0
Silicone antifoam 1.0 0.5 0.5
Brightener 1 0.2 0.2 -
Brightener 2 0.2 - 0.2
Density (g/litre) 850 850 800
Moisture and miscellaneous Up to 100%
Example 4
The following laundry compositions, which may be in the form of granules or
tablet, were prepared in accordance with the invention:
I II III IV V
Base Product
C45 AS/TAS 8.0 5.0 3.0 3.0 3.0
LAS 8.0 - 8.0 - 7.0
C25AE3S 0.5 2.0 1.0 -
LAS/NaSKS-6 5.0 17.0 9.0 20.0 15.0
C25AE5/AE3 2.0 - 5.0 2.0 2.0
QAS - - - 1.0 1.0
Zeolite A 20.0 10.0 10.0 - 10.0
SKS-6 - - 2.0 -
MA/AA 2.0 2.0 2.0 - -
qq _ _ _ - 4.0
Citrate - 2.0 - -
Citric 2.0 - 1.5 2.0 -
DTPA 0.2 0.2 - - -
EDDS - - 0.5 0.1 -
HEDP - - 0.2 0.1 -
PB1 3.0 5.0 10.0 - 4.0
PC - - - 18.0 -
NOBS 3.0 4.0 - - 4.0
NACA OBS - - 2.0 - -
TAED - - 2.0 5.0 -
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Carbonate 15.0 18.0 8.0 15.0 15.0
Sulphate 5.0 12.0 2.0 17.0 3.0
Silicate - 1.0 - - g,0
Protease 0.004 0.004 0.008 0.007 0.01
Lipase 0.006 0.003 0.005 0.003 0.008
Amylase 0.003 0.015 0.007 0.006 0.010
Cellulase 0.001 0.0015 0.001 0.0014 0.003
Pectate lyase 0.001 0.010 0.003 0.001 0.03
Pectin Lyase - - - - 0.001
Mannanase 0.005 0.002 0.003 0.001 0.03
Xyloglucanase 0.001 0.002 0.015 0.001 0.03
Minors 0.5 0.5 0.5 0.5 0.5
Perfume 0.2 0.3 0.5 0.2 0.1
Moisture and miscellaneous Up to 100%
Minors include Brightener
/ SRP1 / CMC / Photobleach
/ MgS04 / PVPVI/ Suds
suppressor /PEG.
5
Example 5
The following high density laundry detergent compositions were prepared
1o according to the present invention:
I II III IV
Agglomerate
QAS 2.0 - 2.0 -
MES - 2.0
LAS 6.0 - - -
TAS - 2.0
C45AS 6.0 4.0 2.0
M BAS 16.5, 4.0 -
1.9
Zeolite A 15.0 6.0 - -
Carbonate 4.0 8.0 4.0 8.0
MA/AA 4.0 2.0 - 2.0
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I II III IV
CMC 0.5 0.5 - 0.5
DETPMP 0.4 0.4 - 0.5
Spray On
C25E3 1.0 1.0 - -
Perfume 0.5 0.5 0.5 0.5
Agglomerate
SKS-6 7.0 15.0 20.0 10.0
LAS 5.8 9.0 15.0 10.0
Zeolite - 0.9 _ _
C45 AS - 3.0 - -
Water 0.08 0.1 - 0.2
Dry Adds
EDDS/HEDP 0.5 0.3 0.5 0.8
NaSKS 6) 5.0 6.0 4.0 11.0
Citrate - 1.0 - -
Citric 2.0 - 2.0 4.0
NAC OBS 4.1 - 5.0 4.0
TAED 0.8 2.0 - 2.0
Percarbonate 20.0 20.0 15.0 17.0
~
SRP 1 0.3 0.3 - 0.3
Pectate Lyase 0.005 0.001 0:004 0.030
Pectin Lyase - - 0.001 -
Mannanase 0.005 0.010 0.004 0.003
Xyloglucanase 0.005 0.001 0.040 0.003
Protease 0.046 0.046 0.033 0.016
Lipase 0.008 0.008 0.006 -
Cellulase 0.0014 0.0014 0.001 0.001
Amylase 0.003 0.003 - 0.0015
QEA 1.0 - 1.0 1.0
Silicone antifoam 1.0 0.5 0.5 1.5
Brightener 1 0.2 0.2 - 6.2
Brightener 2 0.2 - 0.2
Density (g/litre) 850 850 800 775
Moisture and miscellaneous Up to 100%
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Example 6
The following granular detergent were prepared in accordance with the present
invention:
I il III IV
Base granule
STPP - 22.0 - 15.0
Zeolite A 30.0 - 24.0 5.0
Sulfate 5.5 5.0 7.0 7.0
MA/AA 3.0 - - _
AA - 1.6 2.0
MA/AA ( 1 ) - 12.0 - 6.0
LAS 14.0 10.0 9.0 20.0
C45AS 8.0 7.0 9.0 7.0
C45AE 11 S - 1.0 - 1.0
MES 0.5 4.0 6.0 -
SADS 2.5 - - 1.0
Silicate - 1.0 0.5 10.0
Soap - 2.0 - -
Brightener 1 0.2 0.2 0.2 0.2
Carbonate 6.0 9.0 8.0 10.0
PEG 4000 - 1.0 1.5 -
DTPA - 0.4 - -
Spray on
C25E9 - - - 5.0
C45E7 1.0 1.0 - -
C23E9 - 1.0 2.5 -
Perfume 0.2 0.3 0.3 -
Dry additives
Carbonate 5.0 10.0 13.0 8.0
PVPVI/PVNO 0.5 - 0.3 -
Protease 0.033 0.033 0.033 0.0016
Lipase 0.008 - - 0.008
Amylase 0.0016 - - 0.0016
Cellulase 0.0002 0.0005 0.0005 0.0002
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I II III IV
Pectate lyase 0.001 0.02 0.03 0.010
Pectin Lyase 0.001 - - -
Mannanase 0.005 0.002 0.003 0.001
Xyloglucanase 0.001 0.002 0.008 0.001
DTPA 0.5 0.3 0.5 1.0
PB 1 5 3.0 10 4.0
NOBS/ TAED 0.5 0.3 0.5 0.6
Sulfate 4.0 5.0 - 5.0
SRP1 - 0.4 - _
Sud supressor - 0.5 -
speckle 0.9 - 2.7 1.2
Moisture and miscellaneous Up to 100%
Example 7
s The following laundry detergent compositions were prepared in accordance
with
the present invention:
I II III Iv v VI vll
-
LAS 12.0 16.0 23.0 19 18.0 20.0 16.0
C45AS 4.5 - - - 4.0
C45 E0.5S _ _ _ _ _
C45 E3S - - 2.0 - 1.0 1.0 1.0
C45E6.5S 2.0 2.0 - 1.3 - - 0.6
C9-C~4 alkyl - - 1.0 0.5 2.0
dimethyl hydroxy
ethyl quaternary
ammonium salt
Tallow fatty - - - - 1.0
acid
Tallow alcohol - - - _ _ - _
ethoxylate (50)
STPP 23.0 25.0 24.0 22,0 20.0 15.0 20.0
Carbonate 15.0 12.0 15.0 10.0 13.0 11.0 10.0
Sodium 0.5 0.5 0.5 0.5 - - _
Polyacrylate
(45%)
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I II III IV V VI VII
N1~~ - - 1.0 1.0 1.0 2.0 0.5
Silicate (1:6 3.0 6.0 9.0 8.0 9.0 6.0 8.0
ratio
Sulfate 25.0 18.0 20.0 18.0 20.0 22.0 13.0
PB1 5.0 5.0 10.0 8.0 3.0 1.0 2.0
PEG MW 4000 1.5 1.5 1.0 1.0 - - 0.5
(50%)
CMC 1.0 1.0 1.0 - 0.5 0.5 0.5
Citric - - _ _ - _
NOES/ DOBS 0.5 1.0 0.5 0.5 1.0 0.7 0.3
TAED 1.5 1.0 2.5 3.0 0.3 0.2 0.5
SRP1 1.5 1.5 1.0 1.0 - 1.0
SRP2 - - - - 1.0 - 1.0
Moisture 7.5 7.5 6.0 7.0 5.0 3.0 5.0
Mg sulphate - - - - 1.0 0.5 1.5
Chelant - - - - 0.8 0.6 1.0
Protease 0.004 0.004 0.008 0.007 0.01 0.015 0.015
Lipase 0.006 0.003 0.005 0.003 0.008 0.0014 0.0014
Amylase 0.003 0.015 0.007 0.006 0.010 0.002 0.0008
Cellulase 0.001 0.0015 0.001 0.0014 0.003 0.0001 0.0001
Pectate lyase 0.001 0.02 0.001 0.002 0.002 0.015 0.003
Pectin lyase - 0.001 - - 0.001 - -
Mannanase 0.005 0.002 0.001 0.010 0.002 0.003 0.003
Xyloglucanase 0.001 0.002 0.008 0.002 0.02 0.003 0.003
speckle 2.5 4.1 4.2 4.4 5.6 5.0 5.2
Minors 1.0 1.0 1.0 1.0 0.5 1.5 1.0
Example 8
The following laundry detergent compositions were prepared in accordance with
s the present invention:
I II III IV
LAS 13.3 13.7 10.4 8.0
C45 AS 3.9 4.0 4.5 -
C45 E0.5S 2.0 2.0 - -
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C45 E3S - - _ -
C45E6.5S 0.5 0.5 0.5 5.0
C9-C~4 alkyl dimethyl hydroxy1.0 - - 0.5
ethyl quaternary ammonium
salt
Tallow fatty acid 0.5 _ _ _
Tallow alcohol ethoxylate - - 1.0 0.3
(50)
STPP - 41.0 - 20.0
Zeolite A 26.3 - 21.3 1.0
Carbonate 23.9 12.4 25.2 17.0
Sodium Polyacrylate (45%) 3.4 0.0 2.7
M~~ - - 1.0 1.5
Silicate (1:6 ratio) 2.4 6.4 2.1 6.0
Sulfate 10.5 10.9 8.2 15.0
PB 1 1.0 1.0 1.0 2.0
PEG MW --4000 (50%) 1.7 0.4 1.0 -
CMC 1.0 - - 0.3
Citric - - 3.0 -
NOBS/ DOBS 0.2 0.5 0.5 0.1
TAED 0.6 0.5 0.4 0.3
SRP 1 1,5 _ _ _
SRP2 - 1.5 1.0 1.0
Moisture 7.5 3.1 6.1 7.3
Mn sulphate - - - 1.0
Chelant - - - 0.5
speckles 0.5 1.0 3.0 0.5
Pectate lyase 0.01 0.01 0.008 0.001
Pectin Lyase - 0.001 - -
Mannanase 0.01 0.002 0.0008 0.01
Xyloglucanase 0.1 0.002 0.0008 0.001
Protease 0.004 0.004 0.008 0.007
Lipase 0.006 0.003 0.005 0.003
Amylase 0.003 0.015 0.007 0.006
Cellulase 0.001 0.0015 0.001 0.0014
Minors 1.0 1.0 1.0 1.0
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Example 9
The following liquid detergent formulations were prepared according to the
present invention (Levels are given in parts per weight, enzyme are expressed
in
pure enzyme)
I II III IV V
LAS 11.5 9.0 - 4.0
C25E2.5S - 3.0 18.0 - 16.0
C45E2.25S 11.5 3.0 - 16.0 -
C23E9 - 3.0 2.0 2.0 1.0
C23E7 3.2 - _ _ _
CFAA - - 5.0 - 3.0
TPKFA 2.0 - 2.0 0.5 2.0
Citric (50%) 6.5 1.0 2.5 4.0 2.5
Ca formate 0.1 0.06 0.1 - -
Na formate 0.5 0.06 0.1 0.05 0.05
SCS 4.0 1.0 3.0 1.2 -
Borate 0.6 - 3.0 2.0 3.0
Na hydroxide 6.0 2.0 3.5 4.0 3.0
Ethanol 2.0 1.0 4.0 4.0 3.0
1,2 Propanediol 3.0 2.0 8.0 8.0 5.0
Monoethanolamine 3.0 1.5 1.0 2.5 1.0
TEPAE 2.0 - 1.0 1.0 1.0
Pectate lyase 0.05 0.001 0.005 0.045 0.008
Pectin lyase - 0.001 0.001 - -
Mannanase 0.005 0.001 0.050 0.045 0.008
Xyloglucanase 0.005 0.010 0.005 0.045 0.008
Protease 0.03 0.01 0.03 0.02 0.02
Lipase - - 0.002 - -
Amylase - - - 0.002 -
Cellulase - - 0.0002 0.0005 0.0001
SRP1 0.2 - 0.1 - -
DTPA - - 0.3
PVNO - - 0.3 - 0.2
Brightener 1 0.2 0.07 0.1 - -
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I II III IV V
Silicone antifoam 0.04 0.02 0.1 0.1 0.1
Miscellaneous and water
Example 10
s The following liquid detergent formulations were prepared according to the
present invention (Levels are given in parts per weight, enzyme are expressed
in
pure enzyme)
I II III IV I II III IV
LAS 10.0 13.0 9.0 - 25.0 - - -
C25AS 4.0 1.0 2.0 10.0 - 13.0 18.0 15.0
C25E3S 1.0 - - 3.0 - 2.0 2.0 4.0
C25E7 6.0 8.0 13.0 2.5 - - 4.0 4.0
TFAA - - - 4.5 - 6.0 8.0 8.0
APA - 1.4 - - 3.0 1.0 2.0 -
TPKFA 2.0 - 13.0 7.0 - 15.0 11.0 11.0
Citric 2.0 3.0 1.0 1.5 1.0 1.0 1.0 1.0
Dodecenyl 12.0 10.0 - - 15.0 - - -
/
tetradecenyl
succinic acid
Rapeseed fatty4.0 2.0 1.0 - 1.0 - 3.5 -
acid
Ethanol 4.0 4.0 7.0 2.0 7.0 2.0 3.0 2.0
1,2 Propanediol4.0 4.0 2.0 7.0 6.0 8.0 10.0 13.0
Monoethanolam- - - 5.0 - - 9.0 9.0
ine
Triethanolamine- - 8.0 - - - 0.4 0.3
TEPAE 0.5 - 0.5 0.2 2.0 1.2 1.0 -
DETPMP 1.0 1.0 0.5 1.0
Pectate lyase0.001 .001 .001 0.003 0.003 .002 .002 0.005
Pectin lyase - - 0.001 - - 0.001- -
Mannanase 0.001 .001 0.005 0.003 0.030 .002 .002 0.005
Xyloglucanase0.001 0.01 .001 0.030 0.003 0.0020.010 .005
Protease 0.02 0.02 0.01 .008 - - .003 .003
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I II III IV I II III IV
Lipase - .002 - .002 .004 0.01 0.01 0.01
Amylase .004 .004 0.01 .008 - - .004 .003
Cellulase - - - .002 - - 0.004 0.002
SRP 2 0.3 - 0.3 0.1 1.0 1.5 2.5 2.5
Boric acid 0.1 0.2 1.0 2.0 4.0 4.0
Ca chloride - 0.02 - 0.01 0.1 0.2 0.3 -
Brightener - 0.4 - - 0.4 - _ _
1
Suds 0.1 0.3 - 0.1 0.8 0.7 - _
suppressor
Opacifier 0.5 0.4 - 0.3 8.0 7.5 8.0 8.2
NaOH up to 8.0 8.0 7.6 7.7
pH
Miscellaneous
and water
Example 11
The following liquid detergent compositions were prepared according to the
present invention (Levels are given in parts by weight, enzyme are expressed
in
pure enzyme)
I 11
LAS 28.0 19.0
C45AS 14.0 6.0
C 13E8 3.0 3.0
Oleic acid 3.0 2.5
Citric 5.0 5.0
Na hydroxide 0.4 4.0
Ca Formate 0.2 0.1
Na Formate - 0.5
Ethanol 7,0 _
Monoethanolamine 16.5 8.0
1,2 propanediol 6.0 5.5
Xylene sulfonic acid - 2,0
TEPAE 1.5 0.8
Protease 0.05 0.02
Pectate lyase 0.005 0.01
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I II
Pectin lyase - 0.001
Mannanase 0.005 0.01
Xyloglucanase 0.005 0.01
PEG - 0.7
Brightener 2 0.4 0.1
Perfume 0.5 0.3
Water and Minors
Example 12
The following granular fabric detergent compositions which provide "softening
through the wash" capability were prepared according to the present invention
I II
C45AS - 10.0
~S 7.6 -
C68AS 1.3 -
C45E7 4.0 -
C25E3 - 5.0
Coco-alkyl-dimethyl hydroxy-1.4 1.0
ethyl ammonium chloride
Citrate 5.0 3.0
N a-S KS-6 - 11.
0
Zeolite A 15.0 15.0
MA/AA 4.0 4.0
DETPMP 0.4 0.4
PB1 15.0 -
Percarbonate - 15.0
TAED 5.0 5.0
Smectite clay 10.0 10.0
HMWPEO - 0.1
Pectate lyase 0.043 0.001
Pectin lyase 0.001 -
Mannanase 0.043 0.01
Xyloglucanase 0.043 0.001
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Protease 0.02 0.01
Lipase 0.02 0.01
Amylase 0.03 0.005
Cellulase 0.001
Silicate 3.0 5.0
Carbonate 10.0 10.0
Suds suppressor 1.0 4.0
CMC 0.2 0.1
Miscellaneous and minors Up to 100%
Example 13
5 The following rinse added fabric softener composition was prepared according
to
the present invention
DEQA (2) 20.0
Pectate lyase 0.001
Mannanase 0.001
Xyloglucanase 0.001
Cellulase 0.001
HCL 0.03
Antifoam agent 0.01
Blue dye 25ppm
CaCl2 0.20
Perfume 0.90
Miscellaneous and water Up to 100%
Example 14
The following fabric softener and dryer added fabric conditioner compositions
were prepared according to the present invention
I II III IV V
DEQA 2.6 19.0 -
DEQA(2) - - - - 52.0
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I II III IV V
DTMAMS - - - 26.0 -
S DASA - - 70.0 42.0 40.2
Stearic acid of IV=00.3 - - _ _
Neodol45-13 - - 13.0 - -
HCL 0.02 0.02 - -
Ethanol - - 1.0 - -
Pectate lyase 0.005 0.002 0.001 0.01 0.002
Mannanase 0.05 0.002 0.001 0.01 0.002
Xyloglucanase 0.05 0.002 0.001 0.01 0.002
Perfume 0.3 1.0 0.75 1.0 1.5
Glycoperse S-20 - - - - 15.4
Glycerol monostearate- - - 26.0 -
Digeranyl Succinate - - 0.38 - -
Silicone antifoam 0.01 0.01 - - -
Electrolyte - 0.1 - - -
Clay _ _ - 3.0 -
Dye 10ppm 25ppm 0.01 - -
Water and minors 100% 100% - - -
Example 15
The following laundry bar detergent compositions were prepared according to
the
present invention (Levels are given in parts per weight, enzyme are expressed
in
pure enzyme)
I II III VI V III VI V
LAS - - 19.0 15.0 21.0 6.75 8.8 -
C28AS 30.0 13.5 - - - 15.75 11.2 22.5
Na Laurate 2.5 9.0 - - - _ - -
Zeolite A 2.0 1.25 - - - 1.25 1.25 1.25
Carbonate 20.0 3.0 13.0 8.0 10.0 15.0 15.0 10.0
Ca Carbonate27.5 39.0 35.0 - - 40.0 - 40.0
Sulfate 5.0 5.0 3.0 5.0 3.0 - - 5.0
TSPP 5.0 - - - - 5.0 2.5 -
STPP 5'.0 15.0 10.0 - - 7.0 8.0 10.0
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I II III VI V III VI V
Bentonite - 10.0 - - 5.0 - - -
clay
DETPMP - 0.7 0.6 - 0.6 0.7 0.7 0.7
CMC - 1.0 1.0 1.0 1.0 - - 1.0
Talc - - 10.0 15.0 10.0 - - -
Silicate - - 4.0 5.0 3.0 - - -
PVNO 0.02 0. 03 - 0.01 - 0.02 - -
MA/AA 0.4 1.0 - - 0.2 0.4 0.5 0.4
SRP 1 0.3 0.3 0.3' 0.3 0.3 0.3 0.3 0.3
Pectate lyase0.01 0.001 0.005 0.001 0.02 0.004 0.001 .0005
Pectin Lyase- - 0.001 - - 0.001 - -
Mannanase 0.0010.001 .0005 0.001 0.002 0.004 0.001 .0005
Xyloglucanase0.0010.001 .0005 0.001 0.002 0.004 0.005 0.005
Amylase - - 0.01 - - - 0.002 -
Protease - 0.004 - 0.003 0.003 - - 0.003
Lipase - 0.002 - 0.002 - - - -
Cellulase - .0003 - - .0003 .0002 - -
PEO - 0.2 - 0.2 0.3 - _ 0.3
Perfume 1.0 0.5 0.3 0.2 0.4 - - 0.4
Mg sulfate - - 3.fl 3.0 3.0 - - -
Brightener 0.15 0.1 0.15 - - - - 0.1
Photoactivated- 15.0 15.0 15.0 15.0 - - 15.0
bleach (ppm)
Example 16
The following compact high density (0.96Kg/I) dishwashing detergent
s compositions were prepared according to the present invention
I II III IV V VI
STPP - 51.0 51.0 - - 44.3
Citrate 17.0 - - 50.0 40.2 -
Carbonate 17.5 14.0 20.0 - 8.0 33.6
Bicarbonate - . - - 26.0 - -
Silicate 15.0 15.0 8.0 - 25.0 3.6
Metasilicate2.5 4.5 4.5 - - _
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I II III IV V VI
PB1 10.0 8.0 8.0 - - -
PB4 - - - 10.0 -
Percarbonate - - - - 11.8 4.8
Nonionic 2.0 1.5 1.5 3.0 1.9 5.9
TAED 2.0 - - 4.0 - 1.4
HEDP 1.0 - - _ _ -
DETPMP 0.6 - - - - _
MnTACN - - - - 0.01 -
PAAC - 0.01 0.01 - - -
Paraffin 0.5 0.4 0.4 0.6 - -
Pectate lyase 0.01 0.002 0.03 0.05 0.005 0.005
Pectin Lyase - 0.001 - - 0.001 -
Mannanase 0.001 0.002 0.003 0.005 0.005 0.001
Xyloglucanase 0.01 0.002 0.003 0.005 0.005 0.001
Protease 0.072 0.053 0.053 0.026 0.059 0.01
Amylase 0.012 0.012 0.012 0.021 0.021 0.006
Lipase - 0.001 - 0.005 -
BTA 0.3 0.2 0.2 0.3 0.3 0.3
Polycarboxylate6.0 - - - 4.0 0.9
Perfume 0.2 0.1 0.1 0.2 0.2 0.2
pH 11.0 11.0 11.3 9.6 10.8 10.9
Miscellaneous,lfate Up to 100%
su and
water
Example 17
s The following granular dishwashing detergent compositions of bulk density
1.02Kg/L were prepared according to the present invention
I II III IV V VI
STPP 30.0 33.5 27.9 29.6 33.8 22.0
Carbonate 30.5 30.5 30.5 23.0 34.5 45.0
Silicate '7.0 7.5 12.6 13.3 3.2 6.2
Metasilicate - 4.5 - - - -
Percarbonate - - - - 4.0 -
PB1 4.4 4.5 4.3 - - -
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I II III IV V VI
NADCC - - - 2.0 - 0.9
Nonionic 1.0 0.7 1.0 1.9 0.7 0.5
TAED 1.0 - - - 0.9 -
PAAC - 0.004 - - - -
Paraffin 0.25 0.25 - - - -
Pectate lyase0.01 0.005 0.002 0.002 0.02 0.001
Pectin lyase - 0.001 - - - -
Mannanase 0.01 0.005 0.02 0.002 0.02 0.001
Xyloglucanase0.01 0.005 0.002 0.02 0.02 0.005
Protease 0.036 0.021 0.03 - 0.006 -
Amylase 0.03 0.005 0.004 - 0.005 -
Lipase 0.005 - 0.001 - - -
BTA 0.15 0.15 - - 0.2 -
Perfume 0.2 0.2 0.05 0.1 0.2
pH 10.8 11.3 11.0 10.7 11.5 10.9
Miscellaneous, ter Up to 100%
sulfate and
wa
Example 18
s The following tablet detergent compositions were prepared according to the
present invention by compression of a granular dishwashing detergent
composition at a pressure of 13KN/cm2 using a standard 12 head rotary press:
I II III IV V VI VII VIII
STPP - 48.8 54.7 38.2 - 52.4 56.1 36.0
Citrate 20.0 - - - 35.9 - -
Carbonate 20.0 5.0 14.0 15.4 8.0 23.0 20.0 28.0
Silicate 15.0 14.8 15.0 12.6 23.4 2.9 4.3 4.2
Pectate lyase0.01 0.002 0.02 0.001 0.002 0.0330.02 0.02
Pectin lyase- - 0.001- - 0.001- -
Mannanase 0.001 0.002 0.0020.001 0.02 0.0330.02 0.02
Xyloglucanase0.001 0.002 0.02 0.001 0.002 0.0330.02 0.02
Protease 0.042 0.072 0.0420.031 0.052 0.0230.023 0.029
Amylase 0.012 0.012 0.0120.007 0.015 0.0030.017 0.002
Lipase 0.005 - - - - - - -
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I II III IV V VI VII VIII
PB1 14.3 7.8 11.7 12.2 - - 6.7 8.5
PB4 _ _ _ - 22.8 - 3.4 -
Percarbonate - - - - - 10.4 - -
Nonionic 1.5 2.0 2.0 2.2 1.0 4.2 4.0 6.5
PAAC - - 0.02 0.009 - - - -
MnTACN _ - - - 0.007 - - -
TAED 2.7 2.4 - - - 2.1 0.7 1.6
HEDP 1.0 - - 0.9 - 0.4 0.2
DETPMP 0.7 _ _ _ _ _ _ _
Paraffin 0.4 0.5 0.5 0.5 - - 0.5
BTA 0.2 0.3 0.3 0.3 0.3 0.3 0.3
Polycarboxylate4.0 - - - 4.9 0.6 0.8 -
PEG - - - _ - 2.0 - 2.0
Glycerol - _ _ _ - 0.4 - 0.5
Perfume _ _ _ 0.05 0.2 0.2 0.2 0.2
Weight of tablet20g 25g 20g 30g 18g 20g 25g 24g
pH 10.7 10.6 10.7 10.7 10.9 11.2 11.010.8
Miscellaneous,fate Up to 100%
sul and
water
Example 19
5 The following automatic dishwashing tablets were made in accordance with the
present invention (g of raw material and enzymes are expressed in pure enzyme)
Phase 1
STPP 9.6 9.6 10.6
Silicate 0.5 0.7 2.9
SKS-6 1.5 1.5 -
Carbonate 2.3 2.7 2.8
HEDP 0.2 0.2 0.2
PB1 2.4 2.4 2.8
PAAC 0.002 0.002 -
Amylase 0.1 0.1 0.001
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I I) III
Protease 0.06 0.06 0.002
Nonionic 0.4 0.8 0.4
PEG 6000 0.4 0.26 -
BTA 0.04 0.04 0.06
Paraffin 0.1 0.10 0.1
Perfume 0.02 0.02 0.02
Total 17.7g 18.58 20.1 g
Phase 2
Pectate Lyase 0.005 0.5 0.2
Pectin lyase 0.001 - -
Mannanase 0.002 0.025 0.2
Xyloglucanase 0.01 0.03 0.05
Amylase 0.003 0.003 0.004
Protease 0.01 0.009 0.01
Citric acid 0.3 - 0.6
Sulphamic acid - 0.3
Bicarbonate 1.1 0.4 0.6
Carbonate - 0.5 -
Triacetin - - 1.2
CaCl2 - 0.07 0.1
PEG 6000 - - 1.'2
PEG 3000 0.06 0.06 -
Total 2.058 2.50g 23.68
The tablet compositions I and II are prepared as follows. The detergent active
composition of phase 1 is prepared by admixing the granular and liquid
components and is then passed into the die of a conventional rotary press. The
press includes a punch suitably shaped for forming a mould. The cross-section
of the die is approximately 30x38 mm. The composition is then subjected to a
compression force of 940 kg/cm2 and the punch is then elevated exposing the
first phase of the tablet containing the mould in its upper surface. The
detergent
active composition of phase 2 is prepared in similar manner and is passed into
the die. The particulate active composition is then subjected to a compression
~o force of 170 kg/cm2, the punch is elevated, and the multi-phase tablet
ejected
from the tablet press. The resulting tablets dissolve or disintegrate in a
washing
machine as described above within 12 minutes, phase 2 of the tablets
dissolving
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within 5 minutes. The tablets display improved strength, especially on long-
term
storage, together with excellent dissolution characteristics.
The tablet composition III was prepared as follows : The compressed portion is
prepared by delivering the composition of active detergent components to a
punch cavity of a modified rotary tablet press and compressing the composition
at a pressure of 940kg/cm2. The modified tablet press provides tablet wherein
the compressed portion has a mould. For the purposes of Example III, the non-
compressed portion is in particulate form. The non-compressed portion is
1o accurately delivered to the mould of the compressed portion using a nozzle
feeder. The non-compressed portion is adhered to the compressed portion by
coating the non-compressed portion with a coating layer which contacts the
compressed portion.
Example 20
The following liquid dishwashing detergent compositions of density 1.40Kg/L
were prepared according to the present invention
I II III IV
STPP 17.5 17.2 23.2 23.1
Carbonate - 2.4 - -
Silicate 6.1 24.9 30.7 22.4
NaOCI 1.1 1.1 1.1 1.2
Thickener 1.0 1.1 1.1 1.0
Nonionic - 0.1 0.06 0.1
NaBz 0.7 - -
Pectate lyase 0.005 0.001 0.001 0.002
Mannanase 0.001 0.001 0.005 0.002
Xyloglucanase 0.001 0.005 0.001 0.002
NaOH 1,g _ _ -
KOH 3.6 3.0 - _
Perfume 0.05 - - -
pH 11.7 10.9 10.8 11.0
2o Water up to 100%
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Example 21
The following liquid rinse aid compositions were prepared according to the
present invention
I II III IV
Mannanase 0.001 0.001 0.005 0.005
Xyloglucanase 0.01 0.001 0.001 0.001
Pectate lyase 0.001 0.001 0.001 0.001
Pectin lyase 0.001 0.001 0.001 0.001
Nonionic 10.0 13.6 62.3 60.0
Propylene glycol- - 5.0 5.5
Citric 3.5 4.6 - -
SCS 10.0 7.7 - -
pH of the liquid3.0 2.5 7.2 7.2
Miscellaneous, Up to 100%
solvent and
water
Example 22
o The following manual liquid dishwashing compositions were prepared according
to the present invention
I II III IV V VI VII
C12-14E06-2S 25.0 28.0 26.0 30.0 20.0 26.0 26.0
C12-14 alkyl dimethyl2.0 6.0 6.0 7.8 5.0 6.0 6.0
amine oxide
C12-14 alkyl dimethyl2.0 - - - - _ _
betaine
C12-14 glucose 3.0 1.0 - - - - _
amide
C11 E09 - 1.0 - 4.0 2.0 - -
C9-11 E08 5.0 - 3.0 - - 3.0 3.0
DTPA - 0.1 - - - - -
SCS - 1.0 3.5 3.0 2.5 3.5 3.5
Xylene sulfonate - 3.0 - - - - -
Mg hydroxide 1.0 - - - - - _
Mg chloride 0.4 2.6 - - - - -
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I II III IV V VI VII
1,3 bis (methylamino)- - 0.7 1.0 0.3 2.5 0.7
cyclohexane
N,N-dimethylamino)- - 0.2 0.5 0.2 0.2 0.2
ethyl methacrylate
homopolymer
Citric - - 3.0 - - - -
Maleic acid - - - 2.5 - - -
Ethanol 8.0 5.0 7.0 7.0 4.0 7.0 7.0
Protease - - - _ _ - 0.02
Amylase - - - - - 0.005 -
Pectate lyase 0.005 0.0020.005 0.001 0.0050.01 0.001
Mannanase 0.001 0.02 0.005 0.001 0.0050.01 0.01
Xyloglucanase 0.001 0.0020.05 0.002 0.0050.01 0.001
Perfume 0.2 0.5 0.5 0.4 0.3 0.5 0.5
Water and minors Up to %
100
ExamJ~le 23
The following liquid hard surface cleaning compositions were prepared
according
to the present invention
I II III IV V
Pectate lyase 0.005 0.01 0.03 0.02 0.008
Mannanase 0.001 0.01 0.03 0.002 0.008
Xyloglucanase 0.001 0.01 0.03 0.002 0.008
Amylase 0.01 0.002 0.005 - -
Protease 0.05 0.01 0.02 - -
Hydrogen peroxide - - - 6.0 6.8
Acetyl triethyl - - - 2.5
citrate
DTPA - - - 0.2
Butyl hydroxy toluene- - - 0.05 -
EDTA* 0.05 0.05 0.05 - -
Citric / Citrate 2.9 2.9 2.9 1.0
LAS 0.5 0.5 0.5 - -
C 12 AS 0. 5 0.5 0. 5 -
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I II III IV V
C10AS - - - - 1.7
C12(E)S 0.5 0.5 0.5 - -
C12,13 E6.5 nonionic 7.0 7.0 7.0 - -
Neodol23-6.5 - - - 12.0
Neodol23-3 - - - - 1.5
Neodol91-10 - - - - 1.6
C25AE 1.8S - - - 6.0
Na paraffin sulphonate - - - 6.0
Perfume 1.0 1.0 1.0 0.5 0.2
Propanediol - - - 1.5
Ethoxylated tetraethylene - - 1.0
-
pentaimine
2, Butyl octanol - - - - 0.5
Hexyl carbitol** 1.0 1.0 1.0
SCS 1.3 1.3 1.3 - -
pH adjusted to 7-12 7-12 7-12 4 -
Miscellaneous and water Up to 100%
*Na4 ethylenediamine diacetic
acid
**Diethylene glycol monohexyl
ether
Example 24
'fhe following spray composition for cleaning of hard surfaces and removing
household mildew was prepared according to the present invention
Pectate lyase 0.01
Mannanase 0.01
Xyloglucananase 0.01
Amylase 0.01
Protease 0.01
Na octyl sulfate 2.0
Na dodecyl sulfate 4.0
Na hydroxide 0.8
Silicate 0.04
Butyl carbitol* 4.0
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Perfume 0.35
Water/minors up to 100%
*Diethylene glycol monobutyl ether
Example 25
The following disinfecting compositions were prepared according to the present
invention.
I II III
Wipe Spray Liquid
H2O2 1.0 1.5 1.0
Na tetraborate 10.H20 - 1.0
C10 Amine Oxide - 0.9 0.9
C12-14 alkyl dimethyl amine oxide 0.4 - -
C7-10 AS - - 6.0
C9-11 E010 - 0.05 -
C8-18 Fatty acid - 0.1 0.2
Ethanol 9.0 1.0 2.5
Benzyl alcohol - 0.8 -
Propylene or diethylene glycol 1.0 1.5 -
butyl ether
Poly(propylene glycol) monobutyl 0.2 - -
ether
HEDP - 0.1 -
Butylated hydroxytoluene 0.01 0.06 0.03
Salicyclic acid 0.03 - 0.07
Pectate lyase 0.001 0.01 0.005
Mannanase 0.001 0.01 0.001
Xyloglucanase 0.002 0.01 0.001
Perfume 0.1 0.3 0.3
Citric 0.7 - 1.5
Dye - - 2.0
NaOH - 0.1
Miscellaneous and water Up to 100%
