Note : Les descriptions sont présentées dans la langue officielle dans laquelle elles ont été soumises.
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DETERGENT COMPOSITIONS COMPRISING A MALTOGENIC ALPHA-AMYLASE ENZYME
10
Field of the Invention
The present invention relates to detergent compositions comprising a
maltogenic
alpha-amylase enzyme and a detergent ingredient selected from a nonionic
surfactant, a protease enzyme and/or a bleaching agent.
Background of the invention
2o Performance of a detergent product is judged by a number of factors,
including
the ability to remove soils. Therefore, detergent components such a~s
surfactants,
bleaching agents and enzymes, have been incorporated in detergents. One of
such specific example is the use of proteases, lipases, amylases and/or
cellulases.
In particular, 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 and dishwashing
3o applications. Indeed, starchy materials such as amylose and ~amylopectin,
constitute one of the major components of the soils /stains encountered in
laundry, dishwashing or hard surfaces cleaning operations. Moreover, the
textile
industry uses starchy materials in their textile finishing processes.
Therefore,
amylase enzymes have been since a long time incorporated into the detergent
products for the removal of starch-containing stains. However, it has been
1
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surprisingly found that such commonly used detergent amylases could not
hydrolyse retrograded starch or raw starch.
As studied in J. A. Radley "Starch and its Derivatives" Fourth Edition Chapman
s and Hall Ltd p194-201; retrogradation is a term given to the changes which
occur
spontaneously in a starch paste, or gel on ageing. It arises from the inherent
tendency of starch molecules to bind to one another and which leads to an
increase in crystallinity. Solutions of low concentration become increasingly
cloudy due to the progressive association of starch molecules into larger
particles. Spontaneous precipitation takes place and the precipitated starch
appears to be reverting to its original condition of cold-water insolubility.
Pastes
of higher concentration on cooling set to a gel, which on ageing becomes
steadily firmer due to the increasing association of the starch molecules.
This
arises because of the strong tendency for hydrogen bond formation between
~5 hydroxy groups on adjacent starch molecules.
The changes taking place during retrogradation are of considerable importance
in the industrial uses of starch. It is believed to be an important factor in
the
staling of bread and in the textural changes of other starch-containing foods,
e.g.
2o canned soups, peas, meat preparations, etc. Starch and retrograded starch
are
also found in the textile, paper and adhesives industries. Indeed, fabrics are
sized with starch in the textile process. Depending on the sizing process,
retrograded starch can be formed on the fabrics and might not be removed in
the
ulterior desizing processes. Moreover, the majority of the stains/soils found
on
25 fabrics, dishware and other hard surfaces, especially those found in the
kitchen,
contain starch which upon ageing in for e.g., the laundry basket or
dishwashing
machine will retrograde to such associated starchy network. Hence, such
retrograded starch containing materials are found later onto the fabric,
dishware
and/or other hard surfaces to be cleaned. Such retrograded starch shows an
3o increased resistance to hydrolysis by amylolytic enzymes, is only slightly
soluble
at ordinary temperatures and redispersed only with difficulty, especially if
the
retrograded starch has dried first and it further demonstrates a progressive
increase in gel firmness. Indeed, it has been found that retrograded starch
forms
very stable structures and only melts at very high temperature such as
150°C for
35 amylose, 60°C for amylopectin or 120°C for the complex
amylose-lipid. The level
and timing of retrogradation depends upon the starch type: it can vary from
10%
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to 90% of the starch content. It has been found that current detergent
amylases
have very little to no effect on retrograded starch.
In addition, a substantial part of starch material remains indeed under the
raw
s form even when processed within the food or textile industries. In
particular, it
has been found that food stains such as rice, spaghettis, potatoes, corn,
cereals,
etc. retrieved on fabric, dishware and other hard surfaces contain a
substantial
amount of raw starch.
~o. Furthermore, it has been surprisingly found that such retrograded or raw
starch
remaining on the surfaces, entraps further dirt, and when found on a fabric
surface, leads to a dingy appearance of the surface to be cleaned.
As can be seen from the above, there is a need to formulate detergent products
15 which address the removal of such raw or retrograded starch containing
soils/stains. Accordingly, the above objective has been met by formulating a
detergent composition comprising a maltogenic alpha-amylase enzyme and
detergent ingredient selected from a nonionic surfactant, a protease enzyme
and/or a bleaching agent.
It has been surprisingly found that the combination of a maltogenic alpha-
amylase with a detergent ingredient selected from a nonionic surfactant, a
protease enzyme and/or a bleaching agent, provides a synergistic cleaning of
starch containing stains and soils. Indeed, it has been found that maltogenic
2s alpha-amylase have an endo-, exo- as well as transferase hydrolytic
activity on
starch, that can be very useful in a cleaning applications. Moreover, such of
starch containing stains and soils comprise many lipids components as well.
Without wishing to be bound by theory, it is believed that the nonionic
surfactant
removes the lipids contained in the starch-containing stains and soils and
thereby
so facilitate the degradation of starch by the maltogenic alpha-amylase. In
addition,
it is believed that the nonionic surfactant keeps the degraded starch in
solution
and prevents its redeposition onto the surface to be cleaned. It has been
further
surprisingly found that nonionic surfactant prevents the retrogradation of
starch
and therefore is very efficient if used with the maltogenic alpha-amylase in a
pre-
35 treatment step. Similarly, such of starch containing stains and soils
comprise
many proteins components as well. Without wishing to be bound by theory, it is
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believed that the protease enzyme hydrolyses the proteins contained in such
complex stains and thereby induces the synergistic removal of such
stains/soils
with the maltogenic alpha-amylase. In addition, such hydrolysed
proteins/starch
containing stains/soils have a lower molecular weight in the wash solution and
this results in less redeposition of such hydrolysed stains/soils on the
surface to
be cleaned. Finally, it has been found that bleaching agents oxidise the
starch
containing stains and soils. Without wishing to be bound by theory it is
believed
that the oxidising action of the bleaching agent renders the starch more
soluble
and therefore easier to be synergistically removed by the maltogenic alpha-
amylase and the bleaching agent. It results as well in less redeposition on
the
surtace to be cleaned.
Maltogenic alpha-amylases are known for various industrial applications. In
particular, this enzyme finds potential application for retarding or
preventing
~ 5 retrogradation and thus the staling of starch based common food as common
in
the baking industry. These enzymes are useful as well in the process for the
manufacture of linear oligosaccharides or in the production of sweeteners and
ethanol from starch and/or textile industry. A maltogenic alpha-amylase from
Baeillus (EP 120 693) is commercially available under the tradename Novamyl~
20 (Product of Novo Nordisk A/S, Denmark) and is widely used in the baking
industry as an anti-staling agent due to its ability to reduce retrogradation
of
starch. W099/43794 describes variants of maltogenic alpha-amylases with
improved properties : altered pH optimum, improved thermostability, increased
specific activity, altered cleavage pattern or increased ability to educe
25 retrogradation of starch or staling of bread. W099/43793 discloses variants
of
maltogenic alpha-amylases having CGT-ase activity, CGT-ase having maltogenic
alpha-amylase activity and hybrid enzymes with one or more improvements to
the specific properties of the parents enzymes.
3o However, the use of a maltogenic alpha-amylase with a detergent ingredient
specifically selected from a nonionic surfactant, a protease enzyme and/or a
bleaching agent; for the synergistic removal of starch-containing stains-soils
in
a detergent composition, has never been previously recognised.
35 Summary of the invention
4
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The present invention relates to detergent compositions, including laundry,
dishwashing, and/or hard surface cleaner compositions, comprising a maltogenic
alpha-amylase and a detergent ingredient selected from a nonionic surfactant,
a
protease enzyme and/or a bleaching agent. Such compositions provide excellent
s removal of starch-containing stains and soils, and when formulated as
laundry
compositions, excellent whiteness maintenance and dingy cleaning.
Detailed description of the invention
Maltogenic alpha-am r~lase
The first essential componenfi of the detergent compositions of the present
invention is a maltogenic alpha amylase of the IUPAC Classification EC
3.2.1:133 that hydrolyses 1,4-a-D-glucosidic linkages in polysaccharides so as
to
remove successive alpha-maltose units from the nonreducing ends of the chains.
Maltogenic alpha-amylases are thus able to hydrolyse amylose and amylopectin
to maltose in the alpha-configuration and is also able to hydrolyse
maltotriose as
2o well as cyc(odextrin. Such enzymes are also referred to as maltohydrolase
(glucan 1,4-a-maltohydrolase).
Such maltogenic alpha-amylase is generally comprised in the detergent
compositions of the present invention at a level of from 0.0002% to 10%,
preferably 0.001 % to 2%, more preferably 0.001 % to 1 % pure enzyme by weight
of the total detergent composition.
Suitable maltogenic alpha-amylases for the purpose of the present invention
are
described below:
1 ) A suitable maltogenic alpha-amylase is the amylase cloned from Bacillus as
described in EP 120 693 (hereinafter referred to as Novamyl). Novamyl has the
amino acid sequence set forth in amino acids 1-686 of SEQ ID NO: 1 of
W099/47393. Novamyl is encoded in the gene harbored in the Bacillus strain
NCIB 11837 which has the nucleic acid sequence set forth in SEQ ID N0:1 of
W099/47393.
5
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2) W099/43793 describes variants of maltogenic alpha-amylase having CGT-ase
activity and variants of CGT-ase having maltogenic alpha-amylase activity, as
well
as constructed hybrid enzymes ; that demonstrate the maltogenic alpha-amylase
s properties required for the enzymes of the present invention. In particular,
WO99/43793 describes a polypeptide which:
a) has at least 70 % identity to amino acids 1-686 of SEQ ID NO: 1 of
W099/43793;
b) comprises an amino acid modification which is an insertion, substitution or
deletion compared to SEQ ID NO: 1 of W099/43793 in a region corresponding to
amino acids 40-43, 78-85, 136-139, 173-180, 188-195 or 259-268; and
c) has the ability to form cyclodextrin when acting on starch.
W099/47393 further discloses a polypeptide which:
15 a) has an amino acid sequence having at least 70 % identity to a parent
cyclodextrin glucanotransferase (CGT-ase);
b) comprises an amino acid modification which is an insertion, substitution or
deletion compared to the parent CGT-ase in a region corresponding to amino
acids
40-43, 78-85, 136-139, 173-180, 188-195 or 259-268 of SEQ ID NO: 1 of
2o W099/43793; and
c) has the ability to form linear oligosaccharides when acting on starch.
In more details, W099/43793 provides for variants of maltogenic alpha-amylase
and CGT-ase and hybrids wherein the parent maltogenic alpha-amylase used in
25 the invention is an enzyme classified in EC 3.2.1.133, preferably
maltogenic alpha-
amylase used, is the amylase cloned from Bacillus as described in EP 120 693
and wherein the parent CGT-ase used is an enzyme classified in EC 2.4.1.19.
and
has preferably one or more of the following characteristics:
i) an amino acid sequence having at least 50 % identity to amino acids 1-686
of
3o SEQ ID NO: 1 of WO99/43793, preferably at least 60 %;
ii) being encoded by a DNA sequence which hybridizes at conditions described
below to the DNA sequence set forth in SEQ ID N0:1 of W099/43793or to the
DNA sequence encoding Novamyl harbored in the Bacillus strain NCIB 11837; and
iii) a catalytic binding site comprising amino acid residues corresponding to
D228,
35 E256 and D329 as shown in the amino acid sequence set forth in amino acids
1-
686 of SEQ ID NO: 1 of W099/43793.
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W099/43793 describes variants of CGT-ase that has the ability to form linear
oligosaccharides when acting on starch and hence have the desired maltogenic
alpha-amylase properties required within the present invention. Such CGT-ase
variant has a modification of at least one amino acid residue in a region
corresponding to residues 40-43, 78-85, 136-139, 173-180, 189-195 or 259-268
of
SEQ ID NO: 1 of W099/43793. Each modification may be an insertion, a deletion
or a substitution, of one or more amino acid residues in the region indicated.
The
modification of the parent CGT-ase is preferably such that the resulting
modified
~o amino acid or amino acid sequence more closely resembles the corresponding
amino acid or structural region in Novamyl. Thus, the modification may be an
insertion of or a substitution with an amino acid present at the corresponding
position of Novamyl, or a deletion of an amino acid not present at the
corresponding position of Novamyl.
~s The CGT-ase variant may particularly comprise an insertion into a position
corresponding to the region D190-F194 of Novamyl (amino acid sequence shown
in SEQ iD NO: 1 of W099/43793). The insertion may comprise 3-7 amino acids,
particularly 4-6, e.g. 5 amino acids. The insertion may be DPAGF as found in
Novamyl or an analogue thereof, e.g. with the first amino acid being negative,
the
20 last one being aromatic, and the ones in between being preferably P, A or
G. The
variant may further comprise a subsfiitution at the position corresponding to
T189 of
Novamyl with a neutral amino acid which is less bulky than F, Y or W. Other
examples of insertions are DAGF, DPGF, DPF, DPAAGF, and DPAAGGF.
Modifications in the region 78-85 preferably include deletion of 2-5 amino
acids,
2s e.g. 3 or 4. Preferably, any aromatic amino acid in the region 83-85 should
be
deleted or substituted with a non-aromatic.
Modifications in the region 259-268 preferably include deletion of 1-3 amino
acid,
e.g. two. The region may be modified so as to correspond to Novamyl
The CGT-ase variant may comprise further modifications in other regions, e.g.
3o regions corresponding to amino acids 37-39, 44-45, 135, 140-145, 181-186,
269
273, or 377-383 of Novamyl.
Additional modifications of the amino acid sequence may be modeled on a second
CGT-ase, i.e. an insertion of or substitution with an amino acid found at a
given
position in the second CGT-ase, or they may be made close to the substrate
(less
35 than 8 A from the substrate, e.g. less than 5 A or less than 3 A) as
described in
WO 96/33267,
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The following are some examples of variants based on a parent CGT-ase from
Thermoanaerobacter (using 8. circulans numbering). Similar variants may be
made from other CGT-ases.
L194F+ *194aT+ *194bD+ *194cP+ *194dA+ *194eG+ D196S
s L87H+ D89*+ T91 G+ F91 aY+ G92*+ G93*+ S94*+ L194F+ *194aT+ *194bD+
*194cP+ *194dA+ *194eG+ D196S
*194aT+ *194bD+ *194cP+ *194dA+ *194eG+ D196S
L87H+ D89*+ T91 G+ F91 aY+ G92*+ G93*+ S94*+ *194aT+ *194bD+ *194cP+
*194dA+ *194eG+ D196S
~ o Y260F+ L261 G+ G262D+ T263D+ N264P+ E265G+ V266T+ *266aA+ *266bN+
D267H+ P268V
*194aT+ *194bD+ *194cP+ *194dA+ *194eG+ D196S+ Y260F+ L261 G+ G262D+
T263D+ N264P+ E265G+ V266T+ *266aA+ *266bN+ D267H+ P268V
15 W099/43793 further describes Novamyl variants having the desired maltogenic
alpha-amylase properties required within the present invention. Such Novamyl
variant has as well the ability to form cyclodextrin when acting on starch and
has a
modification of at least one amino acid residue in the same regions described
above for CGT-ase variants. However, the modifications are preferably in the
20 opposite direction, i.e. such that the resulting modified amino acid or
amino acid
sequence more closely resembles the corresponding amino acid or structural
region of a CGT-ase. Thus, the modification may be an insertion of or a
substitution with an amino acid present at the corresponding position of a CGT-
ase, or a deletion of an amino acid not present at the corresponding position
of a
2s CGT-ase. Preferred modifications include a deletion in the region 190-195,
preferably the deletion ~ (191-195) and/or a substitution of amino acid 188
and/or
189, preferably F188L and/or Y189Y.
3) Other suitable maltogenic alpha-amylases suitable for the purpose of the
so present invention are described in W099/43794. W099/43794 describes
modified
amino acid sequences of a maltogenic alpha-amylase corresponding to variants
with improved properties, based on the three-dimensional structure of the
maltogenic alpha-amylase Novamyl. The variants have altered physicochemical
properties., e.g, an altered pH optimum, improved thermostability, increased
s5 specific activity, an altered cleavage pattern or an increased ability to
reduce
retrogradation of starch or staling of bread.
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In particular, W099/47394 describes prefierred maltogenic alpha-amylases that
should have one or more of the following properties:
i) a three dimensional structural homology to Novamyl,
s ii) an amino acid sequence having at least 70 % identity to SEQ ID NO: 1 of
W099/47394, preferably at least 80 % or 90 %, e.g. 95 % or 98 %,
iii) a DNA sequence which hybridizes to the DNA sequence set forth in SEQ ID
N0:1 of W099/47394 or to the DNA sequence encoding Novamyl harbored in the
Bacillus strain NCIB 11837;
~o iv) a calcium binding site comprising a coordination equivalent to a
backbone
carbonyl atom from Asn77, sidechain atom OE2 and OE1 from GIu102, a
sidechain atom OD1 from Asp79, a sidechain atom OD1 from Asp76, and a
sidechain atom OE1 from GIu101, and one water molecule WAT V21, atom OWO,
wherein the positions are as shown in Appendix 1 of W099/47394;
15 V) a sequence of five amino acids corresponding to Pro-Ala-Gly-Phe-Ser in a
position equivalent to residues 191-195 in the amino acid sequence shown in
SEQ
ID NO: 1 of W099/47394; and
The structural homology referred to above in i) is based on other sequence
homologies, hydrophobic cluster analysis or by reverse threading (Huber, T ;
2o Torda, AE, PROTEIN SCIENCE Vol. 7 , No. 1 pp. 142-149 (1998)) and which by
any of these methods is predicted to have the same tertiary structure as
Novamyl,
wherein the tertiary structure refers to the overall folding or the folding of
Domains
A, B, and C, more preferably including Domain D, and most preferably including
Domain E. Alternatively, a structural alignment between Novamyl and a
maltogenic
2s alpha-amylase may be used to identify equivalent positions. The calcium
binding
site referred to above in iv) is based on a calcium binding site identified in
the
three-dimensional structure of Novamyl, and is discussed in details in the
section
"Calcium binding sites" of W099/47394. The "equivalent position" referred to
above
in v) is based on amino acid or DNA sequence alignment or structural homology
3o using methods known in the art.
Preferred maltogenic alpha-amylases for the purpose of the present invention
are
the Novamyl enzyme described in EP 120 693 ; the Novamyl variant based on
the amino acid sequence shown in amino acids 1-686 of SEQ ID N0: 1 within
ss which the residues 191-195 were removed, Phe188 was substituted with Leu
and
Thr189 was substituted with Tyr, termed D (191-195)-F188L-T189Y (See
9
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WO 02/02726 PCT/US00/18120
example 4 of W099/43793); as well as the following 2 varianfis of Novamyl (See
example 5 of W099/43794): the variant wherein positions 191-195 have been
deleted and the variant wherein positions 191-195 have been deleted and the
following amino acids at the following positions have been substituted :
s F188L/T189Y/T142A/N327S. More preferred enzyme is Novamyl.
Commercially available maltogenic alpha-amylase is the enzyme product sold
under the tradename Novamyl, by Novo Nordisk A/S.
1o Preferred maltogenic alpha-amylases for specific applications are alkaline
maltogenic alpha-amylase, i.e. enzymes having an enzymatic activity of at
least
10%, preferably at least 25%, more preferably at least 40% of their maximum
activity at a pH ranging from 7 to 12, preferably 10.5. More preferred
maltogenic
alpha-amylases are enzymes having their maximum activity at a pH ranging from
15 7 to 12, preferably 10.5.
In another embodiment of the present invention, the detergent compositions of
the present invention might further comprise one or more starch-binding
domain.
Such starch binding domain might be added in the detergent compositions of the
2o present invention, as such, or might be part of a chimeric maltogenic alpha-
amylase hybrid. Indeed, the maltogenic alpha-amylase of the present inventions
preferably will have or will be added a Starch Binding Domain (SBD). In
general
enzymes such as amylases, cellulases and xylanases. have a modular structure
consisting of a catalyst domain and at least one non-catalytic domain whose
2s function is generally described as that of a polysaccharide-binding domain
(PBD), starch-binding domain (SBD), cellulose-binding domain (CBD) and xylan-
binding domain. The function of these binding domains is to bind selectively
to
the substrate of the enzyme, and in particular, the primary function of SBD is
to
bind to starch. It has been found surprisingly found that the detergent
3o compositions of the present invention comprising further one or more SBD
and/or
wherein the maltogenic alpha-amylases comprise such a SBD will provide a
more effective starch-containing soils/stains removal. It has further been
found
that such enzymes can be formulated in a more cost-effective manner. Without
wishing to be bound by theory, it is believed that such maltogenic alpha-
amylase
3s will be more effectively directed specifically to their substrate from the
wash
solutions and so have improved deposition onto the starch containing
stains/soils
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WO 02/02726 PCT/US00/18120
for improved and/or new performance. Moreover, it is believed that the binding
of
the SBD will disrupt the surface of starch resulting in a higher hydrolytic
rate.
Suitable SBD for use in the present invention are the SBDs comprised in the
glucoamylase from Aspergillus niger ( Sigma) and in the ~i-galactosidase from
A.
s awamori. The recovery and fusion of SBDs can be achieved as described in
Ford, C. et al., J. Cell. Biochem. (Suppl.) 14D:30 (1990) and in Chen, L. et
al.,
Abst. Annu. Meet. Am. Soc. Microbiol. 90:269 (1990).
The above-mentioned enzymes may be of any suitable origin, such as vegetable,
1o 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
be used. Nowadays, it is common practice to modify wild-type enzymes via
protein / genetic engineering techniques in order to optimise their
performance
15 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
2o 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
2s 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.
3o Nonionic surfactants
The detergent compositions of the present invention can comprise as the second
essential element, a nonionic surfactant. As described below, preferred
nonionic
surfactants are selected from polyethylene oxide condensates of alkyl
alcohols,
amide oxide and polyethylene oxide condensates of alkyl acids and/or mixtures
35 thereof.
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The nonionic surfactants are generally comprised at a level of 0.05-30% by
weight, preferably from 0.1-10% by weight of the total composition.
As mentioned above, it has been surprisingly found that the detergent
s compositions of the present invention comprising a nonionic surfactant,
provide
synergistic removal of starch from fabrics, dishware and other hard surfaces.
Without wishing to be bound by theory, it is believed that the nonionic
surfactant
adsorbs onto the granular surface of the starch thereby disrupting the starch
structure and influencing and preventing the retrogradation process of the
starch.
1o Such disruption of the structure increases the maltogenic alpha-amylase
accessibility to its substrate. Moreover, nonionic surfactants can be used
also in
a pre-treatment process and therefore can reduce the retrogradation process of
starch. Hence, the starch-containing stains / soils is more easily hydrolysed
by
the enzyme and a synergistic breakdown of the starch soil by the maltogenic
1s alpha-amylase and the nonionic surfactant occurs.
The nonionic surfactant which can be used in the present invention may
comprise essentially any alkoxylated nonionic surfactant. The ethoxylated and
propoxylated nonionic surfactants are preferred. Preferred alkoxylated
2o surfactants can be selected from the classes of the nonionic condensates of
alkyl
phenols, nonionic ethoxylated alcohols, nonionic ethoxylatedlpropoxylated
fatty
alcohols, nonionic ethoxylate/propoxylate condensates with propylene glycol,
and
the nonionic ethoxylate condensation products with propylene oxide/ethylene
diamine adducts. Highly preferred are nonionic alkoxylated alcohol
surfactants,
25 being the condensation products of aliphatic alcohols with from 1 to 125
moles of
alkylene oxide, in particular about 50 or from 1 to 15 moles, preferably to 11
moles, particularly ethylene oxide and/or propylene oxide, are highly
preferred
nonionic surfactant comprised in the anhydrous component of the particles of
the
invention. The alkyl chain of the aliphatic alcohol can either be straight or
3o branched, primary or secondary, and generally contains from 6 to 22 carbon
atoms. Particularly preferred are the condensation products of alcohols having
an
alkyl group containing from 8 to 20 carbon atoms with from 2 to 9 moles and in
particular 3, 5 or 7 moles, of ethylene oxide per mole of alcohol.
3s The nonionic surtactant which can be used in the present invention may also
comprise polyhydroxy fatty acid amides, in particular those having the
structural
12
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WO 02/02726 PCT/US00/18120
formula R2CONR1Z wherein : R1 is H, C1_1g, preferably C1-C4 hydrocarbyl, 2-
hydroxy ethyl, 2-hydroxy propyl, ethoxy, propoxy, or a mixture thereof,
preferable
C1-C4 alkyl, more preferably C1 or C2 alkyl, most preferably C1 alkyl (i.e.,
methyl); and R2 is a C5-C31 hydrocarbyl, preferably straight-chain C5-C1 g or
C7-C1 g alkyl or alkenyl, more preferably straight-chain Cg-C17 alkyl or
alkenyl,
most preferably straight-chain C11-C17 alkyl or alkenyl, or mixture thereof;
and Z
is a polyhydroxyhydrocarbyl having a linear hydrocarbyl chain with at least 3
hydroxyls directly connected to the chain, or an alkoxylated derivative
(preferably
ethoxylated or propoxylated) thereof. Z preferably will be derived from a
reducing
1o sugar in a reductive amination reaction; more preferably Z is a glycityl. A
preferred nonionic polyhydroxy fatty acid amide surfactant for use herein is a
C12-C14~ a C15-C17 and/or C16-C1g alkyl N-methyl glucamide. It may be
particularly preferred that the composition herein comprises a mixture of a
C12-
C1 g alkyl N-methyl glucamide and condensation products of an alcohol having
~ 5 an alkyl group containing from 8 to 20 carbon atoms with from 2 to 9 moles
and
in particular 3, 5 or 7 moles, of ethylene oxide per mole of alcohol. The
polyhydroxy fatty acid amide can be prepared by any suitable process. One
particularly preferred process is described in detail in WO 9206984. A product
comprising about 95% by weight polyhydroxy fatty acid amide, low levels of
2o undesired impurities such as fatty acid esters and cyclic amides, and which
is
molten typically above about 80°C, can be made by this process.
The nonionic surfactant for use in the present invention may also comprise a
fatty
acid amide surfactant or alkoxylated fatty acid amide. They include those
2s nonionic surfactants having the formula: R6CON(R7) (R8 ) wherein R6 is an
alkyl
group containing from 7 to 21, preferably from 9 to 17 carbon or even 11 to 13
carbon atoms and R7 and R8 are each individually selected from the group
consisting of hydrogen, C1-C4 alkyl, C1-C4 hydroxyalkyl, and -(C2H40)xH,
where x is in the range of from 1 to 11, preferably 1 to 7, whereby it may be
3o preferred that R7 is different to R8~ one having x being 1 or 2, one having
x being
from 3 to 11 or preferably from 3 to 7.
The nonionic surfactant for use in the present invention may also comprise an
alkyl ester of a fatty acid. These nonionic surfactants include those having'
the
35 formula: R9C00(R10) wherein Rg is an alkyl group containing from 7 to 21,
preferably from 9 to 17 carbon or even 11 to 13 carbon atoms and R10 is a C1
13
CA 02414158 2002-11-27
WO 02/02726 PCT/US00/18120
C4 alkyl, C1-C4 hydroxyalkyl, or -(C2H4O)xH, where x is in the range of from 1
to
11, preferably from 1 to 7, more preferably from 1 to 5, whereby it may be
preferred that R10 is a methyl or ethyl group.
The nonionic surfactant for use in the present invention may also comprise an
alkylpolysaccharide, such as those disclosed in US Patent 4,565,647, Llenado,
issued January 21, 1986, having a hydrophobic group containing from 6 to 30
carbon atoms and a polysaccharide, e.g., a polyglycoside, hydrophilic group
containing from 1.3 to 10 saccharide units.
Preferred alkylpolyglycosides have the formula
R~O(CnH~nO)t(9lYcosyl)x
wherein R2 is selected from the group consisting of alkyl, alkylphenyl,
hydroxyalkyl, hydroxyalkylphenyl, and mixtures thereof in which the alkyl
groups
contain from 10 to 18 carbon atoms; n is 2 or 3; t is from 0 to 10, and x is
from
1.3 to 8. The glycosyl is preferably derived from glucose.
2o Also suitable as nonionic surfactants for the purpose of the present
invention are
the semi-polar nonionic surfactants: Semi-polar nonionic surfactants are a
special category of nonionic surfactants which include water-soluble amine
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 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 about 1 to about 3 carbon
atoms; and water-soluble sulfoxides containing one alkyl moiety of from about
10
3o 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
having the formula
0
~'
R3(OR4)xN(R5)2
14
CA 02414158 2002-11-27
WO 02/02726 PCT/US00/18120
wherein R3 is an alkyl, hydroxyalkyl, or alkyl phenyl group or mixtures therof
containing from about 8 to about 22 carbon atori~s; 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
can be attached to each other, e.g., through an oxygen or nitrogen atom, to
form
a ring structure.
These amine oxide surfactants in particular include C10-C1g alkyl dimethyl
1o amine oxides and Cg-C12 alkoxy ethyl dihydroxy ethyl amine oxides.
When included therein, fihe cleaning compositions of the present invention
typically comprise from 0.2% to about 15°l°, preferably from
about 1 % to about
10% by weight of such semi-polar nonionic surfactants.
Also suitable as nonionic surFactants for the purpose of the present invention
are
the co-surfactant 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 Rq.X(CH2)n, X is -O-,-
C(O)NH- or -NH- Rq, is a Cg-C12 alkyl chain n is between 1 to 5, preferably 3.
2o 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.
Suitable tertiary amines for use herein include tertiary amines having the
formula
R1 R2R3N wherein R1 and R2 are C1-Cg alkylchains or
Rs
I
-C CH2-CH-O )~H
so R3 is either a Cg-C12, preferably Cg-C10 alkyl chain, or R3 is Rq.X(CH2)n,
whereby X is -O-, -C(O)NH- or -NH-,Rq. 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 .
R3 and Rq. may be linear or branched; R3 alkyl chains may be interrupted with
up to 12, preferably less than 5, ethylene oxide moieties.
CA 02414158 2002-11-27
WO 02/02726 PCT/US00/18120
Preferred tertiary amines are R1 R2R3N where R1 is a C6-C12 alkyl chain, R2
and R3 are C1-C3 alkyl or
Rs
-( CHZ-CH-O~XH
where R5 is H or CH3 and x = 1-2.
Also preferred are the amidoamines of the formula:
0
R1-C-NH-( CH2 n N-(R2 2
wherein R1 is Cg-C12 alkyl; n is 2-4,
preferably n is 3; R~ and R3 is C1-Cq.
Most preferred amines of the present invention include 1-octylamine, 1
1o hexylamine, 1-decylamine, 1-dodecylamine,CB-10oxypropylamine, N coco 1
3d(aminopropane, coconutalkyldimethylamine, lauryldimethylamine, lauryl
bis(hydroxyethyl)amine, coco bis(hydroxyehtyl)amine, lauryl amine 2 moles
propoxylated, octyl amine 2 moles propoxylated, lauryl
amidopropyldimethylamine, C8-10 amidopropy(dimethylamine 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-
dodecyldimethylamine and bishydroxyethylcoconutalkylamine and oleylamine 7
times ethoxylated, lauryl amido propylamine and cocoamido propylamine.
Protease Enzymes
A second essential element of the detergent compositions of the present
invention can be a protease enzyme. As mentioned above, the starch containing
stains and soils comprise many proteins components as well. Without wishing to
2s be bound by theory it is believed that the protease enzyme hydrolyses the
proteins contains in such complex stains and thereby induces the synergistic
removal of such stains/soils with the maltogenic alpha-amylase. In addition,
such
hydrolysed complex stains/soils have a lower molecular weight in the wash
solution and therefore it results in less redeposition of such hydrolysed
complex
so stains on the surface to be cleaned.
Suitable proteases are the subtilisins which are obtained from particular
strains of
8. subtilis and 8. licheniformis (subtilisin BPN and BPN'). One suitable
protease
16
CA 02414158 2002-11-27
WO 02/02726 PCT/US00/18120
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
enzymes is described in GB 1,243,784 to Novo. Other suitable proteases include
s ALCALASE~, DURAZYM~ and SAVINASE~ (protease Subtilisin 309 from
Bacillius subtilis) from Novo and MAXATASE~~ MAXACAL~, PROPERASE~
and MAXAPEM~ (protein engineered Maxacal) from Gist-Brocades. 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
1o their variants described in WO 95/23221. 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
15 described in WO 95/07791 to Procter & 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.
Proteolytic enzymes also encompass modified bacterial serine proteases, such
as those described in EP 251 446, filed April 28, 1987 (particularly the
variant
2o Y217L described on 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 what is called herein "Protease C",
which
is a variant of an alkaline serine protease from Bacillus in which lysine
replaced
25 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 WO 91/06637. Genetically modified variants,
particularly of Protease C, are also included herein.
A preferred protease referred to as "Protease D" is a carbonyl hydrolase
variant
so 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
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,
35 +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
17
CA 02414158 2002-11-27
WO 02/02726 PCT/US00/18120
according to the numbering of Bacillus amyloliquefaciens subtilisin, as
described
in W095/10591 and W095110592. The "protease D" variants have preferably the
amino acid substitution set 76/103/104, more preferably the substitution set
N76D/S103A/V1041. Also suitable is a carbonyl hydrolase variant of the
protease
s 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
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
subtilisin (co-pending patent application published under W098/55634).
More preferred proteases are multiply-substituted protease variants. These
protease variants comprise a substitution of an amino acid residue with
another
naturally occuring amino acid residue at an amino acid residue position
corresponding to position 103 of Bacillus amyloliquefaciens subtilisin in
combination with a substitution of an amino acid residue positions
corresponding
to positions 1, 3, 4, 8, 9, 10, 12, 13, 16, 17, 18, 19, 20, 21, 22, 24, 27,
33, 37, 38,
42, 43, 48, 55, 57, 58, 61, 62, 68, 72, 75, 76, 77, 78, 79, 86, 87, 89, 97,
98, 99,
101, 102, 104, 106, 107, 109, 111, 114, 116, 117, 119, 121, 123, 126, 128,
130,
131, 133, 134, 137, 140, 141, 142, 146, 147, 158, 159, 160, 166, 167, 170,
173,
174, 177, 181, 182, 183, 184, 185, 188, 192, 194, 198, 203, 204, 205, 206,
209,
210, 211, 212, 213, 214, 215, 216, 217, 218, 222, 224, 227, 228, 230, 232,
236,
237, 238, 240, 242, 243, 244, 245, 246, 247, 248, 249, 251, 252, 253, 254,
255,
256, 257, 258, 259, 260, 261, 262, 263, 265, 268, 269, 270, 271, 272, 274 and
275 of Bacillus amyloliquefaciens subtilisin; wherein when said protease
variant
includes a substitution of amino acid residues at positions corresponding to
positions 103 and 76, there is also a substitution of an amino acid residue at
one
so or more amino acid residue positions other than amino acid residue
positions
corresponding to positions 27, 99, 101, 104, 107, 109, 123, 128, 166, 204,
206,
210, 216, 217, 218, 222, 260, 265 or 274 of Bacillus amyloliquefaciens
subtilisin
and/or multiply-substituted protease variants comprising a substitution of an
amino acid residue with another naturally occuring amino acid residue at one
or
more amino acid residue positions corresponding to positions 62, 212, 230,
232,
252 and 257 of Bacillus amyloliquefaciens subtilisin as described in
18
CA 02414158 2002-11-27
WO 02/02726 PCT/US00/18120
W099/20727, W099/20726 and W099/20723 all filed on October 23, 1998 from
The Procter & Gamble Company. Preferred multiply substituted protease variants
have the amino acid substitution set 101/103/104/159/232/236/245/248/252,
more preferably 101 G/103A/1041/.159D/232V/236H/245R/248D/252K according
to the.numbering of Bacillus amyloliquiefaciens subtilisin.
More preferred proteases for the purpose of the present invention are the
proteolytic enzymes sold under the tradename Savinase by Novo Nordisk A/S,
the "Protease B" variant with the substitution Y217L described in EP 251 446,
the
"protease D" variant with the substitution set N76D/S103A/V1041 and the
protease described in W099/20727, W099/20726 and W099/20723 with the
amino acid substitution set 101 G/103A/1041/159D/232V/236H/245R/248D/252K.
The protease enzymes are norma(Iy incorporated in the detergent composition at
levels from 0.0001 % to 2%, preferably 0.0001 % to 0.1 %, more preferably
0.001 % to 0.05%, of pure enzyme by weight of the detergent composition.
Bleaching agent
A second essential element of the detergent compositions of the present
~o invention can be a bleaching agent. Without wishing to be bound by theory,
it is
believed that the oxidisation of the starch material by a bleaching agent
solubilises the starch materials, which are therefore more easily removed and
results in less redeposition on the surface to be cleaned. Hence, the
compositions of the present invention further comprising a bleaching agent
will
provide synergistic removal of starch-containing stains and soils, and when
formulated as laundry compositions, improved whiteness maintenance and dingy
cleaning.
Preferred bleaching agents for the detergent compositions of fihe present
3o invention are the combination of percarbonate with a bleach activator
selected
from nonanoyloxybenzene-sulfonate (NOBS), Phenolsulfonate ester of N-
nonanoyl-6-aminocaproic acid (NACA-OBS), and/or tetraacetylethylenediamine
(TAED). Also preferred are the bleaching agents referred to as
[Mn(Bcyclam)Ch].
19
CA 02414158 2002-11-27
WO 02/02726 PCT/US00/18120
Suitable bleaching agents for the purpose of the present invention include
hydrogen peroxide, PB1, PB4 and percarbonate with a particle size of 400-800
microns. 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 0.1 % to 30%, preferably 1 % to 20% by weight of the
detergent composition.
The bleaching agent component for use herein can be any of the bleaching
~o 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.
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
are disclosed in U.S. Patent 4,483,781, U.S. Patent Application 740,446,
2o 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
halogen bleaching agents. Examples of hypohalite bleaching agents, for
2s example, include trichloro isocyanuric acid and the sodium and potassium
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.
so 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-
3s aminocaproic acid (NACA-OBS, described in W094/28106), which are
perhydrolyzed to form a peracid as the active bleaching species, leading to
CA 02414158 2002-11-27
WO 02/02726 PCT/US00/18120
improved bleaching effect. Also suitable activators are acylated citrate
esters
such as disclosed in EP 624 154 and the unsymetrical acyclic imide bleach
activator of the following formula as disclosed in the Procter & Gamble
W098/04664
O O
R
1 N R3
t
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
group and R3 is a C1-C4 linear or branched chain saturated or unsaturated
alkyl
group. Those bleach activators are generally used within the detergent
1o compositions of the present invention at a level of 0.1-10%, preferably 0.5-
5% by
weight of the detergent composition.
Useful bleaching agents, including peroxyacids and bleaching systems
comprising bleach activators and peroxygen bleaching compounds for use in
detergent compositions according to the invention are described in our co-
pending applications W095/10592, W097/00937, WO95/27772, WO95/27773,
W095/27774 and W095/27775.
The hydrogen peroxide may also be present by adding an enzymatic system (i.e.
2o 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 537 381.
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
3o patent application No 94870206.3. The bleaching compounds can be catalyzed
by means of a manganese compound. Such compounds are well known in the
art and include, for example, the manganese-based catalysts disclosed in U.S.
21
CA 02414158 2002-11-27
WO 02/02726 PCT/US00/18120
Pat. 5,246,621, U.S. Pat. 5,244,594; U.S. Pat. 5,194,416; U.S. Pat. 5,114,606;
and European Pat. App. Pub. Nos. 549,271A1, 549,272A1, 544,440A2, and
544,490A1; Preferred examples of these catalysts include MnIV2(u-O)3(1,4,7-
trimethyl-1,4,7-triazacyclononane)2(PFg)2, Mnlll2(u-O)1 (u-OAc)2(1,4,7-
trimethyl-
1,4,7-triazacyclononane)2(CI04)2, MnlU4(u-O)g(1,4,7-
triazacyclononane)4(CI04)4, MnlIIMnIV4(u-O)~(u-OAc)2_(1,4,7-trimethyl-1,4,7-
triazacyclononane)2(CI04)3, MnIV(1,4,7-trimethyl-1,4,7-triazacyclononane)-
(OCH3)3(PFg), and mixtures thereof.
1o More preferred for use therein are the transition metal bleach catalysts
being
complexes of a transition metal and a cross bridged macropolycyclic ligands
such as described in Procter & Gamble patent applications WO 98/39405, WO
98/39406 and WO 98/39098. Most preferred is the Mn Complex Bleach Catalyst
of the formula [Mn(Bcyclam)Ch] illustrated as:
~N~
cy I ,..N
CI-~~>>
/N~
"Bcyclam" (5,12-dimethyl-1,5,8,12-tetraaza-bicyclo[6.6.2]hexadecane or 5,12-
diethyl-1,5,8,12-tetraaza-bicyclo[6.6.2]hexadecane). Such transition-metal
bleach
catalyst can be prepared according to Procter & Gamble patent application
W098/39335 or according to J.Amer.Chem.Soc., (1990), 112, 8604. These
2o bleach catalysts are generally encompassed in the detergent compositions of
the
present invention at a level of 0.0007-0.07%, preferably 0.005-0.05% by weight
of the detergent compositions.
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
of oxygen, such as by hanging clothes out to dry in the daylight, the
sulfonated
so 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
22
CA 02414158 2002-11-27
WO 02/02726 PCT/US00/18120
contain about 0.025% to about 1.25%, by weight, of sulfonated zinc
phthalocyanine.
Also suitable as bleaching species for the purpose of the present invention
are a
colour-safe bleach boosters that may be used in conjunction with a peroxygen
source in a bleaching composition. The bleach booster is generally present in
the
detergent compositions at a level of from 0.01-10% and more preferably from
0.05-5% by weight of the composition. Bleach boosters to be included in the
detergent compositions of the present invention comprise zwitterionic imines,
1o anionic imine polyions having a net negative charge of from about -1 to
about -3,
and mixtures thereof.
Suitable imine bleach boosters of the present invention include those of the
general structure:
. R1~0+ ~R4
N
R2~R3
where R1-R4 may be a hydrogen or an unsubstituted or substituted radical
selected from the group consisting of phenyl, aryl, heterocyclic ring, alkyl
and
cycloalkyl radicals except that at least one of R1-R4 contains an anionically
charged moiety.
2o Preferred bleach boosters are the anionically charged moiety bonded to the
imine nitrogen described in W097/10323. Also preferred are the tri:cyclic
oxaziridinium compounds described in US 5,710,116 and the bleach boosters
described in W098/16614. These can be prepared in accordance with the
method described in W097/10323 and/or W098/16614.
Detergent components
The detergent compositions of the present invention will preferably comprise a
so further enzyme selected from a lipase, an a-amylase, a cyclomaltodextrin
glucanotransferase and/or an amyloglucosidase.
23
CA 02414158 2002-11-27
WO 02/02726 PCT/US00/18120
In a preferred embodiment, the present invention relates to a laundry andlor
fabric care composition comprising a malfiogenic alpha-amylase and a detergent
ingredient selected from a nonionic surfactant, a protease enzyme and/or a
bleaching agent (Examples 1-17). !n a second embodiment, the present
invention relates to dishwashing or household cleaning compositions (Examples
18-23 ).
The compositions of the invention may for example, be formulated as hand and
machine dishwashing compositions, hand and machine laundry detergent
compositions including laundry additive compositions and compositions suitable
for use in the soaking and/or pre-treatment of stained fabrics, rinse added
fabric
softener compositions, and compositions for use in general household hard
surface cleaning operations. When formulated as compositions for use in manual
dishwashing methods the compositions of the invention preferably contain a
~5 surfactant and preferably other detergent compounds selected from organic
polymeric compounds, suds enhancing agents, group ll metal ions, solvents,
hydrotropes and additional enzymes.
When formulated as compositions suitable for use in a laundry machine washing
2o method, the compositions of the invention preferably contain both a
surfactant
and a builder compound and additionally one or more detergent 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. Laundry
25 compositions can also contain softening agents, as additional detergent
components. Such compositions containing a detergent ingredient selected from
a nonionic surfactant, a protease enzyme and/or a bleaching agent and a
maltogenic alpha-amylase provide starch-containing stain removal, whiteness
maintenance and dingy cleaning when formulated as laundry detergent
3o compositions.
The compositions of the invention can also be used as detergent additive
products. Such additive products are intended to supplement or boost the
performance of conventional detergent compositions.
24
CA 02414158 2002-11-27
WO 02/02726 PCT/US00/18120
The detergent compositions according to the invention can be liquid, paste,
gels,
bars, tablets, spray, foam, powder or granular. Granular compositions can also
be in "compact" form and the liquid compositions can also be in a
"concentrated"
form. 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
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°/a
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
~5 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
conventional liquid detergents. Typically the water content of the
concentrated
20 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 can comprise in
addition to the nonionic surfactant, a surfactant system wherein the
surfactant
so can be selected from anionic and/or cationic and/or ampholytic and/or
zwitterionic surfactants.
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.
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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.
Anionic surfactants: Suitable anionic surfactants to be used are linear alkyl
benzene sulfonate, alkyl ester sulfonate surfactants including linear esters
of Cg-
C20 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, palm oil, etc.
The preferred alkyl ester sulfonate surfactant, especially for laundry
applications,
comprise alkyl ester sulfonate surfactants of the structural formula:
95 O
R3 - CH - C - OR4
S03M
2o wherein R3 is a Cg-C20 hydrocarbyl, preferably an alkyl, or combination
thereof,
R4 is a C1-Cg 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,
25 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
so 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-C2p
alkyl
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
35 ammonium cations and quaternary ammonium cations such as tetramethyl
ammonium and dimethyl piperdinium cations and quaternary ammonium cations
26
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WO 02/02726 PCT/US00/18120
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).
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
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
~5 glycerol sulfates, alkyl phenol ethylene oxide ether sulfates, paraffin
suifonates,
alkyl phosphates, isethionates such as the acyl isethionates, N-acyi taurates,
alkyl succinamates and sulfosuccinates, monoesters of sulfosuccinates
(especially saturated and unsaturated C12-C1 g monoesters) and diesters of
sulfosuccinates (especially saturated and unsaturated C6-C12 diesters), acyl
2o sarcosinates, sulfates of alkylpolysaccharides such as the sulfates of
alkylpolyglucoside (the nonionic nonsulfated compounds being described below),
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
25 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
so 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
35 3% to about 20% by weight of such anionic surtactants.
27
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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 C10-C24 alkyl or hydroxyalkyl group having a C10-C24 alkyl
component, preferably a C12-C20 alkyl or hydroxyalkyl, more preferably C12-
s C1 g 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
ammonium cations. include methyl-, dimethyl, trimethyl-ammonium cations and
quaternary ammonium cations such as tetramethyl-ammonium and dimethyl
piperdinium canons and those derived from alkylamines such as ethylamine,
diethylamine, triethylamine, mixtures thereof, and the like. Exemplary
surfactants
~ s are C12-C1 g alkyl polyethoxylate (1.0) sulfate (C12-C1 gE(1.0)M), C12-C1
g alkyl
polyethoxylate (2.25)~sulfate (C12-C18E(2.25)M), C12-C1g alkyl polyethoxylate
(3.0) sulfate (C12-C18E(3.0)M), and C12-C1 g alkyl polyethoxylate (4.0)
sulfate
(C12-C18E(4.0)M), wherein M is conveniently selected from sodium and
potassium.
Cationic surfactants: Cationic surfactants suitable for use in the detergent
compositions of the present invention are those having one long-chain
hydrocarbyl group. 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_
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(CHg)-, -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, -
CH2CHOH-CHOHCOR6CHOHCH2OH 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
28
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WO 02/02726 PCT/US00/18120
and the sum of the y values is from 0 to about 15; and X is any compatible
anion.
Quaternary ammonium surfactant suitable for the present invention has the
5 formula (I):
R2 ~~3',',,'Ra
1~O ~R5
X-
Formula I
whereby R1 is a short cliainlength alkyl (C6-C10) or alkylamidoalkyl of the
~o formula (II)
Cs C.~ N
~CH~
O
Formula II
y is 2-4, preferably 3.
~5 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,
2o whereby X- is a counterion, preferably a halide, e.g. chloride or
methylsulfate.
Rs
,,H
O''~z
Formula III
R6 is C1-Cq. and z is 1 or 2.
25 Preferred quat ammonium surfactants are those as defined in formula I
whereby
R1 is Cg, C10 or mixtures thereof, x=o,
R3, R4 = CH3 and R5 = CH2CH20H. .
Highly preferred cationic surfactants are the water-soluble quaternary
ammonium
so compounds useful in the present composition having the formula:
29
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WO 02/02726 PCT/US00/18120
R1 R2R3R4N+X- (i)
wherein R1 is Cg-C1 g alkyl, each of R2, R3 and R4 is independently C1-C4
alkyl,
C1-C4 hydroxy alkyl, benzyl, and -(C2H40)xH where x has a value from 2 to 5,
and X is an anion. Not more than one of R2, R3 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
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;
coconut methyl dihydroxyethyl ammonium chloride or bromide;
~5 decyl triethyl ammonium chloride;
decyl dimethyl hydroxyethyl ammonium chloride or bromide;
C12-15 dimethyl hydroxyethyl ammonium chloride'or bromide;
coconut dimethyl hydroxyethyl ammonium chloride or bromide;
myristyl trimethyl ammonium methyl sulphate;
20 lauryl dimethyl benzyl ammonium chloride or bromide;
lauryl dimethyl (ethenoxy)4 ammonium chloride or bromide;
choline esters (compounds of formula (i) wherein R1 is
CH2-CH2-O-C-C12-14 alkyl and R2RgR4 are methyl).
(I
25 O
di-alkyl imidazolines [compounds of formula (i)].
Other cationic surfactants useful herein are also described in U.S. Patent
4,225,044, Cambre, issued October 14, 1980 and in European Patent
3o Application EP 000,224.
Typical cationic fabric softening components include the water-insoluble
quaternary-ammonium fabric softening actives or their corresponding amine
precursor, the most commonly used having been di-long alkyl chain ammonium
35 chloride or methyl sulfate.
Preferred cationic softeners among these include the following:
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1 ) ditallow dimethylammonium chloride (DTDMAC);
2) dehydrogenated tallow dimethylammonium chloride;
3) dehydrogenated tallow dimethylammonium methylsulfate;
4) distearyl dimethylammonium chloride;
s 5) dioleyl dimethylammonium chloride;
6) dipalmityl hydroxyethyl methylammonium chloride;
7) stearyl benzyl dimethylammonium chloride;
8) tallow trimethylammonium chloride;
9) hydrogenated tallow trimethylammonium chloride;
10) C12-14 alkyl hydroxyethyl dimethylammonium chloride;
11 ) C12-18 alkyl dihydroxyethyl methylammonium chloride;
12) di(stearoyloxyethyl) dimethylammonium chloride
(DSOEDMAC);
13) di(tallow-oxy-ethyl) dimethylammonium chloride;
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
2o 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 (1) or (ll), below:
R3 R3
_ + N/ (CHz)n-CH -CH2 X
(~a~ Q'~T 1 X
Ri
T1 T2
or
wherein Q is selected from -O-C(O)-, -C(O)-O-, -O-C(O)-O-, -NR4-C(O)-, -C(O)-
N R4-;
31
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WO 02/02726 PCT/US00/18120
R1 is (CH2)n-Q-T2 or T3;
R2 is (CH2)m-Q-T4 or T5 or R3;
R3 is C1-Cq. alkyl or C1-Cq. hydroxyalkyl or H;
R~ is H or C1-Cq. alkyl or C1-Cq. 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.
1o The alkyl, or alkenyl, chain T1, T2, T3, T4, T5 must contain at least 11
carbon
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
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
2o sulfate;
3) N,N-di(2-tallowyl-oxjr-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;
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.
32
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Ampholytic surfactants: 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 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
1o examples of ampholytic surfactants.
When included therein, the detergent compositions of the present invention
typically comprise from 0.2% to about 15%, preferably from about 1 % to about
10% by weight of such ampholytic surfactants.
Zwitterionic surfactants: Zwitterionic surfactants are also suitable for use
in
detergent compositions. These surfactants can be broadly described as
derivatives of secondary and tertiary amines, derivatives of heterocyclic
secondary and tertiary amines, or derivatives 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
typically comprise from 0.2% to about 15%, preferably from about 1 % to about
10% by weight of such zwitterionic surfactants.
Conventional detergent enzymes
The detergent compositions of the present invention can comprise in addition
to
the maltogenic alpha-amylase, one or more enzymes which provide cleaning
3o performance, fabric care and/or sanitisation benefits. Said enzymes include
enzymes selected from celiulases, hemicellulases, peroxidases, proteases,
gluco-amylases, amylases, mannanases, xyloglucanases, xylanases, lipases,
phospholipases, esterases, cutinases, pectinases, keratanases, reductases,
oxidases, phenoloxidases, lipoxygenases, ligninases, pullulanases, tannases,
pentosanases, malanases, l3-glucanases, arabinosidases, hyaluronid~se,
chondroitinase, laccase or mixtures thereof.
33
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WO 02/02726 PCT/US00/18120
Preferably, the detergent compositions of the present invention will comprise
an
enzyme selected from a lipase, an a-amylase, a cyclomaltodextrin
giucanotransferase and/or an amyloglucosidase. Indeed, it has been found that
the combination of the maltogenic alpha-amylase and the selected detergent
ingredient, with an alpha-amylase, a cyclomaltodextrin glucanotransferase
and/or
an amyloglucosidase within the detergent compositions of the present
invention,
provides an improved removal of raw andlor retrograded starch. Furthermore,
the
stains most commonly encountered in laundry, dishwashing and hard surface
~o cleaning, generally comprise a significant amount of proteins and
triglyceride
compounds. in particular, it has been found that starch materials are usually
associated with lipid compounds. Therefore, it has been found that the
combination of a maltogenic alpha-amylase, a detergent ingredient selected
from
a nonionic surfactant, a protease enzyme and/or a bleaching agent - preferably
a
~5 nonionic surfactant, with a lipase within the detergent compositions of the
present invention, provides an improved removal of such complex stains.
Hence, the detergent compositions comprising such combination of enzymes
provide enhanced removal of starch-containing stains and soils and when
formulated as a laundry detergent composition, enhanced whiteness
2o maintenance and dingy cleaning,
Alpha-amylase
25 As indicated above, the detergent compositions of the present invention
will
preferably comprise an a-amylase. Suitable a-amylases for the purpose of the
present invention are described in the following : W094/02597, Novo Nordisk
A/S published February 03, 1994, describes cleaning compositions which
incorporate mutant amylases. See also W095/10603, Novo Nordisk A/S,
so published April 20, 1995. Other amylases known for use in cleaning
compositions
include both a- and ~i-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-
35 enhanced amylases described in WO94/18314, published August 18, 1994 and
W096/05295, Genencor, published February 22, 1996 and amylase variants
34
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WO 02/02726 PCT/US00/18120
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-
~o amylase activity assay. Preferred are variants of the above enzymes,
described
in W096/23873 (Novo Nordisk). Preferably, the variants are those demonstrating
improved thermal stability, more preferably those wherein at least one amino
acid
residue equivalent to F180, 8181, 6182, T183, 6184, or K185 has been deleted
from the parent a-amylase. Particularly preferred are those variants having
~5 improved thermal stability which comprise the amino acid deletions R181* +
G182* or T183* + G184'. Other amylolytic enzymes with improved properties with
respect to the activity level and the combination of thermal stability and a
higher
activity level are described in W095/35382. Further suitable amylases are the
H
mutant a-amylase enzymes exhibiting improved stability described in
2o W098/26078 by Genencor.
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.
Cyclomaltodextrin alucanotransferase
Also preferred is the cyciomaitodextrin glucanotransferase, EC 2.4.1.19, which
is
an enzyme that cyclizes part of a 1,4-a-D-glucan chain by formation of a 1,4-a-
D
3o glucosidic bond and has the systematic name of 1,4-a-D-glucan 4-a-D-(1,4-a-
D
glucano)-transferase (cyclizing). Commercially available cyclomaltodextrin
glucanotransferase enzymes are sold under the tradenames CGT-ase by
Amano; EN301 by Hayashibara and Toruzyme by Novo Nordisk A/S.
The cyclomaltodextrin glucanotransferase is generally comprised in the
detergent
composition of the invention in an amount of 0.0001 % to 10% by weight,
preferably 0.001 % to 0.5% by weight.
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WO 02/02726 PCT/US00/18120
Am~oalucosidase
Also preferred are the amyloglucosidases classified under the IUPAC
Classification as EC 3.2.1.3. Such amyloglucosidase is a glucan 1,4-a-
glucosidase; is also referred to as "glucoamylase, y-amylase, lysosomal a-
glucosidase, acid maltase or exo-1,4-a-glucosidase" and its systematic name is
1,4-a-D-glucan glucohydrolase. Suitable amyloglucosidase are described in
W092/00381, WO00/04136 and W099/28448. Commercially available
amyloglucosidases are the enzyme products sold under the tradename
PALKODEX by MAPS; AMG300L by Novo Nordisk A/S, Optimax 7525
(Combinations of enzymes including amyloglucosidase) and Spezyme by
Genencor. Further commercial available amyloglucosidases are those from
Aspergillus niger obtainable from the following companies: Ambazyme, Amano,
Boehringer, Fluka, Sigma, Aldomax, Genzyme, Nagase, UOP. Also suitable are
the amyloglucosidases from Aspergillus species from the companies Biocatalysts
or Danisco and the amyloglucosidases from Rhizopus delemar from Nagase;
from Rhizopus niveus from Amano, (CN, Seikagaku; from Rhizopus oryzae from
Enzyme Development Co-operation.
2o Also preferred are lipases. Suitable I~_ pase enzymes include those
produced by
microorganisms of fihe 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.
2s This lipase is available from Amano 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; Chrvmobacter viscosum lipases from U.S. Biochemical
3o Corp., 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.
36
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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 90109446 (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.
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
~5 Humicola insolens, Trichoderma, Thielavia and Sporotrichum. EP 739 982
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
WO95/26398.
Examples of such cellulases are cellulases produced by a strain of Humicola
2o 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
2s 1800, exhibiting cellulase activity; a preferred endoglucanase component
has the
amino acid sequence disclosed in PCT Patent Application No. WO 91/17243.
Also suitable cellulases are the EGIII cellulases from Trichoderma
longibrachiatum described in WO94/21801, Genencor, published September 29,
1994. Especially suitable cellulases are the cellulases having color care
benefits.
3o 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.
35 Said cellulases are normally incorporated in the detergent composition at
levels
from 0.0001 % to 2% of pure enzyme by weight of the detergent composition.
37
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WO 02/02726 PCT/US00/18120
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",
s 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
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, WO 89/09813 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
15 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.
2o Said peroxidases are normally incorporated in the detergent composition at
levels from . 0.0001 % to 2% of pure enzyme by weight of the detergent
composition.
The above-mentioned enzymes may be of any suitable origin, such as vegetable,
25 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
be used. Nowadays, it is common practice to modify wild-type enzymes via
protein / genetic engineering techniques in order to optimise their
performance
3o 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
35 particular cleaning application.
38
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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
1o these domains.
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
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.
3,519,570. A useful Bacillus, sp. AC13 giving proteases, xylanases and
cellulases, is described in WO 9401532 A to Novo.
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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 absorbancy, 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
1o the co-pending Patent Application No. 96870140.9, filed November 07, 1996.
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
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
2o 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
materials are incorporated
at levels of from 0.5°/a to 5% by weight, normally from 1 % to 3% by
weight whilst
the high molecular weight polyethylene oxide materials and the water soluble
3o 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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Builder system
s The compositions according to the present invention may further comprise a
builder system. Any conventional builder system is suitable for use herein
including aluminosilicate materials, silicates, polycarboxylates, alkyl- or
alkenyl-
succinic acid and fatty acids, materials such as ethylenediamine tetraacetate,
diethylene triamine pentamethyleneacetate, metal ion sequestrants such as
1o 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
1s 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
(Hoechst). SKS-6 is a crystalline layered silicate consisting of sodium
silicate
(Na2Si205).
2o 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
2s 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
containing three carboxy groups include, in particular, water-soluble
citrates,
aconitrates and citraconates as well as succinate derivatives such as the
so 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.
35 Polycarboxylates containing four carboxy groups include oxydisuccinates
disclosed in British Patent No. 1,261,829, 1,1,2,2-ethane tetracarboxylates,
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1,1,3,3-propane tetracarboxylates and 1,1,2,3-propane tetracarboxylates.
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.
Alicyclic and heterocyclic polycarboxylates include cyclopentane-cis,cis,cis-
tetracarboxylates, cyclopentadienide pentacarboxylates, 2,3,4,5-tetrahydro-
furan
~o - 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
2o 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
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
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.
so 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
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.
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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
The detergent compositions herein may also optionally contain one or more iron
~o 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
~s iron and manganese ions from washing solutions by formation of soluble
chelates.
Amino carboxylates useful as optional chelating agents include
ethylenediaminetetracetates, N-hydroxyethylethylenediaminetriacetates,
2o nitrilotriacetates, ethylenediamine tetraproprionates,
triethylenetetraaminehexacetates, diethylenetriaminepentaacetates, and
ethanoldiglycines, alkali metal, ammonium, and substituted ammonium salts
therein and mixtures therein.
Amino phosphonates are also suitable for use as chelating agents in the
2s 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
3o 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
35 ("EDDS"), especially the [S,S] . isomer as described in U.S. Patent
4,704,233,
November 3, 1987, to Hartman and Perkins.
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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
utilized, the chelating agents will comprise from about 0:1 % to about 3.0% by
weight of such compositions.
Suds suppresser
Another optional ingredient is a suds suppresser, 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
suppresser is advantageously releasably incorporated in a water-soluble or
water-dispersible, substantially non-surface-active detergent impermeable
2o carrier. Alternatively the suds suppresser can be dissolved or dispersed in
a
liquid carrier and applied by spraying on to one or more of the other
components.
A preferred silicone suds controlling agent is disclosed in Bartollota et al.
U.S.
Patent 3 933 672. Other particularly useful suds suppressers are the self-
emulsifying silicone suds suppressers, 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
copolymer. Especially preferred suds controlling agent are the suds suppresser
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
so name Isofol 12 R.
Such suds suppresser system are described in Copending European Patent
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
s5 silicone/silica mixture in combination with fumed nonporous silica such as
AerosilR.
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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
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 water soluble encapsulating
materials
~5 comprise dextrins derived from ungelatinized starch acid-esters of
substituted
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
2o 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
25 derivatives such as methylcellulose, carboxymethylcellulose and
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
3o malefic anhydride constituting at least 20 mole percent of the copolymer.
These
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.
35 Preferred optical brighteners are anionic in character, examples of which
are
disodium 4,4'-bis-(2-diethanolamino-4-anilino -s- triazin-6-ylamino)stilbene-
2:2'
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WO 02/02726 PCT/US00/18120
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-
s 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
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
~o 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
15 preferably from 0.25% to 2.5% by weight. These polymers and the previously
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
preferred polymer in accordance with EP-A-0 272 033 has the formula
(CH3(PEG)43)0.75(POH)0.25LT-PO)2.8(T-PEG)0.4~T(PO
H)0.25((PEG)43CH3)0.75
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
esters of ethylene glycol and/or propane-diol. The target is to obtain a
polymer
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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,
thereof consist "secondarily" of such species.
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
~5 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
2~ 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
so 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:
35 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
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WO 02/02726 PCT/US00/18120
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.
s 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.
The compositions of the invention may contain a lime soap peptiser compound,
o which has preferably a time 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
2o 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
sodium oleate required to disperse the lime soap deposits formed by 0.0258 of
25 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
oxides, betaines, sulfobetaines, alkyl ethoxysulfates and ethoxylated
alcohols.
Exemplary surfactants having a LSDP of no more than 8 for use in accord with
the presenfi invention include C1g-C1g dimethyl amine oxide, C12-C1g alkyl
ethoxysulfates with an average degree of ethoxylation of from 1-5,
particularly
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
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ethoxylation of either 12 (LSDP=6) or 30, sold under the tradenames Lutensol
A012 and Lutensol A030 respectively, by BASF GmbH.
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).
Hydrophobic bleaches such as 4-[N-octanoyl-6-aminohexanoyl]benzene
sulfonate, 4-[N-nonanoyl-6-aminohexanoyl]benzene sulfonate, 4-[N-decanoyl-6-
1o 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 also comprise
from 0.001 % to 10 %, preferably from 0.01 % to 2%, more preferably from 0.05%
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
3o 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,
s5 polyvinylpyrrolidone polymers, polyvinyloxazolidones and
polyvinylimidazoles or
mixtures thereof.
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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
I
1o (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
~ 5 combination of both.
O O O
II II II
A is NC, CO, C, -O-,-S-, -N- ; x is O or 1;
2o 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.
25 The N-O group can be represented by the following general structures:
O O
I I
(R1 )x -N- (R2)y =N- (R1 )x
30 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
35 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.
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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
s 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
1o 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.
15 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 po(yamine N-oxides having
the general formula (I) wherein R is an aromatic, heterocyclic or alicyclic
groups
wherein the nitrogen of the N-0 functional group is part of said R group.
2o 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
wherein the nitrogen of the N-0 functional group is attached to said R groups.
25 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
is water-soluble and has dye transfer inhibiting properties. Examples of
suitable
so polymeric backbones are polyvinyls, polyalkylenes, polyesters, polyethers,
polyamide, polyimides, polyacrylates and mixtures thereof.
The amine N-oxide polymers of the presenfi invention typically have a ratio of
amine to the amine N-oxide of 10:1 to 1:1000000. However the amount of amine
35 oxide groups present in the polyamine oxide polymer can be varied by
appropriate copolymerization or by appropriate degree of N-oxidation.
Preferably,
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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
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
s 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.
The degree of polymerisation is not critical provided the material has the
desired
water-solubility and dye-suspending power.
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
15 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
present invention comprise a polymer selected from N-vinylimidazole N
2o 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
described in Barth H.G. and Mays J.W. Chemical Analysis Vol 113,"Modern
25 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.
3o 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
s5 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 .
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c) Polyvinylpyrrolidone
The detergent compositions of the present invention may also utilize
polyvinylpyrrolidone ("PVP") having an average molecular weight of from about
s 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
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
polyvinyipyrrolidones 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
15 256,696).
d) Polyvinyloxazolidone
The detergent compositions of the present invention may also utilize
polyvinyloxazolidone as a polymeric dye transfer inhibiting agent. Said
2o polyyinyloxazolidones 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.
25 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
from about 5,000 to about 200,000, more preferably from about 5,000 to about
30 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
35 active groups n the backbone or on branches; cross-finked polymers have
been
described in the Journal of Polymer Science, volume 22, pages 1035-1039.
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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
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
~o 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.
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
2o 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
the detergent composition. A conventional hard surface method comprises
3o treating soiled hard items with e.g. a sponge, brush, clothe, etc. with an
aqueous
liquid having dissolved or dispensed therein an effective amount of the hard
surtace cleaner and/or with such composition undiluted. It also encompasses or
the soaking in a concentrated solution or in a large volume of dilute solution
of
the detergent composition. The process of the invention is conveniently
carried
out in the course of the cleaning process. The method of cleaning is
preferably
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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
~o 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.
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.
N11 : 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.
NI 2 : C12-C14 alkyldimethyl amine oxide
QAS : R2.N+(CH3)2(C2H40H) with R2 = C12-C14
QAS 1 : R2.N+(CH3)2(C2H4OH) with R2 = Cg-C11.
SADS : Sodium C14-22 alkyl disulphate of fromula 2-(R).C4H7-
1,4-(S04-)2 where R=C10-18
MBAS : C12-18 mid branched alkyl sulphate surfactant
with an
average branching of 1.5 methyl or ethyl branching
groups
MES : x-Sulpho methylester of C18 fatty acid
APA : Cg_1p amido propyl dimethyl amine.
CA 02414158 2002-11-27
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Soap : Sodium linear alkyl carboxylate derived from
a 80/20
mixture of tallow and coconut fatty acids.
STS : Sodium toluene sulphonate.
TFAA : C16-C1 g 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.
SDASA : 1:2 ratio of stearyldimethyl amineariple-pressed
stearic
acid.
DTMAMS : Ditallow dimethyl ammonium methylsulfate.
Silicate : Amorphous Sodium Silicate (Si02:Na20 ratio
= 1.6-
3.2:1 ).
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).
SKS-6 : Crystalline layered silicate of formula ~-Na2Si205.
Citrate : Tri-sodium citrate dihydrate.
Citric : Anhydrous citric acid.
Carbonate : Anhydrous sodium carbonate.
Bicarbonate : Sodium hydrogen carbonate.
Sulphate : Anhydrous sodium sulphate.
Mg Sulphate : Anhydrous magnesium sulfate.
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.
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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.
Clay : Bentonite or smectite clay.
PB1 : Anhydrous sodium perborate monohydrate.
PB4 : Sodium perborate tetrahydrate of nominal
formula
NaB03.4H20.
Percarbonate : Anhydrous sodium percarbonate of nominal
formula
Na2C03.3H202 .
NaDCC : Sodium dichloroisocyanurate.
TAED : Tetraacetyl ethylene diamine.
NOBS ~ : Nonanoyloxybenzene sulfonate in the form
of the sodium
salt.
NACA-OBS : (6-nonamidocaproyl) oxybenzene sulfonate.
LOBS : Dodecanoyloxybenzene sulfonate in the form
of the Na
salt.
DOBA : Dodecanoylbenzoic acid
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
MnTACN : Manganese 1,4,7-trimethyl-1,4,7-triazacyclononane.
Photoactivated : Sulfonated zinc or alumino phtalocyanine
encapsulated
Bleach ~ in dextrin soluble polymer.
PAAC : Pentaamine acetate cobalt(III) salt.
Paraffin : Paraffin oil sold under the tradename Winog
70 by
Wintershall.
NaBz : Sodium benzoate.
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Protease : Proteolytic enzyme sold under the tradename Savinase
by Novo Nordisk A/S, the "Protease B" variant with the
substitution Y217L described in EP 251 446, the
"protease D" variant with the substitution set
N76D/S103A/V1041 and the protease described in
W099/20727, W099/20726 and W099/20723 with the
amino acid substitution set
101 G/103A/1041/159D/232V/236H/245R/248D/252K.
Amylase : Amylolytic enzyme sold under the tradename Termamyl
~ and Duramyl~ available from Novo Nordisk A/S and
those variants having improved thermal stability with
amino acid deletions R181* + G182* or T183* + G184* as
described in W095/35382.
Lipase4 : Lipolytic enzyme sold under the tradename Lipolase,
Lipolase Ultra by Novo Nordisk A/S and Lipomax by Gist-
Brocades.
MaItoH : Maltogenic alpha-amylase sold under the tradename
Novamyl by Novo Nordisk A/S
AMG : Amyloglucosidase sold under the tradename AMG from
Novo Nordisk A/S.
Cellulase : Cellulytic enzyme sold under the tradename Carezyme,
Celluzyme and/or Endolase by Novo Nordisk A/S.
CMC : Sodium carboxymethyl cellulose.
PVP : Polyvinyl polymer, with an average molecular weight of
60,000.
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.
Brightener 3 : Disodium 4,4'bis (4,6-dianilino-1,3,5-triazin-2-yl)amino
stilbene-2-2'-disulfonate.
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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% Silicone/silica, 18% stearyl alcoho1,70%
starch in
granular form.
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 : Soil Release Polymer selected from 1 ) Non-cotton
soil
release polymer according to U.S. Patent 5,415,807,
Gosselink, Pan, Kellett and Hall, issued May
16, 1995 or
and/or from 2) Non-cotton soil release polymer
according
to US application no.60/051517.
QEA : bis((C2H5O)(C2H40)n)(CH3) -N+-C6H12-N+-(CH3)
bis((C2H50)-(C2H40))n, wherein n = from 20
to 30.
PEI : Polyethyleneimine with an average molecular
weight of
between 600-1800 and an average ethoxylation
degree
of 7-20 ethyleneoxy residues per nitrogen.
SCS : Sodium cumene sulphonate.
HMWPEO : High molecular weight polyethylene oxide.
PEG X : Polyethylene glycol, of a molecular weight
of X
PEO : Polyethylene oxide, with an average molecular
weight of
5,000.
TEPAE : Tetreaethylenepentaamine ethoxylate.
BTA : Benzotriazole.
PH : Measured as a 1 % solution in distilled water
at 20C.
Example 1
The following granular laundry detergent compositions were prepared according
to the present invention
I II III IV V
Spray-dried Granules
LAS 10.0 10.0 15.0 5.0 5.0
TAS - 1.0 - - -
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i ii iii iv v
M BAS - - - 5.0 5.0
C45AS - - 1.0 - 2.0
C45AE3S _ _ _ 1.0 -
QAS - - 1.0 1.0 -
DTPA, HEDP and/or EDDS 0.3 0.3 0.5 0.3 -
Mg Sulfate 0.5 0.5 0.1 -
Citrate - - - 3.0 5.0
Carbonate 10.0 7.0 15.0 - -
Sulphate 5.0 5.0 - - 5.0
Silicate - - - - 2.0
Zeolite A 16.0 18.0 20.0 20.0 -
SKS-6 - - - 3.0 5.0
MA/AA or AA 1.0 2.0 11.0 - -
PEG 4000 - 2.0 0.1 - 3.0-
QEA 1.0 - - - 1.0
Brightener 1 or 2 or 3 0.05 0.05 0.05 - 0.05
Silicone oil 0.01 0.01 0.01 - -
A~alomerate
Carbonate - - - - 4.0
SKS-6 6.0 - - - 6.0
LAS 4.0 5.0 - - 5.0
Dry-add particulate components
Malefic acid / carbonate / bicarbonate8.0 10.0 10.0 4.0 -
(40:20:40)
QEA - - - 0.2 0.5
NACA-OBS 3.0 - - 4.5 -
NOBS 1.0 3.0 3.0 - -
TAE D 2.5 - - 1.5 2.5
MBAS _ _ _ 8.0
LAS (flake) 10.0 10.0 - - -
Spray-on
Brightener 1 or 2 or 3 0.2 0.2 0.3 0.1 0.2
Perfume 1.0 0.5 1.1 0.8 0.3
Dry-add
Citrate - - 20.0 4.0 -
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I II III Iv v
Percarbonate 15.0 3.0 6.0 10.0 -
Perborate - - - - 6.0
Photoactivated bleach0.02 0.02 0.02 0.1 0.05
Enzymes (cellulase,amylase, 0.04 0.01 ~ 0.02 0.02 0.05
protease and/or
lipase) .
MaltoH 1.0 0.05 0.002 0.001 0.05
Carbonate 0.0 10.0 - - -
Perfume (encapsulated)- 0.5 0.5 - 0.3
Suds suppressor 1.0 0.6 0.3 - 0.10
Soap 0.5 0.2 0.3 3.0 0.5
Citric - - - 6.0 6.0
SKS-6 - - - 4.0 -
Fillers up to
100%
Example 2
The following granular laundry detergent compositions were prepared according
to the present invention
I II III IV
Blown aowder
MES 2.0 0.5 1.0 -
SADS - - - 2.0
LAS 6.0 5.0 11.0 6.0
TAS 2.0 - - 2.0
Zeolite A 24.0 - - 20.0
STPP 27.0 24.0 -
Sulfate 4.0 6.0 13.0 -
MA/AA 1.0 4.0 6.0 2.0
Silicate 1.0 7.0 3.0 3.0
CMC 1.0 1.0 0.5 0.6
Brightener 1 0.2 0.2 0.2 0.2
Silicone antifoam 1.0 1.0 1.0 0.3
DTPMP 0,4 0.4 0.2 0.4
Spray on
Brightener 1 or 0.02 - - 0.02
2 or 3
C45E7 - - 0.05 5.0
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I II III IV
C45E2 2.5 - -
C45E3 2.6 - 0.05
Pertume 0.5 0.3 0.5 0.2
Silicone antifoam . 0.3 0.3 0.3 _
Dry additives
QEA _ _ - 1.0
EDDS 0.3 - - -
Sulfate 2.0 3.0 5.0 10.0
Carbonate 6.0 13.0 15.0 14.0
Citric 2.5 - - 2.0
QAS 0.5 - - 0.5
SICS-6 10.0 - - -
Percarbonate 4.0 3.0 - 1.9
PB4 _ _ _
NOBS 0.5 - - -
TAED 0.75 4.5 - -
Clay - - 10.0 -
Protease 0.03 - 0.03 -
Lipase 0.008 0.008 0.008 0.004
MaItoH 0.001 0.01 0.01 0.004
Amylase 0.003 - 0.003 0.006
Brightener 1 0.05 - - 0.05
~
Misc/minor and speckles up to 100%
Example 3
The following granular prepared
laundry detergent compositions according
were
to the invention:
I II III IV V VI
Blown powder
LAS 23.0 8.0 7.0 9.0 7.0 7.0
QAS _ - - - 1.0 -
C45AS 6.0 6.0 5.0 8.0 - -
C45AE 11 S - 1.0 1.0 1.0 - -
MES 2.0 - - - 2.0 4.0
Zeolite A 10.0 18.0 14.0 12.0 10.010.0
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V
MA/AA - 0.5 - _ _ 2.0
MA/AA 1 7.0 - - - - -
AA - 3.0 3.0 2.0 3.0 3.0
Sulfate 5.0 6.3 11.1 11.0 11.0 18.1
Silicate 10.0 1.0 1.0 1.0 1.0 1.0
Carbonate 15.0 20.0 10.0 20.7 8.0 6.0
PEG 4000 0.4 1.5 1.5 1.0 1.0 1.0
DTPA - 0.9 0.5 - - 0.5
Brightener 0.3 0.2 0.3 - 0.1 0.3
2
S ray on
C45E7 - - 0.5 - - 2.0
C25E9 0.5 - - - - -
C23E9 - - 2.0 - 2.0
Perfume 0.3 0.3 0.3 2.0 0.3 0.3
Aa_glomerates
C45AS - 5.0 5.0 2.0 - 5.0
LAS - 2.0 2.0 - - 2.0
Zeolite A - 7.5 7.5 8.0 - 7.5
Carbonate - 4.0 4.0 5.0 - 4.0
PEG 4000 - - 0.5 - - 0.5
Misc (water - 2.0 2.0 2.0 - 2.0
etc)
Dry additives
QAS I - - - - 1.0 -
Citric - - - - 2.0 -
PB4 - _ _ _ 5 _
PB1 - - 4 1.0 -
Percarbonate 2.0 - - 1.0 - -
Carbonate - 5.3 1.8 - 4.0 4.0
NOBS 0.5 - 0.4 0.3 - -
Clay - - - - - 10.0
TAED 0.6 - 0.6 0.3 0.9 -
Methyl cellulose0.2 - - - - 0.5
DTPA 0.7 0.5 1.0 0.5 0.5 1.2
speckle - - - 0.2. 0.5
S KS-6 8.0 - - - - -
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I II III IV V VI
STS - - 2.0 - 1.0 -
Cumene sulfonic- 1.0 - - - 2.0
acid
Lipase 0.004 - 0.004 - 0.004 0.008
Cellulase 0.00050.0005 0.0005 0.0007 0.0005 0.0005
Amylase 0.003 - 0.001 - 0.003 -
MaItoH 0.01 5.0 0.05 0.002 0.001 0.05
AMG - - 0.001 0.001 - -
Protease 0.01 0.015 0.015 0.009 - -
PVPVI - - - - 0.5 0.1
PVP - - - - 0.5 -
PVNO - - 0.5 0.3 - -
QEA _ _ _ - 1.0 -
SRP1 0.2 0.5 0.3 - 0.2 -
Silicone antifoam0.2 0.4 0.2 0.4 0.1 -
Mg sulfate - - 0.2 - 0.2 -
Misc/minors
up to
100%
Example 4
The following granular laundry detergent compositions were prepared according
to the present invention:
1 II III IV
Base~ranule
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
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WO 02/02726 PCT/US00/18120
I II III IV
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 - -
Sara~r on
C25E9 - - - 0.5
C45E7 10 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 0.03 0.03 0.03 0.015
Lipase 0.008 - - 0.008
MaItoH 0.01 3.0 0.05 0.005
Amylase 0.002 - - 0.002
Cellulase 0.0002 0.0005 0.0005 0.0003
DTPA 0.5 0.3 0.5 1,0
LOBS - 0.8 - 0.3
PB 1 5 3.0 10 4.0
DOBA 1.0 - 0.4 -
TAED 0.5 0.3 0.5 0.6
Sulfate 4.0 5.0 - 5.0
SRP 1 - 0.4 - -
Suds supressor - 0.5 - . -
speckle 09 - 2.7 1.2
Misc/minor
to 100%
Exama~le 5
The following granular laundry detergent compositions were prepared according
to the present invention
I II 111 IV IV V VI
C13 LAS 3 16.0 23.0 19.0 18.0 20.0 16.0
C45 AS 4.5 - _ _ 4.0
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C45AE (3)S , - - 2.0 - 1.0 1.0 1.0
C45 AE (3.0) 12.0 2.0 - 1.3 - - 0.6
C9 C~4 alkyl dimethyl - - 1.0 0.5 2.0
hydroxy
ethyl quaternary ammonium
salt
Tallow fatty acid - - - - - - 1.0
STPP 23.0 25.0 24.0 22,020.0 15.0 20.0
Carbonate 15.0 12.0 15.0 10.013.0 11.0 10.0
AA 0.5 0.5 0.5 0.5 - - -
MA/AA - - 1.0 1.0 1.0 2.0 0.5
Silicate 3.0 6.0 9.0 8.0 ~9.0 6.0 8.0
Sulfate 25.0 18.0 20.0 18.020.0 22.0 13.0
Sodium perborate 5.0 5.0 10.0 8.0 3.0 1.0 2.0
PEG 4000 1.5 1.5 1.0 1.0 - - 0.5
CMC 1.0 1.0 1.0 - 0.5 0.5 0.5
Citric - - - - - - -
NOBS/ 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
SRP 2 1.5 1.5 1.0 1.0 1.0 1.0 1.0
Moisture 7.5 7.5 6.0 7.0 5.0 3.0 5.0
Mg - - - - 1.0 0.5 1.5
DTPA, HEDP and/or EDDS - - - - 0.8 0.6 1.0
MaItoH 0.01 0.01 .005 0.051.0 1.0 .001
Enzymes (amylase, cellulase- - - - 0.05 0.04 0.05
and/or protease)
Minors, e.g. perfume, Up to
100%
Brightener, photo-bleach,
speckles
Example 6
The following granular laundry detergent compositions were prepared according
to the present invention:
I II III IV
C 13 LAS 13.3 13.7 10 .4 8.0
C45 AS 3.9 4.0 4.5 -
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I II III IV
C45 AE (0.5)S ~ 2.0 2.0 ~ - -
C45 AE (6.5) 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
AA 3.4 0.0 2.7 -
MAIAA - - 1.0 1.5
Silicate 2.4 6.4 2.1 6.0
Sulfate 10.5 10.9 8.2 15.0
Sodium perborate 1.0 1.0 1.0 2.0
PEG 4000 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 2 1.5 1.5 1.0 1.0
Moisture 7.5 3.1 6.1 7.3
Mg sulphate - - - 1.0
DTPA, HEDP and/or EDDS - - - 0.5
Enzymes (amylase, cellulase,- 0.025 - 0.04
protease and/or lipase)
MaItoH 0.02 0.05 0.005 0.008
Misc l~ Minors including Up to 100%
perfume,
brightener, photo-bleach
Example 7
The following laundry detergent compositions in the form of a tablet or
granular
formulation were prepared according to the present invention
I II III IV V VI
C13 LAS 20.0 16.0 8.5 5 20.0 6.0
C45 AS - 4.0 - _ _
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i ii iii iv v vi
y C45 AE(3)S 1.0 1.0 - - - -
C45 AE - 5.0 5.5 4.0 - 0.5
C9 C,4 alkyl dimethyl hydroxy 0.5 2.0 - - - -
ethyl quaternary ammonium
salt
Tallow fatty acid - 1.0 - - - -
STPP / Zeolite 10.0 20.0 30.0 20.0 25.0 25.0
Carbonate 41.0 30.0 30.0 25.0 45.0 24.0
,~ _ _ _ _ _ _
MAIAA 2.0 0.5 0.5 1.0 - _
Silicate ~ 6.0 8.0 5.0 6.0 8.0 5.0
Sulfate 2.0 3.0 - - - 8.0
Sodium perborate/ . 1.0 - 20.0 14.0 - -
percarbonate
PEG 4000 - 0.5 - - - 0.5
CMC 0.5 0.5 0.5 0.5 - 0.5
Citric - - - - - -
NOBS/ DOBS 0.7 - - - - -
TAED / Preformed peracid 0.7 - - 5.0 4.5- -
DTPA, HEDP and/or EDDS - - 0.5 0.5 -
SRP 1.0 - 1.0 1.0 - -
Clay 4.0 3.0 7.0 10.0 6.0 8.0
PEO 1.0 0.5 2.0 0.5 1.0 0.5
Humectant 0.5 - - 0.5 - -
wax 0.5 - - 0.5 - -
Cellulose 2.0 - - 1.5 - 1.0
Sodium acetate - - 1.0 0.5 4.0 1.0
Moisture 3.0 5.0 5.0 5.0 8.0 10.0
Mg sulphate 0.5 1.5 - - - -
Soap/ suds suppressor 0.6 1.0 1.0 0.8 0.5 -
Enzymes (amylase, cellulase, 0.04 0.04 0.01 0.02 0.02 0.03
protease and/or lipase)
MaItoH 0.03 0.01 0.05 .003 0.1 .005
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I II III IV V VI
Minors, e.g. perfume, PVP, Up to 100%
PVPVI/PVNO, brightener,
photo-bleach, speckles,...
Example 8
The following laundry detergent compositions were prepared according to the
present invention
I II III IV V
C 13 LAS 5.0 16.0 23.0 19.0 18.0
C45 AS - 4.5 - - -
C45 AE(3)S - - 2.0 - 1.0
C45 AE 10 2.0 - 1.3 -
C9 C,4 alkyl dimethyl - - - - 1.0
hydroxy
ethyl quaternary ammonium
salt
STPP / Zeolite 23.0 25.0 14.0 22,0 20.0
Carbonate 25.0 22.0 35.0 20.0 28.0
AA 0.5 0.5 0.5 0.5 -
MA/AA ~ - - 1.0 1.0 1.0
Silicate 3.0 6.0 9.0 8.0 9.0
Sodium perborate/ 5.0 5.0 10.0 - 3.0
percarbonate
PEG 4000 1.5 1.5 1.0 1.0 -
CMC ~ 1.0 1.0 1.0 - 0.5
NOES/ DOBS - 1.0 - - 1.0
TAED / Preformed peracid1.5 1.0 2.5 - 3.0
DTPA, HEDP and/or EDDS 0.5 0.5 0.5 - 1.0
SRP 1.5 1.5 1.0 1.0 -
Clay 5.0 ~ 6.0 12.0 7.0 10.0
Flocculating agent PEO 0.2 0.2 3.0 2.0 0.1
Humectant - - - - 0.5
wax 0.5 - - - -
Gellulose 0.5 2.0 - - 3.0
Sodium acetate 2.0 1.0 3.0 - -
Moisture 7.5 7.5 6.0 7.0 5.0
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I II III IV V
Soap/ suds suppressor - , - 0.5 0.5 0.8
MaItoH 0.02 0.02 .005 .005 0.01
Enzymes (amylase, cellulase, - - - - 0.045
protease and/or lipase)
Misc / Minors, e.g. perfume, Up to 100%
PVP, PVPVI/PVNO, speckles,
brightener, photo-bleach,...
Example 9
The following liquid laundry detergent compositions were prepared according to
the present invention
I II III IV V VI
LAS _ _ - 7.0 2.0 -
C25AS 16.0 13.0 14.0 5.0 - 6.5
C25AE3S 5.0 1.0 - 10.0 19.0 3.0
C25E7 2.0 3.5 0.05-2.5 2.0
N12 0.5 1.0 0.03 2.0 - -
TFAA 5.0 4.5 4.5 6.5 4.0 -
APA 2.0 1.0 - 3.0 - 0,5
QAS - - 2.0 - 1.5 -
TPKFA 4.5 8.0 15.0 - 5.0 5.0
Citric 2.2 3.0 - 0.5 1.0 2.0
Rapeseed fatty acid2.0 - - 3.0 6.0 1.5
Ethanol 3.2 2.0 2.5 2.2 - 0.5
1,2 Propandiol 5.7 8.5 6.5 7.0 7.0 5.5
Monoethanolamine 5.0 7.5 - 5.0 1.0 2.0
TEPAE - 1.2 - 0.5 0.5 -
PE12 - 1.5 - 1.0 0.8 -
DTPMP 1.3 0.5 0.8 0.5 - 0.2
HEDP - 0.5 0.2 1.0 - -
Protease 0.02 - 0.02 0.02 0.02 0.01
MaItoH 0.01 0.02 0.0050.01 0.0050.002
AMG ~ 0.001 - - - - 0.001
Lipase 0.002 0.001 0.001- 0.001-
Amylase .0008 .0006 .00060.002 0.0010.001
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I II III Iv v vl
Cellulase 0.002 - 0.002 0.001-
0.002
SRP1 0.20 0.15 0.10 - 0.17 0.04
PVNO - - - 0.05 0.10 -
Brightener 3 0.20 0.15 0.10 0.05 - 0.05
Suds Suppressor 0.25 0.20 0.15 0.15 0.30 0.10
Calcium Chloride 0.02 0.02 - 0.01 0.01 -
Boric acid 2.5 2.0 1.5 2.2 1.5 1.2
Bentonite Clay - - 5.5 - -
NaOH to pH 8.0 7.5 7.7 8.0 7.0 7.5
Water/minors to 100%
Example 10
The following non-aqueousliquid compositions prepared
detergent were in
s accordance with the
present invention I II III
LAS 16.0 16.0 16.0
C23 E05S 21.5 21.5 19.0
Butoxy Propoxy Propanol 18.5 - 16.0
N12 0.05 1.0 2.0
Hexylene Glycol - 18.5 5.0
Sodium citrate dihydrate 6.8 6.8 3.8
[NACA-OBS] Na salt 6.0 6.0 6.0
Methyl sulfate salt of 1.3 1.3 1.3
methyl quaternized
polyethoxylated hexamethylene
diamine
EDDS ~ 1.2 1.2 1.2
MA/AA - - 3.0
Sodium Carbonate 10.0 10.0 10.0
Protease 0.05 - 0.02
MaItoH 1.0 0.01 0.02
Amylase 0.01 0.01 0.01
Cellulase 0.0001 0.0001 0.0001
PB 1 12.0 12.0 12.0
Silicone antifoam 0.75 0.75 1.1
Perfume 1.7 1.7 1.7
Titanium Dioxide 0.5 0.5 0.5
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I II III
Dichloro -5,12-Dimethyl-1,5,8,12- - 0.03 0.03
tetraazabicyclo [6.6.2] hexadecane
Manganese (II)
Brightener 2 0.2 0.2 0.2
Sodium hydrogenated C16-18 fatty soap 1 1 0.5
Coloured Speckles 0.4 0.4 0.4
Miscellaneous up to 100%
Example 11
The following laundry detergent compositions in the form of a tablet were
prepared according to the present invention
i) a detergent base powder of composition I was prepared as follows: ail the
particulate material of base composition I were mixed together in a mixing
drum to form a homogenous particulate mixture. During this mixing, the spray-
ons were carried out.
ii) Tablets were then made the following way: 50g of the matrix was introduced
into a mould of circular shape with a diameter of 5.5 cm, and compressed to
give a tablet tensile strength (or diametrical fracture stress) of lOkPa.
iii) The tablets were then dipped in a bath comprising 90 parts of sebacic
acid
and 10 parts per weight of Nymcel-ZSB16T"" by Metsa Serla at 140 °C.
The
time the tablet was dipped in the heated bath was adjusted to allow
application of 4g of the bath mixture. The tablet was then left to cool at
ambient temperature of 25°C for 24 hours. The tensile strength of the
coated
tablet was increased to a tensile strength of 30 kPa.
I
Anionic agglomerates 1 anionic, zeolite and 33% 21.5
(40% 27%
carbonate)
Anionic agglomerates 2 anionic, zeolite and 32% 13.0
(40% 28%
carbonate)
Cationic agglomerates cationic, zeolite and 24% 5.5
(20% 56%
sulphate)
Layered silicate (95% 10.8
SKS 6 and 5% silicate)
Sodium percarbonate 14.2
Bleach activator agglomerates(81 % TAED,17% acryliclmaleic5.5
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copolymer (acid form) and 2% water
Carbonate 10.98
EDDS/Sulphate particle (58% of EDDS, 23% of sulphate0.5
and 19%
water)
HEDP 0.8
SRP 0.3
Fluorescer 0.2
Photoactivated bleach (Zinc phthalocyanine sulphonate0.02
10% active)
Soap powder 1.4
Suds suppressor (11.5% silicone oil; 59% of zeolite 1.9
and 29.5% of
water)
Citric 7.1
MaItoH 0.05
Protease 0.03
Lipase 0.006
Cellulase 0.0005
Amylase 0.02
PEG4000 1.0
Binder spray-on system (25% of Lutensit K-HD 96;75% 4.0
by weight of
PEG)
Example 12
The following laundry detergent compositions in the form of a tablet were
prepared according to the present invention
I II III IV V VI
First Phase
Percarbonate - 45.0 45.0 45.0 45.0 45.0
TAED - 9.7 9.7 9.7 9.7 9.7
Citric acid 10.0 15.0 20.0 15.0 15.0 15.0
STPP - - - - - 6.0
MA/AA 6.0 6.0 1.0 5.0 - -
Silicates - - - - 6.0 -
Bicarbonate 15.0 15.0 10.0 15.0 15.0 15.0
N11 1.0 0.5 0.2 0.1 1.5 1.0
Carbonate 5.0 - - - - -
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Brightener 1 or 2 0.1 0.1 0.1 0.1 0.1 0.1
Perfume 0.2 0.2 0.2 0.2 0.2 0.2
C12-16 Fatty acid - - - 1.0 - -
Protease 0.03 0.03 0.03 0.03 0.03 0.03
Amylase 0.02 0.02 - 0.02 - -
Second phase
MaItoH 0.01 0.02 0.04 0.01 0.1 0.5
Protease 0.04 0.04 0.04 0.04 0.04 -
Amylase 0.02 0.02 - - - -
Speckles 0.09 0.09 0.09 0.09 0.09 0.09
PEG 4000 0.33 0.33 0.33 0.33 0.33 0.33
Citric 1.06 1.06 1.06 1.06 1.06 1.06
Bicarbonate 2.87 2.87 2.87 2.87 2.87 2.87
Example 13
The following laundry were ing
bar detergent compositions prepared to
accord the
present invention (Levels are arts
given per
in weight,
p 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 11.222.5
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 Carbonate 27.5 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
Bentonite clay - 10.0 - - 5.0 - - -
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
SR_P 1 0.3 0.3 0.3 0.3 0.3 0.3 0.3 0.3
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~~I V~ V I~I V~ V
Amylase - - 0.01 - - - 0.002 -
MaItoH 0.01 0.1 0.02 0.002 0.5 0.01 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 - - 3.0 3.0 3.0 - - -
N12 5.0 - 2.0 - - 0.2 0.1 -
Brightener 0.15 0.1 0.15 - - - - 0.1
Photoactivated- 15.0 15.0 15.0 15.0 - - 15.0
bleach (ppm)
Example 14
The following granular fabric detergent compositions which provide "softening
through the wash" capability were prepared according to the present invention
C45AS - 10.0
LAS 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
MAIAA 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
Protease 0.02 0.01
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I II
Lipase 0.02 0.01
MaItoH 0.05 0.02
Amylase Ø03 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 15
The following rinse added
fabric softener composition
was prepared according
to
s the present invention
DEQA (2) 20.0
Cellulase 0.001
MaItoH 0.005
C45E01-3 1.0
HCL 0.03
Antifoam agent 0.01
Blue dye 25ppm
CaCl2 0.20
Perfume 0.90
Miscellaneous and water Up to 100%
Example 16
The following fabric softener and dryer added fabricditioner compositions
con
o were prepared according
to the present invention
I II III IV V
DEQA 2.6 19.0 - - -
DEQA(2) - - - - 52.0
DTMAMS - - - 26.0 -
SDASA - - 70.0 42.0 40.2
Stearic acid of IV=0 0.3 - - - -
C45E01-3 1.0 0.5 13.0 0.5 0.2
HCL 0.02 0.02 - - -
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I II III IV V
Ethanol - - 1.0 - -
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 - - -
Amylase - 0.2 - 0.2 0.2
MaItoH 1.0 0.2 0.1 0.01 0.01
Clay _ - _ 3.0 -
pye 10ppm 25ppm 0.01 - -
Water and minors 100% 100% - - -
Example 17
The following compact high density (0.96Kg/I) dishwashing detergent
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 - - -
PB1 10.0 8.0 8.0 - - -
PB4 - - - 10.0 - -
Percarbonate- - - - 11.8 4.8
N11 2.0 - 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 - -
Protease 0.07 0.05 0:05 0.03 - 0.01
Amylase 0.01 0.01 0.006
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I II III IV V VI
AMG 0.001 - - - - 0.01
MaItoH 0.02 0.2 2.0 1..0 0.002 0.02
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, Up to 100%
sulfate and
water
Example 18
The followinggranular detergentcompositions bulk density
dishwashing of
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 - - -
NADCC - - - 2.0 - 0.9
NI 1 1.0 0.7 - 1.9 0.7 0.5
TAED - - 1.0 1.0 0.9 -
PAAC - 0.004 - - - -
ParafFin 0.25 0.25 - - - -
Protease 0.036 0.021 0.03 - 0.006 -
Amylase 0.03 0.005 - - 0.005 -
MaItoH 0.2 0.02 2.0 2.0 0.02 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 , sulfate Up to 100%
and water
Example 19
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The fiollowing 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
Protease 0.042 0.072 0.0420.031 0.052 0.023 0.023 0.029
Amylase 0.012 0.012 0.0120.007 0.015 0.003 0.017 0.002
MaItoH 0.02 0.01 0.0020.5 0.008 0.002 1.0 0.02
Lipase 0.005 - - - - - - -
PB1 14.3 7.8 11.7 12.2 - - 6.7 8.5
PB4 ~ - - - - 22.8 - 3.4 -
Percarbonate - - - - - 10.4 - -
Nl 1 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 4,000- - - - - - 2.0 - 2.0
30,000
Glycerol - - - - - 0.4 - 0.5
Perfume - - - 0.05 0.2 0.2 0.2 0.2
Weight of 20g 25g 20g 30g 18g 20g 25g 24g
tablet
pH 10.7 10.6 10.7 10.7 10.9 11.2 11.0 10.8
Miscellaneous, Up %
sulfate and to
water 100
Example 20
The following liquid dishwashing detergent compositions of density 1.40Kg/L
were prepared according to the present invention
I II III Iv
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I 11 111 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
NI 7 0.1 0.1 0.06 0.1
NaBz 0.7 - - -
MaItoH 0.005 1.0 0.005 0.02
NaOH 1.9 - - -
KOH 3.6 3.0 - -
Perfume 0.05 - - -
pH 11.7 10.9 10.8 11.0
Water up to 100%
Example 21
The following dishwashing compositions in the tablet form were prepared
according to the present invention (Levels are indicated in g):
I 11 III IV V VI
Phase 1
STPP 9.6 9.6 10.4 9.6 9.6 17.5
Silicate 0.5 0.7 1.6 1.0 1.0 2.4
SKS-6 1.5 1.50 2.30 2.25
Carbonate ~ 2.3 2.7 3.5 3.6 4.1 5.2
HEDP 0.2 0.2 0.2 0.3 0.3 0.3
PB1 2.4 2.4 2.4 3.7 3.7 3.7
PAAC 0.002 0.002 0.002 0.003 0.004 0.004
MaItoH 0.01 0.02 0.05 0.002 0.001 1.0
Amylase 0.002 0.001 0.001 0.004 0.003 0.003
Protease 0.002 - 0.002 0.003 0.003 0.003
N I 1 0.4 0.8 0.8 1.2 1.2 1.2
PEG 6000 0.4 0.3 0.3 - 0.4 -
BTA 0.04 0.04 0.04 - 0.06 0.06
Paraffin 0.1 0.1 0.1 0.15 0.15 0.15
Perfume 0.02 0.02 0.02 0.01 0.01 0.01
Sulphate - - - 0.5 0.05 2.3
so
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I II III IV V VI
Phase 2
MaItoH 0.003 0.003 0.002 0.01 0.01 0.01
Amylase 0.0005 0.0005 0.0004 0.0005 0.006 0.0004
Protease 0.009 0.008 0.01 0.009 0.008 0.01
Citric 0.3 0.3 0.3 0.30
Sulphamic acid- 0.3 - - 0.3 -
Bicarbonate 1.1 0.4 0.4 1.1 0.4 0.4
Carbonate - 0.5 - - 0.5 -
Silicate - - 0.6 - - 0.6
CaCh - 0.07 - - 0.07 -
PEG 3000 0.06 0.06 0.06 0.06 0.06 0.06
The multi-phase tablet compositions 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 the mould. The cross-
section
of the die is approximately 30x38 mm. The composition is then subjected to to
a
compression force of 940 kg/cm~ 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
1o the die. The particulate active composition is then subjected to a
compression
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
within 5 minutes. The tablets provide excellent dissolution and cleaning
1s characteristics together with good tablet integrity and strength.
Example 22
The following
manual dishwashing
compositions
were prepared
according to
the
present invention
I II III IV V VI VII VIII
C12-14E0-3S 26.0 34.2 25.0 26.0 37.0 26.0 22.0 32.0
C 11 LAS - - - - - - 13.0 -
C12-14 amine oxide2.0 4.9 2.1 - 5.5 6.5 1 -
C12-14 betaine 2.0 5.0 2.1 - - - - 4.0
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I II III IV V VI VII VIII
C12-14 glucose 1.5 1.5 3.1 - - - - -
amide
C9-11 E8-9 4.5 1 4.1 3.0 1.0 3.0 - 1.0
Alkyl Polyglucoside- - - - - - 12.0 3.0
C1-20 Mono Ethanol- - - - - - 1.5 -
Amine
DTPA - 0.1 0 0-500 0-5000-500 0 0
ppm ppm ppm
Succinic acid - - - - - 0 - 4.5
Cumene sulphonate - - 4.5 1 to - 1 to - -
6 6
Ca ou Na xylene - 5.0 - - 4.0 - 2.5 -
Sulphonate
Mg salts (in % 0.5 0.7 0.5 0.04 0.6 0.04 0.3 0
Mg)
1,3 bis (methylamino)- - - 0.5 - 0.5 - -
cyclohexane
N.N-dimethylamino - - - 0.2 - 0.2 - -
ethyl methacrylate
homopolymer
Citric - - - 0-3.5 0-3.5 - -
Ethanol 6-8 5-8 6-9 4-10 7.0 4-10 4.0 4.0
Protease - - - 0.08 - 0-0.08- -
MaItoH 0.05 .002 .005 0.01 0.4 0.05 0.0020.01
Amylase - - - 0.002 . 0.005 0.04 0.05
Carbonate - - - - - 2.5 - -
Poly Propylene - - - 0 to - - - -
Glycol 2
(MW2000-4000)
pH 7-8 7- 7-8 8.5-117-8 8.5-117 7
8
Perfume 0.1-0.7
Balance (water ors) Up
and min to
100%
Examale 23
The following fabric and hard surface cleaner composition waseprepared
according to the present invention
Sulphate 18.5
Bicarbonate 18.6
Polycarboxylate 4.1
s2
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C18 Alpha Olefin 0.2
Enzyme (lipase, protease and/or 0.004
cellulase)
Amylase 0.003
MaItoH 0.05
Brigthener 2 0.1
NI 1 1.0
Photoactivated bleach 0.04
Coated sodium percarbonate 45.0
TAED 8.8
Citric 2.5
Perfume 0.1
Miscellaneous and water up to 100%
83
