Note: Descriptions are shown in the official language in which they were submitted.
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LAUNDRY DETERGENT AND/OR FABRIC CARE COMPOSITIONS
COMPRISING A MODIFIED TRANSFERASE
Field of the Invention
The present invention relates to laundry detergent and/or fabric care
compositions comprising a modified enzyme which comprises a catalytically
active amino acid sequence of a transferase, linked to an amino acid sequence
comprising a Cellulose Binding Domain (CBD).
Background of the invention
Laundry detergent and/or fabric care compositions include nowadays a complex
combination of active ingredients which fulfill certain specific needs : a
surfactant
system, enzymes providing cleaning and fabric care benefits, bleaching agents,
a builder system, suds suppressors, soil-suspending agents, soil-release
agents,
optical brighteners, softening agents, dispersants, dye transfer inhibition
compounds, abrasives, bactericides, perfumes, and their overall performance
has indeed improved over the years.
However, the complex nature of everyday "body" soils typically found on pillow
cases, T-shirts, collars and socks, provides a continuous thorough cleaning
challenge for detergents. These soils are difficult to remove completely and
often residues build up on fabric leading to dinginess and yellowing. In
addition,
removal by detergents of stains stemming from plants, wood, mud-clay based
soil and fruits is one of the toughest cleaning challenges, in particular with
the
tendency to move to low wash temperatures and shorter washing cycles. These
stains typicaNy contain complex mixtures of fibrous material, based mainly on
carbohydrates and their derivatives, fibre and cell wall components. Such
stains
are generally accompanied by amylose, sugars and their derivatives.
In recent years, consumer desirability for fabric conditioning compositions
has
risen. Fabric softening compositions impart several desirable properties to
treated garments including softness and static control. Fabric softness of
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laundered garments is typically achieved by delivering a quaternary ammonium
compound to the surface of the fabric.
Consumer desirability for durable press fabric garments, particularly cotton
fabric
garments, has also risen. Durable press garments include those garments
which resist wrinkling of the fabric both during wear and during the
laundering
process. Durable press garments can greatly decrease the hand work
associated with laundering by eliminating ironing sometimes necessary to
prevent wrinkling of the garment. However, in most commercially available
durable press fabrics, the fabric's ability to resist wrinkling is reduced
over time
as the garment is repeatedly worn and laundered.
Furthermore, coloured garments have a tendency to wear and show appearance
losses. A portion of this colour loss may be attributed to abrasion in the
laundering process, particularly in automatic washing machines and automatic
laundry dryers.
Moreover, tensile strength loss of fabric appears as an unavoidable result of
mechanical / chemical action due to use / wearing or washing.
As indicated above, there is a continuous need for a laundry detergent
composition which provides fabric cleaning and/or fabric stain removal,
especially on body soils and plant based stains and/or fabric whiteness
maintenance and/or fabric colour appearance and/or dye transfer inhibition.
In addition, there is a continuous need for a laundry detergent composition
and/or fabric care composition, which can provide, refurbish or restore
tensile
strength, anti-wrinkle, anti-bobbling and anti-shrinkage properties to
fabrics, as
well as provide static control, fabric softness, colour appearance and fabric
anti-
wear properties and benefits.
The above objectives have been met by formulating laundry detergent and/or
fabric care compositions comprising modified enzyme which comprises a
catalytically active amino acid sequence of a transferase, linked to an amino
acid sequence comprising a Cellulose Binding Domain (CBD).
Transferase enzymes have been described in the art : A process for producing
saccharides of a definite chain length such as maltose and
maltooligosaccharides in an isolated and highly pure form using a saccharide
chain transferase such as cyclodextrin glycosyl transferase or a-amylase, has
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been disclosed in EP 560 982 for pharmaceutical use. US 5,516,689 describes
an enzyme composition comprising transglucosidase and/or pectinase and a
means of reducing the stickiness of honeydew contaminated cotton, to avoid
severe problems during the milling of cotton. Microbial transglutaminases,
their
production and their use in a variety of industrial purposes have been
described
in W096/06931. JP 7-107971 relates to a micro-organism belonging to the
genus Bacillus and having the capacity to produce an alkali resistant
cyclodextrin glucanotransferase for dishwashing applications wherein it
demonstrates decomposition and removal of food soils and the produced
cyclodextrin plays as a masking, desodorisation agent and it improves the
sudsing properties and the emulsification of the soiling. Dishwashing
detergent
compositions containing cyclodextrin glucanotransferase with cleaning benefits
and deodorising effect are described in JP 7-109488.
Enzymes linked to Cellulose Binding Domains are also described in the art
W091/10732 novel derivatives of cellulase enzymes combining a core region
derived from an endoglucanase producible by a strain of Bacillus spp., NICMB
40250 with a CBD derived from another celluiase enzyme or a combining a core
region derived from another cellulase enzyme with a CBD derived from said
endoglucanase, for improved binding properties. W094/07998 describes
cellulase variants of a ceilulase classified in family 45, comprising a CBD, a
Catalytically Active Domain (CAD) and a region linking the CBD to the CAD,
wherein one or more amino acid residues have been added, deleted or
substituted and/or another CBD is added at the opposite end of the CAD.
W095/16782 relates to the cloning and high level expression of novel truncated
cellulase proteins or derivatives thereof in Trichoderma longibrachiatum
comprising different core regions with several CBDs. W097/01629 describes
cellulolytic enzyme preparation wherein the mobility of the cellulase
component
may be reduced by adsorption to an insoluble or soluble carrier e.g. via the
existing or newly introduced CBD. W097/28243 describes a process for removal
or bleaching or soiling or stains from cellulosic fabrics wherein the fabric
is
contacted in aqueous medium with a modified enzyme which comprises a
catalytically active amino acid sequence of a non-cellulolytic enzyme selected
from amylases, proteases, lipases, pectinases and oxidoreductases, linked to
an
amino acid sequence comprising a cellulose binding domain and a detergent
composition comprising such modified enzyme and a surfactant.
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Nevertheless, none of these documents discloses laundry detergent and/or
fabric care compositions comprising a modified enzyme which comprises a
catalytically active amino acid sequence of a transferase linked to an amino
acid
sequence comprising a Cellulose Binding Domain.
Summaryr of the invention
The present invention relates to a modified enzyme which comprises a
catalytically active amino acid sequence of a transferase linked to an amino
acid
sequence comprising a Cellulose Binding Domain (CBD).
In a second embodiment, the present invention relates to a laundry detergent
and/or fabric care composition comprising such modified transferase enzyme,
for improved fabric care and cleaning benefits.
In a third embodiment, the present invention relates to a method comprising
the
step of contacting a fabric with the above laundry detergent and/or fabric
care
composition.
Detailed description of the invention
The present invention relates to a modified enzyme (Enzyme hybrid) which
comprises a catalytically active amino acid sequence of a transferase linked
to
an amino acid sequence comprising a Cellulose Binding Domain (CBD).
Transferase enzyme and substrates
Transferase enzymes catalyse the transfer of functional compounds to a range
of substrates. Particularly, the transferase of the invention have the
potential to
transfer a chemical moiety, for example a methyl group or a gfycosyl group,
from
a small substrate to form oligomeric molecules or elongate polymeric
compounds. Using small substrates, the enzyme improves the properties of
garments by binding functional groups like methyl, hydroxymethyl, formyl,
carboxyl, aldehyde, ketone, acyl, amino and phasphorous functional groups
and/or transferring glycosyl residues to the garment surface. The improved
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garments properties include tensile strength, anti-wrinkle, anti-bobbling and
anti-
shrinkage properties to fabrics, static control, fabric softness, colour
appearance
and fabric anti-wear properties and benefits. When the transferase level is
high
and the substrate concentration is low, the functional groups are transferred
to
water molecules providing cleaning benefits.
Without wishing to be bound by theory, it is believed that the addition of a
cellulose binding domain to a transferase enzyme, allows a higher
concentration
of the transferase onto the fabric, i.e. a closer and/or more lasting contact,
resulting in a more efficient enzymatic activity. Such modified transferases
have
an increased affinity (relative to unmodified enzyme) for binding to a
cellulosic
fabric or textile. It has been surprisingly found that said transferases when
linked
to a CBD provide improved excellent fabric cleaning andlor fabric stain
removal,
especially on body soils and plant based stains and/or fabric whiteness
maintenance and/or fabric colour appearance and/or dye transfer inhibition. In
addition, such modified enzymes provide enhanced fabric care, i.e. they
provide,
refurbish or restore tensile strength, anti-wrinkle, anti-bobbling and anti-
shrinkage properties to fabrics, as well as provide enhanced static control,
fabric
softness, colour appearance and fabric anti-wear properties and benefits.
Suitable transferases for the present invention are represented by the EC 2.1
Transferring one-carbon groups enzymes, EC 2.2 Transferring aldehyde or
ketone residues enzymes, EC 2.3 Acyltransferases, EC 2.4
Glycosyltransferases, EC 2.5 Transferring alkyl or aryl groups other than
methyl
groups enzymes, EC 2.6 Transferring nitrogenous groups enzymes and EC 2.7
Transferring phosphorus-containing groups enzymes.
Examples of suitable transferases are
EC 2.1.1.15 Fatty acid O-methyltransferase
EC 2.1.1.18 Polysaccharide O-methyltransferase
EC 2.1.2.1 Glycine hydroxymethyltransferase
EC 2.1.2.4 Glycine formiminotransferase
EC 2.2.1.3 Formaldehyde transketolase
EC 2.3.1.3 Glucosamine N-acetyltransferase
EC 2.3.1.18 Galactoside acetyl transferase
EC 2.3.1.57 Diamine N-acetyltransferase
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EC 2.3.1.75 Long-chain-alcohol O-fatty-acyltransferase
EC 2.3.1.79 Maltose O-acetyltransferase
EC 2.3.1.84 Alcohol O-fatty acetyltransferase
EC 2.3.1.88 Peptide a-N-acetyltransferase
EC 2.3.1.96 Glycoprotein N-palmitoyltransferase
EC 2.3.1.142 Glycoprotein O-fatty-acyltransferase
EC 2.5.1.10 Geranyltranstransferase
EC 2.5.1.20 Rubber cis-polypremyicistransferase
EC 2.6.1 Aminotransferase
For specific applications, preferred transferases demonstrate some / most of
their activity in the alkaline conditions, 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
transferases are enzymes having their maximum activity at a pH ranging from 7
to 12, preferably 10.5. Other preferred transferase is a transferase having at
least 50% of its maximum activity between 10°C and 50°C.
Preferred transferases for the laundry detergent and/or fabric care
compositions
of the present invention are included in the acyltransferases (EC 2.3) and
glycosyltransferases ( EC 2.4) classes.
Of particular interest is the group of acyltransferases, especially the
aminoacyl
transferases (EC 2.3.2). These are enzymes transferring amino groups from a
donor, generally an amino acid, to an acceptor. Even more preferred is the
protein-glutamine y-glutamyltransferase (EC 2.3.2.13), also available under
the
name transglutaminase. Without wishing to be bound by theory, it is believed
that enzymatic crosslinking of amino acids, diltri/poly-peptides and/or
proteins
will occur on the fabric, resulting in increased tensile strength and improved
appearance. Moreover, hydrolysis by an aminoacyl transferase of said
substrates present in the soils/stains, will provide cleaning benefits.
Of particular interest is also the group of glycosyltransferases. The general
properties of these enzymes is to transfer a sugar from oligosaccharides to
another carbohydrate as acceptor. Both hexosyltransferases and
pentosyltransferases can be used in the invention. Glycosyltransferases
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catalyse both hydrolytic and transfer reactions in incubation with
oligosaccharides. As a result of the enzymatic activity, oligosaccharides are
converted into a new class of polysaccharides. It has been surprisingly found
that glycosyltransferases linked to a cellulose binding domain improve the
tensile strength and appearance of fabrics, e.g. reduce fabric wrinkles.
Without
wishing to be limited by any theory, it is indeed believed that due to the
glycosyltransferase activity, oligosaccharides are bound to the cellulose
polymers of cotton fabrics resulting in improved tensile strength and
demonstrating appearance benefits especially after multiple wash cycles.
Without wishing to be bound by theory, the glycosyttransferase activity is
believed to have 3 potential modes of action providing fabric care benefits
- Enzymatic stitching wherein the enzyme is thought to bind oligosaccharides
to
cellulose fibers with reduced tensile strength;
- Enzymatic cross-linking wherein the glycosyltransferase is thought to bind
cellulose fibers with reduced tensile strength together; and
- Enzymatic polymer linking wherein polymers are linked to cellulose fibers
with
reduced tensile strength;
In addition, in presence of a low level of substrate and a high level of
glycosyltransferase, the glycosyl groups are transferred to water molecules
thereby providing cleaning benefits.
For example, transglucosidase is an enzyme that catalyses both hydrolytic and
transfer reactions in solutions containing a-D- gluco-oligosaccharides. As a
result of the transglucosidase enzymatic reactions, the malto-oligosaccharides
are converted to isomalto-oligosaccharides providing a new class of
polysaccharides characterised by a higher proportion of saccharides linked by
a-
D-1,6 linkages from the non-reducing end.
These transglucosidases have been found to provide fabric care performance. It
is believed that the improved tensile strength, the reduced wrinkling and
better
appearance are due to oligosaccharides bound to the cellulose polymers fibers
of cotton.
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Examples suitable glycosyltransferases are galactosyl transferases
of and
fructosyltransferases,
such as
1,4-(3-galactosyltransferase;
1,3-a-
fructosyltransferase;
2,3-sialyl
transferase;
cyclodextrin
glycosyltransferase;
N-
acetylgluco-
or -galactosaminyltransferase;
and
EC 2.4.1.2 1,4-a-D-glucan:l,6-a-D-glucan 6-a-D-glucosyltransferase
EC 2.4.1.4 Sucrose:1,4-a-D-glucan 4-a-D-glucosyltransferase
EC 2.4.1.5 Sucrose:1,6-a-D-glucan 6-a-D-glucosyltransferase
EC 2.4.1.9 Sucrose:2,1-(i-D-fructan 1-~i-D-fructosyltransferase
EC 2.4.1.10Sucrose:2,6-~i-D-fructan 6-~-D-fructosyltransferase
EC 2.4.1.11UDP glucose:glycogen 4-a-D-glucosyltransferase
EC 2.4.1.12UDPglucose : 1,4-~-D-glucan 4-~i-D-glucosyl transferase
EC 2.4.1.13UDPgIucose:D-fructose 2-a-D-glucosyltransferase
EC 2.4.1.16UDP-N-acetylglucosamine : chitin 4-~i-N-acetylglucosaminyl
transferase
EC 2.4.1.181,4-a-D-glucan:l,4-a,-D-glucan 6-a-D-(1,4-a-D-glucano)-
transferase
EC 2.4.1.191,4-a-D-glucan 4-a-D-(1,4-a-D-glucano)-transferase
(cyclizing)
EC 2.4.1.21ADPglucose:1,4-a-D-glucan 4-a-Dglucosyltransferase
EC 2.4.1.241,4-a-D-glucan : 1,4-a-D-glucan(D-glucose) 6-a-D-
glucosyltransferase
EC 2.4.1.251,4-a-D-glucan : 1,4-a-D-glucan 4-a-D-glycosyl
transferase
EC 2.4.1.29GDPglucose:1,4-~3-D-glucan 4-~3-D-glucosyl transferase
EC 2.4.1.341,3-~i-glucan synthetase
EC 2.4.1.35UDPglucose:phenol (i-D-glucosyltransferase
EC 2.4.1.491,4-(i-D-oligo-D-glucan:orthophosphate a-d-
glucosyltransferase
EC 2.4.1.671-a-D-galactosyl-myo-inositol:raffinosegalactosyl
transferase
EC 2.4.1.71UPDglucose:arylamine N-D-glucosyltransferase
EC 2.4.1.75UDPgalacturonate (3-D-galacturonosyl transferase
EC 2.4.1.821-a-D-galactosyl-myo-inositolaucrose 6-a-D-
galactosyltransferase
EC 2.4.1.90UDPgalactose:N-acetyl-D-glucosamine 4-~i-
galactosyltransferase
EC 2.4.1.93Inulin D-fructosyl-D-fructosyltransferase
EC 2.4.1.99Sucrose : 1 F-fructosyltransferase
EC 2.4.1.1001,2-~i-D-fructan : 1,2-(3-D-fructan 1-~i-D-fructosyltransferase
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EC 2.4.1.113ADPglucose:protein 4-a-D-glucosyltransferase
EC 2.4.1.721UDPglucose:indole-3-acetate (3-D-glucosyltransferase
EC 2.4.1.125Sucrose : 1,6-a-D-glucan 3(6)-a-D-glucosyl
transferase
EC 2.4.1.140Sucrose : 1,6(1,3}-a-D-glucan 6(3)-a-D-glucosyl
transferase
EC 2.4.1.1611,4-a-D-glucan:1,4-a-D-glucan 4-a-D-glucosyltransferase
EC 2.4.1.168UDPglucose : xyloglucan 1,4-~i-D-glucosyl
transferase
EC 2.4.1.169UDP-D-xylose : xyloglucan 1,6-(3-D-xylosyl
transferase
EC 2.4.1.183UDPglucose:a-D-(1,3)-glucan 3-a-D-glucosyltransferase
Of particular interest is EC 2.4.1.24 1,4-a-D-glucan : 1,4-a-D-glucan(D-
glucose) 6-a-D-glucosyl transferase. A particulate member of this enzyme is
commercially available under the name Transglucosidase L-500.
In addition to the glycosyltransferases discussed above, it has been found
that
mutant glycosyltransferases and/or mutant glycosidases, examples of which are
described in PCT Application Publication No. WO 97/21822, its Canadian
equivalent Canadian Patent No. 2,165,041, and its U.S. equivalent U.S. Patent
No. 5,716,812, all to S.G. Withers et al., improve the tensile strength and
appearance of fabrics, e.g., reduce fabric wrinkles, enhance shape retention
and reduce shrinkage. The mutant forms of glycosyl-transferases and/or
glycosidases provide enzymatic stitching, enzymatic cross-linking and
enzymatic polymer linking, as discussed above in greater detail.
The mutant glycosyltransferases and/or mutant glycosidases only have one
nucleophilic amino acid on the active site of the enzyme, rather than two,
like
non-mutated glycosyltransferases and/or non-mutated glycosidases,
respectively. In other words, the mutant glycosyltransferases and/or mutant
glycosidases are formed in which one of the normal nucleophilic amino acids
within the active site has been changed to a non-nucieophilic amino acid. As a
result, the mutant glycosyltransferases and/or mutant glycosidases only
exhibit
transferase activity; no hydrolytic activity is exhibited by the mutant
glycosyitransferases nor the mutant glycosidases. Accordingly, unlike non-
mutated glycosyltransferases and/or non-mutated glycosidases, the mutant
glycosyltransferases and/or mutant glycosidases convert oligosaccharides into
a new class of polysaccharides without the detrimental hydrolyzation of the
new
class of polysaccharides back into oligosaccharides or without water acting as
acceptor for the transfer reaction.
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These mutant glycosyltransferases and/or mutant glycosidases can be
extracted from plant, yeast, bacteria or other organisms. The DNA of the
mutant glycosyltransferases andlor mutant glycosidases can be cloned and
expressed in bacteria, yeast or fungi and obtained in this way.
These mutant glycosyltransferases and/or mutant glycosidases can be
incorporated into heavy duty liquid detergents, heavy duty granular
detergents,
fabric care compositions, and the like.
The novel characteristics and properties of the mutated glycosyltransferases
and/or the mutated glycosidases make them highly suitable for use in laundry
detergent and fabric care compositions because the absence of hydrolytic
activity implies no loss in tensile strength of fabrics, even in the absence
of
donors in the transferase reaction.
When mutant glycosyltransferases and/or mutant giycosidases are present in
the compositions of the present invention, it is desirable that the saccharide
concentration in the compositions is in the range of from about 0.01 % to 30%
by
weight of the total composition, more preferably, 1 % to 10% by weight of the
total composition. Furthermore, the compositions of the present invention can
have saccharides of high molecular weight added to the compositions to obtain
the benefits discussed above.
Another enzyme that is of particular interest is endoxyloglucan transferase
("EXT"), which is described in J. Plant Res. 108, 137-148, 1995 by Nishitani,
Kagoma University, and now called "EXGT" in Int. Review of Cytology, Vol. 173,
p. 157, 1997 by Nishitani, Kagoma University and the xyloglucan
endotransglycosylase ("XET") which is described in Novo Nordisk patent
application W097/23683.
Like the mutant glycosyltransferases discussed above, this endoxylo-glucan
transferase improves the tensile strength and appearance of fabrics, e.g.,
reduce fabric wrinkles, enhance shape retention and reduce shrinkage. The
endoxyloglucan transferase stitch cellulose fibrils. These stitching
properties of
the enzyme on cellulose fibrils delivers the above mentioned benefits.
Endoxyloglucan transferase is responsible for rejoining intermicrofibrillar
xyloglucan chains, the xyloglucan chains between cellulosic microfibrils
during
the formation of plant cell walls. By rejoining the cellulosic microfibrils
through
xyloglucan linkages, the cellulose structure acquires improved strength of the
fibers. Since the structure of fabrics is of cellulosic nature, the enzyme has
a
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stitching activity on the microfibrils. Also shape retention, anti-shrinkage
and
anti-wrinkle benefits can be explained by the stitching properties of the
enzyme.
Endoxyloglucan transferase differs in activity from xyloglucan
endotransglycosylase ("XET transferase"), which is described in WO 97/23683
to Novo Nordisk A/S. The difference being that the xyloglucan endotrans-
glycosylase shows both transferase activity and hydrolase activity. In
contrast,
endoxyloglucan transferase only shows transferase activity. No hydrolase
activity is shown by endoxyloglucan transferase. Accordingly, unlike
xyloglucan
endotransglycosylase, the endoxyloglucan transferase converts
oligosaccharides into a new class of polysaccharides without the detrimental
hydrolyzation of the new class of polysaccharides back into oligosaccharides.
Furthermore, the endoxyloglucan transferase exhibits strict donor specificity
for
high Mr (molecular weight) xyloglucan polymers and does not act on xyloglucan
oligomers.
The novel characteristics and properties of endoxyloglucan transferase make it
highly suitable for use in laundry detergent and fabric care compositions
because the absence of hydrolytic activity implies no loss in tensile strength
of
fabrics, even in the absence of donors in the transferase reaction.
Furthermore,
lower levels of substrate donor can be used. Without desiring to be limited,
it is
believed that high benefits can be obtained even in the absence of a donor
substrate if the endoxyloglucan transferase uses xylogiucans of the primary
wall
of the cotton fiber within fabrics.
Endoxyloglucan transferase can be extracted from plants and other organisms.
Endoxyloglucan transferase can be obtained from a large number of plants
including, but not limited to, A. thaliana and V. angularis. Alternatively,
the
DNA of the enzyme can be cloned and expressed in bacteria, yeast or fungi and
obtained in this way.
The endoxyloglucan transferase can be incorporated into heavy duty liquid
detergents, heavy duty granular detergents, fabric care compositions, and the
like.
When endoxyloglucan transferase is present in the compositions of the present
invention, it is desirable that the xyloglucan concentration in the
compositions is
in the range of from about 0.01 % to 30% by weight of the total composition,
more preferably, 1 % to 10% by weight of the total composition. Furthermore,
the compositions of the present invention can have xylogiucan polymers of high
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molecular weight added to the compositions to obtain the benefits discussed
above.
Yet another enzyme that is of particular interest is cyclomaltodextrin
glucanotransferase ("CGT-ase") (EC 2.4.1.19), which is commercially available
from Amano and Novo Nordisk A/S.
Covalent linking of carbohydrates, oligo and polysaccharides to cotton
surfaces,
such as fabrics, with a transferase delivers benefits such as anti-wrinkling,
color
maintenance, dye fixation an,d soil repulsion. Covalent linkage of glucose
units
to the cellulose surface versus a physical absorption of polymers, which are
produced by the transferase in situ (or others), make the observed benefits
durable.
Cyclomaltodextrin glucanotransferase is a transferase that exhibits several
different actions on starch. It produces from starch a, (i, and Y
cyclodextrins,
hydrolyzes starch and cross links starch. In these types of reactions, a
sugars
are both donor and acceptor for the transferase reaction. Up to now, it was
not
clear if these transferase enzymes could covalently link sugar units to
cotton.
Surprisingly, it has been found that cyclomaltodextrin glucanotransferase can
covalently link glucose units from a-cyclodextrine to the cotton surfaces of
fabrics at the non-reducing end of the cellulose polymers. Accordingly,
cyclomaltodextrin glucanotransferase has the ability to make the benefits
discussed above more durable.
As discussed above, it is known that covalently linking cellulose polymers
with
cross-linking agents delivers benefits to fabrics, such as anti-wrinkle
benefits,
but anti-wrinkle benefits can also be obtained by a physical absorption of
polymers on the cotton surface. This physical absorption of polymers on the
cotton surface can now be made more durable since one of the polymer units is
covalently linked to the cotton surface by the action of cyclomaltodextrin
glucanotransferase. Since these more durable benefits are produced
enzymatically, the covalent linking occurs at a much lower temperature, thus,
much lower temperatures as compared to conventional wash cycles are feasible
in the wash cycle. In addition, conventional cross-linking chemicals (some of
them are potentially toxic), which are used in the textile industry, are not
applicable at the lower temperatures in the wash cycle.
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Other benefits, such as dye fixation and improved soil release, are obtained
through the covalent incorporation of cationic or anionic glucose units to the
cotton surface.
Accordingly, the use of cyclomaltodextrin glucanotransferase in laundry
detergent and fabric care compositions provides improved anti-wrinkle, shape
retention, anti-shrinkage, dye fixation, soil repulsion and tensile strength
benefits for fabrics.
The cyclomaltodextrin glucanotransferase can be incorporated into heavy duty
liquid detergents, heavy duty granular detergents, fabric care compositions,
and
the like.
When cyclomaltodextrin glucanotransferase is present in the compositions of
the present invention, it is desirable that the starch concentration in the
compositions is in the range of from about 0.01 % to 30% by weight of the
total
composition, more preferably, 1 % to 10% by weight of the total composition.
Furthermore, the compositions of the present invention can have cyclodextrins
or types of starch and sucrose added to the compositions to obtain the
benefits
discussed above.
Yet still another group of enzymes that is of particular interest are
glucansucrases, of which dextransucrase (EC 2.4.1.5) and
glycosyltransferases, are examples. Other glucansucrases that are suitable for
use in the compositions described herein include, but are not limited to,
various
dextransucrases, alternansucrase and levansucrase, which is commercially
available from Genencor.
Dextransucrase enzymes can be obtained from any suitable source known in
the art, and are used in conjunction with appropriate substrates (sucrose +/-
maltose). Dextransucrase catalyzes transfer reactions of glycosyl residues
from
one polysaccharide to another. As a result of dextransucrase reactions, high
molecular weight dextrans are produce on fabric surfaces. In dextrans, glucose
residues are linked by 1-6-a linkages. Modification of cotton fiber with
carbohydrates, oligo and polysaccharides, delivers benefits such as anti-
wrinkling, color maintenance, dye fixation and soil repulsion. The durability
of
these benefits may require covalent linkage of the oligosaccharides.
It has been found that dextransucrase can bind oligosaccharides to cellulose
polymers in cotton. As a result of this binding via the transfer reactions
catalyzed by the dextransucrase, improved fabric appearance benefits are
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provided i.e., improved anti-wrinkling, shape retention, anti-shrinkage, dye
fixation, soil repulsion and tensile strength benefits. When the reaction
products
are bound (may or may not be a covalent linkage) to cotton, they modify the
cotton surface and fibrils, which in turn delivers the fabric care benefits
discussed above. Dextransucrase with sucrose also provides improved
whiteness benefits (dyes from other color garments are not deposited on white
fabrics). The dextransucrase/sucrose combination forms high molecular weight
dextran {and smaller oligomers when other saccharides such as maltose,
cellobiose, etc., are present).
Furthermore, it has been found that the deposition efficiency of reaction
products on the fabrics is high, and that the reaction products are not all
washed
off in the following wash cycle.
When glucansucrase is present in the compositions of the present invention, it
is
desirable that the substrate (typically sucrose or other disaccharides)
concentration in the compositions is in the range of from about 0.01 % to 30%
by
weight of the total composition, more preferably, 1 % to 10% by weight of the
total composition. Furthermore, the compositions of the present invention can
have smaller polysaccharides such as sucrose, maltose, maltdextrins,
cellosaccharides, and types of starch added to the compositions to obtain the
benefits discussed above.
These modified transferase enzymes are preferably incorporated into the
laundry detergent and/or fabric care compositians in accordance with the
invention at a level of from 0.0001 % to 10%, more preferably from 0.0005% to
5
%, most preferred from 0.001 % to 1 % pure modified enzyme by weight of the
total composition.
The fabric care and/or cleaning benefits can be obtained by the laundry and/or
fabric care compositions of the present invention in presence or absence of
the
corresponding natural enzymatic substrate. In general, the first part of the
enzyme name indicates the substrate for the enzyme reaction and the second
part is the acceptor to which the group is transferred. The substrate of the
transferase enzyme can be the fabric fibre itself, stains and/or soils, added
in
any treatment including pre- or post-treatment from the textile industry
and/or
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from any washing and/or fabric care process, and/or added together with the
transferase-containing composition.
Examples of substrates for some of the transferases listed above are : S-
adenosyl-L-methionine, 5,10-methylenetetrahydrofolate or formiminotetra-
hydrofolate (hydroxymethyl or formyl group transfer to glycine), formaldehyde,
acetyl Co A, methyl-a,w-diamine, palmityl Co A, geranoyl di phosphate.
In particular, the substrate for the aminoacyl transferases is an amino
containing
compound such as an amino acid, a di/tri/polypeptide and/or a protein.
Among the glycosyltransferases, though the transferring group is a glycosyl
residue, the specifics of the substrate for each enzyme is derived from the
first
part of the name. Especially for the glycosyltransferases, the natural
substrate
could be any alpha-glucosyl saccharide chosen from amylaceous substances in
a dimer, otigomer and/or polymer. Examples are preferably different forms of
starch (gelatinized, liquefied, solubilized), partial starch hydrolysate, more
preferably malto-oligosaccharides, and most preferably maltose. Of interest
are
also substituted starch/sugar substrates, containing methylation and
carboxylation substitution. Alternatively, the following substrates could be
used
for the mentioned glycosyltransferases: dextrins, sucrose, raffinose,
fructosyl
polymers, UDP glucose, xyloglucan, GDP glucose, arylamine, UDP
galacturonate, ADP glucose, indole-3-acetate, a-D-glucans, UDP-xylan.
The transferase-substrates are preferably incorporated into the compositions
in
accordance with the invention at a level of from 0.01 % to 30%, more
preferably
from 0.1 % to 20%, most preferably from 1 % to 10% by weight of the total
composition.
The above-mentioned enzymes may be of any suitable origin, such as
vegetable, animal, bacterial, fungal and yeast origin. Origin can further be
mesophilic or extremophilic (psychrophilic, psychrotrophic, thermophilic,
barophilic, alkalophilic, acidophilic, halophific, 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 efficiency in the cleaning compositions of the invention.
For
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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 and/or chelant stability, catalytic activity and the like, of the
enzyme
variant is tailored to suit the particular fabric conditioning and/or cleaning
application.
In particular, attention should be focused on amino acids sensitive to
oxidation in
the case of bleach stability and on surface charges for the surfactant
compatibility. The isoelectric point of such enzymes may be modified by the
substitution of some charged amino acids, e.g. an increase in isoelectric
point
may help to improve compatibility with anionic surfactants. The stability of
the
enzymes may be further enhanced by the creation of e.g. additional salt
bridges
and enforcing calcium binding sites to increase chelant stability.
The catalytically active amino acid sequence of the transferase enzyme may
comprise or consist of the whole of - or substantially the whole of - the full
amino
acid sequence of the mature enzyme in question, or it may consist of a portion
of the full sequence which retains substantially the same catalytic
(enzymatic)
properties as the full sequence.
Modified enzymes (enzyme hybrids) of the type in question, as well as detailed
descriptions of the preparation and purification thereof, are known in the art
[see, e.g., W090/00609, W094/24158 and W095/16782, as well as Greenwood
et al., Biotechnology and Bioengineering 44 (1994) pp. 1295 - 1305]. The
production of enzymes hybrid is given in W091/10732 wherein novel derivatives
of cellulase enzymes combining a core region derived from a Bacillus NICB
40250 endoglucanase with a CBD derived from another cellulase enzyme or
combining a core region derived from another cellulase enzyme with a CBD
derived from a Bacillus NICE 40250 endoglucanase, are constructed.
W095/16782 describes the combinations of different core regions with several
CBD and the cloning and high level expression of these novel truncated
cellulase proteins or derivatives thereof, in Trichodenna longibrachiatum.
They may, e.g., be prepared by transforming into a host cell a DNA construct
comprising at least a fragment of DNA encoding the cellulose-binding domain
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ligated, with or without a linker, to a DNA sequence encoding the enzyme of
interest, and growing the transformed host cell to express the fused gene. One
relevant, but non-limiting, type of recombinant product (enzyme hybrid)
obtainable in this matter - often referred to in the art as a "fusion protein"
- may
be described by one of the following general formulae:
A-CBD-MR-X-B
A-X-MR-CBD-B
In the latter formulae, CBD is an amino acid sequence comprising at least the
cellulose-binding domain (CBD) per se.
MR (the middle region; a linking region) may be a bond, or a linking group
comprising from 1 to about 100 amino acid residues, in particular of from 2 to
40
amino acid residues, e.g. from 2 to 15 amino acid residues. MR may, in
principle, alternatively be a non-amino-acid linker (See below).
X is an amino acid sequence comprising the above-mentioned, catalytically
(enzymatically) active sequence of amino acid residues of a polypeptide
encoded by a DNA sequence encoding the transferase enzyme of interest.
The moieties A and B are independently optional. When present, a moiety A or
B constitutes a terminal extension of a CBD or X moiety, and normally
comprises one or more amino acid residues.
It will thus, inter alia, be apparent from the above that a CBD in an enzyme
hybrid of the type in question may be positioned C-terminally, N-terminally or
internally in the enzyme hybrid. Correspondingly, an X moiety in an enzyme
hybrid of the type in question may be positioned N-terminally, C-terminally,
or
internally in the enzyme hybrid.
Enzyme hybrids of interest in the context of the invention include enzyme
hybrids which comprise more than one CBD, e.g. such that two or more CBDs
are linked directly to each other, or are separated from one another by means
of
spacer or linker sequences (consisting typically of a sequence of amino acid
residues of appropriate length). Two CBDs in an enzyme hybrid of the type in
question may, for example, also be separated from one another by means of an
-MR-X- moiety as defined above. One or more cellulose binding domain can be
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linked to the N-terminal and/or C-terminal parts of the cellulase core region.
Any
part of a CBD can be selected, modified, truncated etc.
Preferably, attention will be paid in the construction of enzyme hybrids of
the
type in question to the stability towards proteolytic degradation. Two- and
multi-
domain proteins are particularly susceptible towards proteolytic cleavage of
linker regions connecting the domains. Proteases causing such cleavage may,
for example, be subtilisins, which are known to often exhibit broad substrate
specificities [see, e.g. : Gram et al., Biochemistry 31 (1992), pp. 6011-6018;
Teplyakov et al., Protein Engineering 5 (1992), pp. 413-4.20]. Glycosylation
of
linker residues in eukaryotes is one Nature's ways of preventing proteolytic
degradation. Another is to employ amino acids which are less favoured by the
surrounding proteases. The length of the linker also plays a role in relation
to
accessibility by proteases. Which "solution" is optimal depends on the
environment in which the enzyme hybrid is to function. When constructing new
enzyme hybrid molecules, preferably attention will be paid to the linker
stability.
Plasmids
Preparation of plasmids capable of expressing fusion proteins having the amino
acid sequences derived from fragments of more than one polypeptide is well
known in the art (see, for example, WO 90/00609 and WO 95/16782). The
expression cassette may be included within a replication system for episomal
maintenance in an appropriate cellular host or may be provided without a
replication system, where it may become integrated into the host genome. The
DNA may be introduced into the host in accordance with known techniques such
as transformation, microinjection or the like.
Once the fused gene has been introduced into the appropriate host, the host
may be grown to express the fused gene. Normally it is desirable additionally
to
add a signal sequence which provides for secretion of the fused gene. Typical
examples of useful genes are:
1) Signal sequence -- (pro-peptide) -- carbohydrate-binding domain -- linker --
enzyme sequence of interest, or
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2) Signal sequence -- (pro-peptide) -- enzyme sequence of interest -- linker --
carbohydrate-binding domain,
in which the pro-peptide sequence normally contains 5-100, e.g. 5-25, amino
acid residues. The recombinant product may be giycosylated or non-
glycosylated.
Cellulose Binding Domain (CBD)
In the present context, the terms "amino acid sequence comprising a CBD or
Cellulose Binding Domain or CBD" are intended to indicate an amino acid
sequence capable of effecting binding of the cellulase to a cellulosic
substrate
(e.g. as described in P. Kraulis et al., Determination of the three-
dimensional
structure of the C terminal domain of cellobiohydrolase I from Trichoderma
reesei. A study using nuclear magnetic resonance and hybrid distance
geometry-dynamically simulated annealing. Biochemistry 28:7241-7257, 1989).
The classification and properties of cellulose binding domains are presented
in
P. Tomme et al., in the symposium "Enzymatic degradation of insoluble
polysaccharides" (ACS Symposium Series 618, edited by J.N. Saddler and M.H.
Penner, ACS, 1995).
Cellulose-binding (and other carbohydrate-binding) domains are polypeptide
amino acid sequences which occur as integral parts of large polypeptides or
proteins consisting of two or more polypeptide amino acid sequence regions,
especially in hydrolytic enzymes (hydrolases) which typically comprise a
catalytic
domain containing the active site for substrate hydrolysis and a carbohydrate-
binding domain for binding to the carbohydrate substrate in question. Such
enzymes can comprise more than one catalytic domain and one, two or three
carbohydrate-binding domains, and they may further comprise one or more
polypeptide amino acid sequence regions linking the carbohydrate-binding
domains) with the catalytic domain(s), a region of the latter type usually
being
denoted a "linker".
Examples of hydrolytic enzymes comprising a cellulose-binding domain are
cellulase, xylanases, mannanases, arabinofuranosidases, acetylesterases and
chitinases. "Cellulose-binding domains" have also been found in algae, e.g. in
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the red alga porphyra purpurea in the form of a non-hydrolytic polysaccharide-
binding protein [see P. Tomme et al., Cellulose-binding domains -
Classification
and Properties in Enzymatic Degradation of Insoluble Carbohydrates , John N.
Saddler and Michael H. Penner (Eds.), ACS Symposium Series, No. 618
(1996)]. However, most of the known CBDs (which are classified and referred to
by P. Tomme et al. (op. cit.) as "cellulose-binding domains"] derive from
cellulases and xylanases.
In the present context, the term "cellulose-binding domain" is intended to be
understood in the same manner as in the latter reference (P. Tomme et al., op.
cit. ) The P. Tomme et al. reference classifies more than 120 "cellulose-
binding
domains" into 10 families (I-X) which may have different functions or roles in
connection with the mechanism of substrate binding. However, it is to be
anticipated that new family representatives and additional families will
appear in
the future.
In proteins/polypeptides in which CBDs occur (e.g. enzymes, typically
hydrolytic
enzymes such as cellulases), a CBD may be located at the N or C terminus or at
an internal position.
The part of a polypeptide or protein (e.g. hydrolytic enzyme) which
constitutes a
CBD per se typically consists of more than about 30 and less than about 250
amino acid residues. For example, those CBDs listed and classified in Family I
in accordance with P. Tomme et al. (op. cit.) consist of 33-37 amino acid
residues, those listed and classified in Family Ila consist of 95-108 amino
acid
residues, those listed and classified in Family VI consist of 85-92 amino acid
residues, whilst one CBD (derived from a cellulase from Clostridium
thermocellum) listed and classified in Family VII consists of 240 amino acid
residues. Accordingly, the molecular weight of an amino acid sequence
constituting a CBD per se will typically be in the range of from about 4kD to
about 40kD, and usually below about 35kD.
Cellulose binding domains can be produced by recombinant techniques as
described in H. Stalbrand et al., Applied and Environmental Microbiology, Mar.
1995, pp. 1090-1097; E. Brun et al., (1995) Eur. J. Biochem. 231, pp. 142-148;
J.B. Coutinho et al., (1992) Molecular Microbiology 6(9), pp. 1243-1252
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In order to isolate a cellulose binding domain of, e.g. a cellulase, several
genetic
engineering approaches may be used. One method uses restriction enzyme to
remove a portion of the gene and then to fuse the remaining gene-vector
fragment in frame to obtain a mutated gene that encodes a protein truncated
for
a particular gene fragment. Another method involves the use of exonucleases
such as Ba131 to systematically delete nucleotides either externally from the
5'
and the 3' ends of the DNA or internally from a restricted gap within the
gene.
These gene-deletion methods result in a mutated gene encoding a shortened
gene molecule whose expression product may then be evaluated for substrate-
binding (e.g. cellulose-binding) ability. Appropriate substrates for
evaluating the
binding ability include cellulosic materials such as Avicel T"" and cotton
fibres.
Other methods include the use of a selective or specific protease capable of
cleaving a CBD, e.g. a terminal CBD, from the remainder of the polypeptide
chain of the protein in question.
As already indicated (vide supra), once a nucleotide sequence encoding the
substrate-binding (carbohydrate-binding) region has been identified, either as
cDNA or chromosomal DNA, it may then be manipulated in a variety of ways to
fuse it to a DNA sequence encoding the enzyme or enzymatically active amino
acid sequence of interest. The DNA fragment encoding the carbohydrate-
binding amino acid sequence, and the DNA encoding the enzyme or
enzymatically active amino acid sequence of interest are then ligated with or
without a linker. The resulting ligated DNA may then be manipulated in a
variety
of ways to achieve expression. Preferred microbial expression hosts include
certain Aspergillus species (e.g. A. niger or A. oryzae), Bacillus species,
and
organisms such as Escherichia coli or Saccharomyces cerevisiae.
Preferred GBDs for the purpose of the present invention are selected from the
group consisting of : CBDs CBHII from Trichoderma reesei, CBDs CenC, CenA
and Cex from Cellulomonas frmi, CBD CBHI from Trichoderma reesei, CBD
Cellulozome from Clostridium cellulovorans, CBD E3 from Thermonospora
fusca, CBD-dimer from Clostridium stecorarium (NCIMB11754) XynA, CBD from
Bacillus agaradherens (NCIMB40482) and/or CBD family 45 from Humicola
insolens. More preferred CBDs for the purpose of the present invention are the
CBD CenC from Cellulomonas fimi, CBD Cellulozome from Clostridium
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cellulovorans and/or the CBD originating from the fungal Humicola Insolens
cellulase sold under the tradename "Carezyme" by Novo Nordisk A/S. Carezyme
is an endoglucanase from family 45, derived from Humicola insolens DSM1800,
having a molecular weight of about 43kDa and exhibiting cellulolytic activity
Linking region
The term "linker" or "linking region" or "Middle region- MR" is intended to
indicate
a region that might adjoin the CBD and connect it to the catalytically active
amino acid sequence of the transferase enzyme. When present, this linking can
be achieved chemically or by recombinant techniques.
An example of the recombinant technique describing the expression of an
enzyme with the CBD of different origin is described in S. Karita et al.,
(1996)
Journal of Fermentation and Bioengineering, Vol. 81, No. 6, pp. 553-556.
Preferred finking regions are amino acid linking regions (peptides), some
examples thereof are described in N.R. Gilkes et al., Microbiol. Rev. 55,
1991,
pp. 303-315. The linking region can comprise from 1 to about 100 amino acid
residues, in particular of from 2 to 40 amino acid residues, e.g. from 2 to 15
amino acid residues. As stated above, it is preferred to use amino acids which
are less favoured by the surrounding proteases. Suitable amino acid linking
regions are the Humicola insolens family 45 cellulase linker, the NifA gene of
Klebsiella pneumoniae-CiP linker, the E. coli OrnpA gene-CiP linker, the E3
cellulase Thennomonospora fusca linker and the CenA cellulase linker;
preferably the Humicola insolens family 45 cellulase linker and the E3
celluiase
Thermomonospora fusca linker.
Non amino acid/proteinic compounds, referred to as "non-amino acid" can also
be used for the linking of the catalytically active amino acid sequence to the
CBD:
1) Suitable non-amino acid linking regions are the polyethylene glycol
derivatives described in the Shearwater polymers, Inc. catalog of January
1996,
such as the nucleophilic PEGs, the carboxyl PEGs, the electrophilically
activated
PEGs, the sulfhydryl-selective PEGs, the heterofunctional PEGs, the biotin
PEGs, the vinyl derivatives, the PEG silanes and the PEG phospholipids. In
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particular, suitable non-amino acid linking regions are the heterofunctional
PEG,
(X-PEG-Y) polymers from Shearwater such as PEG(NPC)2, PEG-(NH2)2, t-
BOC-NH-PEG-NH2, t-BOC-NH-PEG-C02NHS, OH-PEG-NH-tBOC, FMOC-NH-
PEG-C02NHS or PEG(NPC)2 MW 3400 from Sigma, glutaric dialdehyde 50
wt% solution in water from Aldrich, disuccinimidyl suberate (DSS) form Sigma,
y-
maleimidobutyric acid N-hydroxysuccinimide ester (GMBS) from Sigma, 1-ethyl-
3-(3-dimethylaminopropyl)carbodiimide hydrochloride (EDC) from Sigma and
dimethyl suberimidate hydrochloride (DMS) from Sigma.
2) Other suitable non-amino acid linking regions are 1-ethyl-3-(3-
dimethylaminopropyl} carbodiimide, N-ethyl-5-phenylisoaxolium-3-sulphonate, 1-
cyclohexyl-3(2morpholinoethyl) carbodide metho-p-toluene sulphonate, N-
ethoxycarbonyf-2-ethoxy 1,2, dihydroquinoline or glutaraldehyde.
3) Also suitable are the crosslinkers described in the 1999/2000 Pierce
Products
Catalogue from the Pierce Company, under the heading "Cross linking reagents
the SMPH, SMCC, LC-SMCC compounds, and preferably the Sulfo-KMUS
compound.
Preferred chemical linking regions are PEG(NPC)2, (NH2)2-PEG, t-BOC-NH-
PEG-NH2, MAL-PEG-NHS, VS-PEG-NHS polymers from Shearwater andlor the
Sulfo-KMUS compound from Pierce.
Detergent components
The laundry detergent and/or fabric care compositions of the invention must
contain at least one additional detergent and/or fabric care components. The
precise nature of these additional components, and levels of incorporation
thereof will depend on the physical form of the composition, and the nature of
the cleaning operation for which it is to be used.
The laundry detergent and/or fabric care compositions of the present invention
preferably further comprise a detergent ingredient selected from a surfactant
selected from nonionic andlor anionic and/or cationic andlor mixtures thereof,
another detergent enzyme, a bleaching agent, a dye transfer inhibiting
polymer,
a dispersant andlor a smectite clay.
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The laundry detergent and/or fabric care compositions according to the
invention
can be liquid, paste, gels, bars, tablets, spray, foam, powder or granular
forms.
Granular compositions can also be in "compact" form, the liquid compositions
can also be in a "concentrated" form.
The compositions of the invention may for example, be formulated as hand and
machine laundry detergent compositions including laundry additive compositions
and compositions suitable for use in the soaking and/or pretreatment of
stained
fabrics, rinse added fabric softener compositions. Pre-or post treatment of
fabric
include gel, spray and liquid fabric care compasitions. A rinse cycle with or
without the presence of softening agents is also contemplated.
When formulated as compositions suitable for use in a laundry machine washing
method, the compositions of the invention preferably contain both a surfactant
and a builder compound and additionally one or more detergent components
preferably selected from organic polymeric compounds, bleaching agents,
additional enzymes, suds suppressors, dispersants, lime-soap dispersants, soil
suspension and anti-redeposition agents and corrosion inhibitors. Laundry
compositions can also contain softening agents, as additional detergent
components.
The compositions of the invention can also be used as detergent additive
products in solid or liquid form. Such additive products are intended to
supplement or boost the performance of conventional detergent compositions
and can be added at any stage of the cleaning process.
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
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composition, preferably not exceeding 10%, most preferably not exceeding 5%
by weight of the composition. The inorganic filler salts, such as meant in the
present compositions are selected from the alkali and alkaline-earth-metal
salts
of sulphates and chlorides. A preferred filler salt is sodium sulphate.
Liquid detergent compositions according to the present invention can also be
in
a "concentrated form", in such case, the liquid detergent compositions
according
the present invention will contain a lower amount of water, compared to
conventional liquid detergents. Typically the water content of the
concentrated
liquid detergent is preferably less than 40%, more preferably less than 30%,
most preferably less than 20% by weight of the detergent composition.
Surfactant system
Preferably, the laundry detergent and/or fabric care compositions according to
the present invention further comprise a surfactant system wherein the
surfactant can be selected from nonionic and/or anionic and/or cationic
surfactants.
It has been surprisingly found that the combination of modified transferase
with
at least 5% of anionic surfactant, especially alkyl sulfate, alkyl ethoxy
sulaftes
and linear alkylene sulfonate and/or at least 2% of nonionic surfactant of the
alkyl ethoxylate type and/or cationic surfactant in the presence of anionic
surfactant, provides refurbishes or restores improved tensile strength,
enhanced
anti-wrinkle, anti-shrinkage and anti-bobbling properties to fabrics, as well
as
provide better static control, fabric softness, colour appearance and fabric
anti-
wear properties and benefits. In addition, improved cleaning benefits are
achieved with said combinations.
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 laundry detergent and/or fabric care compositions
in accord with the invention.
The surfactant is preferably formulated to be compatible with enzyme
components present in the composition. In liquid or gel compositions the
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surfactant is most preferably formulated such that it promotes, or at least
does
not degrade, the stability of any enzyme in these compositions.
Polyethylene, polypropylene, and polybutylene oxide condensates of alkyl
phenols are suitable for use as the nonionic surfactant of the surfactant
systems
of the present invention, with the polyethylene oxide condensates being
preferred. These compounds include the condensation products of alkyl phenols
having an alkyl group containing from about 6 to about 14 carbon atoms,
preferably from about 8 to about 14 carbon atoms, in either a straight-chain
or
branched-chain configuration with the alkylene oxide. In a preferred
embodiment, the ethylene oxide is present in an amount equal to from about 2
to about 25 moles, more preferably from about 3 to about 15 moles, of ethylene
oxide per mole of alkyl phenol. Commercially available nonionic surtactants of
this type include IgepaITM CO-630, marketed by the GAF Corporation; and
TritonTM X-45, X-114, X-100 and X-102, all marketed by the Rohm & Haas
Company. These surfactants are commonly referred to as alkylphenol
alkoxylates (e.g., alkyl phenol ethoxylates).
The condensation products of primary and secondary aliphatic alcohols with
from about 1 to about 25 moles of ethylene oxide are suitable for use as the
nonionic surfactant of the nonionic surfactant systems of the present
invention.
The alkyl chain of the aliphatic alcohol can either be straight or branched,
primary or secondary, and generally contains from about 8 to about 22 carbon
atoms. Preferred are the condensation products of alcohols having an alkyl
group containing from about 8 to about 20 carbon atoms, more preferably from
about 10 to about 18 carbon atoms, with from about 2 to about 10 moles of
ethylene oxide per mole of alcohol. About 2 to about 7 moles of ethylene oxide
and most preferably from 2 to 5 moles of ethylene oxide per mole of alcohol
are
present in said condensation products. Examples of commercially available
nonionic surfactants of this type include TergitoITM 15-S-9 (the condensation
product of C11-C15 linear alcohol with 9 moles ethylene oxide), TergitoITM 24-
L-6 NMW (the condensation product of C12-C14 primary alcohol with 6 moles
ethylene oxide with a narrow molecular weight distribution), both marketed by
Union Carbide Corporation; NeodoITM 45-9 (the condensation product of C14-
C15 linear alcohol with 9 moles of ethylene oxide), NeodoITM 23-3 (the
condensation product of C12-C13 linear alcohol with 3.0 moles of ethylene
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oxide), NeodoITM 45-7 (the condensation product of C14-C15 linear alcohol with
7 moles of ethylene oxide), NeodoITM 45-5 (the condensation product of C14-
C15 linear alcohol with 5 moles of ethylene oxide) marketed by Shell Chemical
Company, KyroTM EOB (the condensation product of C13-C15 alcohol with 9
moles ethylene oxide), marketed by The Procter & Gamble Company, and
Genapol LA 030 or 050 (the condensation product of C12-C14 alcohol with 3
or 5 moles of ethylene oxide) marketed by Hoechst. Preferred range of HLB in
these products is from 8-11 and most preferred from 8-10.
Also useful as the nonionic surfactant of the surfactant systems of the
present
invention are the alkylpolysaccharides disclosed in U.S. Patent 4,565,647,
Llenado, issued January 21, 1986, having a hydrophobic group containing from
about 6 to about 30 carbon atoms, preferably from about 10 to about 16 carbon
atoms and a polysaccharide, e.g. a polyglycoside, hydrophilic group containing
from about 1.3 to about 10, preferably from about 1.3 to about 3, most
preferably
from about 1.3 to about 2.7 saccharide units. Any reducing saccharide
containing 5 or 6 carbon atoms can be used, e.g., glucose, galactose and
galactosyl moieties can be substituted for the glucosyl moieties (optionally
the
hydrophobic group is attached at the 2-, 3-, 4-, etc. positions thus giving a
glucose or galactose as opposed to a glucoside or galactoside). The
intersaccharide bonds can be, e.g., between the one position of the additional
saccharide units and the 2-, 3-, 4-, and/or 6- positions on the preceding
saccharide units.
The preferred alkylpolyglycosides have the formula
R20(CnH2n0)t(glYcosyl)x
wherein R2 is selected from the group consisting of alkyl, alkylphenyl,
hydroxyalkyl, hydroxyalkylphenyl, and mixtures thereof in which the alkyl
groups
contain from about 10 to about 18, preferably from about 12 to about 14,
carbon
atoms; n is 2 or 3, preferably 2; t is from 0 to about 10, preferably 0; and x
is
from about 1.3 to about 10, preferably from about 1.3 to about 3, most
preferably
from about 1.3 to about 2.7. The glycosyl is preferably derived from glucose.
To
prepare these compounds, the alcohol or alkylpolyethoxy alcohol is formed
first
and then reacted with glucose, or a source of glucose, to form the glucoside
(attachment at the 1-position). The additional glycosyl units can then be
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28
attached between their 1-position and the preceding glycosyl units 2-, 3-, 4-
and/or 6-position, preferably predominately the 2-position.
The condensation products of ethylene oxide with a hydrophobic base formed
by the condensation of propylene oxide with propylene glycol are also suitable
for use as the additional nonionic surfactant systems of the present
invention.
The hydrophobic portion of these compounds will preferably have a molecular
weight of from about 1500 to about 1800 and will exhibit water insolubility.
The
addition of polyoxyethylene moieties to this hydrophobic portion tends to
increase the water solubility of the molecule as a whole, and the liquid
character
of the product is retained up to the point where the polyoxyethylene content
is
about 50% of the total weight of the condensation product, which corresponds
to
condensation with up to about 40 moles of ethylene oxide. Examples of
compounds of this type include certain of the commercially-available
PlurafacTM
LF404 and PluronicTM surfactants, marketed by BASF.
Also suitable for use as the nonionic surfactant of the nonionic surfactant
system
of the present invention, are the condensation products of ethylene oxide with
the product resulting from the reaction of propylene oxide and
ethylenediamine.
The hydrophobic moiety of these products consists of the reaction product of
ethylenediamine and excess propylene oxide, and generally has a molecular
weight of from about 2500 to about 3000. This hydrophobic moiety is
condensed with ethylene oxide to the extent that the condensation product
contains from about 40% to about 80% by weight of polyoxyethylene and has a
molecular weight of from about 5,000 to about 11,000. Examples of this type of
nonionic surfactant include certain of the commercially available TetronicTM
compounds, marketed by BASF.
Preferred for use as the nonionic surfactant of the surfactant systems of the
present invention are polyethylene oxide condensates of alkyl phenols,
condensation products of primary and secondary aliphatic alcohols with from
about 1 to about 25 moles of ethylene oxide, alkylpolysaccharides, and
mixtures
thereof. Most preferred are Cg-C14 alkyl phenol ethoxylates having from 3 to
15
ethoxy groups and Cg-C1g alcohol ethoxylates (preferably C1p avg.) having
from 2 to 10 ethoxy groups, and mixtures thereof.
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Highly preferred nonionic surfactants are polyhydroxy fatty acid amide
surfactants of the formula.
R2-C-N-Z,
II I
O R1
wherein R1 is H, or R1 is C1_4 hydrocarbyl, 2-hydroxy ethyl, 2-hydroxy propyl
or
a mixture thereof, R2 is C5_31 hydrocarbyl, and Z is a polyhydroxyhydrocarbyl
having a linear hydrocarbyl chain with at least 3 hydroxyls directly connected
to
the chain, or an alkoxylated derivative thereof. Preferably, R1 is methyl, R2
is a
straight C11-15 alkyl or C16-18 alkyl or alkenyl chain such as coconut alkyl
or
mixtures thereof, and Z is derived from a reducing sugar such as glucose,
fructose, maltose, lactose, in a reductive amination reaction.
Suitable anionic surfactants to be used are linear alkyl benzene sulfonate,
alkyl
ester sulfonate surfactants including linear esters of Cg-C2p carboxylic acids
(i.e., fatty acids) which are sulfonated with gaseous S03 according to "The
Journal of the American Oil Chemists Society", 52 (1975), pp. 323-329.
Suitable
starting materials would include natural fatty substances as derived from
tallow,
palm oil, etc.
The preferred alkyl ester sulfonate surfactant, especially for laundry
applications,
comprise alkyl ester sulfonate surfactants of the structural formula:
O
I I
R3 - CH - C - OR4
I
S03M
wherein R3 is a Cg-C2p 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 suifonate.
Suitable
salt-forming cations include metals such as sodium, potassium, and lithium,
and
substituted or unsubstituted ammonium cations, such as monoethanolamine,
diethanolamine, and triethanolamine. Preferably, R3 is C1p-C1g alkyl, and R4
is
methyl, ethyl or isopropyl. Especially preferred are the methyl ester
sulfonates
wherein R3 is C1p-C1g alkyl.
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Other suitable anionic surfactants include the alkyl sulfate surfactants which
are
water soluble salts or acids of the formula ROS03M wherein R preferably is a
C10-C24 hYdrocarbyl, preferably an alkyl or hydroxyalkyl having a C1p-C20
alkyl
component, more preferably a C12-C1 g alkyl or hydroxyalkyl, and M is H or a
cation, e.g., an alkali metal cation (e.g. sodium, potassium, lithium), or
ammonium or substituted ammonium (e.g. methyl-, dimethyl-, and trimethyl
ammonium cations and quaternary ammonium cations such as tetramethyl-
ammonium and dimethyl piperdinium cations and quaternary ammonium cations
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 laundry detergent and/or fabric care 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 glycerol sulfates, alkyl phenol ethylene oxide ether sulfates, paraffin
sulfonates, alkyl phosphates, isethionates such as the acyl isethionates, N-
acyl
taurates, alkyl succinamates and sulfosuccinates, monoesters of
sulfosuccinates
(especially saturated and unsaturated C12-C1g monoesters) and diesters of
sulfosuccinates (especially saturated and unsaturated C6-C12 diesters), acyl
sarcosinates, sulfates of alkylpolysaccharides such as the sulfates of
alkylpolyglucoside (the nonionic nonsulfated compounds being described
below), branched primary alkyl sulfates, and alkyl polyethoxy carboxylates
such
as those of the formula RO(CH2CH20)k-CH2C00-M+ wherein R is a Cg-C22
alkyl, k is an integer from 1 to 10, and M is a soluble salt-forming cation.
Resin
acids and hydrogenated resin acids are also suitable, such as rosin,
hydrogenated rosin, and resin acids and hydrogenated resin acids present in or
derived from tall oil.
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Further examples are described in "Surface Active Agents and Detergents" (Vol.
I and II by Schwartz, Perry and Berch). A variety of such surfactants are also
generally disclosed in U.S. Patent 3,929,678, issued December 30, 1975 to
Laughlin, et al. at Column 23, line 58 through Column 29, line 23 (herein
incorporated by reference).
When included therein, the laundry detergent compositions of the present
invention typically comprise from about 1 % to about 40%, preferably from
about
3% to about 20% by weight of such anionic surfactants.
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-
C1g alkyl or hydroxyalkyl, A is an ethoxy or propoxy unit, m is greater than
zero,
typically between about 0.5 and about 6, more preferably between about 0.5 and
about 3, and M is H or a cation which can be, for example, a metal cation
(e.g.,
sodium, potassium, lithium, calcium, magnesium, etc.), ammonium or
substituted-ammonium cation. Alkyl ethoxylated sulfates as well as alkyl
propoxylated sulfates are contemplated herein. Specific examples of
substituted
ammonium cations include methyl-, dimethyl, trimethyl-ammonium cations and
quaternary ammonium cations such as tetramethyl-ammonium and dimethyl
piperdinium cations and those derived from alkylamines such as ethylamine,
diethylamine, triethylamine, mixtures thereof, and the like. Exemplary
surfactants
are C12-C1g alkyl polyethoxylate (1.0) sulfate (C12-C18E(1.0)M), C12-C1g alkyl
polyethoxylate (2.25) sulfate (C12-C18E(2.25)M), C12-C1 g alkyl polyethoxylate
(3.0) sulfate (C12-C18E(3.0)M), and C12-C1g alkyl polyethoxylate (4.0) sulfate
(C12-CIgE(4.0)M), wherein M is conveniently selected from sodium and
potassium.
The laundry detergent andlor fabric care compositions of the present invention
may also contain cationic, ampholytic, zwitterionic, and semi-polar
surtactants,
as well as the nonionic and/or anionic surfactants other than those already
described herein.
Cationic detersive surfactants suitable for use in the laundry detergent
and/or
fabric care compositions of the present invention are those having one long-
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32
chain hydrocarbyl group. Examples of such cationic surfactants include the
ammonium surfactants such as alkyltrimethylammonium halogenides, and those
surfactants having the formula
[R2(OR3)y1[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(CH3)-, -CH2CH(CH20H)-, -CH2CH2CH2-, and mixtures
thereof; each R4 is selected from the group consisting of C1-Cq, alkyl, C1-C4
hydroxyalkyl, benzyl ring structures formed by joining the two R4 groups, -
CH2CHOH-CHOHCOR6CHOHCH20H wherein R6 is any hexose or hexose
polymer having a molecular weight less than about 1000, and hydrogen when y
is not 0; R5 is the same as R4 or is an alkyl chain wherein the total number
of
carbon atoms of R2 plus R5 is not more than about 18; each y is from 0 to
about
and the sum of the y values is from 0 to about 15; and X is any compatible
anion.
Quaternary ammonium surfactant suitable for the present invention has the
formula (I):
R2 R3 ,,,R4
O ~ ,,,
R~ N°
~O 'R5 X-
Formula I
whereby R1 is a short chainlength alkyl (C6-C10) or alkylamidoalkyl of the
formula (II)
Cs-Cro N
~CH~
O
Formula II
y is 2-4, preferably 3.
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,
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33
whereby X- is a counterion, preferably a halide, e.g. chloride or
methylsulfate.
Rs
~H
O')z
Formula III
R6 is C1-C4 and z is 1 or 2.
Preferred quat ammonium surfactants are those as defined in formula I whereby
R1 is Cg, C1p or mixtures thereof, x=o,
Rg, R4 = CH3 and R5 = CH2CH20H.
Highly preferred cationic surfactants are the water-soluble quaternary
ammonium compounds useful in the present composition having the formula
R1 R2R3R4N+X- (i)
wherein R1 is Cg-C1g alkyl, each of R2, R3 and R4 is independently C1-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, Rg or R4 should be benzyl.
The preferred alkyl chain length for R1 is C12-C15 particularly where the
alkyl
group is a mixture of chain lengths derived from coconut or palm kernel fat or
is
derived synthetically by olefin build up or OXO alcohols synthesis. Preferred
groups for R2R3 and R4 are methyl and hydroxyethyl groups and the anion X
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;
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;
lauryl dimethyl benzyl ammonium chloride or bromide;
lauryl dimethyl (ethenoxy)4 ammonium chloride or bromide;
choline esters (compounds of formula (i) wherein R1 is
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34
CH2-CH2-O-C-C12-14 alkyl and R2R3R4 are methyl).
I I
O
di-alkyl imidazolines [compounds of formula (i}].
Other cationic surfactants useful herein are also described in U.S. Patent
4,228,044, Cambre, issued October 14, 1980 and in European Patent
Application EP 000,224.
Typical cationic fabric softening components include the water-insoluble
quaternary-ammonium fabric softening actives or thei corresponding amine
precursor, the most commonly used having been di-long alkyl chain ammonium
chloride or methyl sulfate.
Preferred cationic softeners among these include the following:
1) ditallow dimethylammonium chloride (DTDMAC);
2) dihydrogenated tallow dimethylammonium chloride;
3) dihydrogenated tallow dimethylammonium methylsulfate;
4) distearyl dimethylammonium chloride;
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
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.
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The quaternary ammonium compounds and amine precursors herein have the
formula (I) or (II), below
3 2 R3 R3
R~ R _ + N/ (CH2)~~-CH -CH2 X
~« Q-T 1 X R3 Q
T~ T?
or
wherein Q is selected from -O-C(O)-, -C(O)-O-, -O-C(O)-O-, -NR4-C(O)-, -C(O)-
N R4-;
R1 is (CH2)n-Q-T2 or T3;
R2 is (CH2)m-Q-T4 or T5 or R3;
R3 is C1-C4 alkyl or C1-C4 hydroxyalkyl or H;
R4 is H or C1-C4 alkyl or C1-C4 hydroxyalkyl;
T1, T2, T3, T4, T5 are independently C~ ~-C22 alkyl or alkenyl;
n and m are integers from 1 to 4; and
X- is a softener-compatible anion. Non-limiting examples of softener-
compatible
anions include chloride or methyl sulfate.
The alkyl, or alkenyl, chain T1, T2, T3, T4, T5 must contain at least 11
carbon
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
sulfate;
3) N,N-di(2-tallowyl-oxy-2-oxo-ethyl)-N,N-dimethyl ammonium chloride;
4) N,N-di(2-tallowyl-oxy-ethylcarbonyl-oxy-ethyl)-N,N-dimethyl ammonium
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36
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 laundry detergent and/or fabric care 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.
Conventional detergent enzymes
The laundry detergent and/or fabric care compositions can in addition to the
modified transferase enzyme, further comprise one or more enzymes which
provide cleaning performance, fabric care and/or sanitisation benefits.
It has also been surprisingly found that the combination of a modified
transferase with a detergent enzyme - especially a protease, cellulase, lipase
and/or amylase - provides, refurbishes or restores improved tensile strength,
enhanced anti-wrinkle, anti-shrinkage, anti-bobbling properties to fabrics, as
well
as provide better static control, fabric softness, colour appearance and
fabric
anti-wear properties and benefits. In addition, improved cleaning benefits are
achieved with said combinations.
Said enzymes include enzymes selected from cellulases, hemicellulases,
peroxidases, proteases, gluco-amylases, amylases, xylanases, lipases,
phospholipases, esterases, cutinases, pectinases, keratanases, reductases,
oxidases, phenoloxidases, lipoxygenases, ligninases, pullulanases, tannases,
pentosanases, malanases, f3-glucanases, arabinosidases, hyaluronidase,
chondroitinase, laccase or mixtures thereof.
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A preferred combination is a laundry detergent and/or fabric care composition
having cocktail of conventional applicable enzymes like protease, amylase,
lipase, cutinase andlor cellulase in conjunction with one or more plant cell
wall
degrading enzymes.
The cellulases usable in the present invention include both bacterial or
fungal
cellulases. Preferably, they will have a pH optimum of between 5 and 12 and a
specific activity above 50 CEVU/mg (Cellulose Viscosity Unit). Suitable
cellulases are disclosed in U.S. Patent 4,435,307, Barbesgoard et al,
J61078384 and W096/02653 which discloses fungal cellulase produced
respectively from Humicola insolens, Trichoderma, Thielavia and Sporotrichum.
EP 739 982 describes cellulases isolated from novel Bacillus species. Suitable
cellulases are also disclosed in GB-A-2.075.028; GB-A-2.095.275; DE-OS-
2.247.832 and W095/26398.
Examples of such cellulases are cellulases produced by a strain of Humicola
insolens (Humicola grisea var. thermoidea), particularly the Humicola strain
DSM
1800.
Other suitable cellulases are cellulases originated from Humicola insolens
having a molecular weight of about 50KDa, an isoelectric point of 5.5 and
containing 415 amino acids; and a -43kD endoglucanase derived from Humicola
insoiens, DSM 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 EGlli cellulases from
Trichoderma iongibrachiatum described in W094/21801, Genencor, published
September 29, 1994. Especially suitable cellulases are the cellulases having
color care benefits. Examples of such cellulases are cellulases described in
European patent application No. 91202879.2, filed November 6, 1991 (Novo).
Carezyme and Celluzyme (Novo Nordisk A/S) are especially useful. See also
W091/17244 and W091/21801. Other suitable cellulases for fabric care and/or
cleaning properties are described in W096/34092, W096/17994 and
W095/24471.
Said cellulases are normally incorporated in the laundry detergent andlor
fabric
care composition at levels from 0.0001 % to 2% of pure enzyme by weight of the
laundry detergent and/or fabric care composition.
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Peroxidase enzymes are used in combination with oxygen sources, e.g.
percarbonate, perborate, persulfate, hydrogen peroxide, etc and with a
phenolic
substrate as bleach enhancing molecule. They are used for "solution
bleaching",
i.e. to prevent transfer of dyes or pigments removed from substrates during
wash operations to other substrates in the wash solution. Peroxidase enzymes
are known in the art, and include, for example, horseradish peroxidase,
iigninase
and haloperoxidase such as chloro- and bromo-peroxidase. Peroxidase-
containing detergent compositions are disclosed, for example, in PCT
International Application WO 89/099813, W089/09813 and in European Patent
application EP No. 91202882.6, filed on November 6, 1991 and EP No.
96870013.8, filed February 20, 1996. Also suitable is the laccase enzyme.
Enhancers are generally comprised at a level of from 0.1 % to 5% by weight of
total composition. Preferred enhancers are substituted phenthiazine and
phenoxasine 10-Phenothiazinepropionicacid (PPT), 10-ethylphenothiazine-4-
carboxylic acid (EPC), 10-phenoxazinepropionic acid (POP) and 10-
methylphenoxazine (described in WO 94/12621 ) and substituted syringates (C3-
C5 substituted alkyl syringates) and phenols. Sodium percarbonate or perborate
are preferred sources of hydrogen peroxide.
Said peroxidases are normally incorporated in the laundry detergent and/or
fabric care composition at levels from 0.0001 % to 2% of pure enzyme by weight
of the laundry detergent and/or fabric care composition.
Other preferred enzymes that can be included in the laundry detergent and/or
fabric care compositions of the present invention include lipases. Suitable
lipase
enzymes for detergent usage include those produced by microorganisms of the
Pseudomonas group, such as Pseudomonas stutzeri ATCC 19.154, as
disclosed in British Patent 1,372,034. Suitable lipases include those which
show
a positive immunological cross-reaction with the antibody of the lipase,
produced
by the microorganism Pseudomonas fluorescent IAM 1057. This lipase is
available from Amano Pharmaceutical Co. Ltd., Nagoya, Japan, under the trade
name Lipase P "Amano," hereinafter referred to as "Amano-P". Other suitable
commercial lipases include Amano-CES, lipases ex Chromobacter viscosum,
e.g. Chromobacter viscosum var, lipolyticum NRRLB 3673 from Toyo Jozo Co.,
Tagata, Japan; Chromobacter viscosum lipases from U.S. Biochemical Corp.,
U.S.A. and Disoynth Co., The Netherlands, and lipases ex Pseudomonas
gladioli. Especially suitable lipases are lipases such as M 1 LipaseR and
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39
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
258 068, WO 92/05249 and WO 95/22615 by Novo Nordisk and in WO
94/03578, WO 95/35381 and WO 96/00292 by Unilever.
Also suitable are cutinases [EC 3.1.1.50] which can be considered as a special
kind of lipase, namely lipases which do not require interfacial activation.
Addition
of cutinases to detergent compositions have been described in e.g. WO-A-
88/09367 (Genencor); WO 90/09446 (Plant Genetic System) and WO 94/14963
and WO 94/14964 (Unilever).
The lipases andlor cutinases are normally incorporated in the laundry
detergent
and/or fabric care composition at levels from 0.0001 % to 2% of pure enzyme by
weight of the laundry detergent and/or fabric care composition.
Suitable proteases are the subtilisins which are obtained from particular
strains
of 8. subtilis and 8. lichenifonnis (subtilisin BPN and BPN'). One suitable
protease is obtained from a strain of Bacillus, having maximum activity
throughout the pH range of 8-12, developed and sold as ESPERASE~ by Novo
Industries A/S of Denmark, hereinafter "Novo". The preparation of this enzyme
and analogous enzymes is described in GB 1,243,784 to Novo. Other suitable
proteases include ALCALASE~, DURAZYM~ and SAVINASE~ from Novo and
MAXATASE~. MAXACAL~, PROPERASE~ and MAXAPEM~ (protein
engineered Maxacal) from Gist-Brocades. Proteolytic enzymes also encompass
modified bacterial serine proteases, such as those described in European
Patent Application Serial Number 87 303761.8, filed April 28, 1987
{particularly
pages 17, 24 and 98), and which is called herein "Protease B", and in European
Patent Application 199,404, Venegas, published October 29, 1986, which refers
to a modified bacterial serine protealytic enzyme which is called "Protease A"
herein. Suitable is the protease called herein "Protease C", which is a
variant of
an alkaline serine protease from Bacillus in which lysine replaced arginine at
position 27, tyrosine replaced valine at position 104, serine replaced
asparagine
at position 123, and alanine replaced threonine at position 274. Protease C is
described in EP 90915958:4, corresponding to WO 91/06637, Published May
16, 1991. Genetically modified variants, particularly of Protease C, are also
included herein.
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A preferred protease referred to as "Protease D" is a carbonyl hydrolase
variant
having an amino acid sequence not found in nature, which is derived from a
precursor carbonyl hydrolase by substituting a different amino acid for a
plurality
of amino acid residues at a position in said carbonyl hydrolase equivalent to
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,
+103, +104, +107, +123, +27, +105, +109, +126, +128, +135, +156, +166, +195,
+197, +204, +206, +210, +216, +217, +218, +222, +260, +265, and/or +274
according to the numbering of Bacillus amyloliquefaciens subtilisin, as
described
in W095110591 and in the patent application of C. Ghosh, et al, "Bleaching
Compositions Comprising Protease Enzymes" having US Serial No. 08/322,677,
filed October 13, 1994. Also suitable is a carbonyl hydrolase variant of the
protease described in W095/10591, having an amino acid sequence derived by
replacement of a plurality of amino acid residues replaced in the precursor
enzyme corresponding to position +210 in combination with one or more of the
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 US Serial No. 60/048,550, filed June
04,
1997).
Also preferred proteases are multiply-substituted protease variants. These
protease variants comprise a substitution of an amino acid residue with
another
naturally occurring 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
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41
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 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
occurring 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 PCT application Nos.
PCT/US98/22588, PCT/US98/22482 and PCT/US98/22486 all filed on October
23, 1998 from The Procter & Gamble Company.
Also suitable for the present invention are proteases described in patent
applications EP 251 446 and WO 91/06637, protease BLAP~ described in
W091I02792 and 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 described in WO 95/07791 to Procter
8~
Gamble. A recombinant trypsin-like protease for detergents suitable herein is
described in WO 94/25583 to Novo. Other suitable proteases are described in
EP 516 200 by Unilever.
The proteolytic enzymes are incorporated in the laundry detergent and/or
fabric
care compositions of the present invention a level of from 0.0001 % to 2%,
preferably from 0.001 % to 0.2%, more preferably from 0.005% to 0.1 % pure
enzyme by weight of the composition.
Amylases (a and/or f3) can be included for removal of carbohydrate-based
stains. W094/02597, Novo Nordisk A/S published February 03, 1994, describes
cleaning compositions which incorporate mutant amylases. See also
W095/10603, Novo Nordisk A/S, published April 20, 1995. Other amylases
known for use in cleaning compositions include both a- and ~3-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; end British Patent specification no. 1,296,839 (Novo). Other
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42
suitable amylases are stability-enhanced amylases described in W094/18314,
published August 18, 1994 and W096/05295, Genencor, published February
22, 1996 and amylase variants having additional modification in the immediate
parent available from Novo Nordisk A/S, disclosed in WO 95/10603, published
April 95. Also suitable are amylases described in EP 277 216, W095/26397
and W096/23873 (all by Novo Nordisk).
Examples of commercial a-amylases products are Purafect Ox Am~ from
Genencor and Termamyl~, Ban~ ,Fungamyl~ and Duramyl~, all available from
Novo Nordisk A/S Denmark. W095/26397 describes other suitable amylases : a
-amylases characterised by having a specific activity at least 25% higher than
the specific activity of Termamyl~ at a temperature range of 25°C to
55°C and
at a pH value in the range of 8 to 10, measured by the Phadebas~ a-amylase
activity assay. Suitable are variants of the above enzymes, described in
W096/23873 (Novo Nordisk). Other amylolytic enzymes with improved
properties with respect to the activity level and the combination of
thermostability
and a higher activity level are described in W095/35382.
The amylolytic enzymes are incorporated in the laundry detergent and/or fabric
care compositions of the present invention a level of from 0.0001 % to 2%,
preferably from 0.00018% to 0.06%, more preferably from 0.00024% to 0.048%
pure enzyme by weight of the composition.
The above-mentioned enzymes may be of any suitable origin, such as
vegetable, animal, bacterial, fungal and yeast origin. Origin can further be
mesophilic or extremophilic (psychrophilic, psychrotrophic, thermophilic,
barophilic, alkalophilic, acidophilic, halophilic, etc.). Purified or non-
purified forms
of these enzymes may be used. Nowadays, it is common practice to modify wild-
type enzymes via protein / genetic engineering techniques in order to optimise
their performance efficiency in the cleaning compositions of the invention.
For
example, the variants may be designed such that the compatibility of the
enzyme to commonly encountered ingredients of such compositions is
increased. Alternatively, the variant may be designed such that the optimal
pH,
bleach or chelant stability, catalytic activity and the like, of the enzyme
variant is
tailored to suit the particular cleaning application.
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
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43
compatibility. The isoelectric point of such enzymes may be modified by the
substitution of some charged amino acids, e.g. an increase in isoelectric
point
may help to improve compatibility with anionic surfactants. The stability of
the
enzymes may be further enhanced by the creation of e.g. additional salt
bridges
and enforcing calcium binding sites to increase chelant stability. Special
attention must be paid to the cellulases as most of the cellulases have
separate
binding domains (CBD). Properties of such enzymes can be altered by
modifications in these domains.
Said enzymes are normally incorporated in the laundry detergent and/or fabric
care composition at levels from 0.0001 % to 2% of pure enzyme by weight of the
laundry detergent and/or fabric care composition. The enzymes can be added
as separate single ingredients (prills, granulates, stabilized liquids, etc...
containing one enzyme ) or as mixtures of two or more enzymes ( e.g.
cogranulates ).
Other suitable detergent ingredients that can be added are enzyme oxidation
scavengers which are described in Copending European Patent application
92870018.6 filed on January 31, 1992. Examples of such enzyme oxidation
scavengers are ethoxylated tetraethylene polyamines.
A range of enzyme materials and means for their incorporation into synthetic
detergent compositions is also disclosed in WO 9307263 A and WO 9307260 A
to Genencor International, WO 8908694 A to Novo, and U.S. 3,553,139,
January 5, 1971 to McCarty et al. Enzymes are further disclosed in U.S.
4,101,457, Place 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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Bleaching agent
The laundry detergent and/or fabric care compositions of the present invention
can comprise in addition to the modified transferase, a bleaching agent.
It has also been surprisingly found that the combination of a modified
transferase with a bleaching agent achieved improved whiteness, provides,
refurbishes or restores improved tensile strength, enhanced anti-wrinkle, anti-
shrinkage, anti-bobbling properties to fabrics, as well as provide better
static
control, fabric softness, colour appearance and fabric anti-wear properties
and
benefits, especially enhances the fabric feel properties. In addition,
improved
cleaning benefits are achieved with said combination.
Bleaching agents include as 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 about 1 % to
about 25%.
The bleaching agent component for use herein can be any of the bleaching
agents useful for cleaning 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,
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
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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.
The hydrogen peroxide releasing agents can be used in combination with bleach
activators such as tetraacetylethylenediamine (TAED), nonanoyloxybenzene-
sulfonate (NOBS, described in US 4,412,934), 3,5,-
trimethylhexanoloxybenzenesulfonate (ISONOBS, described in EP 120,591) or
pentaacetylglucose (PAG)or Phenolsulfonate ester of N-nonanoyl-6-
aminocaproic acid (NACA-OBS, described in W094/28106), which are
perhydrolyzed to form a peracid as the active bleaching species, leading to
improved bleaching effect. Also suitable activators are acylated citrate
esters
such as disclosed in Copending European Patent Application No. 91870207.7.
Useful bleaching agents, including peroxyacids and bleaching systems
comprising bleach activators and peroxygen bleaching compounds for use in
laundry detergent and/or fabric care compositions according to the invention
are
described in our co-pending applications USSN 08/136,626, PCT/US95/07823,
W095/27772, W095/27773, W095/27774 and WO95/27775.
The hydrogen peroxide may also be present by adding an enzymatic system
(i.e. an enzyme and a substrate therefore) which is capable of generating
hydrogen peroxide at the beginning or during the washing and/or rinsing
process. Such enzymatic systems are disclosed in EP Patent Application
91202655.6 filed October 9, 1991.
Metal-containing catalysts for use in bleach compositions, include cobalt-
containing catalysts such as Pentaamine acetate cobalt(III) salts and
manganese-containing catalysts such as those described in EPA 549 271; EPA
549 272; EPA 458 397; US 5,246,621; EPA 458 398; US 5,194,416 and US
5,114,611. Bleaching composition comprising a peroxy compound, a
manganese-containing bleach catalyst and a chelating agent is described in the
patent application No 94870206.3.
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46
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
andlor 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 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, laundry detergent
and/or fabric care compositions will contain about 0.025% to about 1.25%, by
weight, of sulfonated zinc phthalocyanine.
Dye transfer inhibition
The laundry detergent and/or fabric care compositions of the present invention
preferably further include compounds for inhibiting dye transfer from one
fabric
to another of solubilised and suspended dyes encountered during fabric
laundering operations involving coloured fabrics.
It has also been surprisingly found that the combination of a modified
transferase with a dye transfer inhibiting agent provides, refurbishes or
restores
improved tensile strength, enhanced anti-wrinkle, anti-shrinkage, anti-
bobbling
properties to fabrics, as well as provide better static control, fabric
softness,
colour appearance and fabric anti-wear properties and benefits. In addition,
improved cleaning benefits are achieved with said combination.
Polymeric dye transfer inhibiting agents
The laundry detergent and/or fabric care compositions according to the present
invention may 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 laundry detergent and/or fabric care compositions in order to inhibit the
transfer of dyes from colored fabrics onto fabrics washed therewith. These
polymers have the ability to complex or adsorb the fugitive dyes washed out of
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47
dyed fabrics before the dyes have the opportunity to become attached to other
articles in the wash.
Especially suitable polymeric dye transfer inhibiting agents are polyamine N-
oxide polymers, copolymers of N-vinylpyrrolidone and N-vinylimidazole,
polyvinylpyrrolidone polymers, polyvinyloxazolidones and polyvinylimidazoles
or
mixtures thereof.
Addition of such polymers also enhances the performance of the enzymes
according the invention. .
a) Poiyamine N-oxide polymers
The polyamine N-oxide polymers suitable for use contain units having the
following structure formula
P
I
(I) Ax
I
R
wherein P is a polymerisable unit, whereto the R-N-O group can be
attached to or wherein the R-N-O group forms part of the polymerisable unit or
a
combination of both.
O O O
II II II
A is NC, CO, C, -O-,-S-, -N- ; x is O or 1;
R are aliphatic, ethoxylated aliphatics, aromatic, heterocyclic or alicyclic
groups or any combination thereof whereto the nitrogen of the N-O group can be
attached or wherein the nitrogen of the N-O group is part of these groups.
The N-O group can be represented by the following general structures
O O
I
(R1)x -N- (R2)y =N- (R1)x
I
(R3)z
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48
wherein R1, R2, and R3 are aliphatic groups, aromatic, heterocyclic or
alicyclic groups or combinations thereof, x orland y or/and z is 0 or 1 and
wherein the nitrogen of the N-O group can be attached or wherein the nitrogen
of the N-O group forms part of these groups.
The N-O group can be part of the polymerisable unit (P) or can be attached to
the polymeric backbone or a combination of both.
Suitable polyamine N-oxides wherein the N-O group forms part of the
polymerisable unit comprise polyamine N-oxides wherein R is selected from
aliphatic, aromatic, alicyclic or heterocyclic groups.
One class of said polyamine N-oxides comprises the group of polyamine N-
oxides wherein the nitrogen of the N-O group forms part of the R-group.
Preferred polyamine N-oxides are those wherein R is a heterocyclic group such
as pyrridine, pyrrole, imidazole, pyrrolidine, piperidine, quinoline, acridine
and
derivatives thereof.
Another class of said polyamine N-oxides comprises the group of polyamine N-
oxides wherein the nitrogen of the N-O group is attached to the R-group.
Other suitable polyamine N-oxides are the polyamine oxides whereto the N-O
group is attached to the polymerisable unit.
Preferred class of these polyamine N-oxides are the polyamine N-oxides having
the general formula (I) wherein R is an aromatic, heterocyclic or alicyclic
groups
wherein the nitrogen of the N-0 functional group is part of said R group.
Examples of these classes are polyamine oxides wherein R is a heterocyclic
compound such as pyrridine, pyrrole, imidazole and derivatives thereof.
Another preferred class of polyamine N-oxides are the polyamine oxides having
the general formula (I) wherein R are aromatic, heterocyclic or alicyclic
groups
wherein the nitrogen of the N-0 functional group is attached to said R groups.
Examples of these classes are polyamine oxides wherein R groups can be
aromatic such as phenyl.
Any polymer backbone can be used as long as the amine oxide polymer formed
is water-soluble and has dye transfer inhibiting properties. Examples of
suitable
polymeric backbones are polyvinyls, polyalkylenes, polyesters, polyethers,
polyamide, polyimides, polyacrylates and mixtures thereof.
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49
The amine N-oxide polymers of the present invention typically have a ratio of
amine to the amine N-oxide of 10:1 to 1:1000000. However the amount of amine
oxide groups present in the polyamine oxide polymer can be varied by
appropriate copolymerization or by appropriate degree of N-oxidation.
Preferably, the ratio of amine to amine N-oxide is from 2:3 to 1:1000000. More
preferably from 1:4 to 1:1000000, most preferably from 1:7 to 1:1000000. The
polymers of the present invention actually encompass random or block
copolymers where one monomer type is an amine N-oxide and the other
monomer type is either an amine N-oxide or not. The amine oxide unit of the
polyamine N-oxides has a PKa < 10, preferably PKa < 7, more preferred PKa <
6.
The polyamine oxides can be obtained in almost any degree of polymerisation.
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
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 laundry detergent and/or fabric care
compositions according to the present invention comprise a polymer selected
from N-vinylimidazole N-vinylpyrrolidone copolymers wherein said polymer has
an average molecular weight range from 5,000 to 50,000 more preferably from
8,000 to 30,000, most preferably from 10,000 to 20,000.
The average molecular weight range was determined by light scattering as
described in Barth H.G. and Mays J.W. Chemical Analysis Vol 113,"Modern
Methods of Polymer Characterization".
Highly preferred N-vinylimidazole N-vinylpyrrolidone copolymers have an
average molecular weight range from 5,000 to 50,000; more preferably from
8,000 to 30,000; most preferably from 10,000 to 20,000.
The N-vinylimidazole N-vinylpyrrolidone copolymers characterized by having
said average molecular weight range provide excellent dye transfer inhibiting
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properties while not adversely affecting the cleaning performance of laundry
detergent and/or fabric care compositions formulated therewith.
The N-vinylimidazole N-vinylpyrrolidone copolymer of the present invention has
a molar ratio of N-vinylimidazole to N-vinylpyrrolidone from 1 to 0.2, more
preferably from 0.8 to 0.3, most preferably from 0.6 to 0.4 .
c) Polyvinylpyrrolidone
The laundry detergent and/or fabric care compositions of the present invention
may also utilize polyvinylpyrrolidone ("PVP"} having an average molecular
weight
of from about 2,500 to about 400,000, preferably from about 5,000 to about
200,000, more preferably from about 5,000 to about 50,000, and most preferably
from about 5,000 to about 15,000. Suitable polyvinylpyrrolidones are
commercially vailable from ISP Corporation, New York, NY and Montreal,
Canada under the product names PVP K-15 (viscosity molecular weight of
10,000), PVP K-30 (average molecular weight of 40,000), PVP K-60 (average
molecular weight of 160,000), and PVP K-90 (average molecular weight of
360,000). Other suitable polyvinylpyrrolidones which are commercially
available
from BASF Cooperation include Sokalan HP 165 and Sokaian HP 12;
polyvinylpyrrolidones known to persons skilled in the detergent field (see for
example EP-A-262,897 and EP-A-256,696).
d) Polyvinyloxazolidone
The laundry detergent andlor fabric care compositions of the present invention
may also utilize polyvinyloxazolidone as a polymeric dye transfer inhibiting
agent. Said polyvinyloxazolidones have an average molecular weight of from
about 2,500 to about 400,000, preferably from about 5,000 to about 200,000,
more preferably from about 5,000 to about 50,000, and most preferably from
about 5,000 to about 15,000.
e) Polyvinylimidazole
The laundry detergent andlor fabric- care 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 50,000, and most preferably from
about 5,000 to about 15,000.
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f) Cross-linked polymers
Cross-linked polymers are polymers whose backbone are interconnected to a
certain degree; these links can be of chemical or physical nature, possibly
with
active groups n the backbone or on branches; cross-linked polymers have been
described in the Journal of Polymer Science, volume 22, pages 1035-1039.
In one embodiment, the cross-linked polymers are made in such a way that they
form a three-dimensional rigid structure, which can entrap dyes in the pores
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
Dispersants
The laundry detergent and/or fabric care composition of the present invention
can also further comprise dispersants. It has also been surprisingly found
that
the combination of a modified transferase with a dispersant provides,
refurbishes
or restores improved tensile strength, enhanced anti-wrinkle, anti-shrinkage,
anti-bobbling properties to fabrics, as well as provide better static control,
fabric
softness, colour appearance and fabric anti-wear properties and benefits. In
addition, improved cleaning benefits are achieved with said combination.
Suitable water-soluble organic salts are the homo- or co-polymeric acids or
their
salts, in which the polycarboxylic acid comprises at least two carboxyl
radicals
separated from each other by not more than two carbon atoms.
Polymers of this type are disclosed in GB-A-1,596,756. Examples of such salts
are polyacrylates of MW 2000-5000 and their copolymers with malefic anhydride,
such copolymers having a molecular weight of from 1,000 to 100,000.
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 laundry detergent and/or fabric care compositions of the
present
invention.
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52
The compositions of the invention may contain a lime soap peptiser compound,
which has preferably a lime soap dispersing power (LSDP), as defined
hereinafter of no more than 8, preferably no more than 7, most preferably no
more than 6. The lime soap peptiser compound is preferably present at a level
from 0% to 20% by weight.
A numerical measure of the effectiveness of a lime soap peptiser is given by
the
lime soap dispersant power (LSDP) which is determined using the lime soap
dispersant test as described in an article by H.C. Borghetty and C.A. Bergman,
J. Am. Oil. Chem. Soc., volume 27, pages 88-90, (1950). This lime soap
dispersion test method is widely used by practitioners in this art field being
referred to, for example, in the following review articles; W.N. Linfield,
Surfactant
science Series, Volume 7, page 3; W.N. Linfield, Tenside surf. det., volume
27,
pages 159-163, (1990); and M.K. Nagarajan, W.F. Masler, Cosmetics and
Toiletries, volume 104, pages 71-73, (1989). The LSDP is the % weight ratio of
dispersing agent to sodium oleate required to disperse the lime soap deposits
formed by 0.0258 of sodium oleate in 30m1 of water of 333ppm CaCo3
(Ca:Mg=3:2) equivalent hardness.
Surfactants having good lime soap peptiser capability will include certain
amine
oxides, betaines, sulfobetaines, alkyl ethoxysulfates and ethoxylated
alcohols.
Exemplary surfactants having a LSDP of no more than 8 for use in accord with
the present invention include C16-C1g dimethyl amine oxide, C12-C1g alkyl
ethoxysulfates with an average degree of ethoxylation of from 1-5,
particularly
C12-C15 alkyl ethoxysulfate surfactant with a degree of ethoxylation of amount
3 (LSDP=4), and the C14-C15 ethoxylated alcohols with an average degree of
ethoxylation of either 12 (LSDP=6) or 30, sold under the tradenames Lutensol
A012 and Lutensoi 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-
aminohexanoyl]benzene sulfonate and mixtures thereof; and nonanoyloxy
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53
benzene sulfonate together with hydrophilic I hydrophobic bleach formulations
can also be used as lime soap peptisers compounds.
Colour care and fabric care benefits
Technologies which provide a type of colour care benefit can also be included.
Examples of these technologies are metallo catalysts for colour maintenance.
Such metallo catalysts are described in copending European Patent Application
No. 92870181.2. Dye fixing agents, polyolefin dispersion for anti-wrinkles and
improved water absorbency, perfume and amino-functional polymer for colour
care treatment and perfume substantivity are further examples of colour care /
fabric care technologies and are described in the co-pending Patent
Application
No. 96870140.9, filed November 07, 1996.
Fabric softening agents can also be incorporated into laundry detergent and/or
fabric care 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 inctude 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 ingredients of fabric softening systems include high
molecular weight polyethylene oxide materials as disclosed in EP-A-0 299 575
and 0 313 146.
Preferably, the laundry detergent and/or compositions of the present invention
will comprise in addition to the modified transferase enzyme, a smectite clay.
It
has also been surprisingly found that the combination of a modified
transferase
with a smectite clay provides, refurbishes or restores improved tensile
strength,
enhanced anti-wrinkle, anti-shrinkage, anti-bobbling properties to fabrics, as
well
as provide better static control, fabric softness, colour appearance and
fabric
anti-wear properties and benefits. In addition, improved cleaning benefits are
achieved with said combination.
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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% to 5% by weight, normally
from
1 % to 3% by weight whilst the high molecular weight polyethylene oxide
materials and the water soluble cationic materials are added at levels of from
0.1 % to 2%, normally from 0.15% to 1.5% by weight. These materials are
normally added to the spray dried portion of the composition, although in some
instances it may be more convenient to add them as a dry mixed particulate, or
spray them as molten liquid on to other solid components of the composition.
Other surfactants
Ampholytic surfactants are also suitable for use in the laundry detergent
and/or
fabric care 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-solubifizing
group, e.g. carboxy, sulfonate, sulfate. See U.S. Patent No. 3,929,678 to
Laughlin et al., issued December 30, 1975 at column 19, lines 18-35, for
examples of ampholytic surfactants.
When included therein, the laundry detergent and/or fabric care 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 are also suitable for use in laundry detergent and/or
fabric care 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.
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When included therein, the laundry detergent and/or fabric care 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.
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 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
'r .
R3(OR4)xN(R5)2
wherein R3 is an alkyl, hydroxyalkyl, or alkyl phenyl group or mixtures
thereof
containing from about 8 to about 22 carbon atoms; R4 is an alkylene or
hydroxyalkylene group containing from about 2 to about 3 carbon atoms or
mixtures thereof; x is from 0 to about 3; and each R5 is an alkyl or
hydroxyalkyl
group containing from about 1 to about 3 carbon atoms or a polyethylene oxide
group containing from about 1 to about 3 ethylene oxide groups. The R5 groups
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
amine oxides and Cg-C12 alkoxy ethyl dihydroxy ethyl amine oxides.
When included therein, the cleaning compositions of the present invention
typically comprise from 0.2% to about 15%, preferably from about 1 % to about
10% by weight of such semi-polar nonionic surfactants.
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The laundry detergent and/or fabric care composition of the present invention
may further comprise a cosurfactant selected from the group of primary or
tertiary amines.
Suitable primary amines for use herein include amines according to the formula
R1 NH2 wherein R1 is a Cg-C12, preferably Cg-C10 alkyl chain or R4X(CH2)n, X
is -O-,-C(O)NH- or -NH-, R4 is a Cg-C12 alkyl chain n is between 1 to 5,
preferably 3. R1 alkyl chains may be straight or branched and may be
interrupted with up to 12, preferably less than 5 ethylene oxide moieties.
Preferred amines according to the formula herein above are n-alkyl amines.
Suitable amines for use herein may be selected from 1-hexylamine, 1-
octylamine, 1-decylamine and laurylamine. Other preferred primary amines
include C8-C10 oxypropylamine, octyloxypropylamine, 2-ethylhexyl-
oxypropylamine, lauryl amido propylamine and amido propylamirie.
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
R3 is either a Cg-C12, preferably C6-C10 alkyl chain, or R3 is R4X(CH2)n,
whereby X is -O-, -C(O)NH- or -NH-,R4 is a C4-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 R4 may be linear or branched ; R3 alkyl chains may be interrupted with
up to 12, preferably less than 5, ethylene oxide moieties.
Preferred tertiary amines are R1 R2R3N where R1 is a C6-C12 alkyl chain, R2
and R3 are C1-C3 alkyl or
Rs
-C CHz-CH-O~H
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,
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preferably n is 3; R2 and R3 is C1-C4
Most preferred amines of the present invention include 1-octylamine, 1-
hexylamine, 1-decylamine, 1-dodecylamine,CB-l0oxypropylamine, N coco 1-
3diaminopropane, coconutalkyldimethylamine, lauryldimethylamine, lauryl
bis(hydroxyethyl)amine, coco bis(hydroxyehtyl)amine, lauryl amine 2 moles
propoxylated, octyl amine 2 moles propoxylated, lauryl
amidopropyldimethylamine, C8-10 amidopropyldimethylamine and C10 amido-
propyldimethylamine.
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.
Builder system
The laundry detergent and/or fabric care 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
aminopolyphosphonates, particularly ethylenediamine tetramethylene
phosphonic acid and diethylene triamine pentamethylenephosphonic acid.
Phosphate builders can also be used herein.
Suitable builders can be an inorganic ion exchange material, commonly an
inorganic hydrated aluminosilicate material, more particularly a hydrated
synthetic zeolite such as hydrated zeolite A, X, B, HS or MAP.
Another suitable inorganic builder material is layered silicate, e.g. SKS-6
(Hoechst). SKS-6 is a crystalline layered silicate consisting of sodium
silicate
(Na2Si205).
Suitable polycarboxylates containing one carboxy group include lactic acid,
glycolic acid and ether derivatives thereof as disclosed in Belgian Patent
Nos.
831,368, 821,369 and 821,370. Polycarboxylates containing two carboxy groups
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include the water-soluble salts of succinic acid, malonic acid,
(ethylenedioxy)
diacetic acid, malefic acid, diglycollic acid, tartaric acid, tartronic acid
and fumaric
acid, as well as the ether carboxylates described in German Offenlegenschrift
2,446,686, and 2,446,687 and U.S. Patent No. 3,935,257 and the sulfinyl
carboxylates described in Belgian Patent No. 840,623. Polycarboxylates
containing three carboxy groups include, in particular, water-soluble
citrates,
aconitrates and citraconates as well as succinate derivatives such as the
carboxymethyloxysuccinates described in British Patent No. 1,379,241,
lactoxysuccinates described in Netherlands Application 7205873, and the
oxypolycarboxylate materials such as 2-oxa-1,1,3-propane tricarboxylates
described in British Patent No. 1,387,447.
Polycarboxylates containing four carboxy groups include oxydisuccinates
disclosed in British Patent No. 1,261,829, 1,1,2,2-ethane tetracarboxylates,
1,1,3,3-propane tetracarboxylates and 1,1,2,3-propane tetracarboxyiates.
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
- cis, cis, cis-tetracarboxylates, 2,5-tetrahydro-furan -cis - dicarboxylates,
2,2,5,5-tetrahydrofuran - tetracarboxylates, 1,2,3,4,5,6-hexane -hexacar-
boxylates and and carboxymethyl derivatives of polyhydric alcohols such as
sorbitol, mannitol and xylitol. Aromatic poly-carboxylates include mellitic
acid,
pyromellitic acid and the phthalic acid derivatives disclosed in British
Patent No.
1,425,343.
Of the above, the preferred polycarboxylates are hydroxycarboxylates
containing
up to three carboxy groups per molecule, more particularly citrates.
Preferred builder systems for use in the present compositions include a
mixture
of a water-insoluble aluminosilicate builder such as zeolite A or of a layered
silicate (SKS-6), and a water-soluble carboxylate chelating agent such as
citric
acid.
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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 laundry detergent
and/or
fabric care 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.
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.
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 laundry detergent and/or fabric care compositions herein may also
optionally contain one or more iron and/or manganese chelating agents. Such
chelating agents can be selected from the group consisting of amino
carboxylates, amino phosphonates, polyfunctionally-substituted aromatic
chelating agents and mixtures therein, all as hereinafter defined. Without
intending to be bound by theory, it is believed that the benefit of these
materials
is due in part to their exceptional ability to remove iron and manganese ions
from washing solutions by formation of soluble chelates.
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Amino carboxylates useful as optional chelating agents include
ethylenediaminetetracetates, N-hydroxyethylethylenediaminetriacetates, nitrilo-
triacetates, ethylenediamine tetraproprionates, triethylenetetraamine-
hexacetates, 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
compositions of the invention when at lease low levels of total phosphorus are
permitted in laundry detergent and/or fabric care compositions, and include
ethylenediaminetetrakis (methylenephosphonates) as DEQUEST. Preferred,
these amino phosphonates to not contain alkyl or alkenyl groups with more than
about 6 carbon atoms.
Polyfunctionally-substituted aromatic chelating agents are also useful in the
compositions herein. See U.S. Patent 3,812,044, issued May 21, 1974, to
Connor et al. Preferred compounds of this type in acid form are
dihydroxydisulfobenzenes such as 1,2-dihydroxy-3,5-disulfobenzene.
A preferred biodegradable chelator for use herein is ethylenediamine
disuccinate ("EDDS"), especially the [S,S] isomer as described in U.S. Patent
4,704,233, November 3, 1987, to Hartman and Perkins.
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 laundry detergent and/or fabric care 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 suppressor
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Another optional ingredient is a suds suppressor, exemplified by silicones,
and
silica-silicone mixtures. Silicones can be generally represented by alkylated
polysiloxane materials while silica is normally used in finely divided forms
exemplified by silica aerogels and xerogels and hydrophobic silicas of various
types. These materials can be incorporated as particulates in which the suds
suppressor is advantageously releasably incorporated in a water-soluble or
water-dispersible, substantially non-surface-active detergent impermeable
carrier. Alternatively the suds suppressor can be dissolved or dispersed in a
liquid carrier and applied by spraying on to one or more of the other
components.
A preferred silicone suds controlling agent is disclosed in Bartoilota et al.
U.S.
Patent 3 933 672. Other particularly useful suds suppressors are the self-
emulsifying silicone suds suppressors, described in German Patent Application
DTOS 2 646 126 published April 28, 1977. An example of such a compound is
DC-544, commercially available from Dow Corning, which is a siloxane-glycol
copolymer. Especially preferred suds controlling agent are the suds suppressor
system comprising a mixture of silicone oils and 2-alkyl-alcanols. Suitable 2-
alkyl-alkanols are 2-butyl-octanol which are commercially available under the
trade name Isofol 12 R.
Such suds suppressor system are described in Copending European Patent
application N 92870174.7 filed 10 November, 1992.
Especially preferred silicone suds controlling agents are described in
Copending
European Patent application N°92201649.8. Said compositions can
comprise a
silicone/silica mixture in combination with fumed nonporous silica such as
AerosilR.
The suds suppressors described above are normally employed at levels of from
0.001 % to 2% by weight of the composition, preferably from 0.01 % to 1 % by
weight.
Preservatives
The laundry detergent andlor fabric care compositions herein may also
optionally contain one or more preservatives. The function of the
preservatives
is to prevent organismslmicro-organisms from breeding and growing in the
laundry detergent andlor fabric care composition and on the fabrics treated
with
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the compositions herein. In the absence of such preservatives, organisms/micro-
organisms could grow on the fabrics treated with the laundry detergent and/or
fabric care compositions herein because a significant amount of
carbohydrates/sugar could remain on the fabrics after treatment.
Sanitization of fabrics can be achieved by the compositions of the present
invention containing antimicrobial materials, e.g., antibacterial halogenated
compounds, quaternary compounds, and phenolic compounds.
Suitable preservatives for use with the present invention include, but are not
limited to, the following.
It is preferable to use a broad spectrum preservative, e.g., one that is
effective
on both bacteria (both gram positive and gram negative) and fungi. A limited
spectrum preservative, e.g., one that is only effective on a single group of
microorganisms, e.g., fungi, can be used in combination with a broad spectrum
preservative or other limited spectrum preservatives with complimentary and/or
supplementary activity. A mixture of broad spectrum preservatives can also be
used. In some cases where a specific group of microbial contaminants is
problematic (such as Gram negatives), aminocarboxylate chelators may be used
alone or as potentiators in conjunction with other preservatives. These
chelators
which include, e.g., ethylenediaminetetraacetic acid (EDTA),
hydroxyethylenediaminetriacetic acid, diethylenetriaminepentaacetic acid, and
other aminocarboxylate chelators, and mixtures thereof, and their salts, and
mixtures thereof, can increase preservative effectiveness against Gram-
negative
bacteria, especially Pseudomonas species.
Antimicrobial preservatives useful in the present invention include biocidal
compounds, i.e., substances that kill microorganisms, or biostatic compounds,
i.e., substances that inhibit and/or regulate the growth of microorganisms.
(1). Organic Sulfur Compounds
Preferred water-soluble preservatives for use in the present invention are
organic sulfur compounds. Some non-limiting examples of organic sulfur
compounds suitable for use in the present invention are:
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(a) 3-Isothiazolone Comaounds
A preferred preservative is an antimicrobial, organic preservative containing
3-
isothiazolone groups having the formula:
R /O
N
~Y
wherein
Y is an unsubstituted alkyl, alkenyl, or alkynyl group of from about 1 to
about 18
carbon atoms, an unsubstituted or substituted cycloalkyl group having from
about a 3 to about a 6 carbon ring and up to 12 carbon atoms, an unsubstituted
or substituted aralkyl group of up to about 10 carbon atoms, or an
unsubstituted
or substituted aryl group of up to about 10 carbon atoms;
R1 is hydrogen, halogen, or a (C1-C4) alkyl group; and
R2 is hydrogen, halogen, or a (C1-C4) alkyl group.
Preferably, when Y is methyl or ethyl, R1 and R2 should not both be hydrogen.
Salts of these compounds formed by reacting the compound with acids such as
hydrochloric, nitric, sulfuric, etc. are also suitable.
This class of compounds is disclosed in U.S. Pat. No. 4,265,899, Lewis et al.,
issued May 5, 1981, and incorporated herein by reference. Examples of said
compounds are: 5-chloro-2-methyl-4-isothiazolin-3-one; 2-n-butyl-3-
isothiazolone; 2-benzyl-3-isothiazolone; 2-phenyl-3-isothiazolone, 2-methyl-
4,5-
dichloroisothiazolone; ; 5-chloro-2-methyl-3-isothiazolone; 2-methyl-4-
isothiazolin-3-one; and mixtures thereof. A preferred preservative is a water-
soluble mixture of 5-chloro-2-methyl-4-isothiazolin-3-one and 2-methyl-4-
isothiazolin-3-one, more preferably a mixture of about 77% 5-chloro-2-methyl-4-
isothiazolin-3-one and about 23% 2-methyl-4-isothiazolin-3-one, a broad
spectrum preservative available as a 1.5% aqueous solution under the trade
name Kathon~ CG by Rohm and Haas Company.
When Kathon~ is used as the preservative in the present invention it is
present
at a level of from about 0.0001 % to about 0.01 %, preferably from about
0.0002% to about 0.005%, more preferably from about 0.0003% to about
0.003%, most preferably from about 0.0004% to about 0.002%, by weight of the
composition.
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Other isothiazolins include 1,2-benzisothiazolin-3-one, available under the
trade
name Proxel~ products; and 2-methyl-4,5-trimethylene-4-isothiazolin-3-one,
available under the trade name Promexal~. Both Proxel and Promexal are
available from Zeneca. They have stability over a wide pH range (i.e., 4-12).
Neither contain active halogen and are not formaldehyde releasing
preservatives. Both Proxel and Promexal are effective against typical Gram
negative and positive bacteria, fungi and yeasts when used at a level from
about
0.001 % to about 0.5%, preferably from about 0.005% to about 0.05%, and most
preferably from about 0.01 % to about 0.02% by weight of the usage
composition.
(b) Sodium PYrithione
Another preferred organic sulfur preservative is sodium pyrithione, with water
solubility of about 50%. When sodium pyrithione is used as the preservative in
the present invention it is typically present at a level of from about 0.0001%
to
about 0.01 %, preferably from about 0.0002% to about 0.005%, more preferably
from about 0.0003% to about 0.003%, by weight of the usage composition.
Mixtures of the preferred organic sulfur compounds can also be used as the
preservative in the present invention.
(2). -HaloQenated Compounds
Preferred preservatives for use in the present invention are haiogenated
compounds. Some non-limiting examples of halogenated compounds suitable
for use in the present invention are:
5-bromo-5-nitro-1,3-dioxane, available under the trade name Bronidox L~
from Henkel. Bronidox L~ has a solubility of about 0.46% in water. When
Bronidox is used as the preservative in the present invention it is typically
present at a level of from about 0.0005% to about 0.02%, preferably from about
0.001 % to about 0.01 %, by weight of the usage composition;
2-bromo-2-nitropropane-1,3-diol, available under the trade name Bronopol
~ from Inolex can be used as the preservative in the present invention.
Bronopol has a solubility of about 25% in water. When Bronopol is used as the
preservative in the present invention it is typically present at a level of
from
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about 0.002% to about 0.1 %, preferably from about 0.005% to about 0.05%, by
weight of the usage composition;
1,1'-hexamethylene bis(5-(p-chlorophenyl)biguanide), commonly known as
chlorhexidine, and its salts, e.g., with acetic and gluconic acids can be used
as a
preservative in the present invention. The digluconate salt is highly water-
soluble, about 70% in water, and the diacetate salt has a solubility of about
1.8%
in water. When chlorohexidine is used as the preservative in the present
invention it is typically present at a level of from about 0.0001 % to about
0.04%,
preferably from about 0.0005% to about 0.01 %, by weight of the usage
composition.
1,1,1-Trichloro-2-methylpropan-2-ol, commonly known as chlorobutanol,
with water solubility of about 0.8%; a typical effective level of
chlorobutanol is
from about 0.1 % to about 0.5%, by weight of the usage composition.
4,4'- (Trimethylenedioxy)bis-(3-bromobenzamidine) diisethionate, or
dibromopropamidine, with water solubility of about 50%; when
dibromopropamidine is used as the preservative in the present invention it is
typically present at a level of from about 0.0001 % to about 0.05%, preferably
from about 0.0005% to about 0.01 % by weight of the usage composition.
Mixtures of the preferred halogenated compounds can also be used as the
preservative in the present invention.
(3). Cvcl~ganic Nitrogen Compounds
Preferred water-soluble preservatives for use in the present invention are
cyclic
organic nitrogen compounds. Some non-limiting examples of cyclic organic
nitrogen compounds suitable for use in the present invention are:
(a) Imidazolidinedione Compounds
Preferred preservatives for use in the present invention are imidazolidione
compounds. Some non-limiting examples of imidazolidinedione compounds
suitable for use in the present invention are:
1,3-bis(hydroxymethyl)-5,5-dimethyl-2,4-imidazolidinedione, commonly
known as dimethyloldimethylhydantoin, or DMDM hydantoin, available as, e.g.,
Glydant~ from Lonza. DMDM hydantoin has a water solubility of more than
50% in water, and is mainly effective on bacteria. When DMDM hydantoin is
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used, it is preferable that it be used in ~ combination with a broad spectrum
preservative such as Kathon CG~, or formaldehyde. A preferred mixture is
about a 95:5 DMDM hydantoin to 3-butyl-2-iodopropynylcarbamate mixture,
available under the trade name Glydant Plus~ from Lonza. When Glydant Plus
~ is used as the preservative in the present invention, it is typically
present at a
level of from about 0.005% to about 0.2% by weight of the usage composition;
N-[1,3-bis(hydroxymethyl)2,5-dioxo-4-imidazolidinyl]-N,N'-
bis(hydroxymethyl) urea, commonly known as diazolidinyl urea, available under
the trade name German II~ from Sutton Laboratories, Inc. (Sutton) can be used
as the preservative in the present invention. When Germall II~ is used as the
preservative in the present invention, it is typically present at a level of
from
about 0.01 % to about 0.1 % by weight of the usage composition;
N,N"-methylenebis{N'-[1-(hydroxymethyl)-2,5-dioxo-4-imidazolidinyl]urea},
commonly known as imidazolidinyl urea, available, e.g., under the trade name
Abiol~ from 3V-Sigma, Unicide U-13~ from Induchem, Germall 115~ from
(Sutton) can be used as the preservative in the present invention. When
imidazolidinyl urea is used as the preservative, it is typically present at a
level of
from about 0.05% to about 0.2%, by weight of the usage composition.
Mixtures of the preferred imidazolidinedione compounds can also be used as
the preservative in the present invention.
(b) Polymethoxy Bicyclic Oxazolidine
Another preferred water-soluble cyclic organic nitrogen preservative is
polymethoxy bicyclic oxazolidine, having the general formula:
CH2(OCH2~H
O~N~O
where n has a value of from about 0 to about 5, and is available under the
trade
name Nuosept~ C from Huls America. When Nuosept~ C is used as the
preservative, it is typically present at a level of from about 0.005% to about
0.1 %, by weight of the usage composition.
Mixtures of the preferred cyclic organic nitrogen compounds can also be used
as
the preservative in the present invention.
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(4). Low Molecular Weight Aldehydes
(a). Formaldehyde
A preferred preservative for use in the present invention is formaldehyde.
Formaldehyde is a broad spectrum preservative which is normally available as
formalin which is a 37% aqueous solution of formaldehyde. When formaldehyde
is used as the preservative in the present invention, typical levels are from
about
0.003% to about 0.2%, preferably from about 0.008% to about 0.1 %. more
preferably from about 0.01 % to about 0.05%, by weight of the usage
composition.
(b) Glutaraldehyde
A preferred preservative for use in the present invention is glutaraldehyde.
Glutaraldehyde is a water-soluble, broad spectrum preservative commonly
available as a 25% or a 50% solution in water. When glutaraldehyde is used as
the preservative in the present invention it is typically present at a level
of from
about 0.005% to about 0.1 %, preferably from about 0.01 % to about 0.05%, by
weight of the usage composition.
(5). Quaternary Compounds
Preferred preservatives for use in the present invention are cationic andlor
quaternary compounds. Such compounds include polyaminopropyl biguanide,
also known as polyhexamethylene biguanide having the general formula:
HCLNH2-(CH2)3-[-(CH2)3-NH-C(=NH)-NH-C(=NH~HCI)-NH-(CH2)3-1x-(CH2)3-
NH-C(=NH)-NH~CN
Polyaminopropyl, biguanide is a water-soluble, broad spectrum preservative
which is available as a 20% aqueous solution available under the trade name
Cosmocil CQ~ from ICI Americas, Inc., or under the trade name Mikrokill~ from
Brooks, Inc.
1-(3-Chlorallyl) -3,5,7-triaza-1-azoniaadamantane chloride, available, e.g.,
under
the trade name Dowicil 200 from Dow Chemical, is an effective quaternary
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ammonium preservative; it is freely soluble in water; however, it has the
tendency to discolor (yellow), therefore it is not highly preferred.
Mixtures of the preferred quaternary ammonium compounds can also be used
as the preservative in the present invention.
When quaternary ammonium compounds are used as the preservative in the
present invention, they are typically present at a level of from about 0.005%
to
about 0.2%, preferably from about 0.01 % to about 0.1 %, by weight of the
usage
composition.
(6). Dehydroacetic Acid
A preferred preservative for use in the present invention is dehydroacetic
acid.
Dehydroacetic acid is a broad spectrum preservative preferably in the form of
a
sodium or a potassium salt so that it is water-soluble. This preservative acts
more as a biostatic preservative than a biocidal preservative. When
dehydroacetic acid is used as the preservative it is typically used at a level
of
from about 0.005% to about 0.2%, preferably from about 0.008% to about 0.1 %,
more preferably from about 0.01 % to about 0.05%, by weight of the usage
composition.
(7). Phenyl and Phenolic Compounds
Some non-limiting examples of phenyl and phenolic compounds suitable for use
in the present invention are:
4,4'-diamidino-a,w-diphenoxypropane diisethionate, commonly known as
propamidine isethionate, with water solubility of about 16%; and 4,4'-
diamidino-a
,w-diphenoxyhexane diisethionate, commonly known as hexamidine isethionate.
Typical effective level of these salts is about 0.0002% to about 0.05% by
weight
of the usage composition.
Other examples are benzyl alcohol, with a water solubility of about 4%; 2-
phenylethanol, with a water solubility of about 2%; and 2-phenoxyethanol, with
a
water solubility of about 2.67%; typical effective level of these phenyl and
phenoxy alcohol is from about 0.1 % to about 0.5%, by weight of the usage
composition.
(8) Mixtures thereof
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It is preferred that no, or essentially no, volatile low molecular weight
monohydric
alcohols such as ethanol and/or isopropanol are intentionally added to the
composition of the present invention since these volatile organic compounds
will
contribute both to flammability problems and environmental pollution problems.
If small amounts of iow molecular weight monohydric alcohols are present in
the
composition of the present invention due to the addition of these alcohols to
such things as perfumes and as stabilizers for some preservatives, it is
preferable that the level of monohydric alcohol be less than about 5%,
preferably
less than about 3%, more preferably less than about 1 %.
(9). Mixtures thereof
The preservatives of the present invention can be used in mixtures in order to
control a broad range of microorganisms.
Bacteriostatic effects can sometimes be obtained for aqueous compositions by
adjusting the composition pH to an acid pH, e.g., less than about pH 4,
preferably less than about pH 3, or a basic pH, e.g., greater than about 10,
preferably greater than about 11.
(10). Preferred areservatives
Preferably the preservatives used in the compositions of the present invention
are selected from the group consisting of: isothiazolones; bronopol;
hydantoins;
oxazolidines; glutaraldehyde; isethionates; quats (benzalkoniums); and
mixtures
thereof.
Others
Other components such as soil-suspending agents, soil-release agents, optical
brighteners, abrasives, bactericides, tarnish inhibitors, coloring agents,
and/or
encapsulated or non-encapsulated perfumes may be employed.
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.
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Other suitable water soluble encapsulating materials 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 material consists of a modified
maize starch and glucose. The starch is modified by adding monofunctional
substituted groups such as octenyl succinic acid anhydride.
Antiredeposition and soil suspension agents suitable herein include cellulose
derivatives such as methylcellulose, carboxymethylcellulose and
hydroxyethylcellulose, and homo- or co-polymeric polycarboxylic acids or their
salts. Polymers of this type include the polyacrylates and malefic anhydride-
acrylic acid copolymers previously mentioned as builders, as well as
copolymers
of malefic anhydride with ethylene, methylvinyl ether or methacrylic acid, the
malefic anhydride constituting at least 20 mole percent of the copolymer.
These
materials are normally used at levels of from 0.5% to 10% by weight, more
preferably from 0.75% to 8%, most preferably from 1 % to 6% by weight of the
composition.
Preferred optical brighteners are anionic in character, examples of which are
disodium 4,4'-bis-(2-diethanolamino-4-anilino -s- triazin-6-ylamino)stilbene-
2:2'
disulphonate, disodium 4, - 4'-bis-(2-morpholino-4-anilino-s-triazin-6-ylamino-
stilbene-2:2' - disulphonate, disodium 4,4' - bis-(2,4-dianilino-s-triazin-6-
ylamino)stilbene-2:2' - disulphonate, monosodium 4',4" -bis-(2,4-dianilino-s-
tri-
azin-6 ylamino)stilbene-2-sulphonate, disodium 4,4' -bis-(2-anilino-4-(N-
methyl-
N-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 the specific brighteners of copending European Patent
application No. 95201943.8.
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Other useful polymeric materials are the polyethylene glycols, particularly
those
of molecular weight 1000-10000, more particularly 2000 to 8000 and most
preferably about 4000. These are used at levels of from 0.20% to 5% more
preferably from 0.25% to 2.5% by weight. These polymers and the previously
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)0.25~T-PO)2.8(T-PEG)0.41T(PO
H)0.25((PEG)43CH3)0.75
where PEG is -(OC2H4)O-,PO is (OC3H60) and T is (pcOC6H4C0).
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
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 andlor 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
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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 laundry detergent and/or fabric care compositions.
Therefore, using chlorine 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 90101815 at p. 4 et seq., incorporated
herein by reference. Chemically, these materials comprise polyacrylates having
one ethoxy side-chain per every 7-8 acrylate units. The side-chains are of the
formula -(CH2CH20)m(CH2)nCH3 wherein m is 2-3 and n is 6-12. The side-
chains are ester-linked to the polyacrylate "backbone" to provide a "comb"
polymer type structure. The molecular weight can vary, but is typically in the
range of about 2000 to about 50,000. Such alkoxylated polycarboxylates can
comprise from about 0.05% to about 10%, by weight, of the compositions
herein.
Method of washing
The laundry detergent andlor fabric care compositions of the invention may be
used in essentially any washing, cleaning and/or fabric care methods,
including
soaking methods, pre-treatment methods, methods with rinsing steps for which a
separate rinse aid composition may be added and post-treatment methods.
An example of pre-treatment would consist of treating the fabric with a pre-
treatment composition comprising a transferase andlor its corresponding
enzymatic substrate. This step can be achieved already in the washing machine
or in a basin or this pre-treatment composition can be sprayed onto the
fabric.
Optionally, the pre-treated fabric is dried and is then washed/treated with a
conventional laundry detergent and/or fabric care composition (not comprising
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the transferase nor the substrate of the present invention). An example of
post-
treatment would consist of washing/treating the fabric with a conventional
laundry detergent and/or fabric care composition (not comprising the
transferase
nor the substrate of the present invention). Optionally, the fabric can be
dried.
The fabric would then be treated with a post-treatment composition comprising
a
transferase and/or its corresponding enzymatic substrate. The transferase
enzyme and /or its corresponding enzymatic substrate can also be incorporated
in a rinsing composition which is used at the end of a washing cycle.
In another example, the enzyme and the substrate can be comprised in different
compositions and/or added at different steps. For example, the pre-treatment
or
post-treatment composition comprises exclusively the transferase enzyme or its
corresponding enzymatic substrate and the conventional laundry detergent
and/or fabric care composition comprises exclusively the corresponding
enzymatic substrate or the transferase enzyme.
The process described herein comprises contacting fabrics with a laundering
solution in the usual manner and exemplified hereunder. The process of the
invention is conveniently carried out in the course of the cleaning process.
The
method of cleaning is preferably carried out at 5°C to 95°C,
especially between
10°C and 60°C. The pH of the treatment solution is preferably
from 7 to 12.
The following examples are meant to exemplify compositions of the present
invention, but are not necessarily meant to limit or otherwise define the
scope of
the invention.
In the laundry detergent and/or fabric care compositions, the enzymes levels
are
expressed by pure enzyme by weight of the total composition and unless
otherwise specified, the detergent ingredients are expressed by weight of the
total compositions. The abbreviated component identifications therein have the
following meanings:
~S : 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.
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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.
QAS : R2.N+(CH3)2(C2Fi40H) with R2 = C12-C14~
QAS 1 ; R2.N+(CH3)2(C2H40H) with R2 = Cg-C11.
APA : C8-10 amido propyl dimethyl amine.
Soap : Sodium linear alkyl carboxylate derived
from a 80/20
mixture of tallow and coconut fatty acids.
STS : Sodium toluene sulphonate.
CFAA : C12-C14 alkyl N-methyl glucamide.
TFAA : C16-C18 alkyl N-methyl glucamide.
TPKFA : C12-C14 topped whole cut fatty acids.
DEQA : Di-(tallow-oxy-ethyl) dimethyl ammonium
chloride.
DEQA (2) : Di-(soft-tallowyloxyethyl) hydroxyethyl
methyl
ammonium methylsulfate.
DTDMAMS : Ditalllow dimethyl ammonium methylsulfate.
SDASA : 1:2 ratio of stearyidimethyl amineariple-pressed
stearic
acid.
Silicate : Amorphous Sodium Silicate (Si02:Na20 ratio
= 1.6-
3.2).
Zeolite A : Hydrated Sodium Aluminosilicate of formula
Nal2(A102Si02)12. 27H20 having a primary particle
size in the range from 0.1 to 10 micrometers
(Weight
expressed on an anhydrous basis).
Na-SKS-6 : Crystalline layered silicate of formula
8-Na2Si205.
Citrate : Tri-sodium citrate dehydrate of activity
86.4% with a
particle size distribution between 425 and
850
micrometres.
Citric . : Anhydrous citric acid.
Borate : Sodium borate
Carbonate : Anhydrous sodium carbonate with a particle
size
between 200 and 900 micrometres.
Bicarbonate : Anhydrous sodium hydrogen carbonate with
a particle
size distribution between 400 and 1200 micrometres.
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Sulphate : Anhydrous sodium sulphate.
Mg Sulphate : Anhydrous magnesium sulfate.
STPP : Sodium tripolyphosphate.
TSPP : Tetrasodiurn pyrophosphate.
M,o,/Ap, : 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.
qq : Sodium polyacrylate polymer of average molecular
weight 4,500.
pg1 : Anhydrous sodium perborate monohydrate of
nominal
formula NaB02.H202.
pg4 : Sodium perborate tetrahydrate of nominal
formula
NaB02.3H20.H202.
Percarbonate : Anhydrous sodium percarbonate of nominal
formula
2Na2C03.3H202 .
TAED : Tetraacetylethylenediamine.
NOBS : Nonanoyloxybenzene sulfonate in the form
of the
sodium salt.
NACA-OBS : (6-nonamidocaproyl) oxybenzene sulfonate.
DTPA : Diethylene triamine pentaacetic acid.
HEDP : 1,1-hydroxyethane diphosphonic acid.
DETPMP : Diethyltriamine yenta (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
Photoactivated : Sulfonated zinc phtalocyanine encapsulated
in dextrin
Bleach soluble polymer.
Photoactivated : Sulfonated alumino phtalocyanine encapsulated
in
Bleach 1 dextrin soluble polymer.
Protease : Proteolytic enzyme sold under the tradename
Savinase, Alcalase, Durazym by Novo Nordisk
A/S,
Maxacal, Maxapem sold by Gist-Brocades and
proteases described in patents W091/06637
and/or
W095/10591 and/or EP 251 446.
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Amylase : Amylolytic enzyme sold under the tradename Purafact
Ox AmR described in WO 94/18314, W096105295
sold by Genencor; Termamyl~, Fungamyl~ and
Duramyl~, all available from Novo Nordisk A/S and
those described in W095/26397.
Lipase : Lipolytic enzyme sold under the tradename Lipolase,
Lipolase Ultra by Novo Nordisk A/S and Lipomax by
Gist-Brocades.
CBD-transferase : Transferase EC 2.4.1.5 sold by Sigma under the
tradename dextransucrase; Transferase EC 2.3.2.13
available from Novo Nordisk A/S under the tradename
Transglutaminase and/or Transferase EC 2.4.1.19
sold by Novo Nordisk A/S under the tradename
Toruzyme; linked by PEG(NPC)2 MW 3400 from
Sigma to the CBD Cellulozome from Clostridium
cellulovorans , sold under the tradename Cellulose
Binding Domain by Sigma; and/or
Transferase EC 2.4.1.5 sold by Sigma under the
tradename dextransucrase, linked by the Humicola
Insolens family 45 cellulase linker to the CBD of the
cellulytic enzyme sold under the tradename Carezyme
by Novo Nordisk A/S.
Substrate : Maltose, e.g. Maltose M5885 sold by Sigma and/or
starch, e.g. YES2760 sold by Sigma; an amino acid,
di/tri/poly/peptide and/or protein and/or cycodextrin (a,
~3, y) and/or sucrose.
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.
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Brightener 1 : Disodium 4,4'-bis(2-sulphostyryl)biphenyl.
Brightener 2 : Disodium 4,4'-bis(4-anilino-6-morpholino-1.3.5-triazin-
2-yl) stilbene-2:2'-disulfonate.
Silicone antifoam: Pofydimethylsiloxane 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.
Opacifier : Water based monostyrene latex mixture,
sold by BASF
Aktiengeseilschaft under the tradename Lytron
621.
SRP 1 : Anionically end capped poly esters.
SRP 2 : Diethoxylated poly (1,2 propylene terephtalate)
short
block polymer.
QEA : bis((C2H50)(C2H40)n)(CH3) -N+-C6H12-N+-(CH3)
bis((C2H50)-(C2H40))n, wherein n = from 20
to 30.
PEI : Polyethyleneimine with an average molecular
weight
of 1800 and an average ethoxytation degree
of 7
ethyleneoxy residues per nitrogen.
SCS : Sodium cumene sulphonate.
HMWPEO : High molecular weight polyethylene oxide.
PEGx : Polyethylene glycol, of a molecular weight
of x .
PEO : Polyethylene oxide, with an average molecular
weight
of 5,000.
TEPAE : Tetreaethylenepentaamine ethoxylate.
Example 1
The following high density laundry detergent compositions were prepared
according to the present invention
I II III IV V VI
LAS 8.0 8.0 8.0 2.0 6.0 6.0
TAS - 0.5 - 0.5 1.0 0.1
C46(S)AS 2.0 2.5 - - - -
C25AS - - - 7.0 4.5 5.5
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I II III IV V VI
C68AS 2.0 5.0 7.0 - - -
C25E5 - - 3.4 10.0 4.6 4.6
C25E7 3.4 3.4 1.0 - - -
C25E3S - - - 2.0 5.0 4.5
QAS - 0.8 - _ _ _
QAS 1 - - - 0.8 0.5 1.0
Zeolite A 18.1 18.0 14.1 18.1 20.0 18.1
Citric - - - 2.5 - 2.5
Carbonate 13.0 13.0 27.0 10.0 10.0 13.0
Na-SKS-6 - - - 10.0 - 10.0
Silicate 1.4 1.4 3.0 0.3 0.5 0.3
Citrate - 1.0 - 3.0 - -
Sulfate 26.1 26.1 26.1 6.0 - -
Mg sulfate 0.3 - - , 0.2 - 0.2
MA/AA 0.3 0.3 0.3 4.0 1.0 1.0
CMC 0.2 0.2 0.2 0.2 0.4 0.4
PB4 9.0 9.0 5.0 - _ _
Percarbonate - - - - 18.0 18.0
TAED 1.5 0.4 1.5 - 3.9 4.2
NACA-OBS - 2.0 1.0 - - -
DETPMP 0.25 0.25 0.25 0.25 - -
SRP 1 - - - 0.2 - 0.2
EDDS - 0.25 0.4 - 0.5 0.5
CFAA - 1.0 - 2.0 - _
HEDP 0.3 0.3 0.3 0.3 0.4 0.4
QEq - - - 0.2 - 0.5
CBD-transferase 1.0 0.1 0.05 0.02 0.1 0.5
Substrate 0.1 - 5.0 - 10.0 15.0
Protease 0.009 0.009 0.01 0.04 0.05 0.03
Amylase 0.002 0.002 0.002 0.006 0.008 0.008
Cellulase 0.0007 - - 0.0007 0.0007 0.0007
Lipase 0.006 - - 0.01 0.01 0.01
Photoactivated 15 15 15 - 20 20
bleach (ppm)
PVNO/PVPVI - - - 0.1 - -
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1 II III IV V VI
Brightener 1 0.09 0.09 0.09 - 0.09 0.09
Perfume 0.3 0.3 0.3 0.4 0.4 0.4
Silicone antifoam 0.5 0.5 0.5 - 0.3 0.3
Density in g/litre 850 850 850 850 850 850
Miscellaneous and minors Up to 100%
Example 2
The following granular laundry detergent compositions of particular utility
under
European machine wash conditions were prepared according to the present
invention
I II III IV V VI
BAS 5.5 7.5 5.0 5.0 6.0 7.0
TAS 1.25 1.9 - 0.8 0.4 0.3
C24AS/C25AS - 2.2 5.0 5.0 5.0 2.2
C25E3S - 0.8 1.0 1.5 3.0 1.0
C45E7 3.25 - - - - 3.0
TFAA - - 2.0 - - -
C25E5 - 5.5 - - - -
QAS 0.8 - -
QAS 1 - 0.7 1.0 0.5 1.0 0.7
STPP 19.7 - - - - -
Zeolite A - 19.5 25.0 19.5 20.0 17.0
NaSKS-6/citric- 10.6 - 10.6 - -
acid (79:21
)
Na-SKS-6 - - . 9.0 - 10.0 10.0
Carbonate 6.1 21.4 9.0 10.0 10.0 18.0
Bicarbonate - 2.0 7.0 5.0 - 2.0
Silicate 6.8 - - 0.3 0.5 -
Citrate - - 4.0 4.0 - -
Sulfate 39.8 - - 5.0 - 12.0
Mg sulfate - - 0.1 0.2 0.2 -
MA/AA 0.5 1.6 3.0 4.0 1.0 1.0
CMC 0.2 0.4 1.0 1.0 0.4 0.4
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I II III IV V VI
PB4 5.0 12.7 - _ _ _
Percarbonate - - - - 18.0 15.0
TAED 0.5 3.1 - - 5.0 -
NACA-OBS 1.0 3.5 - - - 2.5
DETPMP 0.25 0.2 0.3 0.4 - 0.2
HEDP - 0.3 - 0.3 0.3 0.3
QEA - - 1.0 1.0 1.0 -
CBD- 0.02 1.5 0.1 0.5 0.0008 0.02
transferase
Substrate - 0.1 5.0 10.0 12.0 0.1
Protease 0.009 0.03 0.03 0.05 0.05 0.02
Lipase 0.003 0.003 0.006 0.006 0.006 0.004
Cellulase 0.0006 0.0006 0.0005 0.0005 0.0007 0.0007
Amylase 0.002 0.002 0.006 0.006 0.01 0.003
PVNO/PVPVI - - 0.2 0.2 - -
PVP 0.9 1.3 - - - 0.9
SRP 1 - - 0.2 0.2 0.2 -
Photoactivated15 27 - - 20 20
bleach (ppm)
Photoactivated15 - - - - -
bleach 1 (ppm)
Brightener 0.08 0.2 - - 0.09 0.15
1
Brightener - 0.04 - - - -
2
Perfume 0.3 0.5 0.4 0.3 0.4 0.3
Silicone 0.5 2.4 0.3 0.5 0.3 2.0
antifoam
Density in 750 750 750 750 750 750
g/litre
Miscellaneousd minors Up to
an 100%
Example 3
The following detergent compositions of particular utility under European
machine wash conditions were prepared according to the present invention
I II III IV
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I 11 III IV
Blown Powder
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
DETPMP 0.4 0.4 0.2 0.4
Spray On
Brightener 0.02 - - 0.02
C45E7 - - ~ - 5.0
C45E2 2.5 2.5 2.0 -
C45E3 2.6 2.5 2.0 -
Perfume 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 1 0.5 - - 0.5
Na-SKS-6 10.0 - - -
Percarbonate 18.5 - - -
PB4 - 18.0 10.0 21.5
TAED 2.0 2.0 - 2.0
NACA-OBS 3.0 2.0 4.0 -
CBD-transferase 0.005 1.0 0.1 0.2
Substrate - 0.1 10.0 10.0
Protease 0.03 0.03 0.03 0.03
Lipase 0.008 0.008 0.008 0.004
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I II III IV
Amylase 0.003 0.003 0.003 0.006
Brightener 1 0.05 - - 0.05
Miscellaneous and minors Up to 100%
Example 4
The following granular detergent compositions were prepared according to the
present invention
I II III IV V VI
Blown Powder
LAS 23.0 8.0 7.0 9.0 7.0 7.0
TAS - - - - 1.0 -
C45AS 6.0 6.0 5.0 8.0 - -
C45AES - 1.0 1.0 1.0 - -
C45E35 - - - - 2.0 4.0
Zeolite A 10.0 18.0 14.0 12.0 10.0 10.0
MAIAA - 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 14.3 11.0 15.0 19.3
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 2 0.3 0.2 0.3 - 0.1 0.3
Spray On
C45E7 - 2.0 - - 2.0 2.0
C25E9 3.0 - - - - -
C23E9 - - 1.5 2.0 - 2.0
Perfume 0.3 0.3 0.3 2.0 0.3 0.3
Agglomerates
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
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I II III IV V Vi
Carbonate - 4.0 4.0 5.0 - 4.0
PEG 4000 - 0.5 0.5 - - 0.5
Misc (Water etc.)- 2.0 2.0 2.0 - 2.0
Dry additives
QAS - - - - 1.0 -
Citric - - - - 2.0 -
PB4 - - - - 12.0 1.0
PB1 4.0 1.0 3.0 2.0 - -
Percarbonate - - - - 2.0 10.0
Carbonate - 5.3 1.8 - 4.0 4.0
NOBS 4.0 - 6.0 - - 0.6
Methyl cellulose0.2 - - - - -
Na-SKS-6 8.0 - - - - -
STS - - 2.0 - 1.0 -
Culmene sulfonic- 1.0 - - - 2.0
acid
CBD-transferase 0.025 0.8 0.5 0.01 0.025 0.8
Substrate - 0.1 10.0 5.0 0.02 -
Protease 0.02 0.02 0.02 0.01 0.02 0.02
Lipase 0.004 - 0.004 - 0.004 0.008
Amylase 0.003 - 0.002 - 0.003 -
Cellulase 0.0005 0.0005 0.00050.0007 0.0005 0.0005
PVPVI - - - - 0.5 0.1
PVP - - - - 0.5 -
PVNO - - 0.5 0.3 - -
QEA - - - - 1.0 -
SRP 1 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 -
Miscellaneous minors Up to
and 100%
Example 5
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The following nil bleach-containing detergent compositions of particular use
in
the washing of coloured clothing were prepared according to the present
invention
Blown Powder
Zeolite A 15.0 15.0 -
Sulfate - 5.0 -
LAS 3.0 3.0 -
DETPMP 0.4 0.5 -
CMC 0.4 0.4 -
MA/AA 4.0 4.0 -
Agglome~ates
C45AS - - 11.0
LAS 6.0 5.0 -
TAS 3.0 2.0 -
Silicate 4.0 4.0 -
Zeolite A 10.0 15.0 13.0
CMC - - 0.5
MA/AA - - 2.0
Carbonate 9.0 7.0 ~.0
Spray-on
Perfume 0.3 0.3 0.5
C45E7 4.0 4.0 4.0
C25E3 2.0 2.0 2.0
Dry additives
MA/AA - - 3.0
Na-SKS-6 - - 12.0
Citrate 10.0 - 8~0
Bicarbonate 7.0 3.0 5.0
Carbonate 8.0 5.0 7.0
PVPVI/PVNO 0.5 0.5 0.5
CBD-transferase 0.001 1.0 0.01
Substrate 0.1 - 5.0
Protease 0.03 0.02 0.05
Lipase 0.008 0.008 0.008
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I II III
Amylase 0.01 0.01 0.01
Cellulase 0.001 0.001 0.001
Silicone antifoam 5.0 5.0 5.0
Sulfate - 9.0 -
Density (g/litre) 700 700 700
Miscellaneous and minors Up to 100%
Examale 6
The following detergent
compositions were prepared
according to the present
invention
1 II III IV
Base granule
Zeolite A 30.0 22.0 ~ 24.0 10.0
Sulfate 10.0 5.0 10.0 7.0
MA/AA 3.0 - -
p - 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
C45AES - 1.0 1.0 -
Silicate - 1.0 0.5 10.0
Soap - 2.0 - -
Brightener 1 0.2 0.2 0.2 0.2
Carbonate 6.0 9.0 10.0 10.0
PEG 4000 - 1.0 1.5 -
DTPA - 0.4 - -
Spray On
C25E9 - - - 5~0
C45E7 1.0 1.0 - -
C23E9 - 1.0 2.5 -
Perfume 0.2 0.3 0.3
Dry additives
Carbonate 5.0 10.0 18.0 8.0
PVPVI/PVNO 0.5 - 0.3 -
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I II 111 IV
CBD-transferase 1.0 0.01 0.5 0.1
Substrate 0.1 - 10.0 10.0
Protease 0.03 0.03 0.03 0.02
Lipase 0.008 - - 0.008
Amylase 0.002 - - 0.002
Cellulase 0.0002 0.0005 0.0005 0.0002
NOBS - 4.0 - 4.5
PB1 1.0 5.0 1.5 6.0
Sulfate 4.0 5.0 - 5.0
SRP 1 - 0.4 - -
Suds suppressor - 0.5 0.5
Miscellaneous and Up to 100%
minors
Example 7
The following granular according
detergent compositions to the
were prepared
present invention
Blown Powder
Zeolite A 20.0 - 15.0
STPP - 20.0 -
Sulfate - - 5.0
Carbonate - - 5.0
TAS - - 1.0
LAS 6.0 6.0 fi.0
C68AS 2.0 2.0 -
Silicate 3.0 8.0 -
MA/AA 4.0 2.0 2.0
CMC 0.6 0.6 0.2
Brightener 1 0.2 0.2 0.1
DETPMP 0.4 0.4 0.1
STS - - 1.0
Spray On
C45E7 5.0 5.0 4.0
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I II III
Silicone antifoam 0.3 0.3 0.1
Perfume 0.2 0.2 0.3
Dry additives
QEA - - 1.0
Carbonate 14.0 9.0 10.0
PB1 1.5 2.0 -
PB4 18.5 13.0 13.0
TAED 2.0 2.0 2.0
QAS - - 1.0
Photoactivated bleach 15 ppm 15 ppm 15
ppm
Na-SKS-6 - - 3.0
CBD-transferase 0.001 1.0 0.01
Substrate - - 5.0
Protease 0.03 0.03 0.007
Lipase 0.004 0.004 0.004
Amylase 0.006 0.006 0.003
Cellulase 0.0002 0.0002 0.0005
Sulfate 10.0 20.0 5.0
Density (g/litre) 700 700 700
Miscellaneous and minors Up to 100%
Examele 8
The following detergent compositions were prepared according to the present
invention
Blown Powder
Zeolite A 15.0 15.0 15.0
Sulfate - 5.0 -
LAS 3.0 3.0 3.0
QAS - 1.5 1.5
DETPMP 0.4 0.2 0.4
EDDS - 0.4 0.2
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I II III
CMC 0.4 0.4 0.4
MA/AA 4.0 2.0 2.0
Agglomerate
LAS 5.0 5.0 5.0
TAS 2.0 2.0 1.0
Silicate 3.0 3.0 4.0
Zeolite A 8.0 8.0 8.0
Carbonate 8.0 8.0 4.0
Spray On
Perfume 0.3 0.3 0.3
C45E7 2.0 2.0 2.0
C25E3 2.0 - -
Dry Additives
Citrate 5.0 - 2.0
Bicarbonate - 3.0 -
Carbonate 8.0 15.0 10.0
TAED 6.0 2.0 5.0
PB1 14.0 7.0 10.0
PEO - - 0.2
Bentonite clay - - 10.0
CBD-transferase 0.025 0.5 0.1
Substrate 0.01 - 12.0
Protease 0.03 0.03 0.03
Lipase 0.008 0.008 0.008
Cellulase 0.001 0.001 0.001
Amylase 0.01 0.01 0.01
Silicone antifoam 5.0 5.0 5.0
Sulfate - 3.0 -
Density (g/litre) 850 850 850
Miscellaneous and minors Up to 100%
Example 9
The following detergent to the present
compositions were prepared
according
invention
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1 II III IV
~S 18.0 14.0 24.0 20.0
QAS 0.7 1.0 - 0.7
TFAA - 1.0 - _
C23E56.5 - - 1.0 -
C45E7 - 1.0 - -
C45E3S 1.0 2.5 1.0 -
STPP 32.0 18.0 30.0 22.0
Silicate 9.0 5.0 9.0 8.0
Carbonate 11.0 7.5 10.0 5.0
Bicarbonate - 7.5 - -
pg1 3.0 1.0 - -
PB4 - 1.0 - _
NOBS 2.0 1.0 - -
DETPMP - 1.0 - -
DTPA 0.5 - 0.2 0.3
SRP 1 0.3 0.2 - 0.1
Mq/qp 1.0 1.5 2.0 0.5
CMC 0.8 Ø4 0.4 0.2
PEI - - 0.4
Sulfate 20.0 10.0 20.0 30.0
Mg sulfate 0.2 - 0.4 0.9
CBD-transferase 0.001 0.5 0.01 0.5
Substrate - 0.05 5.0 10.0
Protease 0.03 0.03 0.02 0.02
Amylase 0.008 0.007 - 0.004
Lipase 0.004 - 0.002 -
Cellulase 0.0003 - - 0.0001
Photoactivated bleach 30 ppm 20 ppm - 10 ppm
Perfume 0.3 0.3 0.1 0.2
Brightener 1/2 0.05 0.02 0.08 0.1
Miscellaneous and minors up to 00%
1
Example 10
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The following liquid detergent formulations were prepared according to the
present invention (Levels are given in parts per weight, enzyme are expressed
in
pure enzyme)
I II III IV V
LAS 11.5 8.8 - 3.9 -
C25E2.5S - 3.0 18.0 - 16.0
C45E2.25S 11.5 3.0 - 15.7 -
C23E9 - 2.7 1.8 2.0 1.0
C23E7 3.2 - - - -
C FAA - - 5.2 - 3.1
TPKFA 1.6 - 2.0 0.5 2.0
Citric (50%) 6.5 1.2 2.5 4.4 2.5
Ca formate 0.1 0.06 0.1 - -
Na formate 0.5 0.06 0.1 0.05 0.05
SCS 4.0 1.0 3.0 1.2 -
Borate 0.6 - 3.0 2.0 2.9
Na hydroxide 5.8 2.0 3.5 3.7 2.7
Ethanol 1.75 1.0 3.6 4.2 2.9
1,2 Propanediol 3.3 2.0 8.0 7.9 5.3
Monoethanolamine 3.0 1.5 1.3 2.5 0.8
TEPAE 1.6 - 1.3 1.2 1.2
CBD-transferase 0.001 0.01 1.0 0.05 0.5
Substrate 0.1 - 0.01 - 10.0
Protease 0.03 0.01 0.03 0.02 0.02
Lipase - - 0.002 - -
Amylase - - - 0.002 -
Cellulase - - 0.0002 0.0005 0.0001
SRP 1 0.2 - 0.1 - _
DTPA - - 0.3 - -
PVNO - - 0.3 - 0.2
Brightener 1 0.2 0.07 0.1 - -
Silicone antifoam 0.04 0.02 0.1 0.1 0.1
Miscellaneous and
water
Examale 11
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The following liquid detergent formulations were prepared according to the
present invention (Levels are given in parts per weight, enzyme are expressed
in
pure enzyme)
I II III IV
LqS 10.0 13.0 9.0 -
C25AS 4.0 1.0 2.0 10.0
C25E3S 1.0 - - 3.0
C25E7 6.0 8.0 13.0 2.5
TFAA _ _ - 4.5
APA - 1.4 - -
TPKFA 2.0 - 13.0 7.0
Citric 2.0 3.0 1.0 1.5
Dodecenyl / tetradecenyi 12.0 10.0 - -
succinic
acid
Rapeseed fatty acid 4.0 2.0 1.0 -
Ethanol 4.0 4.0 7.0 2.0
1,2 Propanediol 4.0 4.0 2.0 7.0
Monoethanolamine - - - 5.0
Triethanolamine ' - - 8.0 -
TEPAE 0.5 - 0.5 0.2
DETPMP 1.0 1.0 0.5 1.0
CBD-transferase 0.01 0.01 0.01 0.001
Substrate 5.0 - 5.0 0.1
Protease 0.02 0.02 0.01 0.008
Lipase - 0.002 - 0.002
Amylase 0.004 0.004 0.01 0.008
Cellulase - - - 0.002
SRP 2 0.3 - 0.3 0.1
Boric acid 0.1 0.2 1.0 2.0
Ca chloride - 0.02 - 0.01
Brightener 1 - 0.4 - -
Suds suppressor 0.1 0.3 - 0.1
Opacifier 0.5 0.4 - 0.3
NaOH up to pH 8.0 8.0 7.6 7.7
Miscellaneous and water
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example 12
The following liquid detergent compositions were prepared according to the
present invention (Levels are given in parts per weight, enzyme are expressed
in
pure enzyme)
I II III IV
LAS 25.0 - - _
C25AS - 13.0 18.0 15.0
C25E3S - 2.0 2.0 4.0
C25E7 - - 4.0 4.0
TFAA - 6.0 8.0 8.0
APA 3.0 1.0 2.0 -
TPKFA - 15.0 11.0 11.0
Citric 1.0 1.0 1.0 1.0
Dodecenyl / tetradecenyi 15.0 - - -
succinic
acid
Rapeseed fatty acid 1.0 - 3.5 -
Ethanol 7.0 2.0 3.0 2.0
1,2 Propanediol 6.0 8.0 10.0 13.0
Monoethanolamine - - 9.0 9.0
TEPAE - - 0.4 0.3
DETPMP 2.0 1.2 1.0 -
CBD-transferase 0.01 1.0 0.05 0.5
Substrate 5.0 0.01 - 10.0
Protease 0.08 0.02 0.01 0.02
Lipase - - 0.003 0.003
Amylase 0.004 0.01 0.01 0.01
Cellulase - - 0.004 0.003
SRP 2 - - 0.2 0.1
Boric acid 1.0 1.5 2.5 2.5
Bentonite clay 4.0 4.0 - -
Brightener 1 0.1 0.2 0.3 -
Suds suppressor 0.4 - - -
Opacifier 0.8 0.7 - -
NaOH up to pH 8.0 7.5 8.0 8.2
Miscellaneous and water
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Example 13
The following liquid detergent compositions were prepared according to the
present invention (Levels are given in parts by weight, enzyme are expressed
in
pure enzyme)
LAS 27.6 18.9
C45AS 13.8 5.9
C13E8 3.0 3.1
Oleic acid 3.4 2.5
Citric 5.4 5.4
Na hydroxide 0.4 3.6
Ca Formate 0.2 0.1
Na Formate - 0.5
Ethanol 7.0 -
Monoethanoiamine 16.5 8.0
1,2 propanediol 5.9 5.5
Xylene sulfonic acid - 2.4
TEPAE 1.5 0.8
Protease 0.05 0.02
CBD-transferase 0.05 0.5
Substrate - 10.0
PEG - 0.7
Brightener 2 0.4 0.1
Perfume 0.5 0.3
Water and Minors
Example 14
The following granular fabric detergent compositions which provide "softening
through the wash" capability were prepared according to the present invention
I II
C45AS - 10.0
LAS 7.6 -
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I II
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
Na-SKS-6 - 11.0
Zeolite A 15.0 15.0
MA~,4,q 4.0 4.0
DETPMP 0.4 0.4
pg1 15.0 -
Percarbonate - 15.0
TAED 5.0 5.0
Smectite clay 10.0 10.0
HMWPEO - 0.1
CBD-transferase 0.001 0.01
Substrate - 5.0
Protease 0.02 0.01
Lipase 0.02 0.01
Amylase 0.03 0.005
Cellulase 0.001 -
Silicate 3.0 5.0
Carbonate 10.0 10.0
Suds suppressor 1.0 4.0
CMC 0.2 0.1
Miscellaneous and minors Up to 100%
Examele 15
The following rinse added fabric softener composition was prepared according
to
the present invention
DEQA (2) 20.0
CBD-transferase 0.5
S a bstrate 0.1
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Cellulase 0.001
HCL 0.03
Antifoam agent 0.01
Blue dye 25ppm
CaCl2 0.20
Preservatives 0.05
Perfume 0'90
Miscellaneous and water Up to 100%
Example 16
The following fabric softener and dryer added fabric conditioner compositions
were prepared according to the present invention
I II III IV V
DEQA 2.6 19.0 - - _
DEQA(2) - - - - 51.8
DTMAMS - - - 26.0 -
SDASA - - 70.0 42.0 40.2
Stearic acid of 0.3 - - - -
IV=0
Neodol45-13 - - 13.0 - -
Hydrochioride 0.02 0.02 - - -
acid
Ethanol - - 1.0 - -
CBD-transferase 0.001 0.5 0.01 0.1 0.001
Substrate - 0.1 5.0 5.0 1.0
Perfume 1.0 1.0 0.75 1.0 1.5
Glycoperse S-20 - - - - 15.4
Glycerol - - - 26.0 -
monostearate
Digeranyl Succinate- - 0.38 - -
Silicone antifoam0.01 0.01 - - -
Electrolyte - 0.1 - -
Clay - - - 3.0 -
Preservatives 0.05 0.05 - - -
Dye 10ppm 25ppm 0.01 - -
Water and minors 100% 100% - - -
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Example 17
The following laundry bar detergent compositions were prepared according to
the present invention (Levels are given in parts per weight, enzyme are
expressed in pure enzyme)
I II III VI V III VI V
LpS - - 19.0 15.0 21.0 6.75 8.8 -
C28AS 30.0 13.5 - - - 15.75 11.2 22.5
Na Laurate 2.5 9.0 - - - - - -
Zeolite A 2.0 1.25 - - - 1.25 1.25 1.25
Carbonate 20.0 3.0 13.0 8.0 10.0 15.0 15.0 10.0
Ca Carbonate27.5 39.0 35.0 - - 40.0 - 40.0
Sulfate 5.0 5.0 3.0 5.0 3.0 - - 5.0
TSPP 5.0 - - - - 5.0 2.5 -
STPP 5.0 15.0 10.0 - - 7.0 8.0 10.0
Bentonite - 10.0 - - 5.0 - - -
clay
DETPMP - 0.7 0.6 - 0.6 0.7 0.7 0.7
CMC - 1.0 1.0 1.0 1.0 - - 1.0
Talc - - 10.0 15.0 10.0 - - -
Silicate - - 4.0 5.0 3.0 - - -
PVNO 0.02 0.03 - 0.01 - 0.02 - -
MA/AA 0.4 1.0 - - 0.2 0.4 0.5 0.4
SRP 1 0.3 0.3 0.3 0.3 0.3 0.3 0.3 0.3
CBD- 0.001 0.05 0.5 0.01 0.00 0.05 0.5 0.01
transferase 1
Substrate 0.1 5.0 8.0 5.0 - 0.1 2.0 5.0
Amylase - - 0.01 - - - 0.002 -
Protease - 0.004 - 0.003 0.00 - - 0.003
3
Lipase - 0.002 - 0.002 - - - -
Celluiase - .0003 - - .000 .0002 - -
3
PEO - 0.2 - 0.2 0.3 - - 0.3
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I II 111 VI V III VI V
Perfume 1.0 0.5 0.3 0.2 0.4 - - 0.4
Mg sulfate - - 3.0 3.0 3.0 - - -
Brightener 0.15 0.1 0.15 - - - - 0.1
Photo - 15.0 15.0 15.0 15.0 - - 15.0
activated
bleach (ppm)
Example 18
The following pre- or post treatment compositions were prepared in accord with
the present invention
I II III IV V VI
DEQA (2) - - 20.0 - 20.0 20.0
CBD-transferase0.8 0.05 0.05 0.005 0.05 0.15
Substrate - 10.0 10.0 1.0 0.1 5.0
Cellulase - - 0.001 - 0.001 0.001
HCL - - 0.03 - 0.03 0.03
Antifoam agent- - 0.01 - 0.01 0.01
Blue dye 25ppm 25ppm 25ppm 25ppm 25ppm 25ppm
CaCl2 - - 0.20 - 0.20 0.20
Preservatives 0.05 0.05 0.05 0.05 0.05 0.05
Perfume 0.90 0.90 0.90 0.90 0.90 0.90
Water / minors Up to 100%
