FIELD OF THE INVENTION
[0001] This invention relates to cleaning compositions comprising cellulose derivatives.
The invention also relates to detergent compositions comprising cellulose enzyme,
such as bacterial alkaline enzyme exhibiting endo-beta-1,4-glucanase activity (E.C.
3.2.1.4). The invention also relates to processes for making and using such products.
BACKGROUND OF THE INVENTION
[0002] Cellulase enzymes have been used in detergent compositions for many years now for
their known benefits of depilling, softness and colour care. However, the use of most
of cellulases has been limited because of the negative impact that cellulase may have
on the tensile strength of the fabrics' fibers by hydrolysing crystalline cellulose.
Recently, cellulases with a high specificity towards amorphous cellulose have been
developed to exploit the cleaning potential of cellulases while avoiding the negative
tensile strength loss. Especially alkaline endo-glucanases have been developed to
suit better the use in alkaline detergent conditions.
[0003] For example, Novozymes in
WO02/099091 discloses a novel enzyme exhibiting endo-betaglucanase activity (EC 3.2.1.4) endogenous
to the strain
Bacillus sp., DSM 12648; for use in detergent and textile applications. Novozymes further describes
in
WO04/053039 detergent compositions comprising an anti-redeposition endo-glucanase and its combination
with certain cellulases having increased stability towards anionic surfactant and/or
further specific enzymes. Kao's
EP 265 832 describes novel alkaline cellulase K, CMCase I and CMCase II obtained by isolation
from a culture product
of Bacillus sp KSM-635. Kao further describes in
EP 1 350 843, alkaline cellulase which acts favourably in an alkaline environment and can be mass
produced readily because of having high secretion capacity or having enhanced specific
activity.
[0004] Anionically modified cellulose derivatives such as carboxymethyl cellulose (CMC)
are established anti-redeposition polymers in detergent compositions. The combination
of celluloses with CMC has been disclosed, for example in
GB-A-2095275. The present inventors have found that the combination of a specific alkaline bacterial
cellulose and specific modified celluloses leads to a significant improvement in cotton
stain repellency. Whilst not wishing to be bound by theory, it is believed that over
multiple wash cycles, the modified cellulose derivatives deposit on cotton items and
are acted upon by the bacterial alkaline cellulose so as to seal pores in the fibres
of the laundered fabric surface. This results in a fabric surface which is less likely
to form strong associations with particulate soils. There is therefore an improvement
in the appearance of the laundered fabric and improved cleaning.
SUMMARY OF THE INVENTION
[0005] The present invention relates to a composition comprising a modified cellulose derivative
and a cellulose enzyme, characterised in that the cellulose enzyme is a bacterial
alkaline enzyme exhibiting endo-beta 1,4-glucanase activity (E.C.3.2.1.4) and the
weight ratio of the modified cellulose component to the active cellulose enzyme protein
is from 1:1 to 10000:1. The compositions of the invention typically do not contain
0.7 to 0.9 wt % sodium nonanoyloxybenzene sulphonate. The compositions of the invention
typically do not contain 10 wt % sodium perborate monohydrate. The compositions of
the invention typically do contain less than 8 % by weight and/or greater than 8.5
% by weight sodium sulphate (anhydrous), more specifically do not contain 8.0 to 8.3
wt% sodium sulphate.
The present invention also includes a composition comprising a modified cellulose
derivative or mixtures thereof and a cellulase enzyme characterised in that the weight
ratio of the modified cellulose derivative to the active cellulase enzyme protein
is from 1:1 to 10000:1 1 and wherein the composition does not contain 0.7 to 0.9 %
by weight of the total composition, of sodium nonanoyl oxybenzene sulfonate, and does
not contain 10 % by weight based on the total composition, of sodium perborate monohydrate,
the enzyme producing reducing ends levels of greater than 5mM in the Enzyme Test defined
below.
Enzyme Test
[0006] The inventors have found that the effectiveness of the endo-beta-(1,4)-glucanase
/ modified cellulose derivative combination is driven by short oligosaccharide products
formed on hydrolysis of the polymer. The present inventors have found that the most
effective combinations involve the use of modified cellulose derivative as described
herein and an endo-beta-(1,4)-glucanase which provides effective hydrolysis of CMC
polymer down to small oligosaccharides as measured using reducing ends analysis as
follows, adapted from
J. Karlsson et al., Biopolymers, 2002, v63, pp. 32-40
[0007] CMC (250kDa weight average molecular mass, DS 0.7, supplied by Aldrich, Stenheim,
Germany), 10g/L, in 50mM sodium acetate pH 5.0 was hydrolysed with an excess of enzyme,
2betaM, for a prolonged hydrolysis time, 72hours. The hydrolysates were then cooled
to +4°C before carrying out reducing ends analysis using the dinitrosalicyclic acid
reagent, according to the protocol described in
M. Bailey et al, Enzyme Microb. Technol.,1981, v3, pp 153-157, with glucose being used for the standard curve.
[0008] The endo-beta-(1,4)-glucanase enzymes required for the present invention produce
reducing ends levels of greater than 5mM in this test, which correlates to ~10% reducing
ends. Preferred enzymes produce reducing end levels of greater than 10%, preferably
greater than 12% or even greater than 15%, using the Enzyme Test.
SEQUENCE LISTINGS
[0009]
SEQ ID NO: 1 shows the amino acid sequence of an endoglucanase from Bacillus sp. AA349
SEQ ID NO: 2 shows the amino acid sequence of an endoglucanase from Bacillus sp KSM-S237
DETAILED DESCRIPTION OF THE INVENTION
Definitions
[0010] As used herein, the term "cleaning composition" includes, unless otherwise indicated,
granular or powder-form all-purpose or "heavy-duty" washing agents, especially laundry
detergents; liquid, gel or paste-form all-purpose washing agents, especially the so-called
heavy-duty liquid types; liquid fine-fabric detergents; as well as cleaning auxiliaries
such as bleach additives and "stain-stick" or pre-treat types.
As used herein the term "modified cellulose derivative" comprises polymers comprising
a cellulose backbone wherein the cellulose is substituted with at least one substituent
or modifying group. A monomer of cellulose is shown below.

R1, R2 and R3 show the positions in the cellulose monomer available for substitution.
In the natural cellulose polymer, these groups comprise a hydrogen atom. The modified
cellulose derivative required according to the present invention comprise a substituent
at one or more of these positions in the polymer. Typically the modifying groups will
be non-ionic or anionic groups, producing nonionically or anionically modified cellulose,
respectively. Alternatively, the modified cellulose derivative may be provided by
other beta-1,4-linked polysaccharides such as xyloglucan (e.g. derived from Tamarind
seed gum), glucomannan (e.g. Konjac glucomannan), galactomannan (e.g. derived from
guar gum or locust bean gum), side-chain branched galactomannan (e.g. Xanthan gum),
chitosan or a chitosan salt. Derivatives of starch, an alpha-1,4-linked polysaccharide
may also be present. The natural polysaccharides, whether beta-1,4 or alpha-1,4, can
be modified with amines (primary, secondary, tertiary), amides, esters, ethers, urethanes,
alcohols, carboxylic acids, tosylates, sulfonates, sulfates, nitrates, phosphates
and mixtures thereof. Examples of suitable derivatives are given in
WO 06/117071 (Unilever), such as carboxymethyl Locust Bean gum and Locust Bean gum ethyl sulfonate.
Preferred are anionically modified cellulose derivatives such as carboxymethyl cellulose.
COMPOSITIONS
[0011] The compositions of the present invention typically may contain from 0.00002% to
0.15%, from 0.00005% to 0.12%, or even from 0.0002% to 0.02% or even 0.005% to 0.025%
by weight of pure enzyme, of one or more endoglucanase(s). The balance of any aspects
of the aforementioned cleaning compositions is made up of cellulose derivative and
one or more adjunct materials.
SUITABLE ENDOGLUCANASE
[0012] The endoglucanase to be incorporated into the detergent composition of the present
invention is one or more bacterial alkaline enzyme(s) exhibiting endo-beta-1,4-glucanase
activity (E.C. 3.2.1.4).
[0013] As used herein, the term "alkaline endoglucanase", shall mean an endoglucanase having
an optimum pH above 7 and retaining greater than 70% of its optimal activity at pH10.
[0014] Preferably, the endoglucanase is a bacterial polypeptide endogenous to a member of
the genus
Bacillus.
More preferably, the alkaline enzyme exhibiting endo-beta-1,4-glucanase activity (E.C.
3.2.1.4), is a polypeptide containing (i) at least one family 17 carbohydrate binding
module (Family 17 CBM) and/or (ii) at least one family 28 carbohydrate binding module
(Family 28 CBM). Please refer for example to: Current Opinion in Structural Biology,
2001, 593-600 by Y. Bourne and B.
[0015] Henrissat in their article entitled: "Glycoside hydrolases and glycosyltransferases:
families and functional modules" for the definition and classification of CBMs. Please
refer further to
Biochemical Journal, 2002, v361, 35-40 by A.B. Boraston et al in their article entitled: "Identification and glucan-binding properties of
a new carbohydrate-binding module family" for the properties of the family 17 and
28 CBM's.
[0016] In a more preferred embodiment, said enzyme comprises a polypeptide (or variant thereof)
endogenous to one of the following
Bacillus species:
Bacillus sp. |
As described in: |
AA349 (DSM 12648) |
WO 2002/099091A (Novozymes) p2, line 25 WO 2004/053039A (Novozymes) p3, line19 |
KSM S237 |
EP 1350843A (Kao) p3, line 18 |
1139 |
EP 1350843A (Kao) p3, line 22 |
KSM 64 |
EP 1350843A (Kao) p3, line 24 |
KSM N131 |
EP 1350843A (Kao) p3, line 25 |
KSM 635, FERM BP 1485 |
EP 265 832A (Kao) p7, line 45 |
KSM 534, FERM BP 1508 |
EP 0271044 A (Kao) p9, line 21 |
KSM 539, FERM BP 1509 |
EP 0271044 A (Kao) p9, line 22 |
KSM 577, FERM BP 1510 |
EP 0271044 A (Kao) p9, line 22 |
KSM 521, FERM BP 1507 |
EP 0271044 A (Kao) p9, line 19 |
KSM 580, FERM BP 1511 |
EP 0271044 A (Kao) p9, line 20 |
KSM 588, FERM BP 1513 |
EP 0271044 A (Kao) p9, line 23 |
KSM 597, FERM BP 1514 |
EP 0271044 A (Kao) p9, line 24 |
KSM 522, FERM BP 1512 |
EP 0271044 A (Kao) p9, line 20 |
KSM 3445, FERM BP 1506 |
EP 0271044 A (Kao) p10, line 3 |
KSM 425. FERM BP 1505 |
EP 0271044 A (Kao) p10, line 3 |
Suitable endoglucanases for the compositions of the present invention are:
1) An enzyme exhibiting endo-beta-1,4-glucanase activity (E.C. 3.2.1.4), which has
a sequence of at least 90%, preferably 94%, more preferably 97% and even more preferably
99%, 100% identity to the amino acid sequence of position 1 to position 773 of SEQ
ID NO:1 (Corresponding to SEQ ID NO:2 in
WO02/099091); or a fragment thereof that has endo-beta-1,4-glucanase activity, when identity
is determined by GAP provided in the GCG program using a GAP creation penalty of 3.0
and GAP extension penalty of 0.1. The enzyme and the corresponding method of production
is described extensively in patent application
WO02/099091 published by Novozymes A/S on December 12, 2002. Please refer to the detailed description pages 4 to 17 and to the examples page
20 to page 26. One of such enzyme is commercially available under the tradename Celluclean
™ by Novozymes A/S. GCG refers to the sequence analysis software package provided by
Accelrys, San Diego, CA, USA. This incorporates a program called GAP which uses the
algorithm of Needleman and Wunsch to find the alignment of two complete sequences
that maximises the number of matches and minimises the number of gaps.
2) Also suitable are the alkaline endoglucanase enzymes described in
EP 1 350 843A published by Kao corporation on October 8, 2003. Please refer to the detailed description [0011] to [0039] and examples 1 to 4 [0067]
to [0077] for a detailed description of the enzymes and its production. The alkaline
cellulase variants are obtained by substituting the amino acid residue of a cellulase
having an amino acid sequence exhibiting at least 90%, preferably 95%, more preferably
98% and even 100% identity with the amino acid sequence represented by SEQ. ID NO:2
(Corresponding to SEQ. ID NO:1 in
EP 1 350 843 on pages 11-13) at (a) position 10, (b) position 16, (c) position 22, (d) position
33, (e) position 39, (f) position 76, (g) position 109, (h) position 242, (i) position
263, (j) position 308, (k) position 462, (1) position 466, (m) position 468, (n) position
552, (o) position 564, or (p) position 608 in SEQ ID NO:2 or at a position corresponding
thereto with another amino acid residue
Examples of the "alkaline cellulase having the amino acid sequence represented by
SEQ. ID NO:2" include Egl-237 [derived from
Bacillus sp. strain KSM-S237 (FERM BP-7875),
Hakamada, et al., Biosci. Biotechnol. Biochem., 64, 2281-2289, 2000]. Examples of the "alkaline cellulase having an amino acid sequence exhibiting at
least 90% homology with the amino acid sequence represented by SEQ. ID NO:2" include
alkaline cellulases having an amino acid sequence exhibiting preferably at least 95%
homology, more preferably at least 98% homology, with the amino acid sequence represented
by SEQ. ID NO:2. Specific examples include alkaline cellulase derived from
Bacillus sp. strain 1139 (Eg1-1139) (
Fukumori, et al., J. Gen. Microbiol., 132, 2329-2335) (91.4% homology), alkaline cellulases derived from
Bacillus sp. strain KSM-64 (Eg1-64) (
Sumitomo, et al., Biosci. Biotechnol. Biochem., 56, 872-877, 1992) (homology: 91.9%), and cellulase derived from
Bacillus sp. strain KSM-N131 (Eg1-N131b) (
Japanese Patent Application No. 2000-47237) (homology: 95.0%).
The amino acid is preferably substituted by: glutamine, alanine, proline or methionine,
especially glutamine is preferred at position (a), asparagine or arginine, especially
asparagine is preferred at position (b), proline is preferred at position (c), histidine
is preferred at position (d), alanine, threonine or tyrosine, especially alanine is
preferred at position (e), histidine, methionine, valine, threonine or alanine, especially
histidine is preferred at position (f), isoleucine, leucine, serine or valine, especially
isoleucine is preferred at position (g), alanine, phenylalanine, valine, serine, aspartic
acid, glutamic acid, leucine, isoleucine, tyrosine, threonine, methionine or glycine,
especially alanine, phenylalanine or serine is preferred at position (h), isoleucine,
leucine, proline or valine, especially isoleucine is preferred at position (i), alanine,
serine, glycine or valine, especially alanine is preferred at position (j), threonine,
leucine, phenylalanine or arginine, especially threonine is preferred at position
(k), leucine, alanine or serine, especially leucine is preferred at position (1),
alanine, aspartic acid, glycine or lysine, especially alanine is preferred at position
(m), methionine is preferred at position (n), valine, threonine or leucine, especially
valine is preferred at position (o) and isoleucine or arginine, especially isoleucine
is preferred at position (p).
The "amino acid residue at a position corresponding thereto" can be identified by
comparing amino acid sequences by using known algorithm, for example, that of Lipman-Pearson's
method, and giving a maximum similarity score to the multiple regions of similarity
in the amino acid sequence of each alkaline cellulase. The position of the homologous
amino acid residue in the sequence of each cellulase can be determined, irrespective
of insertion or depletion existing in the amino acid sequence, by aligning the amino
acid sequence of the cellulase in such manner (Fig. 1 of
EP 1 350 843). It is presumed that the homologous position exists at the three-dimensionally same
position and it brings about similar effects with regard to a specific function of
the target cellulase.
With regard to another alkaline cellulase having an amino acid sequence exhibiting
at least 90% homology with SEQ. ID NO:2, specific examples of the positions corresponding
to (a) position 10, (b), position 16, (c) position 22, (d) position 33, (e) position
39, (f) position 76, (g) position 109, (h) position 242, (i) position 263, (j) position
308, (k) position 462, (1) position 466, (m) position 468, (n) position 552, (o) position
564 and (p) position 608 of the alkaline cellulase (Eg1-237) represented by SEQ. ID
NO: 2 and amino acid residues at these positions will be shown below:
|
Egl-237 |
Egl-1139 |
Egl-64 |
Egl-N131b |
(a) |
10Leu |
10Leu |
10Leu |
10Leu |
(b) |
16Ile |
16Ile |
16Ile |
Nothing corresponding thereto |
(c) |
22Ser |
22Ser |
22Ser |
Nothing corresponding thereto |
(d) |
33Asn |
33Asn |
33Asn |
19Asn |
(e) |
39Phe |
39Phe |
39Phe |
25Phe |
(f) |
76I1e |
76I1e |
76I1e |
62I1e |
(g) |
109Met |
109Met |
109Met |
95Met |
(h) |
242Gln |
242Gln |
242Gln |
228Gln |
(i) |
263Phe |
263Phe |
263Phe |
249Phe |
(j) |
308Thr |
308Thr |
308Thr |
294Thr |
(k) |
462Asn |
461Asn |
461Asn |
448Asn |
(l) |
466Lys |
465Lys |
465Lys |
452Lys |
(m) |
468Val |
467Val |
467Val |
454Val |
(n) |
552Ile |
550Ile |
550Ile |
538Ile |
(o) |
564Ile |
562Ile |
562Ile |
5501le |
(p) |
608Ser |
606Ser |
606Ser |
594Ser |
3) Also suitable is the alkaline cellulase K described in
EP 265 832A published by Kao on May 4, 1988. Please refer to the description page 4, line 35 to page 12, line 22 and examples
1 and 2 on page 19 for a detailed description of the enzyme and its production. The
alkaline cellulase K has the following physical and chemical properties:
- (1) Activity: Having a Cx enzymatic activity of acting on carboxymethyl cellulose
along with a weak C1 enzymatic activity and a weak beta-glucoxidase activity;
- (2) Specificity on Substrates: Acting on carboxymethyl cellulose(CMC), crystalline
cellulose, Avicell, cellobiose, and p-nitrophenyl cellobioside(PNPC);
- (3) Having a working pH in the range of 4 to 12 and an optimum pH in the range of
9 to 10;
- (4) Having stable pH values of 4.5 to 10.5 and 6.8 to 10 when allowed to stand at
40°C for 10 minutes and 30 minutes, respectively;
- (5) Working in a wide temperature range of from 10 to 65°C with an optimum temperature
being recognized at about 40°C;
- (6) Influences of chelating agents: The activity not impeded with ethylenediamine
tetraacetic acid (EDTA), ethyleneglycol-bis-(β-aminoethylether) N,N,N',N"-tetraacetic
acid (EGTA), N,N-bis(carboxymethyl)glycine (nitrilotriacetic acid) (NTA), sodium tripolyphosphate
(STPP) and zeolite;
- (7) Influences of surface active agents: Undergoing little inhibition of activity
by means of surface active agents such as sodium linear alkylbenzenesulfonates (LAS),
sodium alkylsulfates (AS), sodium polyoxyethylene alkylsulfates (ES), sodium alphaolefinsulfonates
(AOS), sodium alpha-sulfonated aliphatic acid esters (alpha-SFE), sodium alkylsulfonates
(SAS), polyoxyethylene secondary alkyl ethers, fatty acid salts (sodium salts), and
dimethyldialkylammonium chloride;
- (8) Having a strong resistance to proteinases; and
- (9) Molecular weight (determined by gel chromatography): Having a maximum peak at
180,000 ±10,000.
Preferably such enzyme is obtained by isolation from a culture product of
Bacillus sp KSM-635.
Cellulase K is commercially available by the Kao Corporation: e.g. the cellulase preparation
Eg-X known as KAC® being a mixture of E-H and E-L both from Bacillus sp. KSM-635 bacterium.
Cellulases E-H and E-L have been described in
S. Ito, Extremophiles, 1997, v1, 61-66 and in
S. Ito et al, Agric Biol Chem, 1989, v53, 1275-1278.
4) The alkaline bacterial endoglucanases described in
EP 271 004A published by Kao on June 15, 1988 are also suitable for the purpose of the present invention. Please refer to the description
page 9, line 15 to page 23, line 17 and page 31, line 1 to page 33, line 17 for a
detailed description of the enzymes and its production. Those are:
Alkaline Cellulase K-534 from KSM 534, FERM BP 1508,
Alkaline Cellulase K-539 from KSM 539, FERM BP 1509,
Alkaline Cellulase K-577 from KSM 577, FERM BP 1510,
Alkaline Cellulase K-521 from KSM 521, FERM BP 1507,
Alkaline Cellulase K-580 from KSM 580, FERM BP 1511,
Alkaline Cellulase K-588 from KSM 588, FERM BP 1513,
Alkaline Cellulase K-597 from KSM 597, FERM BP 1514,
Alkaline Cellulase K-522 from KSM 522, FERM BP 1512,
Alkaline Cellulase E-II from KSM 522, FERM BP 1512,
Alkaline Cellulase E-III from KSM 522, FERM BP 1512.
Alkaline Cellulase K-344 from KSM 344, FERM BP 1506, and
Alkaline Cellulase K-425 from KSM 425, FERM BP 1505.
5) Finally, the alkaline endoglucanases derived from Bacillus species KSM-N described
in
JP2005287441A, published by Kao on the October 20th, 2005, are also suitable for the purpose of the present invention. Please refer to the
description page 4, line 39 to page 10, line 14 for a detailed description of the
enzymes and its production. Examples of such alkaline endoglucanases are:
Alkaline Cellulase Egl-546H from Bacillus sp. KSM-N546
Alkaline Cellulase Eg1-115 from Bacillus sp. KSM-N115
Alkaline Cellulase Egl-145 from Bacillus sp. KSM-N145
Alkaline Cellulase Egl-659 from Bacillus sp.KSM-N659
Alkaline Cellulase Egl-640 from Bacillus sp.KSM-N440
Also encompassed in the present invention are variants of the above described enzymes
obtained by various techniques known by persons skilled in the art such as directed
evolution.
MODIFIED CELLULOSE DERIVATIVE
[0017] The modified cellulose derivative required in the present invention comprises a polymer
comprising a cellulose backbone. The cellulose may be anionically or nonionically
modified, preferably anionically modified. A monomer of cellulose is shown below.

R1, R2 and R3 show the positions in the cellulose monomer available for substitution.
In the natural cellulose polymer, these groups comprise a hydrogen atom. The modified
cellulose derivative useful herein comprises substituents at one or more of these
positions. For example for anionic substitution, one or more of these positions in
the polymer are substituted with an anionic group for example, one of the following
anionic groups, in its acid or salt form, preferably sodium (given here) or potassium
salt form.
- L-CO2Na
- L-SO3Na
- PO3Na
- SO3Na
Wherein:
L is C1-6 alkyl, more preferably C1-4 alkyl
[0018] The anionically modified cellulose derivative may also comprise non-ionic substituent
groups in which one or more of positions R1, R2 and R3 may be substituted with nonionic
groups, for example,
-A
-L-OH
-L-CN
-C(=O)A
-C(=O)NH2
-C(=O)NHA
-C(=O)N(A)B
-C(=O)OA
-(CH2CH2CH2O)nZ
-(CH2CH2O)nZ
-(CH2CH(CH3)O)nZ
-(CH2O)nZ
Wherein:
A and B are C1-30 alkyl
L is C1-6 alkyl
n=1 to 100
Z is H or C1-6 alkyl
[0019] Non-limiting examples of suitable modified cellulose derivatives are the sodium or
potassium salts of carboxymethyl cellulose, carboxyethyl cellulose, sulfoethyl cellulose,
sulfopropyl cellulose, cellulose sulfate, phosphorylated cellulose, carboxymethyl
hydroxyethyl cellulose, carboxymethyl hydroxypropyl cellulose, sulfoethyl hydroxyethyl
cellulose, sulfoethyl hydroxypropyl cellulose, carboxymethyl methyl hydroxyethyl cellulose,
carboxymethyl methyl cellulose, sulfoethyl methyl hydroxyethyl cellulose, sulfoethyl
methyl cellulose, carboxymethyl ethyl hydroxyethyl cellulose, carboxymethyl ethyl
cellulose, sulfoethyl ethyl hydroxyethyl cellulose, sulfoethyl ethyl cellulose, carboxymethyl
methyl hydroxypropyl cellulose, sulfoethyl methyl hydroxypropyl cellulose, carboxymethyl
dodecyl cellulose, carboxymethyl dodecoyl cellulose, carboxymethyl cyanoethyl cellulose
and sulfoethyl cyanoethyl cellulose,
Nonionically modified cellulose
[0020] The modified cellulose derivative may be provided by a nonionically modified cellulose
derivative instead of or in addition to the anionically modified cellulose polymer.
Examples of nonionically modified cellulose polymers include methyl cellulose, ethyl
cellulose, propyl cellulose, hydroxyethyl cellulose, hydroxypropyl cellulose, methyl
hydroxyethyl cellulose, ethyl hydroxyethyl cellulose, dodecyl hydroxyethyl cellulose,
ethyl hydroxypropyl cellulose, cellulose acetate, methyl hydroxypropyl cellulose,
methyl ethyl hydroxyethyl cellulose, butyl glycidyl ether-hydroxyethyl cellulose,
and lauryl glycidyl ether-hydroxyethyl cellulose
[0021] Specific examples include Finnfix BDA (from Noviant), Tylose CR1500 G2 (from Clariant),
Carbose codes D65, D72, LT-30 and LT-20 (from Penn Carbose); hydrophobically modified
cellulose derivatives for example as described in
WO99/61479 (Noviant); cellulose derivatives modified with polyethylene glycol, for example as
described in
DE102004063766
[0022] Particularly preferred modified cellulose derivatives have a weight average molecular
mass of at least 20 000 or at least 50 000 or even at least 100 000 or even at least
150 000 kDaltons. The weight average molecular mass of the modified cellulose derivative
will generally be no greater than 500 000, or no greater than 300 000 or no greater
than 250 000kDa. Preferred degrees of substitution (DS) are from 0.3, or 0.4, or 0.45
up to for example 0.7 or even 0.8 or even 0.9. Particularly preferred are modified
methyl celluloses, such as CMC, with such molecular weights and/or degrees of substitution
and/or levels as described herein.
[0023] The level of modified cellulose derivative in the detergent compositions of the invention
is typically from at least 0.005 or 0.01 wt% or 0.02 or at least 0.05 wt% or even
at least 0.1 wt% based on the total weight of detergent composition. Typically, the
levels will be no greater than 5% by weight or even no greater than 2% by weight or
even no greater than 1.5% by weight of the detergent composition. In a particularly
preferred embodiment of the invention the weight ratio of modified cellulose derivative
to active cellulase enzyme protein is from 1:1 to 10000:1, preferably 20:1 to 1000:1,
most preferably 30:1 to 800:1.
[0024] Cellulose derivatives such as methyl celluloses have been incorporated into detergent
compositions for many years. They deposit onto cotton fabric surfaces to form a negatively
charged soil-repellant layer, which repels soils reducing deposition onto a fabric
surface. The present inventors have found that cellulose derivatives having a much
lower molecular weight than is traditionally used can provide further surprising benefits
as they act as anti-redeposition aids by suspending soils in the wash liquor. These
cellulose derivatives may be formed in situ by reaction of specific cellulose agent
pre-cursors.
[0025] The modified cellulose derivative may be added as a dry particulate component comprising
for example greater than 50 % or even greater than 60 % or 70 % or 80% by weight,
up to 100 % by weight modified cellulose derivative. The modified cellulose derivative
may be incorporated into the detergent compositions of the invention as part of a
processed particle formed by a conventional detergent particle-making process, such
as spray-drying, agglomeration or extrusion. In such cases, the amount of modified
cellulose derivative in such particle will be at least 0.1 % or 0.5 or 1 % by weight
and is likely to be less than 70% and more likely, less than 60 % or 50 %, 40%, 30%
or even less than 20 % or 10% by weight of the processed particle. Introducing the
modified cellulose derivative as part of a processed detergent particle may be particularly
preferred especially for detergent compositions containing low levels of phosphate
and/or zeolite builders; for example less than 15% by weight of the total detergent
composition or even less than 14% or 12 % or 10 % or 8 % down to 0 % by weight phosphate
and/or zeolite builders. This may be preferred as it may promote uniform distribution
of the cellulose throughtout the wash liquor on addition of the detergent composition
to water, by helping solubility of the cellulose derivative. Where the modified cellulose
derivative is present in a processed detergent particle, the processed detergent particle
may comprise any other conventional detergent ingredients or components thereof such
as any of the adjunct materials described below or, for example as described in
JP 2002 265999 (Kao) or in any of the processes described below under the sub-heading "Processes of Making
Compositions". In particular such particles may comprise at least 1, or at least 5
or 10 % by weight up to 15 or 20 or 30 % by weight polymeric polycarboxylate polymer
such as acrylic acid and/or maleic acid-based homo-or co- polymers (e.g. Sokalan polymers
from BASF), based on the weight of the processed particle. The processed particles
may comprise anionic, non-ionic, cationic, zwitterionic and/or amphoteric surfactants
or mixtures thereof. Amounts may be form 1 to 70 % by weight, or 2 to 60% or from5
to 850 % by weight based on the total weight of the processed particle. For example,
processed particles may comprise non-ionic surfactant optionally in combination with
anionic and/or cationic surfactants. Suitable surfactants are described in the "Surfactants"
section of the description. In particular, suitable non-ionic surfactants include
alkyl alkoxylated surfactant, e.g ethoxylated surfactants having a degree of alkoxylation
from 3 to 20 or even higher such as 20 to 50.
Processed particles may comprise sodium silicate (especially 1 to 2 ratio) in amounts
from 1 to 30 % by weight or 2 to 25 % by weight or from 5 to 20 % by weight.
Preferred compositions according to the invention comprise polymeric polycarboxylate
polymers and in such an amount that the weight ratio of polymeric polycarboxylate
to modified cellulose derivative is at least 2:1, more preferably at least 2.5:1 and
most preferably at least 3:1 or even 4:1 or 5:1. Such ratios may also be preferred
in the processed particles discussed above, where polymeric polycarboxylate is present.
The bulk density of the composition of the invention and/or more specifically the
modified cellulose derivative-containing particles is typically at least 450 g/l or
at least 550g/l or 650g/l or at least 700g/l, up to 1500g/l. Bulk density is measured
by means of a simple funnel and cup device consisting of a conical funnel mounted
rigidly on a base and provided with a flap valve at its lower extremity to allow the
contents of the funnel to be emptied into an axially aligned cylindrical cup disposed
below the funnel. The funnel is 130 mm high and has internal diameters of 130 mm and
40 mm at its respective upper and lower extremities. It is mounted so that the lower
extremity is 140 mm above the upper surface of the base. The cup has an overall height
of 90 mm, an internal height of 87 mm and an internal diameter of 84 mm. Its nominal
volume is 500 ml. To carry out a measurement, the funnel is filled with powder by
hand pouring, the flap valve is opened and powder is allowed to overfill the cup.
The filled cup is removed from the frame and excess powder is removed from the cup
by passing a straight edged implement eg. a knife, across its upper edge. The filled
cup is then weighed and the value obtained for the weight of powder doubled to provide
a bulk density of g/litre. Replicate measurements are made and an average of three
results provides the bulk density.
[0026] The present inventors have further provided detergent compositions which provide
soil suspension properties.
In accordance with a further embodiment of the invention, there is therefore provided
a detergent composition comprising oligosaccharides having a weight average molecular
mass of less than 20 000 kDa, such oligosaccharide being obtainable by reaction of
an enzyme as defined above with an anionically modified cellulose having an average
molecular weight from 30 000 to 500 000 kDa. In a further embodiment of said invention,
there is provided an aqueous wash liquor comprising a detergent composition wherein
the oligosaccharide is comprised in amounts from 0.5ppm to 1000 ppm, or from 0.8 to
1500 ppm or from 1.0 to 1000ppm.
In accordance with a further embodiment of the invention, there is provided use of
oligosaccharide having a weight average molecular mass of less than 20 000 kDa, such
oligosaccharide being obtainable by reaction of an enzyme as described above, with
an anionically or nonionically, preferably anionically modified cellulose derivative
having a weight average molecular mass from 30 000 to 500 000 kDa, for preparation
of a detergent composition, for soil suspension.
In accordance with a further aspect of the invention there is also provided a detergent
composition comprising an enzyme as described above and at least 2 wt%, or even at
least 5 wt%, 10 wt%, 15, 20 wt% or higher for example up to 50 wt% or 40 wt% or 30
wt% or 25 wt% , of a phosphate builder salt, at least 25, or 30 or 40 or 45 or 50
or even 55 wt% up to 100 wt% or 90 wt% or 80 wt% of said phosphate builder comprising
pyrophosphate builder.
This pyrophosphate builder may be formed in situ by spray drying a composition comprising
sodium or other salt of tri polyphosphate or acid form in a spray drying process in
which the temperature and/or air flow and/or other chemical constituents in the spray
drying slurry are controlled to provide the desired reaction of the tripolyphosphate
to pyrophosphate salt. The process may be operated for example as described in
WO03/091378 or
US4310431.
Adjunct Materials
[0027] While not essential for the purposes of the present invention, the non-limiting list
of adjuncts illustrated hereinafter are suitable for use in the instant compositions
and may be desirably incorporated in certain embodiments of the invention, for example
to assist or enhance cleaning performance, for treatment of the substrate to be cleaned,
or to modify the aesthetics of the cleaning composition as is the case with perfumes,
colorants, dyes or the like. 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. Suitable adjunct
materials include, but are not limited to, surfactants, builders, chelating agents,
dye transfer inhibiting agents, dispersants, additional enzymes, and enzyme stabilizers,
catalytic materials, bleach activators, hydrogen peroxide, sources of hydrogen peroxide,
preformed peracids, polymeric dispersing agents, clay soil removal/anti-redeposition
agents, brighteners, suds suppressors, dyes, perfumes, structure elasticizing agents,
fabric softeners, carriers, hydrotropes, processing aids, solvents and/or pigments.
In addition to the disclosure below, suitable examples of such other adjuncts and
levels of use are found in
U.S. Patent Nos. 5,576,282,
6,306,812 B1 and
6,326,348 B1 that are incorporated by reference. When one or more adjuncts are present, such one
or more adjuncts may be present as detailed below:
[0028] Bleaching Agents - The cleaning compositions of the present invention may comprise
one or more bleaching agents. Suitable bleaching agents other than bleaching catalysts
include other photobleaches, bleach activators, hydrogen peroxide, sources of hydrogen
peroxide, pre-formed peracids and mixtures thereof. In general, when a bleaching agent
is used, the compositions of the present invention may comprise from about 0.1% to
about 50% or even from about 0.1 % to about 25% bleaching agent by weight of the subject
cleaning composition. Examples of suitable bleaching agents include:
- (1) other photobleaches for example Vitamin K3;
- (2) preformed peracids: Suitable preformed peracids include, but are not limited to,
compounds selected from the group consisting of percarboxylic acids and salts, percarbonic
acids and salts, perimidic acids and salts, peroxymonosulfuric acids and salts, for
example, Oxone ®, and mixtures thereof. Suitable percarboxylic acids include hydrophobic
and hydrophilic peracids having the formula R-(C=O)O-O-M wherein R is an alkyl group,
optionally branched, having, when the peracid is hydrophobic, from 6 to 14 carbon
atoms, or from 8 to 12 carbon atoms and, when the peracid is hydrophilic, less than
6 carbon atoms or even less than 4 carbon atoms; and M is a counterion, for example,
sodium, potassium or hydrogen;
- (3) sources of hydrogen peroxide, for example, inorganic perhydrate salts, including
alkali metal salts such as sodium salts of perborate (usually mono- or tetra-hydrate),
percarbonate, persulphate, perphosphate, persilicate salts and mixtures thereof. In
one aspect of the invention the inorganic perhydrate salts are selected from the group
consisting of sodium salts of perborate, percarbonate and mixtures thereof. When employed,
inorganic perhydrate salts are typically present in amounts of from 0.05 to 40 wt%,
or 1 to 30 wt% of the overall composition and are typically incorporated into such
compositions as a crystalline solid that may be coated. Suitable coatings include,
inorganic salts such as alkali metal silicate, carbonate or borate salts or mixtures
thereof, or organic materials such as water-soluble or dispersible polymers, waxes,
oils or fatty soaps; and
- (4) bleach activators having R-(C=O)-L wherein R is an alkyl group, optionally branched,
having, when the bleach activator is hydrophobic, from 6 to 14 carbon atoms, or from
8 to 12 carbon atoms and, when the bleach activator is hydrophilic, less than 6 carbon
atoms or even less than 4 carbon atoms; and L is leaving group. Examples of suitable
leaving groups are benzoic acid and derivatives thereof - especially benzene sulphonate.
Suitable bleach activators include dodecanoyl oxybenzene sulphonate, decanoyl oxybenzene
sulphonate, decanoyl oxybenzoic acid or salts thereof, 3,5,5-trimethyl hexanoyloxybenzene
sulphonate, tetraacetyl ethylene diamine (TAED) and nonanoyloxybenzene sulphonate
(NOBS). Suitable bleach activators are also disclosed in WO 98/17767. While any suitable bleach activator may be employed, in one aspect of the invention
the subject cleaning composition may comprise NOBS, TAED or mixtures thereof.
[0029] When present, the peracid and/or bleach activator is generally present in the composition
in an amount of from about 0.1 to about 60 wt%, from about 0.5 to about 40 wt % or
even from about 0.6 to about 10 wt% based on the composition. One or more hydrophobic
peracids or precursors thereof may be used in combination with one or more hydrophilic
peracid or precursor thereof.
[0030] The amounts of hydrogen peroxide source and peracid or bleach activator may be selected
such that the molar ratio of available oxygen (from the peroxide source) to peracid
is from 1:1 to 35:1, or even 2:1 to 10:1.
[0031] Surfactants - The cleaning compositions according to the present invention may comprise
a surfactant or surfactant system wherein the surfactant can be selected from nonionic
surfactants,
[0032] anionic surfactants, cationic surfactants, ampholytic surfactants, zwitterionic surfactants,
semi-polar nonionic surfactants and mixtures thereof. When present, surfactant is
typically present at a level of from about 0.1% to about 60%, from about 1% to about
50% or even from about 5% to about 40% by weight of the subject composition.
[0033] Builders - The cleaning compositions of the present invention may comprise one or
more detergent builders or builder systems. When a builder is used, the subject composition
will typically comprise at least about 1%, from about 5% to about 60% or even from
about 10% to about 40% builder by weight of the subject composition.
[0034] Builders include, but are not limited to, the alkali metal, ammonium and alkanolammonium
salts of polyphosphates, alkali metal silicates, alkaline earth and alkali metal carbonates,
aluminosilicate builders and polycarboxylate compounds, ether hydroxypolycarboxylates,
copolymers of maleic 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 polyacetic acids such as
ethylenediamine tetraacetic acid and nitrilotriacetic acid, as well as polycarboxylates
such as mellitic acid, succinic acid, citric acid, oxydisuccinic acid, polymaleic
acid, benzene 1,3,5-tricarboxylic acid, carboxymethyloxysuccinic acid, and soluble
salts thereof.
[0035] Chelating Agents - The cleaning compositions herein may contain a chelating agent.
Suitable chelating agents include copper, iron and/or manganese chelating agents and
mixtures thereof. When a chelating agent is used, the subject composition may comprise
from about 0.005% to about 15% or even from about 3.0% to about 10% chelating agent
by weight of the subject composition.
[0036] Dye Transfer Inhibiting Agents - The cleaning compositions of the present invention
may also include one or more dye transfer inhibiting agents. Suitable polymeric dye
transfer inhibiting agents include, but are not limited to, polyvinylpyrrolidone polymers,
polyamine N-oxide polymers, copolymers of N-vinylpyrrolidone and N-vinylimidazole,
polyvinyloxazolidones and polyvinylimidazoles or mixtures thereof. When present in
a subject composition, the dye transfer inhibiting agents may be present at levels
from about 0.0001 % to about 10%, from about 0.01% to about 5% or even from about
0.1% to about 3% by weight of the composition.
[0037] Fluorescent whitening agent - The cleaning compositions of the present invention
will preferably also contain additional components that may tint articles being cleaned,
such as fluorescent whitening agent. Any fluorescent whitening agent suitable for
use in a laundry detergent composition may be used in the composition of the present
invention. The most commonly used fluorescent whitening agents are those belonging
to the classes of diaminostilbene-sulphonic acid derivatives, diarylpyrazoline derivatives
and bisphenyl-distyryl derivatives. Examples of the diaminostilbene-sulphonic acid
derivative type of fluorescent whitening agents include the sodium salts of:
4,4'-bis-(2-diethanolamino-4-anilino-s-triazin-6-ylamino) stilbene-2,2'-disulphonate,
4,4'-bis-(2,4-dianilino-s-triazin-6-ylamino) stilbene-2.2'-disulphonate,
4,4'-bis-(2-anilino-4(N-methyl-N-2-hydroxy-ethylamino)-s-triazin-6-ylamino) stilbene-2,2'-disulphonate,
4,4'-bis-(4-phenyl-2,1,3-triazol-2-yl)stilbene-2,2'-disulphonate,
4,4'-bis-(2-anilino-4(1-methyl-2-hydroxy-ethylamino)-s-triazin-6-ylamino) stilbene-2,2'-disulphonate
and,
2-(stilbyl-4"-naptho-1.,2':4,5)-1,2,3-trizole-2"-sulphonate.
Preferred fluorescent whitening agents are Tinopal® DMS and Tinopal® CBS available
from Ciba-Geigy AG, Basel, Switzerland. Tinopal® DMS is the disodium salt of 4,4'-bis-(2-morpholino-4
anilino-s-triazin-6-ylamino) stilbene disulphonate. Tinopal® CBS is the disodium salt
of 2,2'-bis-(phenyl-styryl) disulphonate.
[0038] Also preferred are fluorescent whitening agents of the structure:

wherein R1 and R2, together with the nitrogen atom linking them, form an unsubstituted
or C1-C4 alkyl-substituted morpholino, piperidine or pyrrolidine ring, preferably
a morpholino ring (commercially available as Parawhite KX, supplied by Paramount Minerals
and Chemicals, Mumbai, India)
Other fluorescers suitable for use in the invention include the 1-3-diaryl pyrazolines
and the 7-alkylaminocoumarins.
Suitable fluorescent brightener levels include lower levels of from about 0.01, from
0.05, from about 0.1 or even from about 0.2 wt % to upper levels of 0.5 or even 0.75
wt %.
[0039] Fabric hueing agents- dyes or pigments which when formulated in detergent compositions
can deposit onto a fabric when said fabric is contacted with a wash liquor comprising
said detergent compositions thus altering the tint of said fabric through absorption
of visible light. Fluorescent whitening agents emit at least some visible light. In
contrast, fabric hueing agents alter the tint of a surface as they absorb at least
a portion of the visible light spectrum. Suitable fabric hueing agents include dyes
and dye-clay conjugates, and may also include pigments. Suitable dyes include small
molecule dyes and polymeric dyes. Suitable small molecule dyes include small molecule
dyes selected from the group consisting of dyes falling into the Colour Index (C.I.)
classifications of Direct Blue, Direct Red, Direct Violet, Acid Blue, Acid Red, Acid
Violet, Basic Blue, Basic Violet and Basic Red, or mixtures thereof, for example as
described in
WO2005/03274,
WO2005/03275,
WO2005/03276 and co-pending
European application no 06116780.5 filed 7 July 2006.
[0040] Dispersants - The compositions of the present invention can also contain dispersants.
Suitable water-soluble organic materials include 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.
[0041] Enzymes - In addition to the bacterial alkaline endoglucanase, the cleaning compositions
can comprise one or more other enzymes which provide cleaning performance and/or fabric
care benefits. Examples of suitable enzymes include, but are not limited to, hemicellulases,
peroxidases, proteases, other cellulases, xylanases, lipases, phospholipases, esterases,
cutinases, pectinases, mannanases, pectate lyases, keratinases, reductases, oxidases,
phenoloxidases, lipoxygenases, ligninases, pullulanases, tannases, pentosanases, malanases,
β-glucanases, arabinosidases, hyaluronidase, chondroitinase, laccase, and amylases,
or mixtures thereof. In a preferred embodiment, the compositions of the present invention
will further comprise a lipase, for further improved cleaning and whitening performance.
A typical combination is an enzyme cocktail that may comprise, for example, a protease
and lipase in conjunction with amylase. When present in a cleaning composition, the
aforementioned additional enzymes may be present at levels from about 0.00001 % to
about 2%, from about 0.0001 % to about 1% or even from about 0.001% to about 0.5%
enzyme protein by weight of the composition.
[0042] Enzyme Stabilizers - Enzymes for use in detergents can be stabilized by various techniques.
The enzymes employed herein can be stabilized by the presence of water-soluble sources
of calcium and/or magnesium ions in the finished compositions that provide such ions
to the enzymes. In case of aqueous compositions comprising protease, a reversible
protease inhibitor, such as a boron compound, can be added to further improve stability.
[0043] Catalytic Metal Complexes - Applicants' cleaning compositions may include catalytic
metal complexes. One type of metal-containing bleach catalyst is a catalyst system
comprising a transition metal cation of defined bleach catalytic activity, such as
copper, iron, titanium, ruthenium, tungsten, molybdenum, or manganese cations, an
auxiliary metal cation having little or no bleach catalytic activity, such as zinc
or aluminum cations, and a sequestrate having defined stability constants for the
catalytic and auxiliary metal cations, particularly ethylenediaminetetraacetic acid,
ethylenediaminetetra(methylenephosphonic acid) and water-soluble salts thereof. Such
catalysts are disclosed in
U.S. 4,430,243.
[0044] If desired, the compositions herein can be catalyzed by means of a manganese compound.
Such compounds and levels of use are well known in the art and include, for example,
the manganese-based catalysts disclosed in
U.S. 5,576,282.
[0045] Cobalt bleach catalysts useful herein are known, and are described, for example,
in
U.S. 5,597,936;
U.S. 5,595,967. Such cobalt catalysts are readily prepared by known procedures, such as taught for
example in
U.S. 5,597,936, and
U.S. 5,595,967.
[0046] Compositions herein may also suitably include a transition metal complex of ligands
such as bispidones (
WO 05/042532 A1) and/or macropolycyclic rigid ligands - abbreviated as "MRLs". 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 one part per hundred million of the active MRL
species in the aqueous washing medium, and will typically provide from about 0.005
ppm to about 25 ppm, from about 0.05 ppm to about 10 ppm, or even from about 0.1 ppm
to about 5 ppm, of the MRL in the wash liquor.
[0047] Suitable transition-metals in the instant transition-metal bleach catalyst include,
for example, manganese, iron and chromium. Suitable MRLs include 5,12-diethyl-1,5,8,12-tetraazabicyclo[6.6.2]hexadecane.
[0048] Suitable transition metal MRLs are readily prepared by known procedures, such as
taught for example in
WO 00/32601, and
U.S. 6,225,464.
[0049] Solvents - Suitable solvents include water and other solvents such as lipophilic
fluids. Examples of suitable lipophilic fluids include siloxanes, other silicones,
hydrocarbons, glycol ethers, glycerine derivatives such as glycerine ethers, perfluorinated
amines, perfluorinated and hydrofluoroether solvents, low-volatility nonfluorinated
organic solvents, diol solvents, other environmentally-friendly solvents and mixtures
thereof.
[0050] Softening system - the compositions of the invention may comprise a softening agent
such as clay and optionally also with flocculants and enzymes; optionally for softening
through the wash.
Processes of Making Compositions
[0051] The compositions of the present invention can be formulated into any suitable form
and prepared by any process chosen by the formulator, non-limiting examples of which
are described in Applicants' examples and in
U.S. 4,990,280;
U.S. 20030087791A1;
U.S. 20030087790A1;
U.S. 20050003983A1;
U.S. 20040048764A1;
U.S. 4,762,636;
U.S. 6,291,412;
U.S. 20050227891A1;
EP 1070115A2;
U.S. 5,879,584;
U.S. 5,691,297;
U.S. 5,574,005;
U.S. 5,569,645;
U.S. 5,565,422;
U.S. 5,516,448;
U.S. 5,489,392;
U.S. 5,486,303 all of which are incorporated herein by reference.
Method of Use
[0052] The present invention includes a method for laundering a fabric. The method comprises
the steps of contacting a fabric to be laundered with a said cleaning laundry solution
comprising at least one embodiment of Applicants' cleaning composition, cleaning additive
or mixture thereof. The fabric may comprise most any fabric capable of being laundered
in normal consumer use conditions. The solution preferably has a pH of from about
8 to about 10.5. The compositions may be employed at concentrations of from about
500 ppm to about 15,000 ppm in solution. The water temperatures typically range from
about 5 °C to about 90 °C. The water to fabric ratio is typically from about 1:1 to
about 30:1.
EXAMPLES
[0053] Unless otherwise indicated, materials can be obtained from Aldrich, P.O. Box 2060,
Milwaukee, WI 53201, USA.
(a) Examples 1-6
[0054] Granular laundry detergent compositions designed for handwashing or top-loading washing
machines.
|
1 (wt %) |
2 (wt %) |
3 (wt %) |
4 (wt %) |
5 (wt %) |
6 (wt %) |
Linear alkylbenzenesulfonate |
20 |
22 |
20 |
10 |
20 |
20 |
C12-14 Dimethylhydroxyethyl ammonium chloride |
0.7 |
0.2 |
1 |
0 |
0.0 |
0 |
AE3S |
0.9 |
1 |
0.9 |
3.2 |
0.5 |
0.9 |
AE7 |
0.0 |
0.0 |
0.0 |
0.0 |
0.0 |
3 |
Sodium tripolyphosphate |
5 |
25 |
4 |
3 |
2 |
0.0 |
Zeolite A |
0.0 |
1 |
0.0 |
1 |
4 |
1 |
1.6R Silicate (SiO2:Na2O at ratio 1.6:1) |
4 |
5 |
2 |
3 |
3 |
5 |
Sodium Carbonate |
9 |
20 |
10 |
17 |
5 |
23 |
Polyacrylate MW 4500 |
1 |
0.6 |
1 |
1 |
1.5 |
1 |
Carboxymethyl Cellulose |
1 |
0.3 |
0.3 |
0.1 |
1.1 |
0.9 |
Celluclean® (15.6mg/g) |
0.1 |
0.2 |
0.1 |
0.2 |
0.3 |
0.1 |
Savinase® 32.89mg/g |
0.1 |
0.1 |
0.1 |
0.1 |
0.1 |
0.1 |
Natalase® 8.65mg/g |
0.1 |
0.0 |
0.1 |
0.0 |
0.1 |
0.1 |
Lipex® 18mg/g |
0.03 |
0.07 |
0.3 |
0.1 |
0.0 |
0.4 |
Fluorescent Brightener 1 |
0.06 |
0.0 |
0.06 |
0.18 |
0.06 |
0.06 |
Fluorescent Brightener 2 |
0.1 |
0.06 |
0.1 |
0.0 |
0.1 |
0.1 |
Diethylenetriamine pentaacetic acid or Ethylene diamine tetraacetic acid |
0.6 |
0 |
0.6 |
0.25 |
0.6 |
0.6 |
MgSO4 |
1 |
1 |
1 |
0.5 |
1 |
1 |
Sodium Percarbonate |
0.0 |
0 |
0.1 |
0.0 |
0.0 |
0.0 |
Sodium Perborate Monohydrate |
4.4 |
0.0 |
3.85 |
2.09 |
0.78 |
3.63 |
NOBS |
1.9 |
0.0 |
1.66 |
0.0 |
0.33 |
0.75 |
TAED |
0.58 |
0 |
0.51 |
0.0 |
0.015 |
0.28 |
Perfume spray-on |
0.4 |
0.4 |
0.6 |
1 |
0.3 |
0.2 |
Starch encapsulated perfume |
0.3 |
0.2 |
0.3 |
0.2 |
0.3 |
0.3 |
Sulfate/Moisture |
Balance to 100% |
Balance to 100% |
Balance to 100% |
Balance to 100% |
Balance to 100% |
Balance to 100% |
Examples 7-12
[0055] Granular laundry detergent compositions designed for front-loading automatic washing
machines.
|
7 (wt%) |
8 (wt%) |
9 (wt%) |
10 (wt%) |
11 (wt%) |
12 (wt%) |
Linear alkylbenzenesulfonate |
8 |
7.1 |
7 |
6.5 |
7.5 |
7.5 |
AE3S |
0 |
4.8 |
0 |
5.2 |
4 |
4 |
AE7 |
2.2 |
0 |
3.2 |
0 |
0 |
0 |
C10-12 Dimethyl hydroxyethylammonium chloride |
0.75 |
0.94 |
0.98 |
0.98 |
0 |
0 |
Crystalline layered silicate (δ-Na2Si2O5) |
2.0 |
0 |
2.0 |
0 |
0 |
0 |
Zeolite A |
7 |
0 |
7 |
0 |
2 |
2 |
Citric Acid |
3 |
5 |
3 |
4 |
2.5 |
3 |
Sodium Carbonate |
15 |
20 |
14 |
20 |
23 |
23 |
Silicate 2R (SiO2:Na2O at ratio 2:1) |
0.08 |
0 |
0.11 |
0 |
0 |
0 |
Soil release agent |
0.75 |
0.72 |
0.71 |
0.72 |
0 |
0 |
Acrylic Acid/Maleic Acid Copolymer |
1.1 |
3.7 |
1.0 |
3.7 |
2.6 |
3.8 |
Carboxymethylcellulose |
0.15 |
1.4 |
0.2 |
1.4 |
1 |
0.5 |
Protease (84mg active/g) |
0.2 |
0.2 |
0.3 |
0.15 |
0.12 |
0.13 |
Celluclean® (15.6mg active/g) |
0.2 |
0.15 |
0.2 |
0.3 |
0.15 |
0.15 |
Lipex®(18.00mg active/g) |
0.05 |
0.15 |
0.1 |
0 |
0 |
0 |
Termamyl® (25mg active/g) |
0.1 |
0.1 |
0.1 |
0.12 |
0.1 |
0.1 |
Natalase® (8.65mg active/g) |
0.1 |
0.2 |
0 |
0 |
0.15 |
0.15 |
Termamyl® (25 mg active/g) |
0.2 |
0.1 |
0.2 |
0 |
0.1 |
0.1 |
TAED |
3.6 |
4.0 |
3.6 |
4.0 |
2.2 |
1.4 |
Percarbonate |
13 |
13.2 |
13 |
13.2 |
16 |
14 |
Na salt of Ethylenediamine-N,N'-disuccinic acid, (S,S) isomer (EDDS) |
0.2 |
0.2 |
0.2 |
0.2 |
0.2 |
0.2 |
Hydroxyethane di phosphonate (HEDP) |
0.2 |
0.2 |
0.2 |
0.2 |
0.2 |
0.2 |
MgSO4 |
0.42 |
0.42 |
0.42 |
0.42 |
0.4 |
0.4 |
Perfume |
0.5 |
0.6 |
0.5 |
0.6 |
0.6 |
0.6 |
Starch Encapsulated Perfume |
0.2 |
0.5 |
0.3 |
0.4 |
0.3 |
0.2 |
Suds suppressor agglomerate |
0.05 |
0.1 |
0.05 |
0.1 |
0.06 |
0.05 |
Soap |
0.45 |
0.45 |
0.45 |
0.45 |
0 |
0 |
Sulfate/ Water & Miscellaneous |
Balance to 100% |
Balance to 100% |
Balance to 100% |
Balance to 100% |
Balance to 100% |
Balance to 100% |
Any of the above compositions is used to launder fabrics at a concentration of 7000
to 10000 ppm in water, 20-90 °C, and a 5:1 water:cloth ratio. The typical pH is about
10.
[0056] The ratio of CMC to active enzyme protein in the above formulations is shown in the
table below:
Example |
1 |
2 |
3 |
4 |
5 |
6 |
7 |
8 |
9 |
10 |
11 |
12 |
CMC% |
1 |
0.3 |
0.3 |
0.1 |
1.1 |
0.9 |
0.15 |
1.4 |
0.2 |
1.4 |
1 |
0.5 |
Celluclean 5T % (15.6mg/g) |
0.1 |
0.2 |
0.1 |
0.2 |
0.3 |
0.1 |
0.2 |
0.15 |
0.2 |
0.3 |
0.15 |
0.15 |
Active cellulase % |
0.00156 |
0.00312 |
0.00156 |
0.00312 |
0.00468 |
0.00156 |
0.00312 |
0.00234 |
0.00312 |
0.00468 |
0.00234 |
0.00234 |
Ratio CMC:cellulase |
641 |
96 |
192 |
32 |
235 |
577 |
48 |
598 |
64 |
299 |
427 |
214 |
Raw Materials and Notes For Composition Examples 1-12
[0057] Linear alkylbenzenesulfonate having an average aliphatic carbon chain length C
11-C
12 supplied by Stepan, Northfield, Illinois, USA
C12-14 Dimethylhydroxyethyl ammonium chloride, supplied by Clariant GmbH, Sulzbach, Germany
AE3S is C12-15 alkyl ethoxy (3) sulfate supplied by Stepan, Northfield, Illinois, USA
AE7 is C12-15 alcohol ethoxylate, with an average degree of ethoxylation of 7, supplied by Huntsman,
Salt Lake City, Utah, USA
Sodium tripolyphosphate is supplied by Rhodia, Paris, France
Zeolite A was supplied by Industrial Zeolite (UK) Ltd, Grays, Essex, UK
1.6R Silicate was supplied by Koma, Nestemica, Czech Republic
Sodium Carbonate was supplied by Solvay, Houston, Texas, USA
Polyacrylate MW 4500 is supplied by BASF, Ludwigshafen, Germany
Carboxy Methyl Cellulose is Finnfix® BDA supplied by the Noviant division of CPKelco,
Arnhem, Netherlands
Savinase®, Natalase®, Lipex®, Termamyl®, Mannaway®, Celluclean® supplied by Novozymes,
Bagsvaerd, Denmark
Protease (examples 7-12) described in patent application US 6312936B1 was supplied by Genencor International, Palo Alto, California, USA
Fluorescent Brightener 1 is Tinopal® AMS, Fluorescent Brightener 2 is Tinopal® CBS-X.
Sulphonated zinc phthalocyanine supplied by Ciba Specialty Chemicals, Basel, Switzerland
Diethylenetriamine pentacetic acid was supplied by Dow Chemical, Midland, Michigan,
USA
Sodium percarbonate supplied by Solvay, Houston, Texas, USA
Sodium perborate was supplied by Degussa, Hanau, Germany
NOBS is sodium nonanoyloxybenzenesulfonate, supplied by Eastman, Batesville, Arkansas,
USA
TAED is tetraacetylethylenediamine, supplied under the Peractive® brand name by Clariant
GmbH, Sulzbach, Germany
Soil release agent is Repel-o-tex® PF, supplied by Rhodia, Paris, France
Acrylic Acid/Maleic Acid Copolymer is molecular weight 70,000 and acrylate:maleate
ratio 70:30, supplied by BASF, Ludwigshafen, Germany
Na salt of Ethylenediamine-N,N'-disuccinic acid, (S,S) isomer (EDDS) was supplied
by Octel, Ellesmere Port, UK
Hydroxyethane di phosphonate (HEDP) was supplied by Dow Chemical, Midland, Michigan,
USA
Suds suppressor agglomerate was supplied by Dow Corning, Midland, Michigan, USA
Annex to the application documents - subsequently filed sequences listing
1. A composition comprising a modified cellulose derivative or mixtures thereof and a
cellulase enzyme characterised in that the weight ratio of the modified cellulose derivative to the active cellulase enzyme
protein is from 1:1 to 10000:1 and wherein the composition does not contain 0.7 to
0.9 % by weight of the total composition, of sodium nonanoyl oxybenzene sulfonate,
and does not contain 10 % by weight based of the total composition, of sodium perborate
monohydrate, in which the enzyme is a bacterial alkaline enzyme exhibiting endo-beta-1,4-glucanase
activity (E.C. 3.2.1.4).
2. A composition comprising a modified cellulose derivative or mixtures thereof and a
cellulase enzyme characterised in that the weight ratio of the modified cellulose derivative to the active cellulase enzyme
protein is from 1:1 to 10000:1 and wherein the composition does not contain 0.7 to
0.9 % by weight of the total composition, of sodium nonanoyl oxybenzene sulfonate,
and does not contain 10 % by weight based on the total composition, of sodium perborate
monohydrate, the enzyme producing reducing ends levels of greater than 5mM in the
Enzyme Test defined herein.
3. A composition according to claim 1 or claim 2 wherein the enzyme is a bacterial polypeptide
endogenous to a member of the genus Bacillus.
4. A composition according to any of claims 1 to 3 wherein the enzyme is a polypeptide
containing (i) at least one family 17 carbohydrate binding module and/or (ii) at least
one family 28 carbohydrate binding module.
5. A composition according to any of claims 1 to 4 wherein the enzyme comprises a polypeptide
endogenous to one of the following Bacillus species selected from the group consisting of: AA349 (DSM 12648), KSM S237, 1139,
KSM 64, KSM N131, KSM 635 (FERM BP 1485), KSM 534 (FERM BP 1508), KSM 53 (FERM BP
1509), KSM 577 (FERM BP 1510), KSM 521 (FERM BP 1507), KSM 580 (FERM BP 1511), KSM
588 (FERM BP 1513), KSM 597 (FERM BP 1514), KSM 522 (FERM BP 1512), KSM 3445 (FERM
BP 1506), KSM 425 (FERM BP 1505), and mixtures thereof.
6. A composition according to any of claims 1 to 5 wherein the enzyme is selected from
the group consisting of:
(i) the endoglucanase having the amino acid sequence of positions 1 to position 773
of SEQ ID NO:1;
(ii) an endoglucanase having a sequence of at least 90%, preferably 94%, more preferably
97% and even more preferably 99%, 100% identity to the amino acid sequence of position
1 to position 773 of SEQ ID NO:1; or a fragment thereof has endo-beta-1,4-glucanase
activity, when identity is determined by GAP provided in the GCG program using a GAP
creation penalty of 3.0 and GAP extension penalty of 0.1; (iii) mixtures thereof.
7. A composition according to any of claims 1 to 6 wherein the enzyme is an alkaline
endoglucanase variant obtained by substituting the amino acid residue of a cellulase
having an amino acid sequence exhibiting at least 90%, preferably 95%, more preferably
98%, 100% identity with the amino acid sequence represented by SEQ. ID NO:2 at (a)
position 10, (b) position 16, (c) position 22, (d) position 33, (e) position 39, (f)
position 76, (g) position 109, (h) position 242, (i) position 263, (j) position 308,
(k) position 462, (1) position 466, (m) position 468, (n) position 552, (o) position
564, and/or (p) position 608 in SEQ ID NO:2 and/or at a position corresponding thereto
with another amino acid residue.
8. A composition according to claim 6 wherein the enzyme is
characterised by at least one of the following substitutions:
(a) at position 10: glutamine, alanine, proline or methionine, preferably glutamine;
(b) at position 16: asparagine or arginine, preferably asparagine;
(c) at position 22: proline;
(d) at position 33: histidine;
(e) at position 39: alanine, threonine or tyrosine, preferably alanine;
(f) at position 76: histidine, methionine, valine, threonine or alanine, preferably
histidine;
(g) at position 109: isoleucine, leucine, serine or valine, preferably isoleucine;
(h) at position 242: alanine, phenylalanine, valine, serine, aspartic acid, glutamic
acid, leucine, isoleucine, tyrosine, threonine, methionine or glycine, preferably
alanine, phenylalanine or serine;
(i) at position 263: isoleucine, leucine, proline or valine, preferably isoleucine;
(j) at position 308: alanine, serine, glycine or valine, preferably alanine;
(k) at position 462: threonine, leucine, phenylalanine or arginine, preferably threonine;
(l) at position 466: leucine, alanine or serine, preferably leucine;
(m) at position 468: alanine, aspartic acid, glycine or lysine, preferably alanine;
(n) at position 552: methionine;
(o) at position 564: valine, threonine or leucine, preferably valine; an/or
(p) at position 608: isoleucine or arginine, preferably isoleucine.
9. A composition according to claim 7 or claim 8 wherein the enzyme is selected from
the group consisting of the following endoglucanase variants: Egl-237, Egl-1139, Egl-64,
Egl-N131b and mixtures thereof.
10. A composition according to any of claims 1 to 4 wherein the enzyme is an alkaline
cellulase K having the following physical and chemical properties:
(1) Activity: Having a Cx enzymatic activity of acting on carboxymethyl cellulose
along with a weak C1 enzymatic activity and a weak beta-glucoxidase activity;
(2) Specificity on Substrates: Acting on carboxymethyl cellulose(CMC), crystalline
cellulose, Avicell, cellobiose, and p-nitrophenyl cellobioside(PNPC);
(3) Having a working pH in the range of 4 to 12 and an optimum pH in the range of
9 to 10;
(4) Having stable pH values of 4.5 to 10.5 and 6.8 to 10 when allowed to stand at
40°C for 10 minutes and 30 minutes, respectively;
(5) Working in a wide temperature range of from 10 to 65°C with an optimum temperature
being recognized at about 40°C;
(6) Influences of chelating agents: The activity not impeded with ethylenediamine
tetraacetic acid (EDTA), ethyleneglycol-bis-(β-aminoethylether) N,N,N',N"-tetraacetic
acid (EGTA), N,N-bis(carboxymethyl)glycine (nitrilotriacetic acid) (NTA), sodium tripolyphosphate
(STPP) and zeolite;
(7) Influences of surface active agents: Undergoing little inhibition of activity
by means of surface active agents such as sodium linear alkylbenzenesulfonates (LAS),
sodium alkylsulfates (AS), sodium polyoxyethylene alkylsulfates (ES), sodium alphaolefinsulfonates
(AOS), sodium alpha-sulfonated aliphatic acid esters (alpha-SFE), sodium alkylsulfonates
(SAS), polyoxyethylene secondary alkyl ethers, fatty acid salts (sodium salts), and
dimethyldialkylammonium chloride;
(8) Having a strong resistance to proteinases; and
(9) Molecular weight (determined by gel chromatography): Having a maximum peak at
180,000 ±10,000.
11. A composition according to any preceding claim wherein the bacterial alkaline enzyme
exhibiting endo-beta-1,4-glucanase activity is comprised at a level of from 0.00005%
to 0.15%, preferably from 0.0002% to 0.02%, or more preferably from 0.0005% to 0.01%
by weight of pure enzyme.
12. A composition according to any preceding claim wherein the weight ratio of modified
cellulose derivative to active cellulase enzyme protein is from 20:1 to 1000:1, preferably
from 30:1 to 800:1.
13. A composition according to any preceding claim in which the modified cellulose derivative
has a molecular weight from 20 000 to 500 000, preferably from 100 000 to 300 000
kDaltons.
14. A composition according to any preceding claim in which the modified cellulose derivative
is comprised in the composition at a level of from 0.02 to 5 %, preferably from 0.05
to 2 % by weight or more preferably from 0.1 to 1.5 % by weight.
15. A composition according to any preceding claim wherein the modified cellulose derivative
is selected from the group consisting of anionically and nonionically modified celluloses,
preferably being anionically modified.
16. A composition according to any preceding claim wherein the modified cellulose derivative
has an average degree of substitution of 0.3 to 0.9, preferably 0.4 to 0.8.
17. A detergent composition comprising oligosaccharides having an average molecular weight
of less than 20 000 kDa, such oligosaccharide being obtainable by reaction of an enzyme
as defined in any of claims 1 to 10, with an anionically modified cellulose having
a weight average molecular mass from 30 000 to 500 000 kDa.
18. An aqueous wash liquor comprising a detergent composition according to claim 17 wherein
the oligosaccharide is comprised in amounts from 0.5ppm to 1000 ppm, preferably from
0.1 to 500ppm.
19. A process of cleaning and/or treating a surface or fabric comprising the steps of
optionally washing and/or rinsing said surface or fabric, contacting said surface
or fabric with the composition of any of the preceding claims, then optionally washing
and/or rinsing said surface or fabric.
20. Use of oligosaccharide having an average molecular weight of less than 20 000 kDa,
such oligosaccharide being obtainable by reaction of an enzyme as defined in any of
claims 1 to 10 with an anionically modified cellulose having an average molecular
weight from 30 000 to 500 000 kDa, for preparation of a detergent composition, for
soil suspension.