Note: Descriptions are shown in the official language in which they were submitted.
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WO 96/20997 PCT/US95/16432
_ DETERGENT COMPOSITION COMPRISING CELLULASE ENZYME
AND NONIONIC CELLULOSE ETHER
Field of the invention
The present invention relates to detergent compositions for improved
clay stain removal comprising a nonionic polysaccharide ether and a
celluiolytic enzyme.
Back4round of the Invention
During the laundering operation of fabrics it is highly desirable to
provide the fabric, particularly man-made fabrics produced from synthetic
fibres, with soil release properties.
Due to the hydrophobic nature of fabrics composed of partially or
completely synthetic fibres, the removal of greasy soils and stains therefrom
is particularly difficult. In order to address this problem, soil release
polymers may be incorporated into the detergent composition. During
laundering the soil release agents are adsorbed onto the surface of the
fabric, thereby inducing greater hydrophobicity to the fabric surface. Once
the fabric is treated with a soil release agent, the ease of removal of soils
and stains from the surface of the fabric is considerably improved.
The main types of soil release agents incorporated info detergent
compositions, which provide benefits to primarily hydrophobic synthetic
fabrics include synthetic soil release agents, preferably terephthalate based
and polysaccharide ethers. Polysaccharide ethers such as cellulose ethers
have been described for example in GB 1 534 641, which discloses
nonionic surtactant detergent compositions comprising cellulose ether soil
release agents such as alkyl and hydroxyalkyl cellulose ethers.
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The soil release performance of the polysaccharide ethers may be
improved upon greasy/oily stains by increasing the degree of substitution '
and the chain length of the subsitutent. This results in the polysaccharide
ether being only weakly and temporarily bound to the fabric surtace and
thus easily removed once soiling has occurred.
The soil release performance of the polysaccharide ethers may
further improved by increasing the amount of polysaccharide ether used and
or by increasing the molecular weight or degree of polymerisation (dp).
t-lowever, high molecular weight polysaccharide ethers are known to have
detrimental effects on the clay soil removal and anti-redeposition
performance of the detergent composition in which they are incorporated.
This is particularly evident on fabrics after a number of repeated washing
cycles or when high dosage or concentrations of detergent composition are
utilised to clean heavily soiled fabric. Furthermore, this problem is also
~~cute on fabrics which contain a high percentage of synthetic fibres.
During the laundering operation it is also desirable reduce the effects
of aging on the fabrics. Aging of naturally based fabrics results in the
damage of the top surface fibres which increases the number of soil
collection sites and results in the fabric gaining an unhomogeneous feel.
This may be addressed by the incorporation of cellulolytic enzymes into
detergent compositions. The cellulolytic enzyme removes the damaged
surface fibres and thereby improves stain removal, fabric appearance and
reduces the hardness of the fabric after multiple washing. However, the
celfulolytic enzyme by its very nature hydrolyses and depolymerises
polysaccharide ethers having 1,4 (3-glucosidic bonds. This problem of
cellulase and polysaccharide ether incompatibility is particularly acute for
low substituted polysaccharide ethers which appear more 'cellufosic' in
nature.
Thus, it is an aim of the present invention to provide a detergent ,
composition comprising a cellufolytic enzyme and a nonionic
polysaccharride ether, whereby the soil release performance of the
polysaccharide is enhanced by the presence of the cellulolytic enzyme.
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3
It has now been found that this objective can be achieved by the use
of selected nonionic polysaccharide ethers having specified degrees of
' polymerisation and substitution. It is believed that the nonionic
polysaccharide ethers of the present invention can be deposited onto the
fabric surface prior to the start of degradation by the cellulolytic enzyme .
fn addition, a further advantage of the present invention is that the
subsequent celfulolytic enzyme attack upon the polysaccharides after their
deposition on the fabric, aids the removal of trapped particulate soils and
clay soil removal.
Another advantage of the present invention is that high molecular
nonionic polysaccharide ethers may be used in combination with cellulase
to provide soil release benefits without affecting the clay soil removal
performance.
A further advantage of the present invention is that the detergent
conposition delivers improved whiteness performance and fabric feel.
Nonionic polysacchairdes and cellulolytic enzymes have been
described in the art. EPO 495 257 discloses a compact detergent
composition comprising high activity cellulolytic enzyme. Anti-redeposition
agents such as cellulose derivatives are disclosed, in particular methyl
cellulose, carboxymethyfcellulose (CMC) and hydroxyethyl cellulose. Only
CMC and cellulolytic enzyme is exemplified and there is no disclosure of the
specific combination of cellulolytic enzyme and cellulose ether.
EPO 320 296 discloses fabric softening additives for detergent
compositions comprising a water soluble nonionic ethyl hydroxyethyl
cellulose having an HLB of 3.3 to 3.8, a dp of 50 to 1200 and a ds of 1.9 to
2.9. Enzymes including cellulolytic enzyme are disclosed. 't'he combination
of cellulose ether and cellulolytic enzyme is not exemplified.
EPO 213 730 discloses detergent compositions with fabric softening
properties comprising a nonionic substituted cellulose ether derivative,
having a ds of from 1.9 to 2.9 and dp of 50 to 1200. Enzymes such as
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4
cellulolytic enzyme are mentioned The combination of cellulose ether and
celluolytic enzyme is not exemplified.
EPO 173 397 discloses detergent compositions comprising a cationic
softening agent and a fungal cellulolytic enzyme. Soil suspending agents such
as water soluble salts of CMC, carboxyhydroxymethyl cellulose are disclosed.
Their preferred dp or ds values are not mentioned.
Summary of the Invention
The present invention is directed to a detergent composition comprising the
following: (a) 1 % to 80% by weight of a detergent surfactant; (b) a nonionic
polysaccharide ether having a 1,4 ~-glucosidic bond, a degree of
polymerization of 100 or more and a degree of substitution of from 0.5 to 2.8
inclusive; (c) a cellulolytic enzyme; (d) 0.1 % to 10% by weight of a
chelating
agent selected from the group consisting of amino carboxylates,
aminophosphonates, dihydroxydisulfobenzenes and mixtures thereof; and (e)
0.01 % to 10% by weight of a dye transfer inhibiting agent selected from the
group consisting of polyamine N-oxide polymers, copolymers of N-
vinylpyrrolidone and N-vinylimidazole and mixtures thereof.
All amounts, weights and ratios as used herein are as a % weight of the
detergent composition.
Detailed Description of the Invention
Nonionic Polysaccharide Ethers
According to the present invention an essential component of the
detergent composition is a nonionic polysaccharide ether having a 1, 4 f3-
glucosidic bond. Chemically, the polysaccharides are composed of pentoses or
hexoses. Suitable polysaccharide ethers for use herein are selected from
CA 02206523 2000-06-28
4a
cellulose ethers, starch ethers, dextran ethers and mixtures thereof.
Preferably
said nonionic polysaccharide ether is a cellulose ether. Cellulose ethers are
generally obtained from vegetable tissues and fibres, including cotton and
wood pulp.
The hydroxy group of the anhydro glucose unit of cellulose can be
reacted with various reagents thereby replacing the hydrogen of the hydroxyl
group with other chemical groups. Various alkylating and hydroxyalkylating
agents can be reacted with cellulose ethers to produce either alkyl-,
hydroxyalkyl- or alkylhydroxyalkyl-cellulose ether or mixtures.
CA 02206523 2000-06-28
5
thereof. fihe most preferred for use in the present invention are C1-C4 alkyl
cellulosei ether or a C1-C4 hydroxyalkyl cellulose ether or a C1-C4
alkylhyd~oxy alkyl cellulose ether or mixtures thereof. Preferably the
polysaccharides of the present invention have a degree of substitution of
from 0.5 to 2.8, preferably from 0.5 to 2.2, most preferably from 0.5 to 2
inclusive.
Suikable cellulose ethers include methylcellulose ether, hydroxypropyl
methylc~llulose ether, hydroxyethyl methylcellulose ether, hydroxypropyl
cellulose ether, hydroxybutyl methylcellulose ether, ethylhydroxy
ethylcellulose ether, ethylcellulose ether and hydroxy ethylcellulose ether.
Most preferably said polysaccharide is a methylcellulose ether. Such
agents are commercially available such as METHOCEL (Dow Chemicals)
and 8enmocol (Nobel). The nonionic polysaccharides of the present
invention in addition to the nonionic substituent may also be partially
charged. For example by replacing one of the hydroxy groups with an
anionic group.
Ac,~ording to the present invention said polysaccharide ether has a
degree of polymerisation of more than 100. As used herein the term degree
of polymierisation (dp) is the ratio of the weight average molecular weight on
average molecular unit weight, i.e. dp=MWH,IMUW. The weight average
molecular weight (MWw) is obtained by standard analytical methods as
describeid in Polymer handbooks. A preferred method is light scattering from
polymer solutions as originally defined by Debye.
For example the average molecular unit weight (MUW) for
methylc~llulose ether may be determined from the sum of the molecular
weight of the unsubstituted cellulose unit and the product of the degree of
polymerisation and the molecular weight of the substituent less the
hydrogen mass ( 1 ).
i.e, MUW= 162 + (15-1)' ds -for methyl substituents found in methyl
cellulose ethers.
MUW may also be determined from the "°~ methoxyl content" value
(mc) alsi~ used by manufactures of methyl cellulose ethers instead of the
degree Qf substitution, such that;
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MUW= 100 - [(mol. wt. of CH2/mol. wt. of OCH3)*mc]
l-he compositions of the present invention comprise from 0.01 °~ to
10°~, '
preferably from 0.01 °~ to 3%, most preferably from 0.1 °~ to 2%
of said
nonionic polysaccharide ethers.
Cellulolvtic enzyme
In the present specification and claims, the terms "cellulase" and
"cellulolytic" denote an enzyme that hydrolyses cellulose. The cellulase
component may be a component occurring in a cellulase system produced
b~y a given microorganism, such a cellufase system mostly comprising
several different cellulase enzyme components including those usually
identified as e.g. cellobiohydrolases, exo-cellobiohydrolases,
endoglucanases, [i-glucosidases.
Alternatively, the cellulase component may be a single component, i.e.
a component essentially free of other cellulase components usually
occurring in a cellulase system produced by a given microorganism, the
single component being a recombinant component, i.e. produced by cloning
of a DNA sequence encoding the single component and subsequent cell
transformed with the DNA sequence and expressed in a host, cf. e.g.
International Patent Applications WO 91/17243 and WO 91/17244 which
are hereby incorporated by reference. The host is preferably a heterofogous
host, but the host may under certain conditions also be the homologous
host.
The term "particulate soil removal", as used herein, refers to enhanced
cleaning of cellulose-containing fabrics or garment, e.g. cotton,
contaminated by particles of soil or of other insoluble matter entrapped by
microfibrills spreading out on the fibre surtace.
The term "retaining-type activity", as used herein, is intended to mean
the stereochemical course of hydrolysis catalysed by a cellulase wherein
the mechanism (of a retaining glycosidase) is as shown in Chem. Rev., 90,
p. 1171-1202 (1990) (Sinott, M.L.: Catalytic mechanism of enzymatic
gfycosyl transfer). Both the cleavage product leaving the active site of the
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cellulase having retaining-type activity as well as the substrate _is in ~i-
con-
figuration, cf. Eur. J. Biochem, 217, p. 947-953 (1993).
The term "inverting-type activity", as used herein, is intended to mean
the stereochemical course of hydrolysis catalysed by a cellulase wherein
the mechanism (of an inverting glycosidase) is as shown in Chem. Rev., 90,
p. 1171-1202 (1990) (Sinott, M.L.: Catalytic mechanism of enzymatic
glycosyl transfer) and Eur. J. Biochem, 217, p. 947-953 (1993).
The stereochemistry of hydrolysis of the giycosidic bond is firmly
dictated by the structure and topology of the enzyme active site and is
usually interpreted as the result of a single-displacement or double
displacement catalytic mechanism. It is believed that all enzymes in a given
cellulase family, cf. Gene (Amst.), 81, p. 83-95 (1989) and Biochem. J., 293,
p. 781-788 (1993), have a similar fold even when their amino acid
conservation is extremely low, and it is furthermore shown that members of
a given cellulase family all have the same general fold and topology (J.
Biochem, 217, p. 947-953 (1993)).
Furthermore, it is contemplated that the cellulase may have an exo-
mode of action, the term "exo-mode of action" being intended to mean initi-
ating degradation of cellulose from the non-reducing chain ends by remov-
ing cellobiose units.
Alternatively, it is contemplated that the cellulase may have an endo-
mode of action, the "endo-mode of action" being intended to mean hydrolys-
ing amorphous regions of low crystallinity in cellulose fibres.
The term "domain", as used herein, is intended to indicate an amino
acid sequence capable of effecting a specific task. For example is the term
"carbohydrate binding domain" or "cellulose binding domain" ("CBD")
intended to indicate an amino acid sequence capable of effecting binding of
the enzyme to a carbohydrate substrate, in particular cellulose, and the term
"catalytic active domain" ("CAD") is intended to indicate an amino sequence
capable of effecting catalytic cleavage and having one or more active sites.
A CBD is an example of a non-catalytic domain. CAD's and CBD's may be
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8
finked or attached by (inking regions. Cf. Trends Biotechnol., 5, p. 255-261
(1987) and Microbiol. Rev., 55, p. 303-315 (1991).
The term "core enzyme", as used herein, is intended to indicate an
enzyme consisting essentially of a single domain, i.e. a catalytic active
domain, the core enzyme having no "tail".
The term "activity towards dyed microcrystalline cellulose" as used
herein refers to a hydrolytic activity towards microcrystalfine cellulose
covalently labelled with a light absorbing/fluorogenic compound, e.g. a
reactive dye, determined spectroscopically by measuring the liberation of la-
belled products resulting from hydrolysis under conditions simulating
washing conditions with respect to alkaline pH, temperature, duration, agita-
tion and detergent concentrations.
Accordingly, a cellulase exhibiting catalytic activity towards dyed
microcrystalfine cellulose must be active in releasing labelled soluble prod-
ucts from modified microcrystalline cellulose under simulated washing con-
ditions.
The term "activity towards short cellooiigosaccharides" as used herein,
refers to an activity towards cellooligosaccharides containing two glucose
units and an additional leaving group, such as e.g. a glucose unit, or a
modified glucose unit, or a chromogeniclfluorogenic group, or other groups,
resulting in splitting the glycosidic bond and measured as reducing end
recovery or chromogenic or fluorogenic label compound liberation under
hydrolysis under conditions simulating washing conditions with respect to
alkaline pH, temperature, duration, agitation and detergent concentrations.
Accordingly, a cellufase exhibiting a catalytic activity towards short
celloofigosaccharides must be active in hydrolysis of short cellooligo-
saccharides under washing conditions, the cellooligosaccharides containing
two glucose units and an additional leaving group, such as e.g. a glucose .
unit, or a modified glucose unit, or a chromogenic/fluorogenic group, or
other groups.
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In the present context, the term "immunoreactive" is intended to indi-
cate that the produced protein is reactive with an antibody raised against a
' native cellulose- or tiemicellulose-degrading enzyme.
fn the present context, the term "homologue" is intended to indicate a
polypeptide encoded by DNA which hybridizes to the same probe as the
DNA coding for the cellulase component with the amino acid sequence in
question under certain specifred conditions (such as presoaking in 5xSSC
and prehybridising for 1 h at ~40°C in a solution of 20% formamide,
SxDenhard't's solution, 50 mM sodium phosphate, pH 6.8, and 50 p,g of
denatured sonicated calf thymus DNA, followed by hybridization in the same
solution supplemented with 100 p,M ATP for 18 h at ~40°C). The term is
intended to include derivatives of the sequence in question obtained by
addition of one or more amino acid residues to either or both the C- and N-
terminal of the native sequence substitution of one or more amino acid
residues at one or more sites in the native sequence, deletion of one or
more amino acid residues at either or both ends of the native amino acid
sequence or at one or more sites within the native sequence, or insertion of
one or more amino acid residues at one or more sites in the native
sequence. It is to be understood that any derivative also hybridizes to the
same probe as mentioned above which indicates that the cellufase enzyme
derivatives within the scope of the present invention all have the same
advantageous activity and effect as the cellulase component having the
amino acid sequence in question. Also, any additions or substitutions or
deletions or insertions may preferably relate to a relatively limited number
of
amino acids of the sequence in question, i.e. minor additions, substitutions,
deletions or insertions, since it is to be expected that major additions,
substitutions, deletions or insertions may result in cellufase components
(polypeptides) which do not fulfil the above-mentioned hybridizing
requirement.
The present invention relates to a detergent composition comprising a
cellulase having retaining-type activity and being capable of particulate soil
removal or a cellulase having multiple domains comprising at least one non-
catalytic domain attached to a catalytic domain and being capable of colour
clarification. Preferably the celiulase is a single (recombinant) component.
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l
The celluiase may be obtained from the microorganism in question by
use of any suitable technique. For instance, a cellulase preparation may be
obtained by fermentation of a microorganism and subsequent isolation of a
c;ellulase containing preparation from the fermented broth or microorganism
by methods known in the art, but more preferably by use of recombinant
DNA techniques as known in the art. Such method normally comprises
cultivation of a host cell transformed with a recombinant DNA vector capable
of expressing and carrying a DNA sequence encoding the cellulase
component in question, in a culture medium under conditions permitting the
expression of the enzyme and recovering the enzyme from the culture.
CLONING A DNA SEQUENCE ENCODING A CELLULASE
The DNA sequence encoding a parent cellulase may be isolated from
any cell or microorganism producing the cellufase in question by various
methods, well known in the art. First a genomic DNA and/or cDNA library
should be constructed using chromosomal DNA or messenger RNA from the
organism that produces the cellulase to be studied. Then, if the amino acid
sequence of the cellufase is known, homologous, labelled oligonucleotide
probes may be synthesized and used to identify cellulase-encoding clones
from a genomic library of bacterial DNA, or from a fungal cDNA library.
Alternatively, a labelled oligonucleotide probe containing sequences
homologous to cellulase from another strain of bacteria or fungus could be
used as a probe to identify ceilulase-encoding clones, using hybridization
and washing conditions of lower stringency.
Yet another method for identifying celluiase-producing clones would
involve inserting fragments of genomic DNA into an expression vector, such
a5 a plasmid, transforming cellufase-negative bacteria with the resulting
genomic DNA library, and then plating the transformed bacteria onto agar
containing a substrate for cellufase. Those bacteria containing cellulase-
bearing plasmid will produce colonies surrounded by a halo of clear agar,
due to digestion of the substrate by secreted cellulose.
Alternatively, the DNA sequence encoding the enzyme may be
prepared synthetically by established standard methods, e.g. the
phosphoamidite method described by S.L. Beaucage and M.H. Caruthers,
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Tetrahedron Letters 22, 1981, pp. 1859-1869, or the method described by
Matthes et al., The EMBO J. 3, 1984, pp. 801-805. According to the
phosphoamidite method, oligonucleotides are synthesized, e.g. in an
automatic DNA synthesizer, purified, annealed, ligated and cloned in
appropriate vectors.
Finally, the DNA sequence may be of mixed genomic and synthetic,
mixed synthetic and cDNA or mixed genomic and cDNA origin prepared by
ligating fragments of synthetic, genomic or cDNA origin (as appropriate), the
fragments corresponding to various parts of the entire DNA sequence, in
accordance with standard techniques. The DNA sequence may also be pre-
pared by polymerase chain reaction (PCR) using specific primers, for
instance as described in US 4,683,202 or R. K. Saiki et al., Science 239,
1988, pp. 487-491.
EXPRESSION OF CELLULASE VARIANTS
According to the invention, a mutated ce(lulase-coding sequence
produced by methods described above, or any alternative methods known in
the art, can be expressed, in enzyme form, using an expression vector
which typically includes control sequences encoding a promoter, operator,
ribosome binding site, translation initiation signal, and, optionally, a
repressor gene or various activator genes. To permit the secretion of the ex-
pressed protein, nucleotides encoding a "signal sequence" may be inserted
prior to the cellulase-coding sequence. For expression under the direction
of control sequences, a target gene to be treated according to the invention
is operably linked to the control sequences in the proper reading frame.
Promoter sequences that can be incorporated into plasmid vectors, and
which can support the transcription of the mutant cellulase gene, include but
are not limited to the prokaryotic t3-lactamase promoter (Villa-Kamaroff, et
al., 1978, Proc. Natl. Acad. Sci. U.S.A. 75:3727-3731 ) and the tac promoter
(DeBoer, et al., 1983, Proc. Natl. Acad. Sci. U.S.A. 80:21-25). Further
references can aiso be found in "Useful proteins from recombinant bacteria"
in Scientific American, 1980, 242:74-94.
According to one embodiment B. subtilis is transformed by an
expression vector carrying the mutated DNA. If expression is to take place
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in a secreting microorganism such as B. subtilis a signal sequence may
follow the translation initiation signal and precede the DNA sequence of
interest. The signal sequence acts to transport the expression product to the
'
cell wall where it is cleaved from the product upon secretion. The term
"control sequences" as defined above is intended to include a signal
sequence, when is present.
fn a currently preferred method of producing cellulase variants of the
invention, a filamentous fungus is used as the host organism. The
filamentous fungus host organism may conveniently be one which has
previously been used as a host for producing recombinant proteins, e.g. a
strain of Asper4illus sp., such as A. ni4er, A. nidulans or A. orvzae. The use
of A. orvzae in the production of recombinant proteins is extensively
described in, e.g. EP 238 023.
For expression of cellulase variants in Asperpillus, the DNA sequence
coding for the cellulase variant is preceded by a promoter. The promoter
may be any DNA sequence exhibiting a strong transcriptional activity in
~lsper4illus and may be derived from a gene encoding an extracellular or
intracellular protein such as an amylase, a glucoamylase, a protease, a
lipase, a cellulase or a glycofytic enzyme.
Examples of suitable promoters are those derived from the gene
encoding A. onrzae TAKA amylase, Rhizomucor miehei aspartic proteinase,
A. ni er neutral a-amylase, A. ni er acid stable a-amylase, A. niyer
giucoamylase, Rhizomucor miehei lipase, A. orvzae alkaline protease or A.
orvzae triose phosphate isomerase.
In particular when the host organism is A. o ae, a preferred promoter
for use in the process of the present invention is the A. o ae TAKA
amylase promoter as it exhibits a strong transcriptional activity in A.
oryzae.
The sequence of the TAKA amylase promoter appears from EP 238 023.
Termination and pofyadenylation sequences may suitably be derived
from the same sources as the promoter.
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The techniques used to transform a fungal host cell may suitably be as
described in EP 238 023.
To ensure secretion of the cellulase variant from the host cell, the DNA
sequence encoding the cellulase variant may be preceded by a signal
sequence which may be a naturally occurring signal sequence or a
functional part thereof or a synthetic sequence providing secretion of the
protein from the cell. fn particular, the signal sequence may be derived from
a gene encoding an Asper4illus sp. amylase or glucoamylase, a gene
encoding a Rhizomucor miehei lipase or protease, or a gene encoding a
Humicola cellufase, xylanase or lipase. The signal sequence is preferably
derived from the gene encoding A. o ae TAKA amylase, A. nicer neutral a
-amylase, A. nicer acid-stable a-amylase or A. ni er glucoamylase.
The medium used to culture the transformed host cells may be 'any
conventional medium suitable for growing Asper4illus cells. The
transformants are usually stable and may be cultured in the absence of
selection pressure. However, if the transformants are found to be unstable,
a selection marker introduced into the cells may be used for selection.
The mature cellulase protein secreted from the host cells may
conveniently be recovered from the culture medium by well-known
procedures including separating the cells from the medium by centrifugation
or filtration, and precipitating proteinaceous components of the medium by
means of a salt such as ammonium sulphate, followed by chromatographic
procedures such as ion exchange chromatography, affinity chromatography,
or the like.
Both the cellulase may be recombinant (single), i.e. produced by clon-
ing of the DNA sequence encoding the single component and cell transform-
ation with the DNA sequence and expression in a host which may be hetero-
fogous or homologous. However, the celluiase may also be cloned and
expressed in the same heterologous or homologous host.
Accordingly, the detergent composition claimed in the present
invention should preferably comprise the cellulase in a concentration corre-
sponding to a concentration in the resulting washing liquor of from 0.001 mg
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to 100 mg, preferably from 0.005mg to 50mg of cellulase protein per litre of
washing liquor.
Preferably, the cellulase is a fungal or bacterial cellulase component,
i.e. of fungal or bacterial origin.
It is contemplated that the cellulase may be derived or isolated and
purified from microorganisms which are known to be capable of producing
celluloiytic enzymes, e.g. species of Humicola, Bacillus, Trichoderma, Fu-
sarium, Myceliophthora, Phanerochaete, Schizophyllum, Penicillium, As-
peraillus, and Geotricum. The derived components may be either ho-
mologous or heterofogous components. Preferably, the components are
homologous. However, a heterologous component which is immunoreactive
with an antibody raised against a highly purified cellulase component
possessing the desired property or properties and which heterologous
component is derived from a specific microorganism is also preferred.
Preferably, the cellulase exhibits catalytic activity on low molecular
weight carbohydrate substrates, especially a catalytic activity on cellotriose
at pH 8.5 corresponding to kit of at least 0.01 s 1 .
The cellulase may be inadequate or unable of providing colour clarifi-
cation, thus exhibiting low catalytic activity on dyed microcrystaliine
cellulo-
se.
In a preferred embodiment of the invention, the celluiase is a core
enzyme, i.e. a cellulase having no "tail" or being a single domain protein.
A convenient cellulase useful in the detergent composition of the
present invention may be a cellobiohydrolase component which is immuno-
reactive with an antibody raised against a highly purified "'70kD cellobiohy- -
drolase (EC 3.2.1.91 ) derived from Humicola insoiens, DSM 1800, or which
i: a homologue or derivative of the ~70kD cellobiohydrofase exhibiting
cellulase activity. A preferred cellobiohydrolase component has the amino
acid sequence disclosed in Nucleic Acid Research, vol. 18 (1990), page 668
(De Oiiviera, Alzevedo, M. and Radford, A.) which is shown in the appended
SEQ ID N0:1 or a variant of said cellobiohydrolase having an amino acid
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IS
sequence being at least 60%, preferably at least 70%, more preferably 75%,
more preferably at least 80%, more preferably 85%, especially at least 90%
' homologous with said sequence.
Another preferred celfobiohydrolase component is a core enzyme
("core CBH I") having an amino acid sequence consisting of 449 amino
acids corresponding to the (partial) amino acid sequence numbered 1-449
of the appended SEQ ID N0:1. The core CBH I has an apparant molecular
weight of ~48 kD.
Alternatively, the cellulase may be an endoglucanase component
which is immunoreactive with an antibody raised against a highly purified
'50kD endoglucanase derived from Humicola insolens, DSM 1800, or which
is a homologue or derivative of the ~50kD endogiucanase exhibiting
cellulase activity. A preferred endogiucanase component has the amino acid
sequence disclosed in PCT Patent Application No. W091 /17244, Fig. 14A-
E, which is shown in the appended SEQ ID NO:2, or a variant of said
endoglucanase having an amino acid sequence being at least 60%,
preferably at least 70%, more preferably 75%, more preferably at least
80°~,
more preferably 85%, especially at least 90% homologous with said
sequence.
Alternatively, the celluiase may be an endoglucanase component
which is immunoreactive with an antibody raised against a highly purified
'50kD (apparant molecular weight, the amino acid composition corresponds
to 45kD with 2n glycosylation sites) endoglucanase derived from Fusarium
oxysporum, DSM 2672, or which is a homologue or derivative of the "'SOkD
endoglucanase exhibiting cellulase activity. A preferred endoglucanase
component has the amino acid sequence disclosed in PCT Patent Applica-
tion No. W091117244, Fig. 13, which is shown in the appended SEQ ID
N0:3, or a variant of said endoglucanase having an amino acid sequence
being at least 60%, preferably at least 70%, more preferably 75%, more pre-
ferably at least 80%, more preferably 85%, especially at least 90%
homologous with said sequence.
The endoglucanse herein referred to as EG I-F cellulase component is
producible by Aspergillus oryzae after transformation with a piasmid
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16
containing the DNA sequence corresponding to the amino acid sequence of
the appended SEQ ID N0:3 and using the conventional Taka promotor and
AMG terminator. The EG I-F may be purified to homogeneity using cationic '
c~,hromatography and has a pl >9. The calculated pl is 9 based on the amino
~3cid composition using the PHKa values from Adv. Protein Chem. 17, p. 69- '
165 (1962)(C. Tanford). The molar exctinction coefficient is calculated to be
58180.
Yet another preferred cellulose may be any of the cellulases disclosed
in the published European Patent Application No. EP-A2-271 004, the
cellulose having a non-degrading index (NDI) of not less than 500 and being
an alkalophilic cellulose having an optimum pH not less than 7 or whose
relative activity at a pH of not less than 8 is 50% or over. of the activity
under
optimum conditions when carboxy methyl cellulose (CMC) is used as a
substrate; the cellulose preferably being selected from the group consisting
of alkaline cellulose K (produced by Bacillus sp. KSM-635, FERM BP 1485);
alkaline cellulose K-534 (produced by Bacillus sp. KSM-534, FERM BP
1508); alkaline cellulose K-539 (produced by Bacillus sp. KSM-539, FERM
BP 1509); alkaline cellulose K-577 (produced by Bacillus sp. KSM-577,
FERM BP 1510); alkaline cellulose K-521 (produced by Bacillus sp. KSM-
521, FERM BP 1507); alkaline cellulose K-580 (produced by Bacillus sp.
KSM-580, FERM BP 1511 ); alkaline cellulose K-588 (produced by Bacillus
sp. KSM-588, FERM BP 1513); alkaline cellulose K-597 (produced by
B~acilius sp. KSM-597, FERM BP 1514); alkaline cellulose K-522 (produced
by Bacillus sp. KSM-522, FERM BP 1512); CMCase I, CMCase II (both
produced by Bacillus sp. KSM-635, FERM BP 1485); alkaline cellulose E-II
and alkaline cellulose E-III (both produced by Bacillus sp. KSM-522, FERM
BP 1512).
Altemativefy, the cellulose may be capable of colour clarification and
has multiple domains, i.e. one or more catalytic domains attached to one or
more non-catalytic domains, e.g. cellulose binding domains, since the
activity in respect of colour clarification is enhanced by the presence of
e.g.
a cellulose binding domain.
This cellulose may have retaining-type activity or inverting-type
activity.
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17
Preferably, the cellulase exhibits high catalytic activity on
' cellodextrin(s), more preferably on relatively long-chained cellodextrin(s),
especially on reduced longer-chained cellodextrin(s).
In a preferred embodiment of the invention, the cellulase exhibits high
catalytic activity on dyed microcrystalline cellulose, especially on Red
Avicel.
Cellulase useful as colour clarifying components in the detergent
composition of the present invention usually exhibits essentially no catalytic
activity on low molecular weight carbohydrate substrates. Preferably, the
cellulase has a catalytic activity on low molecular weight carbohydrate sub-
strates, especially on cellotriose, at pH 8.5 corresponding to kit of below
0.01 s-1; more preferably the cellulase exhibits essentially no catalytic
activ-
ity on cellotriose, i.e. the component is not capable of hydrolysing
cellotriose
but capable of hydrolysing higher oligomers of (i-1,4-glucose units.
A convenient cellulase useful in the detergent composition of the
present invention may be an endoglucanase component which is im-
munoreactive with an antibody raised against a highly purified '43kD endo-
glucanase derived from Humicola insolens, DSM 1800, or which is a
homologue or derivative of the "43kD endoglucanase exhibiting cellufase
activity. A preferred endoglucanase component has the amino acid
sequence disclosed in PCT Patent Application No. WO 91117243, SEQ
ID#2, which is shown in the appended SEQ ID N0:4, or a variant of said
endoglucanase having an amino acid sequence being at least 60°~,
preferably at least 70%, more preferably 75°~, more preferably at least
80°~,
more preferably 85%, especially at least 90% homologous with said
sequence.
Another preferred endoglucanase component comprises an amino acid
sequence encoded by the partial DNA sequence disclosed in PCT Patent
Application No. W093/11249; SEQ ID#11, which is shown in the appended
SEQ ID N0:5, or a variant of said endoglucanase having an amino acid
sequence being at least 60%, preferably at least 70%, more preferably 75%,
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I8
more preferably at least 80°~, more preferably 85%, especially at least
90%
homologous with said sequence.
Yet another preferred endoglucanase component comprises an amino
acid sequence encoded by the partial DNA sequence disclosed in PCT
Patent Application No. WO 93/11249, SEQ ID#9, which is hereby
incorporated by reference.
Yet another preferred endoglucanase component comprises an amino
acid sequence encoded by the partial DNA sequence disclosed in PCT
Patent Application No. W093/11249, SEQ ID#7, which is hereby incorpor-
ated by reference. In example 1 below, the endoglucanase component is
referred to as EG III.
Alternatively, the cellulase may be an endoglucanase component
which is immunoreactive with an antibody raised against a highly purified
~60kD endoglucanase derived from Bacillus lautus, NCIMB 40250, or which
is a homologue or derivative of the '60kD endoglucanase exhibiting
cellulase activity. A preferred endoglucanase component has the amino acid
sequence disclosed in PCT Patent Application No. WO 91/10732, SEQ
ID#7, which is shown in the appended SEQ ID N0:6, or a variant of said
endoglucanase having an amino acid sequence being at least
60°!°,
preferably at feast 70%, more preferably 75%, more preferably at least 80%,
more preferably 85%, especially at least 90% homologous with said
sequence.
According to the present invention the detergent composition
comprises from 0.001 % to 2%, preferably from 0.01 % to 1 %, most
preferably from 0.05°~ to 0.5°~ of said 1000CEVU active
cellulolytic enzyme.
According to the present invention the detergent compositions comprise
said polysaccharide and cellulolytic enzyme in a ratio of from 100:1 to
1:100, preferably from 10:1 to 1:10, more preferably from 5:1 to 1:5.
Detersive Surfactants
According to the present invention the detergent composition
comprises at least 1 % of a surfactant system. Surfactants useful herein
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19
include the conventional C11-C1 g alkyl benzene sulphonates (__"LAS") and
primary, branched-chain and random C1p-C2p alkyl sulphates ("AS"), the
" C1 p-C1 g secondary (2,3) alkyl sulphates of the formula
CHg(CH2)x(CHOS03-M+) CH3 and CH3 (CH2)y(CHOSO3 M+) CH2CH3
- where x and (y + 1 ) are integers of at least about 7, preferably at least
about
9, and M is a water-solubilizing ration, especially sodium, unsaturated
sulphates such as oleyl sulphate, the C10-C1 g alkyl alkoxy sulphates
("AEXS"; especially EO 1-7 ethoxy sulphates), C1 p-C1 g alkyl alkoxy
carboxylates (especially the EO 1-5 ethoxycarboxylates), the C10-18
glycerol ethers, the C1p-C1g alkyl polyglycosides and their corresponding
sulphated polyglycosides, and C12-C1g alpha-sulphonated fatty acid esters.
If desired, the conventional nonionic and amphoteric surfactants such
as the C12-C1 g alkyl ethoxylates ("AE") including the so-called narrow
peaked alkyl ethoxylates and C6-C12 alkyl phenol alkoxyiates (especially
ethoxylates and mixed ethoxy/propoxy), C12-C1 g betaines and
sulphobetaines ("sultaines"), C10-C1 g amine oxides, and the like, can also
be included in the overall compositions. The C10-C1 g N-alkyl polyhydroxy
fatty acid amides can also be used. Typical examples include the C12-C18
N-methylglucamides. See WO 9,206,154. Other sugar-derived surfactants
include the N-alkoxy polyhydroxy fatty acid amides, such as C10-C1 g N-(3-
methoxypropyl) glucamide. The N-propyl through N-hexyl C12-C18
glucamides can be used for low sudsing. C1 p-C20 conventional soaps may
also be used. If high sudsing is desired, the branched-chain C1p-C16 soaps
may be used. Mixtures of anionic and nonionic surfactants are especially
useful. Other conventional useful surfactants such as cationics are listed in
standard texts.
According to the present invention the compositions comprise from
1 % to 80%, preferably from 5°~ to 50%, most preferably from
10°~ to 40% of
. a surfactant. Preferred surfactants for use herein are linear alkyl benzene
sulphonate, alkyl sulphates and alkyl alkoxylated nonionics or mixtures
thereof.
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Optional in4redients
According to 'the present invention the detergent compositions may
comprise a number of optional conventional detergent adjuncts such as
builders, chelants, polymers, antiredeposition agents and the like.
Builders
Detergent builders can optionally be included in the compositions
herein to assist in controlling mineral hardness. Inorganic as well as organic
builders can be used. Builders are typically used in fabric laundering
compositions to assist in the removal of particulate soils.
The level of builder can vary widely depending upon the end use of
the composition and its desired physical form. When present, the
compositions will typically comprise at least 1 °~ builder. Liquid
formulations
typically comprise from 5% to 50%, more typically about 5% to 30%, by
weight, of detergent builder. Granular formulations typically comprise from
10% to 80°~, more typically from. 15°r6 to 50°~ by
weight, of the detergent
builder. Lower or higher levels of builder, however, are not meant to be
excluded.
Inorganic or P-containing detergent builders include, but are not
limited to, the alkali metal, ammonium and alkanolammonium salts of
polyphosphates (exemplified by the tripotyphosphates, pyrophosphates,
orthophosphates and glassy polymeric meta-phosphates), phosphonates,
phytic acid, silicates, carbonates (including bicarbonates and
sesquicarbonates), sulphates, and aluminositicates (see, for example, U.S.
Patents 3,159,581; 3,213,030; 3,422,021; 3,400,148 and 3,422,137).
However, non-phosphate builders are required in some locales.
importantly, the compositions herein function surprisingly well even in the
presence of the so-called "weak" builders (as compared with phosphates)
such as citrate, or in the so-called "underbuilt" situation that may occur
with
~eolite or layered silicate buitders.
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21
Examples of silicate builders are the alkali metal silicates, particularly
those having a SiO2:Na20 ratio in the range 1.6:1 to 3.2:1 and layered
silicates, such as the layered sodium silicates described in U.S. Patent
4,664,839, issued May 12, 1987 to H. P. Rieck. NaSKS-6 is the trademark
- for a crystalline layered silicate marketed by Hoechst (commonly
abbreviated herein as "SKS-fi"). Unlike zeolite builders, the Na SKS-fi
silicate builder does not contain aluminum. NaSKS-6 has the delta-
Na2Si205 morphology form of layered silicate. It can be prepared by
methods such as those described in German DE A-3,417,649 and DE-A-
3,742,043. SKS-6 is a highly preferred layered silicate for use herein, but
other such layered silicates, such as those having the general formula
NaMSix02x+1 ~YH20 herein M is sodium or hydrogen, x is a number from
1.9 to 4, preferably 2, and y is a number from 0 to 20, preferably 0 can be
used herein. Various other layered silicates from Hoechst include NaSKS-5,
NaSKS-7 and NaSKS-11, as the alpha, beta and gamma forms. As noted
above, the delta-Na2Si205 (NaSKS-6 form) is most preferred for use
herein. Other silicates may also be useful such as for example magnesium
silicate, which can serve as a crispening agent in granular formulations, as
a stabilizing agent for oxygen bleaches, and as a component of suds control
systems.
Examples of carbonate builders are the alkaline earth and alkali
metal carbonates as disclosed in German Patent Application No. 2,321,001
published on November 15, 1973.
Aluminosilicate builders are useful in the present invention.
Afuminosilicate builders are of great importance in most currently marketed
heavy duty granular detergent compositions, and can also be a significant
builder ingredient in liquid detergent formulations. Aluminosilicate builders
include those having the empirical formula:
Mz~(Si02)w(~102)y]~xH20
wherein w, z and y are integers of at feast 6, the molar ratio of z to y is in
the
range from 1.0 to about 0.5, and x is an integer from about 15 to about 264.
Useful aluminosilicate ion exchange materials are commercially
available. These afuminosificates can be crystalline or amorphous in
structure and can be naturally-occurring afuminosilicates or synthetically
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22
derived. A method for producing aluminosilicate ion exchange materials is
disclosed in U.S. Patent 3,985,669, Krummel, et al, issued October 12,
1976. Preferred synthetic crystalline aluminosilicate ion exchange materials
useful herein are available under the designations Zeolite A, Zeolite P (B),
Zeolite MAP and Zeolite X. In an especially preferred embodiment, the
crystalline aiuminosilicate ion exchange material has the formula:
wal2~(A102)12(Si02)121~xH20
wherein x is from about 20 to about 30, especially about 27. This material is
known as Zeolite A. Dehydrated zeolites (x = 0 - 10) may also be used
herein. Preferably, the aluminosilicate has a particle size of about 0.1-10
microns in diameter.
Organic detergent builders suitable for the purposes of the present
invention include, but are not restricted to, a wide variety of
polycarboxylate
compounds. As used herein, "polycarboxylate" refers to compounds having
a plurality of carboxylate groups, preferably at least 3 carboxylates.
F'olycarboxylate builder can generally be added to the composition in acid
form, but can also be added in the form of a neutralized salt. When utilized
in salt form, alkali metals, such as sodium, potassium, and lithium, or
2~Ikanolammonium salts are prefen-ed.
Included among the polycarboxylate builders are a variety of
categories of useful materials. One important category of polycarboxylate
builders encompasses the ether polycarboxylates, including oxydisuccinate,
as disclosed in Berg, U.S. Patent 3,128,287, issued April 7, 1964, and
L.amberti et al, U.S. Patent 3,635,830, issued January 18, 1972. See also
'rTMS/TDS" builders of U.S. Patent 4,663,071, issued to Bush et al, on May
5, 1987. Suitable ether polycarboxylates also include cyclic compounds,
particularly alicyclic compounds, such as those described in U.S. Patents
3, 923,679; 3, 835,163; 4,158,635; 4,120, 874 and 4,102, 903.
Other useful detergency builders include the ether
hydroxypolycarboxylates, copolymers of malefic anhydride with ethylene or
vinyl methyl ether, 1, 3, 5-trihydroxy benzene-2, 4, 6-trisulphonic acid, and
carboxymethyloxysuccinic acid, the various alkali metal, ammonium and
substituted ammonium salts of pofyacetic acids such as ethyfenediamine
tetraacetic acid and nitrilotriacetic acid, as well as polycarboxylates such
as
CA 02206523 2000-06-28
23
mellitic acid, succinic acid, oxydisuccinic acid, polymaleic acid, benzene
1,3,5-tricarboxylic acid, carboxymethyloxysuccinic acid, and soluble salts
thereof.
Citrate builders, e.g., citric acid and soluble salts thereof (particularly
sodium salt), are polycarboxylate builders of particular importance for heavy
duty liquid detergent formulations due to their availability from renewable
resources and their biodegradability. Citrates can also be used in granular
compositions, especially in combination with zeolite and/or layered silicate
builders. Oxydisuccinates are also especially useful in such compositions
and combinations.
Also suitable in the detergent compositions of the present invention
are the 3,3-dicarboxy-4-oxa-1,6-hexanedioates and the related compounds
disclosed in U.S. Patent 4,566,984, Bush, issued January 28, 1986. Useful
succinic acid builders include the C5-C20 alkyl and alkenyl succinic acids
and salts thereof. A particularly preferred compound of this type is
dodecenylsuccinic acid. Speck examples of succinate builders include:
laurylsuccinate, myristylsuccinate, palmitylsuccinate, 2-dodecenylsuccinate
(preferred), 2-pentadecenylsuccinate, and the like. Laurylsuccinates are the
preferred builders of this group, and are described in European Patent
Application 0,200,263, published November 5, 1986.
Other suitable polycarboxylates are disclosed in U.S. Patent
4,144,226, Crutchfield et al, issued March 13, 1979 and in U. S. Patent
3,308,067, Diehl, issued March 7, 1967. See also Diehl U.S. Patent
3,723,322.
Fatty acids, e.g., C12-C1g monocarboxyiic acids, can also be
incorporated into the compositions alone, or in combination with the
aforesaid builders, especially citrate and/or the succinate builders, to
provide additional builder activity. Such use of fatty acids will generally
result in a diminution of sudsing, which should be taken into account by the
formulator.
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24
Chelatinct Agents
The detergent compositions herein may also optionally contain one '
or' more iron and/or manganese chelating agents. Such chelating agents
can be selected from the group consisting of amino carboxylates, amino '
phosphonates, polyfunctionally-substituted aromatic chelating agents and
mixtures therein, all as hereinafter defined. Without intending to be bound
by theory, it is believed that the benefit of these materials is due in part
to
their exceptional ability to remove iron and manganese ions from washing
solutions by formation of soluble chelates.
Amino carboxylates useful as optional chelating agents include
ethyfenediaminetetracetates, N-hydroxyethylethyienediaminetriacetates,
nitriiotriacetates, 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 least low levels of total
phosphorus are permitted in detergent compositions, and include
ethyienediaminetetrakis (methyienephosphonates) 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 chefator 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.
If utilized, these chelating agents will generally comprise from 0.1
°~
to 10% more preferably, from 0.1 % to 3.0% by weight of such compositions.
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Polymeric Soil Release Accent
Any polymeric soil release agent known to those skilled in the art can
optionally be employed in the compositions and processes of this invention.
' Polymeric soil release agents are characterized by having both hydrophilic
segments, to hydrophilize the surface of hydrophobic fibers, such as
polyester and nylon, and hydrophobic segments, to deposit upon
hydrophobic fibers and remain adhered thereto through completion of
washing and rinsing cycles and, thus, serve as an anchor for the hydrophilic
segments. This can enable stains occurring subsequent to treatment with
the soil release agent to be more easily cleaned in later washing
procedures.
The polymeric soil release agents useful herein especially include
those soil release agents having: (a) one or more nonionic hydrophile
components consisting essentially of (i) polyoxyethyiene segments with a
degree of polymerization of at least 2, or (ii) oxypropylene or
polyoxypropylene segments with a degree of polymerization of from 2 to 10,
wherein said hydrophile segment does not encompass any oxypropylene
unit unless it is bonded to adjacent moieties at each end by ether linkages,
or (iii) a mixture of oxyalkylene units comprising oxyethyfene and from 1 to
about 30 oxypropylene units wherein said mixture contains a sufficient
amount of oxyethylene units such that the hydrophile component has
hydrophilicity great enough to increase the hydrophilicity of conventional
polyester synthetic fiber surfaces upon deposit of the soil release agent on
such surface, said hydrophile segments preferably comprising at least about
25% oxyethylene units and more preferably, especially for such components
having about 20 to 30 oxypropylene units, at least about 50°~
oxyethyfene
units; or (b) one or more hydrophobe components comprising (i) C3
oxyalkylene terephthalate segments, wherein, if said hydrophobe
components also comprise oxyethylene terephthalate, the ratio of
oxyethylene terephthalate:C3 oxyalkyiene terephthalate units is about 2:1 or
lower, (ii) C4-C6 alkylene or oxy C4-Cg alkyfene segments, or mixtures
therein, or (iii) poly (vinyl ester) segments, preferably polyvinyl acetate),
having a degree of polymerization of at feast 2.
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26
Typically, the polyoxyethylene segments of (a)(i) will have a degree of
polymerization of from about 200, although higher levels can be used,
preferably from 3 to about 150, more preferably from 6 to about 100.
Suitable oxy C4-C6 alkylene hydrophobe segments include, but are not
limited to, end-caps of polymeric soil release agents such as
M03S(CH2)nOCH2CH20-, where M is sodium and n is an integer from 4-6,
as disclosed in U.S. Patent 4,721,580, issued January 26, 1988 to
Gosselink.
Polymeric soil release agents useful in the present invention also
include cellulosic derivatives such as copolymeric blocks of ethylene
terephthalate or propylene terephthalate with polyethylene oxide or
polypropylene oxide terephthalate, and the like.
Soil release agents characterized by polyvinyl ester) hydrophobe
segments include graft copolymers of polyvinyl ester), e.g., C1-Cg vinyl
esters, preferably polyvinyl acetate) grafted onto polyalkylene oxide
backbones, such as polyethylene oxide backbones. See European Patent
Application 0 219 048, published .April 22, 1987 by Kud, et al. Commercially
available soil release agents of this kind include the SOKALANT type of
material, e.g., SOKALAN HP-22, available from BASF (West Germany).
One type of prefer-ed soil release agent is a copolymer having random
blocks of ethylene terephthalate and polyethylene oxide (PEO)
terephthalate. The molecular weight of this polymeric soil release agent is in
the range of from about 25,000 to about 55,000. See U.S. Patent 3,959,230
to Hays, issued May 25, 1976 and U.S. Patent 3,893,929 to Basadur issued
July 8, 1975.
Another preferred polymeric soil release agent is a polyester with
repeat units of ethylene terephthalate units contains 10-15°~ by weight
of
ethylene terephthalate units together with 90-80°~ by weight of
polyoxyethylene terephthalate units, derived from a polyoxyethylene glycol
of average molecular weight 300-5,000. Examp~es of this polymer include
the commeMcially available material ZELCON 5126 (from Dupont) and
MILEASE T (from ICI). See also U.S. Patent 4,702,857, issued October 27,
1987 to Gosselink.
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27
Another preferred polymeric soil release agent is a suifonated product
' of a substantially linear ester oligomer comprised of an oligomeric ester
backbone of terephthaloyl and oxyalkyleneoxy repeat units and terminal
moieties covalently attached to the backbone. These soil release agents
are described fully in U.S. Patent 4,968,451, issued November 6, 1990 to
J.J. Scheibel and E.P. Gosselink. Other suitable polymeric soil release
agents include the terephthalate polyesters of U.S. Patent 4,711,730, issued
December 8, 1987 to Gosselink et al, the anionic end-capped oligomeric
esters of U.S. Patent 4,721,580, issued January 26, 1988 to Gosselink, and
the block polyester oligomeric compounds of U.S. Patent 4,702,857, issued
October 27, 1987 to Gosselink.
Preferred polymeric soil release agents also include the soil release
agents of U.S. Patent 4,877,896, issued October 31, 1989 to Maldonado et
al, which discloses anionic, especially sulfoarolyl, end-capped terephthalate
esters.
If utilized, soil release agents will generally comprise from about 0.01
°~
to about 10.0%, by weight, of the detergent compositions herein, typically
from about 0.1 % to about 5%, preferably from about 0.2% to about
3.0°r6.
Still another preferred soil release agent is an oligomer with repeat
units of terephthaloyl units, sulfoisoterephthaloyl units, oxyethyleneoxy and
oxy-1,2-propylene units. The repeat units form the backbone of the ofigomer
and are preferably terminated with modified isethionate end-caps. A
particularly preferred soil release agent of this type comprises about one
sulfoisophthaloyl unit, 5 terephthaloyl units, oxyethyleneoxy and oxy-1,2-
propyleneoxy units in a ratio of from about 1.7 to about 1.8, and two end-cap
units of sodium 2-(2-hydroxyethoxy)-ethanesulfonate. Said soil release
. agent also comprises from about 0.5% to about 20°!°, by weight
of the
oligomer, of a crystalline-reducing stabilizer, preferably selected from the
group consisting of xylene sulfonate, cumene suffonate, toluene suifonate,
and mixtures thereof.
As a practical matter, and not by way of limitation, the compositions
and processes herein can be adjusted to provide on the order of at least
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28
one part per ten million of the active bleach catalyst species in the aqueous
washing liquor, and will preferably provide from about 0.1 ppm to about 700
ppm, more preferably from about 1 ppm to about 500 ppm, of the catalyst
species in the laundry liquor.
Bleaching Compounds - Bleaching Aoents and Bleach Activators
The detergent compositions herein may optionally contain bleaching
agents or bleaching compositions containing a bleaching agent and one or
more bleach activators. When present, bleaching agents will typically be at
levels of from 1 °~ to 40°~, more typically from 5°~ to
30°~, of the detergent
composition, especially for fabric laundering. tf present, the amount of
bleach activators will typically be from 0.1 % to 60°~, more typically
from
0.5°~ to 40°~ of the bleaching composition comprising the
bleaching agent-
pfus-bleach activator.
The bleaching agents used herein can be any of the bleaching
agents useful for detergent compositions in textile cleaning, hard surtace
cleaning, or other cleaning purposes that are now known or become known.
These include oxygen bleaches as well as other bleaching agents.
Peroxygen bleaching agents can also be used. Suitable peroxygen
bleaching compounds inGude sodium carbonate peroxyhydrate and
equivalent "percarbonate" bleaches, sodium pyrophosphate peroxyhydrate,
urea peroxyhydrate, and sodium peroxide. Persutfate bleach (e.g., OXONEM
manufactured commercially by DuPont) can also be used.
A preferred percarbonate bleach comprises dry particles having an
average particle size in the range from about 500 micrometers to about
1,000 micrometers, not more than about 10°~ by weight of said particles
being smaller than about 200 micrometers and not more than about 10°~
by
weight of said particles being larger than about 1,250 micrometers.
Optionally, the percarbonate can be coated with silicate, borate or water-
soluble surfactants. Preferred coatings are based on carbonate/sulphate
mixtures. Percarbonate is available from various commercial sources such
as FMC, Solvay and Tokai Denka.
CA 02206523 2000-06-28
29
Another category of bleaching agent that can be used without
restriction encompasses percarboxylic acid bleaching agents and salts
thereof. Suitable examples of this class of agents include magnesium
monoperoxyphthalate hexahydrate, the magnesium salt of metachloro
perbenzoic acid, 4-nonylamino-4-oxoperoxybutyric acid and
diperoxydodecanedioic acid. Such bleaching agents are disclosed in U.S.
Patent 4,483,781, Hartman, issued November 20, 1984, U.S.
Patent No. 4,806,632, Burns et al, European Patent Application
0,133,354, Banks et al, published February 20, 1985, and U.S.
Patent 4,412,934, Chung et al, issued November 1, 1983. Highly prefer-ed
bleaching agents also include 6-nonylamino-6-oxoperoxycaproic acid as
described in U.S. Patent 4,634,551, issued January 6, 1987 to Bums et al.
Mixtures of bleaching agents can also be used. Peroxygen bleaching
agents, the perborates, e.g., sodium perborate (e.g., mono- or tetra-hydrate)
the percarbonates, etc., are preferably combined with bleach activators,
which lead to the in situ production in aqueous solution (i.e., during the
washing process) of the peroxy acid corresponding to the bleach activator.
Various nonlimiting examples of activators are disclosed in U.S. Patent
4,915,854, issued April 10, 1990 to Mao et al, and U.S. Patent 4,412,934.
The nonanoyloxybenzene sulfonate (NOES) and tetraacetyl ethylene
diamine (TAED) activators are typical, and mixtures thereof can also be
used. See also U.S. 4,634,551 for other typical bleaches and activators
useful herein.
Highly prefened amido-derived bleach activators are those of the
fomnula~:
R1 N(R5)C(O)R2C(0)L or R1 C(O)N(R5)R2C(O)L
wherein R1 is an alkyl group containing from about 6 to about 12 carbon
atoms, R2 is an alkylene containing from 1 to about 6 carbon atoms, R5 is H
or alkyl, aryl, or alkaryl containing from about 1 to about 10 carbon atoms,
and L is any suitable leaving group. A leaving group is any group that is
displaced from the bleach activator as a consequence of the nucleophilic
attack on the bleach activator by the perhydroxyl anion. A preferred leaving
group is phenol sulfonate.
CA 02206523 2000-06-28
30
Preferred examples of bleach activators of the above formulae
include (6-octanamido-caproyl)oxybenzenesulfonate, (6-
nonanamidocaproyl)- oxybenzenesulfonate, (6-decanamido-
caproyl)oxybenzenesulfonate, and mixtures thereof as described in U.S.
Patent 4,634,551, incorporated herein by reference.
Another class of bleach activators comprises the benzoxazin-type
activators disclosed by Hodge et al in U.S. Patent 4,966,723, issued
October 30, 1990. A highly preferred activator of the benzoxazin-type is:
O
II
C~0
I
N~ O
Still another class of preferred bleach activators includes the acyl
lactam activators, especially aryl caprolactams and aryl valerolactarns of
the formulae:
0 0
0 C-CH2-CH2 O C-CH2-CHZ
R6 C N~CH2_CH2 CH2 Rs C ~CH2-C
wherein R6 is H or an alkyl, aryl, alkoxyaryl, or alkaryl group containing
from
1 to about 12 carbon atoms. Highly preferred lactam activators include
benzoyl caprolactam, octanoyl caprolactam, 3,5,5-trimethylhexanoyl
caprolactam, nonanoyl caprolactam, decanoyl caprolactam, undecenoyl
caprolactam, benzoyl valerolactam, octanoyl valerolactam, decanoyl
valerolactam, undecenoyl valerolactam, nonanoyl valerolactam, 3,5,5-
trimethylhexanoyl valerolactam and mixtures thereof. See also U.S. Patent
4,545,784, issued to Sanderson, October 8, 1985, which discloses acyl
caprolactams, adsorbed into sodium perborate. Other prefen-ed
activators are cationic bleach activators.
Bleaching agents other than oxygen bleaching agents are also known
in the art and can be utilized herein. One type of non-oxygen bleaching
agent of particular interest includes photoactivated bleaching agents such
as the sulfonated zinc and/or aluminum phthalocyanines. Ses U.S. Patent
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WO 96/20997 PCTlUS95/16432
31
4,033,718, issued July 5, 1977 to Holcombe et al. If used, detergent
compositions will typically contain from 0.025°~ to 1.25%, by weight,
of such
bleaches, especially suffonate zinc phthalocyanine.
If desired, the bleaching compounds can be catalyzed by means of a
manganese compound. Such compounds are well known in the art and
include, for example, the manganese-based catalysts disclosed in U.S. Pat.
5,246,621, U.S. Pat. 5,244,594; U.S. Pat. 5,194,416; U.S. Pat. 5,114,606;
and European Pat. App. Pub. Nos. 549,271 A1, 549,272A1, 544,440A2, and
544,490A1; Preferred examples of these catalysts include MnlV2(u-
O)3(1,4,7-trimethyl-1,4,7-triazacyclononane)2(PF6)2, Mnlll2(u-O)1(u-
OAc)2(1,4,7-trimethyl-1,4,7-triazacyclononane)2_(C104)2, MnlV4(u-
O)g(1,4,7-triazacyclononane)4(C104)4, MnIIIMnIV4(u-O)1 (u-OAc)2_(1,4,7-
trimethyl-1,4,7-triazacyclononane)2(C104)3, MnIV(1,4,7-trimethyl-1,4,7-
triazacycfononane)- (OCH3)3(PF6), and mixtures thereof. Other metal-
based bleach catalysts include those disclosed in U.S. Pat. 4,430,243 and
U.S. Pat. 5,114,611. The use of manganese with various complex ligands to
enhance bleaching is also reported in the following United States Patents:
4,728,455; 5,284,944; 5,246,692; 5,256,779; 5,280,117; 5,274,147;
5,153,161; 5,227,084;
Polymeric Dispersin4 A4ents
Polymeric dispersing agents can advantageously be utilized at levels
from 0.1 % to 7%, by weight, in the compositions herein, especially in the
presence of zeolite and/or layered silicate builders. Suitable polymeric
dispersing agents include polymeric polycarboxylates and polyethylene
glycois, although others known in the art can also be used. It is believed,
though it is not intended to be limited by theory, that polymeric dispersing
agents enhance overall detergent builder performance, when used in
combination with other builders (including lower molecular weight
poiycarboxylates) by crystal growth inhibition, particulate soil release
peptization, and anti-redeposition.
Polymeric poiycarboxylate materials can be prepared by polymerizing
or copolymerizing suitable unsaturated monomers, preferably in their acid
form. Unsaturated monomeric acids that can be polymerized to form suitable
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32
polymeric polycarboxylates include acrylic acid, malefic acid (or malefic
anhydride), fumaric acid, itaconic acid, aconitic acid, mesaconic acid,
citraconic acid and inethylenemalonic acid. The presence in the polymeric '
po(ycarboxylates herein or monomeric segments, containing no carboxyiate
radicals such as vinylmethyl ether, styrene, ethylene, etc. is suitable '
provided that such segments do not constitute more than about 40°~ by
weight.
Particularly suitable polymeric polycarboxylates can be derived from
acrylic acid. Such acrylic acid-based polymers which are useful herein are
the water-soluble salts of polymerized acrylic acid. The average molecular
weight of such polymers in the acid form preferably ranges from about 2,000
to 10,000, more preferably from about 4,000 to 7,000 and most preferably
from about 4,000 to 5,000. Water-soluble salts of such acrylic acid polymers
can include, for example, the alkali metal, ammonium and substituted
ammonium salts. Soluble polymers of this type are known materials. Use of
polyacrylates of this type in detergent compositions has been disclosed, for
example, in Diehl, U.S. Patent 3,308,067, issued march 7, 1967.
Acrylic/maleic-based copolymers may also be used as a preferred
component of the dispersing/anti-redeposition agent. Such materials include
the water-soluble salts of copolymers of acrylic acid and malefic acid. The
.average molecular weight of such copolymers in the acid form preferably
ranges from about 2,000 to 100,000, more preferably from about 5,000 to
'75,000, most preferably from about 7,000 to 65,000. The ratio of acrylate to
maleate segments in such copolymers will generally range from about 30:1
eto about 1:1, more preferably from about 70:30 to 30:70. Water-soluble salts
of such acrylic acid/maleic acid copolymers can include, for example, the
alkali metal, ammonium and substituted ammonium salts. Soluble
acrylatelmaleate copolymers of this type are known materials which are
described in European Patent Application No. 66915, published December
15, 1982, as well as in EP 193,360, published September 3, 1986, which
also describes such polymers comprising hydroxypropylacrylate. Still other
useful dispersing agents include the maleiGacryliGvinyl alcohol or acetate
i:erpo(ymers. Such materials are also disclosed in EP 193,360, including, for
example, the 45/45/10 terpolymer of acryliclmaleidvinyl alcohol.
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33
Another polymeric material which can be included is polyethylene
glycol (PEG). PEG can exhibit dispersing agent pertormance as well as act
as a clay soil removal-antiredeposition agent. Typical molecular weight
ranges for these purposes range from about 500 to about 100,000,
preferably from about 1,000 to about 50,000, more preferably from about
1,500 to about 10,000.
Polyamino acid dispersing agents such as polyaspartate and
polyglutamatemay also be used, especially in conjunction with zeolite
builders. Dispersing agents such as polyaspartate preferably have a
molecular weight (avg.) of about 10,000.
Dye Transfer Inhibiting A4ents
The compositions of the present invention may also include one or
more materials effective for inhibiting the transfer of dyes from one fabric
to
another during the cleaning process. Generally, such dye transfer inhibiting
agents include polyvinyl pyrroiidone polymers, polyamine N-oxide polymers,
copolymers of N-vinylpyrrolidone and N-vinyiimidazole, manganese
phthalocyanine, peroxidases, and mixtures thereof. If used, these agents
typically comprise from 0.01 % to 10% by weight of the composition,
preferably from 0.01 % to 5%, and more preferably from 0.05% to 2°~.
More specifically, the polyamine N-oxide polymers preferred for use
herein contain units having the following structural formula: R-Ax-P; wherein
P is a poiymerizable unit to which an N-O group can be attached or the N-O
group can form part of the polymerizable unit or the N-O group can be
attached to both units; A is one of the following structures: -NC(O)-, -C(O)O-
,
-S-, -O-, -N=; x is 0 or 1; and R is aliphatic, ethoxylated aliphatics,
aromatics,
heterocyclic or alicyclic groups or any combination thereof to which the
nitrogen of the N-O group can be attached or the N-O group is part of these
groups. Preferred polyamine N-oxides are those wherein R is a heterocyclic
group such as pyridine, pyrrole, imidazole, pyrrolidine, piperidine and
derivatives thereof.
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34
The N-O group can be represented by the following general
structures:
O
~l~c- ~ -~2)y~ =N-(Ri)x
(R3)z
wherein R1, R2, R3 are aliphatic, aromatic, heterocyclic or alicyclic groups
or combinations thereof; x, y and z are 0 or 1; and the nitrogen of the N-O
group can be attached or form part of any of the aforementioned groups.
Z'he amine oxide unit of the polyamine N-oxides has a pKa <10, preferably
pKa <7, more preferred pKa <6.
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, poiyamide, polyimides, polyacrylates and mixtures
thereof. These polymers include random or block copolymers where one
monomer type is an amine N-oxide and the other monomer type is an N-
oxide. The amine N-oxide polymers typically have a ratio of amine to the
amine N-oxide of 10:1 to 1:1,000,000. However, the number of amine oxide
groups present in the polyamine oxide polymer can be varied by appropriate
copolymerization or by an appropriate degree of N-oxidation. The poiyamine
oxides can be obtained in almost any degree of polymerization. Typically,
the average molecular weight is within the range of 500 to 1,000,000; more
preferred 1,000 to 500,000; most preferred 5,000 to 100,000. This preferred
class of materials can be referred to as "PVNO".
The most preferred polyamine N-oxide useful in the detergent
compositions herein is poly(4-vinyipyridine-N-oxide) which as an average
molecular weight of about 50,000 and an amine to amine N-oxide ratio of
about 1:4.
Copolymers of N-vinylpyrrolidone and N-vinylimidazole polymers
(referred to as a class as "PVPVI") are also preferred for use herein.
Preferably the PVPVI has an average molecular weight range from 5,000 to
1,000,000, more preferably from 5,000 to 200,000, and most preferably from
10,000 to 20,000. (The average molecular weight range is determined by
CA 02206523 2000-06-28
35
light scattering as described in Barth et al., Chemical Analvsi~, Vol 113,
°Modern Methods of Polymer Characterization"). The PVPVI copolymers
typically have a molar ratio of N-vinylimidazole to N-vinylpyrrolidone from
1:1 to 0.2:1, more preferably from 0.8:1 to 0.3:1, most preferably from
0.6:1 to 0.4:1. These copolymers can be either linear or branched.
The present invention compositions also may employ a
polyvinylpyrrolidone ("PVP") having an average molecular weight of from
about 5,p00 to about 400,000, preferably from about 5,000 to about
200,000, and more preferably from about 5,000 to about 50,000. PVP's are
known to persons skilled in the detergent field; see, for
example, EP-A-262,897 and EP-A-256,696. Compositions containing
PVP can also contain polyethylene glycol ("PEG") having an
average molecular weight from about 500 to about 100,000, preferably from
about 1,400 to about 10,000. Preferably, the ratio of PEG to PVP on a ppm
basis deliivered in wash solutions is from about 2:1 to about 50:1, and more
preferably from about 3:1 to about 10:1.
The detergent compositions herein may also optionally contain from
0.005°r6 to 5°~ by weight of certain types of hydrophilic
optical brighteners
which also provide a dye transfer inhibition action. If used, the compositions
herein will preferably comprise from 0.01 °~ to 1 °~ by weight
of such optical
brighten~rs.
The hydrophilic optical brighteners useful in the present invention are
those halving the structural formula:
R~ R2
H H IV
N N C-C N N
N H H N
SO R
SO~Ivt 3M i
wherein R1 is selected from anilino, N-2-bis-hydroxyethyl and NH-2-
hydroxy~thyl; R2 is selected from N-2-bis-hydroxyethyl, N-2-hydroxyethyl-N-
methylaranino, morphilino, chloro and amino; and M is a salt-forming ration
such as sodium or potassium.
CA 02206523 2000-06-28
36
When in the above formula, R~ is anilino, R2 is N-2-bis-hydroxyethyl
and M is a ration such as sodium, the brightener is 4,4',-bis[(4-anilino-6-(N-
2-bis-hydroxyethyl)-s-triazine-2-yl)aminoJ-2,2'-stilbenedisulfonic acid and
disodium salt. This particular brightener species is commercially marketed
under the trademark Tinopal-UNPA-GX by Ciba-Geigy Corporation.
Tinopal-4JNPA-GX is the preferred hydrophilic optical brightener useful in
the detergent compositions herein.
When in the above formula, R~ is aniiino, R2 is N-2-hydroxyethyl-N-
2-methylamino and M is a ration such as sodium, the brightener is 4,4'-
bis[(4-anilino-6-(N-2-hydroxyethyl-N-methylamino)-s-triazine-2-yl)aminoJ2,2'-
stilbenedisuifonic acid disodium salt. This particular brightener species is
commercially marketed under the trademark Tinopat 5BM-GX by Ciba-
Geigy Corporation.
When in the above formula, R~ is aniiino, R2 is morphilino and M is a
ration such as sodium, the brightener is 4,4'-bis[(4-anilino-6-morphilino-s-
triazine-2-yl)amino]2,2'-stilbenedisulfonic acid, sodium salt. This particular
brighten~r species is commercially marketed under the trademark Tinopal
AMS-GX by Ciba Geigy Corporation.
This specific optical brightener species selected for use in the present
invention provide especially .effective dye transfer inhibition performance
benefits when used in combination with the selected polymeric dye transfer
inhibiting'agents hereinbefore described. The combination of such selected
polymeric materials (e.g., PVNO and/or PVPVI) with such selected optical
brighteners (e.g., Tinopal UNPA-GX, Tinopal 58M-GX and/or Tinopal AMS-
GX) provides significantly better dye transfer inhibition in aqueous wash
solutions than does either of these two detergent composition components
when used alone. Without being bound by theory, it is believed that such
brighteners work this way because they have high affinity for fabrics in the
wash solwtion and therefore deposit relatively quick on these fabrics. The
extent to which brighteners deposit on fabrics in the wash solution can be
defined by a parameter called the "exhaustion coefficient". The exhaustion
coefficienk is in general as the ratio of a) the brightener material deposited
on fabric', to b) the initial brightener concentration in the wash liquor_
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WO 96/20997 PCT/US95/16432
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Brighteners with relatively high exhaustion coefficients are the most suitable
for inhibiting dye transfer in the context of the present invention.
Of course, it will be appreciated that other, conventional optical
' brightener types of compounds can optionally be used in the present
compositions to provide conventional fabric "brightness" benefits, rather
than a true dye transfer inhibiting effect. Such usage is conventional and
well-known to detergent formulations.
According to the present invention the detergent composition may
comprise any other ingredients commonly employed in conventional
detergent compositions such as soaps, suds suppressors, softeners,
brighteners, additional enzymes and enzyme stabilisers.
Use of the combination of nonionic polysaccharide ethers wand
cellulase enzymes
The compositions of the present invention may be used in laundry
detergent compositions, fabric treatment compositions and fabric softening
compositions in addition to hard surface cleaners. The compositions may
be formulated as conventional granules, bars, pastes or powder or non
aqueous liquid forms. The detergent compositions are manufactured in
conventional manner, for example in the case of powdered detergent
compositions, spray drying or spray mixing processes may be utilised.
The polysaccharide ether and cellulase enzyme combination of the
present invention are present at aqueous concentrations of from 1 ppm to
300ppm, preferably from 5ppm to 1 OOppm in the wash solution, preferably at
a ply of from 7 to 11, more preferably from 9 to 10.5.
The present invention also relates to a method of laundering fabrics
which comprises contacting said fabric with an aqueous laundry liquor
containing conventional detersive ingredients described herein in addition to
the cellulolytic enzyme and nonionic polysaccharide ether of the present
invention. In a preferred method polyester and polyester-cotton blends and
other synthetic fabrics are used. The most preferred method for
simultaneously cleaning and soil release treatment is a "multi-cycle"
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38
method, whereby the best results are obtained after two or more cycles
comprising the steps of:
a) contacting said fabric with said aqueous laundry liquor in a conventional
automatic washing machine or by hand washing for periods of from about 5
minutes to about 1 hour;
b) rinsing said fabrics with water
c) line- or tumble drying said fabrics; and
d) exposing said fabrics to soiling through normal wear or domestic use.
Examples
Abbreviations used in Examples
In the detergent compositions, the abbreviated component identifications
have the following meanings: .
XYAS : Sodium C1X - C1Y alkyl sulphate
25EY : A , C12-15 predominantly linear primary
alcohol condensed with an average of Y
moles of ethylene oxide
XYEZ : A C1x - C1y predominantly linear primary
alcohol condensed with an average of Z
moles of ethylene oxide
XYEZS : C1X - C1Y sodium alkyl sulphate
condensed with an average of Z motes of
ethylene oxide per mole
TFAA : C16-C1g alkyl N-methyl glucamide.
Silicate : Amorphous Sodium Silicate (Si02:Na20
ratio = 2.0)
SUBSTITUTE SHEET (RULE 26)
CA 02206523 2000-06-28
NaSKS-$ : Crystalline layered silicate of formula 8-
Na2Si205
Carbonate : Anhydrous sodium carbonate
MA/AA : Copolymer of 30:70 maleiGacrylic acid,
average molecular weight about 70,000.
Zeolite p : Hydrated Sodium Aluminosilicate of
formula Nal2(A102Si02)12. 27H20
having a primary particle size in the range
from 1 to 10 micrometers
Citrate : Tri-sodium citrate dihydrate
Percarbanate : Anhydrous sodium percarbonate bleach
coated with a coating of sodium silicate
(Si20:Na20 ratio = 2:1 ) at a weight ratio of
percarbonate to sodium silicate of 39:1
CMC : Sodium carboxymethyl cellulose
DETPMP : Diethylene triamine yenta (Methylene
phosphoric acid), marketed by Monsanto
under the Trademark bequest 2060
PVNO : Poly (4-vinylpyridine)-N-oxide copolymer of
vinylimidazole and vinylpyn-olidone having
an average molecular weight of 10,000.
Smectite Clay : Calcium montmorillonite ex. Colin Stewart
Minchem Ltd.
Granular Suds : 12°~ Siliconelsilica, 18°~6 stearyl
Suppres~or alcoho1,70°~ starch in granular form
CA 02206523 2000-06-28
~S : Sodium linear C12 alkyl benzene
sulphonate
TAS : Sodium tallow alkyl sulphate
SS : Secondary soap surfactant of formula
2-
butyl octanoic acid
Phosphate : Sodium tripolyphosphate
TAED : Tetraacetyl ethylene diamine
PVP : Polyvinyl pyrrolidone polymer
HMWPEO : High molecular weight polyethylene
oxide
MC1 : Methyl cellulose ether with dp - 650,
ds=1.8 available from Shin Etsu Chemicals
MC2 : Methyl cellulose ether (Metho1~60 HG)
obtained from Fluka, with a dp >100 and
ds
>1
HPMC : Hydroxypropyl methylcellulose ether with
dp= 300-350, 28-30°~ methoxyl content
Cellulase : Cellulolytic enzyme sold under the
trademark of Carezyme or Celluzyme by
Novo Nordisk A/S
TAE 25 : Tallow alcohol ethoxylate (25)
Exa-
The following laundry detergent compositions A, B, C, D and E were
prepared.
A 8 C D E
45AS/25AS 3:1 9.1 9.1 9.1 9.1 9.1
35AE3S 2.3 2.3 2.3 2.3 2.3
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WO 96/20997 PCTlUS95l16432
41
24E5 4.5 4.5 4.5 4.5 4.5
TFAA 2.0 2.0 2.0 2.0 2.0
Zeolite A 10.2 10.2 10.2 10.2 10.2
Cellulase 1000CEVU 0.1 0.3 0.2 0.6 0.05
' MC2 0.6 0.8 0.16 0.36 0.55
Na SKS-6/citric acid10.6 10.6 10.6 10.6 10.6
79:21
Carbonate 7.6 7.6 7.6 7.6 7.6
TAED 5 6.67 6.67 6.67 6.67
Percarbonate 22.5 22.5 22.5 22.5 22.5
DETPMP 0.5 0.5 0.5 0.5 0.5
Protease 0.55 0.55 0.55 0.55 0.55
Pol carbox late 3.1 3.1 3.1 3.1 3.1
CMC 0.4 0.4 0.4 0.4 0.4
PVNO 0.03 0.03 0.03 0.03 0.03
Granular suds 1.5 1.5 1.5 1.5 1.5
su ressor
Minors/misc to 100~
Example 2
Granular fabric cleaning compositions in accord with the invention are
prepared as follows:
I II
Cellulase (1000CEVU) 0.2 0.1
MC 1 0.75 -
HPMC - 0.5
LAS 22.0 22.0
Phosphate 23.0 23.0
Carbonate 23.0 23.0
Silicate 14.0 14.0
Zeolite A 8.2 8.2
DETPMP 0.4 0.4
Sodium Sulfate 5.5 5.5
Waterlminors Up to 100%
SUBSTITUTE SHEET (RULE 26)
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42
Example 3
Granular fabric cleaning compositions in accord with the invention are t
prepared as follows:
LAS 12.0 12.0
Zeolite A 26.0 26.0
SS 4.0 4.0
24AS 5.0 5.0
Citrate 5.0 5.0
Sodium Sulfate 17.0 17.0
Perborate 16.0 16.0
TAED 5.0 5.0
HPMC 0.3 0.5
MC1 0.75 -
Cellulase (1000CEVU) 0.1 0.3
'Water/minors Up to 100~
Example 4
Granular fabric cleaning compositions in accord with the invention
which are especially useful in the laundering of coloured fabrics are
prepared as follows:
I II III IV V VI
LAS 11.4 10.7 11.4 10.7 - -
TAS 1.8 2.4 1.8 2.4 - -
TI=AA - - - - 4.0 4.0
45AS 3.0 3.1 3.0 3.1 10.0 10.0
45E7 4.0 4.0 4.0 4.0 - ' -
25E3S - - - - 3.0 3.0
68E11 1.8 1.8 1.8 1.8 - -
25E5 - - - - 8.0 8.0
Citrate 14.0 15.0 14.0 15.0 7.0 7.0
Carbonate - - - - 10 10
Citric 3.0 2.5 3.0 2.5 3.0 3.0
acid
Zeolite 32.5 32.1 32.5 32.1 25.0 25.0
A
SUBSTITUTE SHEET (RULE 26)
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43
Na-SKS-6 - - - - 9.0 J.0
MA/AA 5.0 5.0 5.0 5.0 5.0 5.0
DETPMP 1.0 0.2 1.0 0.2 0.8 0.8
HPMC - - 0.5 - 0.5 -
MC1 0.75 0.75 - 0.75 - 0.75
Cellulase 0.1 0.15 0.3 0.2 0.05 0.5
(1000CEVU)
Silicate 2.0 2.5 2.0 2.5 - -
Sulphate 3.5 5.2 3.5 5.2 3.0 3.0
PVP 0.3 0.5 0.3 0.5 - -
Poly(4-vinyl - - - - 0.2 0.2
pyridine)-N-
oxidelcopoly
mer of vinyl-
imidazole &
vinyl-
pyrrolidone
Perborate 0.5 1.0 0.5 1.0 - -
Phenol 0.1 0.2 0.1 0.2 - -
sulfonate
Water/Minor Up to
s 100%
Example
5
Granular fabric cleaning compositi ons invention
in are
accord
with
the
prepared as follows:
I
II
LAS 6.5 8.0
S a (fate 15.0 18. 0
Zeolite A 26.0 22.0
Sodium nitrilotriacetate 5.0 5.0
PVP 0.5 0.7
TAED 3.0 3.0
Boric acid 4.0 -
Perborate 0.5 1.0
Phenol sulphonate 0.1 -
SUBSTITUTE ET
SHE (RULE
26)
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44
I~PMC 0.5 -
MC 1 - 0.75
Cellulase (1000CEVU) 0.1 0.2
S i licate 5.0 5.0
Carbonate 15.0 15.0
lNater/minors Up to 100%
Example 6
A granular fabric cleaning compositions in accord with the invention
which provide "softening through the wash" capability are prepared as
follows:
I II III IV
45AS - - 10.0 10.0
LAS 7.6 7.6 - -
68AS 1.3 1.3 - -
45E7 4.0 4.0 - -
25E3 - - 5.0 5.0
Coco-alkyl-dimethyl 1.4 1.4 1.0 1.0
hydroxy-
ethyl ammonium chloride
Citrate 5.0 5.0 3.0 3.0
Na-SKS-6 - - 11.0 11.0
Zeolite A 15.0 15.0 15.0 15.0
MA/AA 4.0 4.0 4.0 4.0
DETPMP 0.4 0.4 0.4 0.4
Perborate 15.0 15.0 - -
Percarbonate - - 15.0 15.0
TAED 5.0 5.0 5.0 5.0
Smectite clay 10.0 10.0 10.0 10.0
HMWPEO - - 0.1 0.1
HPMC - 0.5 - 0.5
MC1 0.75 - 0.75 -
Cellulase (1000CEVU) 0.1 0.2 0.05 0.37
Silicate 3.0 3.0 5.0 5.0
Carbonate 10.0 10.0 10.0 10.0
Granular suds suppressor 1.0 1.0 4.0 4.0
SUBSTITUTE SHEET (RULE 26)
CA 02206523 1997-OS-30
WO 96/20997 PCTlUS95116432
C M C 0.2 0.2 0.1 0.1
Water/minors Up to 100°~
What is claimed is.
SUBSTITUTE SHEET (RULE 26)
