U.S. patent application number 17/039395 was filed with the patent office on 2021-01-28 for particulate composition.
This patent application is currently assigned to Novozymes A/S. The applicant listed for this patent is Novozymes A/S. Invention is credited to Luise Erlandsen, Carsten Hoerslev Hansen, Ole Simonsen.
Application Number | 20210024857 17/039395 |
Document ID | / |
Family ID | 1000005137328 |
Filed Date | 2021-01-28 |
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United States Patent
Application |
20210024857 |
Kind Code |
A1 |
Simonsen; Ole ; et
al. |
January 28, 2021 |
Particulate Composition
Abstract
Enzymes tend to be inactivated during wash by a bleach catalyst
in combination with a source of organic peroxyacids. The risk of
enzyme inactivation by active bleach catalyst is reduced when the
release of the enzyme into the wash solution is delayed. The enzyme
stability during washing together with a bleach catalyst can be
improved by applying a delayed-release coating to cores which
comprise the enzyme.
Inventors: |
Simonsen; Ole; (Soeborg,
DK) ; Hansen; Carsten Hoerslev; (Vaerloese, DK)
; Erlandsen; Luise; (Frederikssund, DK) |
|
Applicant: |
Name |
City |
State |
Country |
Type |
Novozymes A/S |
Bagsvaerd |
|
DK |
|
|
Assignee: |
Novozymes A/S
Bagsvaerd
DK
|
Family ID: |
1000005137328 |
Appl. No.: |
17/039395 |
Filed: |
September 30, 2020 |
Related U.S. Patent Documents
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Application
Number |
Filing Date |
Patent Number |
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14127712 |
Mar 17, 2014 |
10829721 |
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PCT/EP2012/061307 |
Jun 14, 2012 |
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17039395 |
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61498763 |
Jun 20, 2011 |
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Current U.S.
Class: |
1/1 |
Current CPC
Class: |
C11D 3/38672 20130101;
C12N 9/98 20130101; C11D 3/3932 20130101; C11D 17/0039 20130101;
C11D 3/38627 20130101 |
International
Class: |
C11D 3/386 20060101
C11D003/386; C12N 9/98 20060101 C12N009/98; C11D 3/39 20060101
C11D003/39; C11D 17/00 20060101 C11D017/00 |
Foreign Application Data
Date |
Code |
Application Number |
Jun 20, 2011 |
EP |
11170520.8 |
Claims
1: A particulate composition comprising: a) particles comprising a
source of organic peroxyacids, and b) particles comprising a
non-metal bleach catalyst, and c) particles comprising i) a core
comprising an enzyme surrounded by ii) a delayed-release
coating.
2: The particulate composition of claim 1 wherein the enzyme is an
amylase, a carbohydrase, a protease, a lipolytic enzyme, a
cellulase, an oxidoreductase, a mannanase or a pectate lyase.
3: A particulate composition comprising: a) particles comprising a
source of organic peroxyacids, and b) particles comprising a bleach
catalyst, and c) particles comprising i) a core comprising an
enzyme which is a first-wash lipolytic enzyme, surrounded by ii) a
delayed-release coating.
4: The particulate composition of claim 3 wherein the bleach
catalyst is an organic bleach catalyst, a non-metal bleach catalyst
or a catalytic metal complex.
5: The particulate composition of claim 1 wherein the enzyme is
sensitive to the bleach catalyst.
6: The particulate composition of claim 1 wherein the enzyme is a
lipolytic enzyme which has lipase activity (triacylglycerol lipase,
EC 3.1.1.3), cutinase activity (EC 3.1.1.74), sterol esterase (EC
3.1.1.13), and/or wax-ester hydrolase activity (EC 3.1.1.50).
7: The particulate composition of claim 1 wherein the enzyme is a
lipase having at least 90% identity with the wild-type lipase
derived from Thermomyces lanuginosus strain DSM 4109.
8: The particulate composition of claim 1 wherein the enzyme
comprises a lipase selected from variants of Thermomyces
lanuginosus lipase variants having the mutations T231R and
N233R.
9: The particulate composition of claim 1 wherein the enzyme
comprises a cutinase, preferably selected from variants of
Pseudomonas mendocina cutinase and Humicola insolens cutinase.
10: The particulate composition of claim 1, wherein the source of
organic peroxyacids is a preformed peracid or a diacyl
peroxide.
11: The particulate composition of claim 1, wherein the source of
organic peroxyacids comprises a source of hydrogen peroxide and a
bleach activator.
12: The particulate composition of claim 1 wherein the bleach
catalyst is organic and is selected among iminium cations and
polyions; iminium zwitterions; modified amines; modified amine
oxides; N-sulphonyl imines; N-phosphonyl imines; N-acyl imines;
thiadiazole dioxides; perfluoroimines; and cyclic sugar
ketones.
13: The particulate composition of claim 1 wherein the bleach
catalyst has a structure corresponding to the general formula
below: ##STR00005## wherein R.sup.13 is a branched alkyl group
containing from three to 24 carbon atoms (including the branching
carbon atoms) or a linear alkyl group containing from one to 24
carbon atoms.
14: The particulate composition of claim 1 wherein the
delayed-release coating comprises a hydrophobic substance and a
water-insoluble substance.
15: The particulate composition of claim 14 wherein the hydrophobic
substance is a fat or wax.
16: The particulate composition of claim 14 wherein the
water-insoluble substance is titanium dioxide, calcium carbonate or
kaolin.
17: The particulate composition of claim 1 wherein the
delayed-release coating comprises a substrate for the enzyme.
18: The particulate composition of claim 1 wherein the
enzyme-containinq particles (c) comprise an additional top coating,
which preferably comprises polyethylene glycol (PEG), polyvinyl
alcohol (PVA) or hydroxypropyl methyl cellulose (HPMC).
19: The particulate composition of claim 1 wherein the
enzyme-containing particles (c) have a time for 50% release of
enzyme in detergent solution at 20.degree. C. of at least 300
seconds.
20: The particulate composition of claim 1 wherein the
enzyme-containing particles (c) have a time required for release of
50% of the enzyme activity which is at least 1.5 times longer than
the time required for similar enzyme granules without the
coating.
21: The particulate composition of claim 1 wherein the
enzyme-containing particles (c) have a time required for release of
90% of the enzyme activity which is at least 1.5 times longer than
the time required for similar enzyme granules without the
coating.
22: A method of preparing lipase particles, comprising: a) testing
the bleach-catalyst sensitivity of at least one enzyme by
determining the wash performance for a combination of the enzyme
with a bleach catalyst and a source of organic peroxyacids, and
comparing with the performance without the bleach catalyst, to
identify a bleach-catalyst sensitive enzyme, b) providing a core
comprising the sensitive enzyme, and surrounding the core with a
delayed-release coating.
Description
FIELD OF THE INVENTION
[0001] The present invention relates to a particulate composition
comprising:
[0002] a) particles comprising a source of organic peroxyacids,
and
[0003] b) particles comprising a bleach catalyst, and
[0004] c) particles comprising an enzyme.
BACKGROUND OF THE INVENTION
[0005] Bleaching systems providing a source of organic peroxyacids
are commonly included in particulate detergents to facilitate the
removal of stains and soils. Examples include a combination of a
hydrogen peroxide source such as perborate or percarbonate with a
bleach activator such as TAED (tetraacetyl ethylene diamine) or
NOBS (nonanoyloxybenzene sulphonate).
[0006] WO 2007/001261 and WO 2007/001262 disclose particulate
detergents which contain particles comprising a source of organic
peroxyacids, and particles comprising a bleach catalyst to improve
the bleaching effect.
[0007] Enzymes are commonly used in particulate detergents to
improve the removal of stains and soils. Examples are lipolytic
enzymes (lipid esterases), particularly first-wash lipolytic
enzymes (lipid esterases), e.g. variants of Lipolase.TM. (wild-type
Thermomyces lanuginosus lipase) described in WO 97/07202 and WO
00/60063.
[0008] WO 9723606, WO 9528466, WO 9528468, and WO 9528469 disclose
particulate compositions comprising delayed release enzyme
granulates. GB 2 267 911 A, WO 02/070641 A1, EP 0 723 006 A2, WO
2010/073000 A1 and DE 10 2007 056166 A1 disclose particulate
compositions comprising an enzyme.
SUMMARY OF THE INVENTION
[0009] The inventors have found that enzymes tend to be inactivated
during wash by a bleach catalyst in combination with a source of
organic peroxyacids. The inventors further found that the risk of
enzyme inactivation is reduced when the release of the enzyme into
the wash solution is delayed and that the enzyme stability during
washing together with a bleach catalyst can be improved by applying
a delayed-release coating to cores which comprise the enzyme.
[0010] Based on this insight, the inventors found that the enzyme
stability during washing together with a bleach catalyst can be
improved by applying a delayed-release coating to cores which
comprise the enzyme.
[0011] Accordingly, the invention provides a particulate
composition comprising:
[0012] a) particles comprising a source of organic peroxyacids,
and
[0013] b) particles comprising a bleach catalyst, and
[0014] c) particles comprising [0015] i) a core comprising an
enzyme surrounded by [0016] ii) a delayed-release coating.
[0017] In one aspect of the invention, the bleach catalyst is
non-metal, and in another aspect the enzyme is a first-wash
lipolytic enzyme (lipid esterase).
[0018] The invention also provides a method of preparing enzyme
particles, comprising: [0019] a) testing the bleach-catalyst
sensitivity of at least one enzyme by determining the wash
performance for a combination of the enzyme with a bleach catalyst
and a source of organic peroxyacids, and comparing with the
performance without the bleach catalyst, to identify a
bleach-catalyst sensitive enzyme, and [0020] b) providing a core
comprising the sensitive enzyme, and surrounding the core with a
delayed-release coating.
DETAILED DESCRIPTION OF THE INVENTION
Particulate Composition
[0021] The particulate composition comprises particles with an
organic peroxyacid source, bleach catalyst particles and enzyme
particles.
[0022] The particulate composition may be a detergent, e.g. a
laundry detergent or a dish wash detergent, or it may be a premix
for mixing with adjunct materials in the preparation of a
detergent.
Source of Organic Peroxyacids
[0023] The particulate composition comprises a source of organic
peroxyacids as a bleaching agent. The source of organic peroxyacids
may be a preformed peracid or a diacyl peroxide, or it may comprise
a source of hydrogen peroxide and a bleach activator.
[0024] In general, 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. The bleaching agent is a
source of organic peroxyacids.
[0025] The organic peroxy acid source (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.
[0026] The particles comprising the organic peroxyacids preferably
have a release profile such that the time required to release 50%
of the organic peroxyacids is below 100 seconds, particularly below
50 seconds or below 20 seconds. The test to determine whether these
values are met is defined as Test Method 2: Dissolution test,
below.
Pre-Formed Peracids:
[0027] Suitable preformed peracids include, but are not limited to,
compounds selected from the group consisting of pre-formed
peroxyacids or salts thereof, typically either a peroxycarboxylic
acid or salt thereof, or a peroxysulphonic acid or salt
thereof.
[0028] The pre-formed peroxyacid or salt thereof is preferably a
peroxycarboxylic acid or salt thereof, typically having a chemical
structure corresponding to the following chemical formula:
##STR00001##
[0029] wherein: R.sup.14 is selected from alkyl, aralkyl,
cycloalkyl, aryl or heterocyclic groups; the R.sup.14 group can be
linear or branched, substituted or unsubstituted; and Y is any
suitable counter-ion that achieves electric charge neutrality,
preferably Y is selected from hydrogen, sodium or potassium.
Preferably, R.sup.14 is a linear or branched, substituted or
unsubstituted C.sub.6-9 alkyl. Preferably, the peroxyacid or salt
thereof is selected from peroxyhexanoic acid, peroxyheptanoic acid,
peroxyoctanoic acid, peroxynonanoic acid, peroxydecanoic acid, any
salt thereof, or any combination thereof. Preferably, the
peroxyacid or salt thereof has a melting point in the range of from
30.degree. C. to 60.degree. C.
[0030] The pre-formed peroxyacid or salt thereof can also be a
peroxysulphonic acid or salt thereof, typically having a chemical
structure corresponding to the following chemical formula:
##STR00002##
[0031] wherein: R.sup.15 is selected from alkyl, aralkyl,
cycloalkyl, aryl or heterocyclic groups; the R.sup.15 group can be
linear or branched, substituted or unsubstituted; and Z is any
suitable counter-ion that achieves electric charge neutrality,
preferably Z is selected from hydrogen, sodium or potassium.
Preferably R.sup.15 is a linear or branched, substituted or
unsubstituted C.sub.6-9 alkyl.
Sources of Hydrogen Peroxide
[0032] Examples are 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
Bleach Activators
[0033] Bleach activators having R--(C.dbd.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.
Diacyl Peroxides
[0034] The diacyl peroxide (DAP) bleaching species is preferably
selected from diacyl peroxides of the general formula:
R.sup.1--C(O)--OO--(O)C--R.sup.2
[0035] in which R.sup.1 represents a C.sub.6-C.sub.18 alkyl,
preferably C.sub.6-C.sub.12 alkyl group containing a linear chain
of at least 5 carbon atoms and optionally containing one or more
substituents (e.g. --N.sup.+ (CH.sub.3).sub.3, --COOH or --CN)
and/or one or more interrupting moieties (e.g. --CONH-- or
--CH.dbd.CH--) interpolated between adjacent carbon atoms of the
alkyl radical, and R.sup.2 represents an aliphatic group compatible
with a peroxide moiety, such that R.sup.1 and R.sup.2 together
contain a total of 8 to 30 carbon atoms. In one preferred aspect
R.sup.1 and R.sup.2 are linear unsubstituted C.sub.6-C.sub.12 alkyl
chains. Most preferably R.sup.1 and R.sup.2 are identical. Diacyl
peroxides, in which both R.sup.1 and R.sup.2 are C.sub.6-C.sub.12
alkyl groups, are particularly preferred. Preferably, at least one
of, most preferably only one of, the R groups (R.sub.1 or R.sub.2),
does not contain branching or pendant rings in the alpha position,
or preferably neither in the alpha nor beta positions or most
preferably in none of the alpha or beta or gamma positions. In one
further preferred embodiment the DAP may be asymmetric, such that
preferably the hydrolysis of R1 acyl group is rapid to generate
peracid, but the hydrolysis of R2 acyl group is slow.
[0036] The tetraacyl peroxide bleaching species is preferably
selected from tetraacyl peroxides of the general formula:
R.sup.3--C(O)--OO--C(O)--(CH.sub.2)n-C(O)--OO--C(O)--R.sup.3
[0037] in which R.sup.3 represents a C.sub.1-C.sub.9 alkyl,
preferably C.sub.3-C.sub.7, group and n represents an integer from
2 to 12, preferably 4 to 10 inclusive.
[0038] Preferably, the diacyl and/or tetraacyl peroxide bleaching
species is present in an amount sufficient to provide at least 0.5
ppm, more preferably at least 10 ppm, and even more preferably at
least 50 ppm by weight of the wash liquor. In a preferred
embodiment, the bleaching species is present in an amount
sufficient to provide from about 0.5 to about 300 ppm, more
preferably from about 30 to about 150 ppm by weight of the wash
liquor.
Bleach Catalyst
[0039] Bleach Catalysts may be provided by: non-metal bleach
catalysts, catalytic metal complexes or ligands which form
catalytic metal complexes. The bleach catalyst is typically used in
an amount which provides 0.001-0.02 g of active material per I of
wash liquor.
Non-Metal Bleach Catalysts
[0040] The bleach catalyst is capable of accepting an oxygen atom
from a peroxyacid and/or salt thereof, and transferring the oxygen
atom to an oxidizeable substrate. Suitable bleach catalysts
include, but are not limited to: iminium cations and polyions;
iminium zwitterions; modified amines; modified amine oxides;
N-sulphonyl imines; N-phosphonyl imines; N-acyl imines; thiadiazole
dioxides; perfluoroimines; cyclic sugar ketones and mixtures
thereof.
[0041] Suitable iminium cations and polyions include, but are not
limited to, N-methyl-3,4-dihydroisoquinolinium tetrafluoroborate,
prepared as described in Tetrahedron (1992), 49(2), 423-38 (see,
for example, compound 4, p. 433);
N-methyl-3,4-dihydroisoquinolinium p-toluene sulphonate, prepared
as described in U.S. Pat. No. 5,360,569 (see, for example, Column
11, Example 1); and N-octyl-3,4-dihydroisoquinolinium p-toluene
sulphonate, prepared as described in U.S. Pat. No. 5,360,568 (see,
for example, Column 10, Example 3).
[0042] Suitable iminium zwitterions include, but are not limited
to, N-(3-sulfopropyl)-3,4-dihydroisoquinolinium, inner salt,
prepared as described in U.S. Pat. No. 5,576,282 (see, for example,
Column 31, Example II);
N-[2-(sulphooxy)dodecyl]-3,4-dihydroisoquinolinium, inner salt,
prepared as described in U.S. Pat. No. 5,817,614 (see, for example,
Column 32, Example V);
2-[3-[(2-ethylhexyl)oxy]-2-(sulphooxy)propyl]-3,4-dihydroisoquinolinium,
inner salt, prepared as described in WO05/047264 (see, for example,
page 18, Example 8), and
2-[3-[(2-butyloctyl)oxy]-2-(sulphooxy)propyl]-3,4-dihydroisoquinolinium,
inner salt.
[0043] Suitable modified amine oxygen transfer catalysts include,
but are not limited to,
1,2,3,4-tetrahydro-2-methyl-1-isoquinolinol, which can be made
according to the procedures described in Tetrahedron Letters
(1987), 28(48), 6061-6064. Suitable modified amine oxide oxygen
transfer catalysts include, but are not limited to, sodium
1-hydroxy-N-oxy-N-[2-(sulphooxy)decyl]-1,2,3,4-tetrahydroisoquinoline.
[0044] Suitable N-sulphonyl imine oxygen transfer catalysts
include, but are not limited to, 3-methyl-1,2-benzisothiazole
1,1-dioxide, prepared according to the procedure described in the
Journal of Organic Chemistry (1990), 55(4), 1254-61.
[0045] Suitable N-phosphonyl imine oxygen transfer catalysts
include, but are not limited to,
[R(E)]-N-[(2-chloro-5-nitrophenyl)methylene]-P-phenyl-P-(2,4,6-trimethylp-
henyl)-phosphinic amide, which can be made according to the
procedures described in the Journal of the Chemical Society,
Chemical Communications (1994), (22), 2569-70.
[0046] Suitable N-acyl imine oxygen transfer catalysts include, but
are not limited to, [N(E)]-N(phenylmethylene)acetamide, which can
be made according to the procedures described in Polish Journal of
Chemistry (2003), 77(5), 577-590.
[0047] Suitable thiadiazole dioxide oxygen transfer catalysts
include but are not limited to, 3-methyl-4-phenyl-1,2,5-thiadiazole
1,1-dioxide, which can be made according to the procedures
described in U.S. Pat. No. 5,753,599 (Column 9, Example 2).
[0048] Suitable perfluoroimine oxygen transfer catalysts include,
but are not limited to,
(Z)-2,2,3,3,4,4,4-heptafluoro-N-(nonafluorobutyl)butanimidoyl
fluoride, which can be made according to the procedures described
in Tetrahedron Letters (1994), 35(34), 6329-30.
[0049] Suitable cyclic sugar ketone oxygen transfer catalysts
include, but are not limited to,
1,2:4,5-di-O-isopropylidene-D-erythro-2,3-hexodiuro-2,6-pyranose as
prepared in U.S. Pat. No. 6,649,085 (Column 12, Example 1).
[0050] Preferably, the bleach catalyst comprises an iminium and/or
carbonyl functional group and is typically capable of forming an
oxaziridinium and/or dioxirane functional group upon acceptance of
an oxygen atom, especially upon acceptance of an oxygen atom from a
peroxyacid and/or salt thereof. Preferably, the bleach catalyst
comprises an oxaziridinium functional group and/or is capable of
forming an oxaziridinium functional group upon acceptance of an
oxygen atom, especially upon acceptance of an oxygen atom from a
peroxyacid and/or salt thereof. Preferably, the bleach catalyst
comprises a cyclic iminium functional group, preferably wherein the
cyclic moiety has a ring size of from five to eight atoms
(including the nitrogen atom), preferably six atoms. Preferably,
the bleach catalyst comprises an aryliminium functional group,
preferably a bi-cyclic aryliminium functional group, preferably a
3,4-dihydroisoquinolinium functional group. Typically, the imine
functional group is a quaternary imine functional group and is
typically capable of forming a quaternary oxaziridinium functional
group upon acceptance of an oxygen atom, especially upon acceptance
of an oxygen atom from a peroxyacid and/or salt thereof.
[0051] Preferably, the bleach catalyst has a chemical structure
corresponding to the following chemical formula
##STR00003##
[0052] wherein: n and m are independently from 0 to 4, preferably n
and m are both 0; each R.sup.1 is independently selected from a
substituted or unsubstituted radical selected from the group
consisting of hydrogen, alkyl, cycloalkyl, aryl, fused aryl,
heterocyclic ring, fused heterocyclic ring, nitro, halo, cyano,
sulphonato, alkoxy, keto, carboxylic, and carboalkoxy radicals; and
any two vicinal R.sup.1 substituents may combine to form a fused
aryl, fused carbocyclic or fused heterocyclic ring; each R.sup.2 is
independently selected from a substituted or unsubstituted radical
independently selected from the group consisting of hydrogen,
hydroxy, alkyl, cycloalkyl, alkaryl, aryl, aralkyl, alkylenes,
heterocyclic ring, alkoxys, arylcarbonyl groups, carboxyalkyl
groups and amide groups; any R.sup.2 may be joined together with
any other of R.sup.2 to form part of a common ring; any geminal
R.sup.2 may combine to form a carbonyl; and any two R.sup.2 may
combine to form a substituted or unsubstituted fused unsaturated
moiety; R.sup.3 is a C, to C.sub.20 substituted or unsubstituted
alkyl; R.sup.4 is hydrogen or the moiety Q.sub.t-A, wherein: Q is a
branched or unbranched alkylene, t=0 or 1 and A is an anionic group
selected from the group consisting of OSO.sub.3.sup.-,
SO.sub.3.sup.-, CO.sub.2.sup.-, OPO.sub.2.sup.-, OPO.sub.3.sup.2-,
OPO.sub.3H.sup.- and OPO.sub.2.sup.-; R.sup.5 is hydrogen or the
moiety
--CR.sup.11R.sup.12--Y-G.sub.b-Y.sub.C--[(CR.sup.9R.sup.10).sub.y--O].sub-
.k--R.sup.8, wherein: each Y is independently selected from the
group consisting of O, S, N--H, or N--R.sup.8; and each R.sup.8 is
independently selected from the group consisting of alkyl, aryl and
heteroaryl, said moieties being substituted or unsubstituted, and
whether substituted or unsubsituted said moieties having less than
21 carbons; each G is independently selected from the group
consisting of CO, SO.sub.2, SO, PO and PO.sub.2; R.sup.9 and
R.sup.10 are independently selected from the group consisting of H
and C.sub.1-C.sub.4 alkyl; R.sup.11 and R.sup.12 are independently
selected from the group consisting of H and alkyl, or when taken
together may join to form a carbonyl; b=0 or 1; c can=0 or 1, but c
must=0 if b=0; y is an integer from 1 to 6; k is an integer from 0
to 20; R.sup.6 is H, or an alkyl, aryl or heteroaryl moiety; said
moieties being substituted or unsubstituted; and X, if present, is
a suitable charge balancing counterion, preferably X is present
when R.sup.4 is hydrogen, suitable X, include but are not limited
to: chloride, bromide, sulphate, methosulphate, sulphonate,
p-toluenesulphonate, borontetraflouride and phosphate.
[0053] A preferred bleach catalyst has a structure corresponding to
general formula below:
##STR00004##
[0054] wherein R.sup.13 is a branched alkyl group containing from
three to 24 carbon atoms (including the branching carbon atoms) or
a linear alkyl group containing from one to 24 carbon atoms;
preferably R.sup.13 is a branched alkyl group containing from eight
to 18 carbon atoms or linear alkyl group containing from eight to
eighteen carbon atoms; preferably R.sup.13 is selected from the
group consisting of 2-propylheptyl, 2-butyloctyl, 2-pentylnonyl,
2-hexyldecyl, n-dodecyl, n-tetradecyl, nhexadecyl, n-octadecyl,
iso-nonyl, iso-decyl, iso-tridecyl and iso-pentadecyl; preferably
R.sup.13 is selected from the group consisting of 2-butyloctyl,
2-pentylnonyl, 2-hexyldecyl, iso-tridecyl and isopentadecyl.
[0055] The bleach catalyst may be one described in WO 2007/001261
or WO 2007/001262, e.g. having formula (1) of WO 2007/001262 with
R.sup.1=2-butyl-octyl.
Catalytic Metal Complexes
[0056] Suitable 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. Pat. No.
4,430,243.
[0057] 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. Pat. No. 5,576,282.
[0058] Cobalt bleach catalysts useful herein are known, and are
described, for example, in U.S. Pat. Nos. 5,597,936; 5,595,967.
Such cobalt catalysts are readily prepared by known procedures,
such as taught for example in U.S. Pat. Nos. 5,597,936, and
5,595,967.
[0059] Compositions herein may also suitably include a transition
metal complex of ligands such as bispidones (U.S. Pat. No.
7,501,389) 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.
[0060] 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.
[0061] Suitable transition metal MRLs are readily prepared by known
procedures, such as taught for example in U.S. Pat. No.
6,225,464.
Ligands which Form Catalytic Metal Complexes
[0062] Particularly ligands such as those described above, which
form a complex with a transition metal. Formation of such catalytic
metal complexes from suitable ligands is described, for example in
EP1109965, EP1259522, EP 1240378 and EP 1240379.
Enzyme
[0063] The enzyme may in particular be an enzyme which is sensitive
to the bleach catalyst. The enzyme may be an amylase, a
carbohydrase, a protease, a lipolytic enzyme, a cellulase, an
oxidoreductase, a mannanase or a pectate lyase.
[0064] Preferably the enzyme is present in the composition in
amounts from 0.00001% to 2%, more preferably from to 0.0001% to
0.02%, most preferably from 0.001% to 0.01%.
Lipolytic Enzyme
[0065] The lipolytic enzyme (or lipid esterase) is an enzyme in
class EC 3.1.1 as defined by Enzyme Nomenclature. It may have
lipase activity (triacylglycerol lipase, EC 3.1.1.3), cutinase
activity (EC 3.1.1.74), sterol esterase (EC 3.1.1.13), and/or
wax-ester hydrolase activity (EC 3.1.1.50).
[0066] The lipolytic enzyme may in particular be a lipase with
first-wash activity as described in WO9707202 and WO 00/60063. A
suitable protocol for determining whether a triacylglycerol lipase
exhibits first wash activity is given in Test Method 1. Suitable
triacylglycerol lipases exhibiting first wash activity can be
selected from variants of the Thermomyces lanuginosus (Humicola
lanuginosa) lipase, such as Lipex.TM., Lipolex.TM. and
Lipoclean,.TM. all products of Novozymes, Bagsvaerd, Denmark.
Preferred first wash lipases are described in WO0060063 and
W2006/090335, most preferably the first wash lipase is selected
from Thermomyces lanuginosus lipase variants with mutations T231R
and N233R.
[0067] The lipase may be selected among Thermomyces lanuginosus
lipase (TLL, shown as SEQ ID NO: 2 in WO 2009/109500), Alcaligenes
sp. lipase, Achromobacter sp. lipase, Burkholderia cepacia lipase,
Pseudomonas lipases, e.g., from P. alcaligenes or P.
pseudoalcaligenes (EP 218 272), P. cepacia (EP 331 376), P.
stutzeri (GB 1,372,034), P. fluorescens, Pseudomonas sp. strain SD
705 (WO 95/06720 and WO 96/27002), P. wisconsinensis (WO 96/12012),
Bacillus lipases, e.g., from B. subtilis (Dartois et al. (1993),
Biochemica et Biophysica Acta, 1131, 253-360), B.
stearothermophilus (JP 64/744992) or B. pumilus (WO 91/16422), or
it may be a variant which has an amino sequence with at least 80%
identity to one of these, particularly at least 85%, at least 90%,
at least 95% or at least 98% identity.
[0068] Examples of TLL variants are described in WO 1992/005249,
Lipolase Ultra), WO0060063, WO9707202, WO0032758, WO02055679,
WO04099400, WO07087508 and WO 2009/109500. Commercial lipases
include the following products of Novozymes A/S: Novozym.TM. 435,
Novozym 735, Lipozyme.TM. RM, Novozym 388, Lipolase Ultra.TM.,
Lipex.TM., Lipoprime.TM., Lipolase.TM., Lipoclean.TM. and
Lipolex.TM..
[0069] Suitable cutinases may be derived from a strain of
Aspergillus, in particular Aspergillus oryzae, a strain of
Alternaria, in particular Alternaria brassiciola, a strain of
Fusarium, in particular Fusarium solani, Fusarium solani pisi,
Fusarium oxysporum, Fusarium oxysporum cepa, Fusarium roseum
culmorum, or Fusarium roseum sambucium, a strain of
Helminthosporum, in particular Helminthosporum sativum, a strain of
Humicola, in particular Humicola insolens, a strain of Pseudomonas,
in particular Pseudomonas mendocina, or Pseudomonas putida, a
strain of Rhizoctonia, in particular Rhizoctonia solani, a strain
of Streptomyces, in particular Streptomyces scabies, a strain of
Coprinopsis, in particular Coprinopsis cinerea, a strain of
Thermobifida, in particular Thermobifida fusca, a strain of
Magnaporthe, in particular Magnaporthe grisea, or a strain of
Ulocladium, in particular Ulocladium consortiale.
[0070] In a preferred embodiment, the cutinase is selected from
variants of the Pseudomonas mendocina cutinase described in WO
2003/076580 (Genencor), such as the variant with three
substitutions at 1178M, F180V, and S205G.
[0071] In another preferred embodiment, the cutinase is a wild-type
or variant of the six cutinases endogenous to Coprinopsis cinerea
described in H. Kontkanen et al, App. Environ. Microbiology, 2009,
p 2148-2157
[0072] In another preferred embodiment, the cutinase is a wild-type
or variant of the two cutinases endogenous to Trichoderma reesei
described in W2009007510 (VTT).
[0073] In a most preferred embodiment the cutinase is derived from
a strain of Humicola insolens, in particular the strain Humicola
insolens DSM 1800. Humicola insolens cutinase is described in WO
96/13580 which is hereby incorporated by reference. The cutinase
may be a variant, such as one of the variants disclosed in WO
00/34450 and WO 01/92502. Preferred cutinase variants include
variants listed in Example 2 of WO 01/92502. Preferred commercial
cutinases include Novozym 51032 (available from Novozymes,
Bagsvaerd, Denmark).
[0074] Suitable sterol esterases may be derived from a strain of
Ophiostoma, for example Ophiostoma piceae, a strain of Pseudomonas,
for example Pseudomonas aeruginosa, or a strain of Melanocarpus,
for example Melanocarpus albomyces.
[0075] In a most preferred embodiment the sterol esterase is the
Melanocarpus albomyces sterol esterase described in H. Kontkanen et
al, Enzyme Microb Technol., 39, (2006), 265-273.
[0076] Suitable wax-ester hydrolases may be derived from Simmondsia
chinensis.
Amylase
[0077] The amylase may be an .quadrature.-amylase obtained from
Bacillus, e.g. B. subtilis and B. licheniformis, in particular the
amylase from a special strain of B. licheniformis, described in
more detail in GB 1,296,839.
[0078] Examples of useful amylases are described in WO 94/02597, WO
94/18314, WO 1995/010603, WO 1995/026397, WO 96/23873, WO 97/43424,
and WO 00/60060, WO 2001/066712, WO 2006/002643, especially the
variants with substitutions in one or more of the following
positions: 15, 23, 105, 106, 124, 128, 133, 154, 156, 181, 188,
190, 197, 202, 208, 209, 243, 264, 304, 305, 391, 408, and 444.
[0079] In a particular embodiment the alpha-amylase is derived from
Bacillus sp. strains NCIB 12289, NCIB 12512, NCIB 12513 and DSM
9375. Especially preferred are the alpha-amylases shown in SEQ ID
NOS 1 and 2 of WO 95/26397.
[0080] Commercially available amylases are NATALASE.TM.,
STAINZYME.TM., STAINZYME PLUS.TM., TERMAMYL.TM. ULTRA, DURAMYL.TM.,
TERMAMYL.TM., FUNGAMYL.TM. and BAN.TM. (Novozymes A/S),
RAPIDASE.TM..quadrature..quadrature.PURASTAR.TM. and PURASTAR
OXAM.TM. (from Genencor International Inc.).
Protease
[0081] Suitable proteases include those of animal, vegetable or
microbial origin. Microbial origin is preferred. Chemically
modified or protein engineered mutants are included. The protease
may be a serine protease or a metalloprotease, preferably an
alkaline microbial protease or a trypsin-like protease. Examples of
alkaline proteases are subtilisins, especially those derived from
Bacillus, e.g., subtilisin Novo, subtilisin Carlsberg, subtilisin
309, subtilisin 147 and subtilisin 168 (described in WO 89/06279).
Examples of trypsin-like proteases are trypsin (e.g., of porcine or
bovine origin) and the Fusarium protease described in WO 89/06270
and WO 94/25583.
[0082] Examples of useful proteases are the variants described in
WO 92/19729, WO 98/20115, WO 98/20116, and WO 98/34946, especially
the variants with substitutions in one or more of the following
positions: 27, 36, 57, 76, 87, 97, 101, 104, 120, 123, 167, 170,
194, 206, 218, 222, 224, 235, and 274.
[0083] Preferred commercially available protease enzymes include
Alcalase.TM., Savinase.TM., Primase.TM., Duralase.TM.,
Esperase.TM., and Kannase.TM. (Novozymes A/S), Maxatase.TM.,
Maxacal.TM., Maxapem.TM., Properase.TM., Purafect.TM., Purafect
OxP.TM., FN2.TM., and FN3.TM. (Genencor International Inc.).
Cellulase
[0084] Suitable cellulases include complete cellulases or
mono-component endoglucanases of bacterial or fungal origin.
Chemically or genetically modified mutants are included. The
cellulase may for example be a mono-component or a mixture of
mono-component endo-1,4-beta-glucanase often just termed
endoglucanases (EC 3.2.1.4). Some xyloglucanases may also have
endoglucanase activity and are also considered as suitable
cellulases in the present invention. Suitable cellulases are
disclosed in U.S. Pat. No. 4,435,307, which discloses fungal
cellulases produced from Humicola insolens. Especially suitable
cellulases are the cellulases having textile care benefits.
Examples of such cellulases are cellulases described in European
patent application No. 0 495 257.
[0085] Suitable mono-component endoglucanases may be obtained from
one or more of the following species Exidia glandulosa, Crinipellis
scabella, Fomes fomentarius, Spongipellis sp., Rhizophlyctis rosea,
Rhizomucor pusillus, Phycomyces nitens, and Chaetostylum fresenii,
Diplodia gossypina, Microsphaeropsis sp., Ulospora bilgramii,
Aureobasidium sp., Macrophomina phaseolina, Ascobolus stictoides,
Saccobolus dilutellus, Peziza, Penicillium verruculosum,
Penicillium chrysogenum, and Thermomyces verrucosus, Trichoderma
reesei aka Hypocrea jecorina, -Diaporthe syngenesia, Colletotrichum
lagenarium, Xylaria hypoxylon, Nigrospora sp., Nodulisporum sp.,
and Poronia punctata, Cylindrocarpon sp., Nectria pinea, Volutella
colletotrichoides, Sordaria fimicola, Sordaria macrospora,
Thielavia thermophila, Syspastospora boninensis, Cladorrhinum
foecundissimum, Chaetomium murorum, Chaetomium virescens,
Chaetomium brasiliensis, Chaetomium cunicolorum, Myceliophthora
thermophila, Gliocladium catenulatum, Scytalidium thermophila,
Acremonium sp Fusarium solani, Fusarium anguioides, Fusarium poae,
Fusarium oxysporum ssp. lycopersici, Fusarium oxysporum ssp.
passiflora, Humicola nigrescens, Humicola grisea, Fusarium
oxysporum, Thielavia terrestris or Humicola insolens. One preferred
endoglucanase is disclosed in WO 96/29397 as SEQ ID NO: 9 (hereby
incorporated by reference) or an enzyme with at least 70% identity
thereto and variants thereof as disclosed in Example 1 of WO
98/12307. Another preferred endoglucanase is disclosed in WO
91/017243 (SEQ ID NO:2) or endoglucanases variants as disclosed in
WO 94/007998.
[0086] Endoglucanases with an anti-redeposition effect may be
obtained from fungal endoglucanases lacking a carbohydrate-binding
module (CBM) from a number of bacterial sources. Some sources are
Humicola insolens, Bacillus sp. deposited as DSM 12648, Bacillus
sp. KSMS237 deposited as FERM P-16067, Panibacillus polymyxa, and
Panibacillus pabuli. Specific antiredeposition endoglucanase are
disclosed in WO 91/17244 (FIG. 14) (hereby incorporated by
reference), WO 2002/099091 position 1-773 of SEQ ID NO: 2 (hereby
incorporated by reference), WO 04/053039 SEQ ID NO: 2 (hereby
incorporated by reference), JP 2000210081 position 1 to 824 of SEQ
ID NO: 1 (hereby incorporated by reference).
[0087] Xyloglucanases with an anti-redeposition effect may be
obtained from a number of bacterial sources. Some sources are
Bacillus licheniformis, Bacillus agaradhaerens, (WO 99/02663)
Panibacillus polymyxa, and Panibacillus pabuli (WOO1/62903).
Suitable variants of xyloglucasnes are also described in
PCT/EP2009/056875. A commercially available xyloglucanase is
Whitezyme.RTM. (Novozymes A/S).
[0088] Commercially available cellulases include Celluclast.RTM.
produced from Trichoderma reesei, Celluzyme.RTM. produced from
Humicola insolens. Commercially available endoglucanases are
Carezyme, Renozyme.RTM., Endolase.RTM. and Celluclean (Novozymes
A/S), and KAC-500(B).TM. (Kao Corporation) and Clazinase.TM.,
Puradax.TM. EG L and Puradax HA (Danisco A/S).
Pectate Ivase
[0089] The pectate lyase may be a wild-type enzymes derived from
Bacillus, particularly B. licherniformis or B. agaradhaerens, or a
variant derived of these, e.g. as described in U.S. Pat. No.
6,124,127, WO 1999/027083, WO 1999/027084, WO 2002/006442, WO
2002/092741, or WO 2003/095638.
Mannanase
[0090] The mannanase may be an alkaline mannanase of Family 5 or
26. It may be a wild-type from Bacillus or Humicola, particularly
B. agaradhaerens, B. licheniformis, B. halodurans, B. clausii, or
H. insolens. Suitable mannanases are described in WO
1999/064619.
Sensitivity of Enzyme to Bleach Catalyst
[0091] The delayed-release coating is particularly applicable to
protection of an enzyme which is sensitive to a bleach catalyst.
The sensitivity is determined by testing the wash performance of
the enzyme on fatty soiling in a detergent containing the bleach
catalyst and a source of organic peracids, and comparing with the
performance in a similar detergent without the bleach catalyst. The
enzyme is considered sensitive if the ratio of wash performance
without and with bleach activator is more than 2, particularly more
than 5.
Enzyme-Containing Core
[0092] The core comprises the enzyme and may also include binders
(such as synthetic polymer, wax, fat, or carbohydrate). The core
may further include additional materials such as fillers, fibre
materials (cellulose or synthetic fibres), stabilizing agents,
solubilising agents, suspension agents, viscosity regulating
agents, light spheres, plasticizers, salts, lubricants and
fragrances.
[0093] The core can be prepared by granulation, e.g. by use of
granulation techniques including: crystallisation, precipitation,
pan-coating, fluid bed coating, fluid bed agglomeration, rotary
atomization, extrusion, prilling, spheronization, size reduction
methods, drum granulation, and/or high shear granulation.
[0094] The core may consist of an inert particle with the enzyme
absorbed into it, or with the enzyme applied on to the surface e.g.
via fluid bed coating.
[0095] The core particle may have a diameter of 20-2000 .mu.m,
particularly 50-1500 .mu.m, 100-1500 .mu.m or 250-1200 .mu.m.
Coating
[0096] The granules have a delayed-release coating which may
comprise a hydrophobic substance, e.g. a high-melting wax or fat,
particularly in an amount of 1-50% or 5-15% by weight. The coating
may further comprise a water-insoluble substance, e.g. kaolin, talc
or calcium carbonate, e.g. in an amount of 60-75% by weight. The
coating may constitute 15-35% by weight of the coated particle. The
coating may be as described in WO 92/12645 or WO 97/16076.
[0097] The delayed-release coating may comprise a substrate for the
enzyme. As an example, the enzyme may be a lipolytic enzyme, and
the coating may comprise lipids, mono-, di- and triglycerides such
as tripalmitin, palm oil, beeswax, jojoba oil, carnauba wax,
carnauba wax, polyesters, polyester block copolymers such as
polyethylene terephthalate/polyoxyethylene terephthalate (PET/POET)
block copolymers and polycaprolactone, preferably comprising palm
oil.
[0098] The release profile for the enzyme in the granules is
preferably such that the time required to release 50% of the enzyme
activity is at least 100 seconds, at least 200 seconds or at least
300 seconds. The time required to release 50% or 90% of the enzyme
activity for the coated granules is preferably at least 1.5 times,
at least 2 times or at least 3 times longer than the time required
for similar enzyme granules without a delayed-release coating. The
test to determine whether these values are met is defined as Test
Method 2: Dissolution test, below.
[0099] In addition to the delayed-release coating, the granules may
optionally comprise one or more additional coatings, either as an
undercoat or a topcoat, e.g. to reduce dust formation. Such a
coating may comprise polyethylene glycol (PEG), polyvinyl alcohol
(PVA) or hydroxypropyl methyl cellulose (HPMC).
Detergent Composition
[0100] The granules are particularly suited for incorporation in a
granular detergent composition comprising a surfactant. Enzyme
granules according to the invention result in improved storage
stability of the enzyme when the granules are incorporated in a
detergent, even a detergent comprising aggressive components such
as a bleaching system.
[0101] The detergent composition may for example be formulated as a
laundry detergent composition for hand or machine washings
including a cleaning additive composition suitable for pretreatment
of stained fabrics or a fabric softener composition, or a detergent
composition for use in general household hard surface cleaning
operations, or a composition for hand or machine dishwashing
operations.
[0102] The detergent composition of the invention may be in any
convenient dry form, e.g., a bar, a tablet, a powder, a granulate
or a paste. It may also be a liquid detergent, either an aqueous or
non-aqueous liquid detergent.
Surfactant
[0103] The detergent composition comprises one or more surfactants,
which may be non-ionic including semi-polar and/or anionic and/or
cationic and/or zwitterionic. The surfactants are typically present
at a level of from 0.1% to 60% by weight.
[0104] When included therein the detergent will usually contain
from about 1% to about 40% of an anionic surfactant such as linear
alkylbenzenesulfonate, alpha-olefinsulfonate, alkyl sulfate (fatty
alcohol sulfate), alcohol ethoxysulfate, secondary alkanesulfonate,
alpha-sulfo fatty acid methyl ester, alkyl- or alkenylsuccinic acid
or soap.
[0105] When included therein the detergent will usually contain
from about 0.2% to about 40% of a non-ionic surfactant such as
alcohol ethoxylate, nonylphenol ethoxylate, alkylpolyglycoside,
alkyldimethylamineoxide, ethoxylated fatty acid monoethanolamide,
fatty acid monoethanolamide, polyhydroxy alkyl fatty acid amide, or
N-acyl N-alkyl derivatives of glucosamine ("glucamides").
[0106] The detergent composition may comprise one or more
surfactants, which may be anionic and/or cationic and/or non-ionic
and/or semi-polar and/or zwitterionic, or a mixture thereof. In a
particular embodiment, the detergent composition includes a mixture
of one or more nonionic surfactants and one or more anionic
surfactants. The surfactant(s) is typically present at a level of
from about 0.1% to 60% by weight, such as about 1% to about 40%, or
about 3% to about 20%, or about 3% to about 10%.
[0107] When included therein the detergent will usually contain
from about 1% to about 40% by weight, such as from about 5% to
about 30%, including from about 5% to about 15%, or from about 20%
to about 25% of an anionic surfactant. Non-limiting examples of
anionic surfactants include sulfates and sulfonates, in particular,
linear alkylbenzenesulfonates (LAS), branched
alkylbenzenesulfonates (BABS), phenylalkanesulfonates,
alpha-olefinsulfonates (AOS), olefin sulfonates, alkene sulfonates,
alkane-2,3-diylbis(sulfates), hydroxyalkanesulfonates and
disulfonates, alkyl sulfates (AS) such as sodium dodecyl sulfate
(SDS), fatty alcohol sulfates (FAS), primary alcohol sulfates
(PAS), alcohol ethersulfates (AES or AEOS or FES, also known as
alcohol ethoxysulfates or fatty alcohol ether sulfates), secondary
alkanesulfonates (SAS), paraffin sulfonates (PS), ester sulfonates,
sulfonated fatty acid glycerol esters, alpha-sulfo fatty acid
methyl esters (alpha-SFMe or SES) including methyl ester sulfonate
(MES), alkyl- or alkenylsuccinic acid, dodecenyl/tetradecenyl
succinic acid (DTSA), fatty acid derivatives of amino acids,
diesters and monoesters of sulfo-succinic acid or soap, and
combinations thereof.
[0108] Non-limiting examples of cationic surfactants include
alklydimethylehanolamine quat (ADMEAQ), cetyltrimethylammonium
bromide (CTAB), dimethyldistearylammonium chloride (DSDMAC), and
alkylbenzyldimethylammonium, and combinations thereof.
[0109] When included therein the detergent will usually contain
from about 0.2% to about 40% by weight of a non-ionic surfactant,
for example from about 0.5% to about 30%, in particular from about
1% to about 20%, from about 3% to about 10%, such as from about 3%
to about 5%, or from about 8% to about 12%. Non-limiting examples
of non-ionic surfactants include alcohol ethoxylates (AE or AEO),
alcohol propoxylates, propoxylated fatty alcohols (PFA),
alkoxylated fatty acid alkyl esters, such as ethoxylated and/or
propoxylated fatty acid alkyl esters, alkylphenol ethoxylates
(APE), nonylphenol ethoxylates (NPE), alkylpolyglycosides (APG),
alkoxylated amines, fatty acid monoethanolamides (FAM), fatty acid
diethanolamides (FADA), ethoxylated fatty acid monoethanolamides
(EFAM), propoxylated fatty acid monoethanolamide (PFAM),
polyhydroxy alkyl fatty acid amides, or Nacyl N-alkyl derivatives
of glucosamine (glucamides, GA, or fatty acid glucamide, FAGA), as
well as products available under the trade names SPAN and TWEEN,
and combinations thereof.
[0110] Non-limiting examples of semipolar surfactants include amine
oxides (AO) such as alkyldimethylamineoxide, N-(coco
alkyl)-N,N-dimethylamine oxide and
N-(tallow-alkyl)-N,N-bis(2-hydroxyethyl)amine oxide, fatty acid
alkanolamides and ethoxylated fatty acid alkanolamides, and
combinations thereof.
[0111] Non-limiting examples of zwitterionic surfactants include
betaine, alkyldimethylbetaine, and sulfobetaine, and combinations
thereof.
Builder or Complexing Agent
[0112] The detergent may contain 0-65% of a detergent builder or
complexing agent such as zeolite, diphosphate, triphosphate,
phosphonate, carbonate, citrate, nitrilotriacetic acid,
ethylenediaminetetraacetic acid, diethylenetriaminepentaacetic
acid, alkyl- or alkenylsuccinic acid, soluble silicates or layered
silicates (e.g. SKS-6 from Hoechst).
[0113] In a dish wash detergent, the level of builder is typically
40-65%, particularly 50-65%. The builder and/or co-builder may
particularly be a chelating agent that forms water-soluble
complexes with Ca and Mg. Non-limiting examples of builders include
zeolites, diphosphates (pyrophosphates), triphosphates such as
sodium triphosphate (STP or STPP), carbonates such as sodium
carbonate, soluble silicates such as sodium metasilicate, layered
silicates (e.g., SKS-6 from Hoechst), ethanolamines such as
2-aminoethan-1-ol (MEA), iminodiethanol (DEA) and
2,2',2''-nitrilotriethanol (TEA), and carboxymethylinulin (CMI),
and combinations thereof.
[0114] The detergent composition may include include a co-builder
alone, or in combination with a builder, for example a zeolite
builder. Non-limiting examples of co-builders include homopolymers
of polyacrylates or copolymers thereof, such as poly(acrylic acid)
(PAA) or copoly(acrylic acid/maleic acid) (PAA/PMA). Further
non-limiting examples include citrate, chelators such as
aminocarboxylates, aminopolycarboxylates and phosphonates, and
alkyl- or alkenylsuccinic acid. Additional specific examples
include 2,2',2''-nitrilotriacetic acid (NTA),
etheylenediaminetetraacetic acid (EDTA),
diethylenetriaminepentaacetic acid (DTPA), iminodisuccinic acid
(IDS), ethylenediamineN,N'-disuccinic acid (EDDS),
methylglycinediacetic acid (MGDA), glutamic acid-N,N-diacetic acid
(GLDA), 1-hydroxyethane-1,1-diylbis(phosphonic acid) (HEDP),
ethylenediaminetetrakis(methylene)tetrakis(phosphonic acid)
(EDTMPA), diethylenetriaminepentakis(methylene)pentakis(phosphonic
acid) (DTPMPA), N-(2-hydroxyethyl)iminodiacetic acid (EDG),
aspartic acid-N-monoacetic acid (ASMA), aspartic acid-N,N-diacetic
acid (ASDA), aspartic acid-N-monopropionic acid (ASMP),
iminodisuccinic acid (IDA), N-(2-sulfomethyl) aspartic acid (SMAS),
N-(2-sulfoethyl) aspartic acid (SEAS), N-(2-sulfomethyl) glutamic
acid (SMGL), N-(2-sulfoethyl) glutamic acid (SEGL),
N-methyliminodiacetic acid (MIDA), .alpha.-alanine-N,N-diacetic
acid (.alpha.-ALDA), serine-N,N-diacetic acid (SEDA),
isoserine-N,N-diacetic acid (ISDA), phenylalanineN,N-diacetic acid
(PHDA), anthranilic acid-N,N-diacetic acid (ANDA), sulfanilic
acid-N, N-diacetic acid (SLDA), taurine-N, N-diacetic acid (TUDA)
and sulfomethyl-N,N-diacetic acid (SMDA),
N(hydroxyethyl)-ethylidenediaminetriacetate (HEDTA),
diethanolglycine (DEG), Diethylenetriamine Penta (Methylene
Phosphonic acid) (DTPMP), aminotris(methylenephosphonic acid)
(ATMP), and combinations and salts thereof. Further exemplary
builders and/or co-builders are described in, e.g., WO 09/102854,
U.S. Pat. No. 5,977,053.
Polymer
[0115] The detergent may comprise one or more polymers. Examples
are carboxymethylcellulose, poly(vinylpyrrolidone), poly (ethylene
glycol), poly(vinylalcohol), poly(vinylpyridine-N-oxide),
poly(vinylimidazole), polycarboxylates such as polyacrylates,
maleic/acrylic acid copolymers and lauryl methacrylate/acrylic acid
copolymers.
Hydrotropes
[0116] A hydrotrope is a compound that solubilises hydrophobic
compounds in aqueous solutions (or oppositely, polar substances in
a non-polar environment). Typically, hydrotropes have both
hydrophilic and a hydrophobic character (so-called amphiphilic
properties as known from surfactants); however the molecular
structure of hydrotropes generally do not favor spontaneous
selfaggregation, see e.g. review by Hodgdon and Kaler (2007),
Current Opinion in Colloid & Interface Science 12: 121-128.
Hydrotropes do not display a critical concentration above which
selfaggregation occurs, as found for surfactants and lipids forming
miceller, lamellar or other well defined meso-phases. Instead, many
hydrotropes show a continuous-type aggregation process where the
size of aggregates grow as concentration increases. However, many
hydrotropes alter the phase behavior, stability, and colloidal
properties of systems containing substances of polar and non-polar
character, including mixtures of water, oil, surfactants, and
polymers. Hydrotropes are classically used across industries from
pharma, personal care, food, to technical applications. Use of
hydrotropes in detergent compositions allow for example more
concentrated formulations of surfactants (as in the process of
compacting liquid detergents by removing water) without inducing
undesired phenomena such as phase separation or high viscosity.
[0117] The detergent may contain 0-5% by weight, such as about 0.5
to about 5%, or about 3% to about 5%, of a hydrotrope. Non-limiting
examples of hydrotropes include sodium benzene sulfonate, sodium
p-toluene sulfonates (STS), sodium xylene sulfonates (SXS), sodium
cumene sulfonates (SCS), sodium cymene sulfonate, amine oxides,
alcohols and polyglycolethers, sodium hydroxynaphthoate, sodium
hydroxynaphthalene sulfonate, sodium ethylhexyl sulfate, and
combinations thereof.
Fabric Hueing Agents
[0118] The detergent compositions of the present invention may also
include fabric hueing agents such as 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/reflection 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 W2005/03274, W2005/03275, WO2005/03276 and EP1876226 (hereby
incorporated by reference). The detergent composition preferably
comprises from about 0.00003 wt % to about 0.2 wt %, from about
0.00008 wt % to about 0.05 wt %, or even from about 0.0001 wt % to
about 0.04 wt % fabric hueing agent. The composition may comprise
from 0.0001 wt % to 0.2 wt % fabric hueing agent, this may be
especially preferred when the composition is in the form of a unit
dose pouch. Suitable hueing agents are also disclosed in, e.g., WO
2007/087257, WO2007/087243.
Detergent Formulations
[0119] The enzyme granules may be included in a granular detergent
formulated as described in WO09/092699, EP1705241, EP1382668,
WO07/001262, U.S. Pat. No. 6,472,364, WO04/074419 or WO09/102854.
Other useful detergent formulations are described in WO09/124162,
WO09/124163, WO09/117340, WO09/117341, WO09/117342, WO09/072069,
WO09/063355, WO09/132870, WO09/121757, WO09/112296, WO09/112298,
WO09/103822, WO09/087033, WO09/050026, WO09/047125, WO09/047126,
WO09/047127, WO09/047128, WO09/021784, WO09/010375, WO09/000605,
WO09/122125, WO09/095645, WO09/040544, WO09/040545, WO09/024780,
WO09/004295, WO09/004294, WO09/121725, WO09/115391, WO09/115392,
WO09/074398, WO09/074403, WO09/068501, WO09/065770, WO09/021813,
WO09/030632, WO09/015951, WO2011025615, WO2011016958, WO2011005803,
WO2011005623, WO2011005730, WO2011005844, WO2011005904,
WO2011005630, WO2011005830, WO2011005912, WO2011005905,
WO2011005910, WO2011005813, WO2010135238, WO2010120863,
WO2010108002, WO2010111365, WO2010108000, WO2010107635,
WO2010090915, WO2010033976, WO2010033746, WO2010033747,
WO2010033897, WO2010033979, WO2010030540, WO2010030541,
WO2010030539, WO2010024467, WO2010024469, WO2010024470,
WO2010025161, WO2010014395, WO2010044905, WO2010145887,
WO2010142503, WO2010122051, WO2010102861, WO2010099997,
WO2010084039, WO2010076292, WO2010069742, WO2010069718,
WO2010069957, WO2010057784, WO2010054986, WO2010018043,
WO2010003783, WO2010003792, WO2011023716, WO2010142539,
WO2010118959, WO2010115813, WO2010105942, WO2010105961,
WO2010105962, WO2010094356, WO2010084203, WO2010078979,
WO2010072456, WO2010069905, WO2010076165, WO2010072603,
WO2010066486, WO2010066631, WO2010066632, WO2010063689,
WO2010060821, WO2010049187, WO2010031607, or WO2010000636.
TEST METHODS
Test Method 1: First Wash Lipase Test
[0120] Lard First Wash Test
[0121] Whether any specific lipase enzyme gives better First Wash
lard removal performance than WT Lipolase (from Novozymes,
described in U.S. Pat. No. 5,869,438, SEQ ID:2), can be determined
by comparing the performance results of WT Lipolase with the
performance results of the specific lipase enzyme according to the
following test:
[0122] The wash performance of lipolytic enzymes is tested in a one
cycle wash trial carried out in a thermostated Terg-O-tometer (TOM)
followed by line-drying. The experimental conditions are as
follows:
[0123] Wash liquor: 1000 ml per beaker
[0124] Swatches: 7 flat cotton swatches (9.times.9 cm) (supplied by
Warwick-Equest) per beaker Stain: Lard coloured red with sudan red
dye (Sigma) (0.75 mg Sudan red/g lard). 50 .mu.l of lard/sudan red
heated to 70.degree. C. are applied to the centre of each swatch.
After application of the stain the swatches are heated in an oven
for 25 minutes at 75.degree. C. and then stored overnight at room
temperature.
[0125] Water for preparing wash liquor: 3.2 mM Ca.sup.2+/Mg.sup.2+
(in a ratio of 5:1)
[0126] Detergent: 5 g/l of detergent composition A.
[0127] Detergent Composition A:
[0128] 0.300 g/l alkyl sulphate (AS; C.sub.14-16)
[0129] 0.650 g/l of alcohol ethoxylate (AEO; C.sub.12-14, 6EO)
[0130] 1.750 g/l Zeolite P
[0131] 0.145 g/l Na.sub.2CO.sub.3
[0132] 0.020 g/l Sokalan CP5 (BASF)
[0133] 0.050 g/l CMC (carboxy methyl cellulose--Finnfix BDA ex CP
Kelco)
[0134] 5 g/l of detergent composition A are mixed into deionised
water with added hardness (3.2 mM Ca.sup.2+/Mg.sup.2+ (5:1)) and
the pH artificially adjusted to pH 10.2 by adding NaOH. Lipase
enzyme is added.
[0135] Concentration of lipolytic enzyme: 0 and 12500 LU/I
[0136] Wash time: 20 minutes
[0137] Wash temperature: 30.degree. C.
[0138] Rinse: 15 minutes in running tap water
[0139] Drying: overnight at room conditions (approx. 20.degree. C.,
30-40% RH).
[0140] Evaluation: the reflectance was measured at 460 nm.
[0141] The percentage of lard removed is determined as:
[0142] Delta reflectance (dR) defined as:
[0143] (R(Swatches washed in detergent with lipase)-R(Swatches
washed in detergent without lipase)
[0144] The reflectance (which may also be termed remission) is
measured on an Elrepho 2000 apparatus from Datacolor which
illuminates the sample with 2 xenon blitz lamps and measures the
amount of reflected light so that entirely white corresponds to a
100% reflectance and entirely black a 0% reflectance. Comparing the
results for lard removal due to the presence of enzyme, lipase
enzymes giving better performance than WT Lipolase.TM. are suitable
for use in the compositions of the present invention.
Test Method 2: Dissolution Test
[0145] A detergent solution is prepared according to test detergent
description in Example 2 in 18 dH water. The detergent solution is
stirred for 30 min and filtered through a sheet of gauze. The
detergent solution is adjusted to 20.degree. C..+-.2.degree. C. and
placed under a 4-bladed propeller stirrer adjusted to 600 rpm.+-.10
rpm. 75 mg enzyme containing particle/I detergent solution is added
at T.sub.0. After addition of the enzyme containing particles the
concentration of the enzyme released to the detergent solution is
measured every 15 seconds for the first 60 seconds by withdrawing
samples from the detergent solution. Subsequently samples are taken
out every 30 seconds until 120 seconds and every 60 seconds until
1100 seconds. The enzyme activity in the withdrawn samples are
measured in a suitable analytical method, e.g. for a lipase enzyme
by use of assays involving synthetic substrates such as
p-nitrophenyl butyrate or p-nitrophenyl palmitate. The time for 50%
resp. 90% release of the enzyme from the enzyme containing
particles are calculated.
[0146] The same method is applied to organic peroxyacid source
particles to determine the time for 50% resp. 90% release of the
organic peroxyacid source.
EXAMPLES
Example 1: Preparation of Lipase Granules with Delayed-Release
Coating
[0147] A coated lipase was prepared as follows. The lipase was
Lipex.TM. (product of Novozymes A/S, described in WO 00/60063). It
was formulated as a T-granulate produced essentially as in example
1 of WO2004/003188 (Int'l App. No. PCT/DK03/000456) (containing
enzyme, Na-sulfate, cellulose fibers, calcium carbonate and a
binder, e.g. sucrose or dextrin). This was coated with a coating
consisting of 31% of palm oil, 50% of kaolin or calcium carbonate
and 19% of titanium dioxide (% by weight). The amount of the
coating material made up 25% by weight of the coated granules.
TABLE-US-00001 In outer In core coating Total Ingredient (wt %) (wt
%) (wt %) Sodium sulfate 67 49 Kaolin 9 50 19 Cellulose 10 8
Dextrin 3 2 Sucrose 2 2 Lipase (and other dry matter 9 7 from
concentrate) Palm oil 31 8 Titanium dioxide 19 5
Example 2: Washing Tests with Coated Lipase and Organic
Catalyst
[0148] The wash performance and the resistance to organic catalyst
of the coated lipase were tested in washing tests with a model
detergent (described below) using textile swatches soiled with
various fatty stains (also described below).
[0149] The invention formulation was the coated lipase granulate
prepared in Example 1. For comparison, the same lipase in the form
of a conventional granulate coated with PEG(polyethylene glycol)
was used as a conventional formulation. The organic non-metal
bleach catalyst was a compound according to Formula 1 in
WO2007/001262 with R=2-butyl-octyl.
Experimental Conditions
TABLE-US-00002 [0150] Machine Miele Softtronic W2245 (EU) Program
Minimum Iron , Water Plus, approx 15 L water Temperature 30.degree.
C. Water hardness Water hardness Wash: 18 dH (molar ratio between
Ca.sup.2+/Mg.sup.2+/HCO3.sup.- 4:1:7.5) Test detergent LAS 0.9 g/l
AEO 0.2 g/l Na2CO3 0.53 g/l Zeolite A4 1.07 g/l Na3citrate 0.52 g/l
Percarbonate 1 g/l TAED 0.25 g/l Bleach catalyst -/+125 mg/l (2.5
ppm active) pH As is 2 of each of the below stains attached to
tea-towels in 3 corners Substrate Product code Manufacturer
Measurements Swatches/test Mustard CS67 (4 .times. 9 cm) CFT Color
eye, material Reflectance, 540 nm Hamburger 10 .times. 10 cm blue
Equest Scanner, Intensity grease knitted cotton, Stain Lard
diameter 5 cm Margarine Bacon grease Butter Drying Lying flat on
blotting paper, 24 h, room temperature, in dark Ballast 2.7 kg
cotton ballast Enzymes Dosage 0.25 mg enzyme protein (EP)/I
Repetitions 3 repeated washes per condition
Wash Performance Evaluation of Blue Equest Stains
[0151] The wash performance of the blue Equest stains is measured
after 24 hours +/-2 hours of drying as the brightness of the color
of the textile washed. Brightness can also be expressed as the
intensity of the light reflected from the sample when illuminated
with white light. When the sample is stained the intensity of the
reflected light is lower than that of a clean sample. Therefore the
intensity of the reflected light can be used to measure wash
performance.
[0152] Color measurements are made with a professional flatbed
scanner (Kodak iQsmart, Kodak, Midtager 29, DK-2605 Brondby,
Denmark), which is used to capture an image of the washed
textile.
[0153] To extract a value for the light intensity from the scanned
images, 24-bit pixel values from the image are converted into
values for red, green and blue (RGB). The scans are made with a
resolution of 200 dpi.
[0154] The intensity value (Int) is calculated by adding the RGB
values together as vectors and then taking the length of the
resulting vector:
Int= {square root over (r.sup.2+g.sup.2+b.sup.2)}.
[0155] The wash performance (P) of the lipase formulation is
calculated in accordance with the below formula:
P=.DELTA.Int=Int(v)-Int(r)
[0156] where
[0157] Int(v) is the light intensity value of textile surface
washed with the lipase formulation, and
[0158] Int(r) is the light intensity value of textile surface
washed without the lipase formulation.
Wash Performance Evaluation of CS67
[0159] Wash performance is expressed as a delta remission value
(.DELTA.Rem). Light reflectance evaluations of the swatches were
done after 24 hours of drying using a Macbeth Color Eye 7000
reflectance spectrophotometer with very small aperture. The
measurements were made without UV in the incident light and
remission at 540 nm was extracted. Measurements were made on washed
swatches. The test swatch to be measured was placed on top of
another swatch of same type and color (twin swatch).
P=.DELTA.REM=Rem(v)-Rem(r)
[0160] where
[0161] Rem(v) is the light intensity value of textile surface
washed with the lipase formulation, and
[0162] Rem(r) is the light intensity value of textile surface
washed without the lipase formulation.
Calculation of Relative Performance Score
[0163] A relative performance score is given as the result of the
full scale was washed in accordance with the definition:
[0164] Relative Performance scores (RP) give performance (P) of the
tested lipase formulation against the conventional lipase
formulation:
RP.dbd.P(invention formulation)/P(conventional formulation).
[0165] RPavg indicates the average relative performance compared to
the conventional lipase formulation on each swatch type at all
repetitions (3 repeated washes with 2 stains in each wash)
[0166] A lipase formulation is considered to exhibit improved wash
performance, if it performs better than the conventional lipase
formulation.
[0167] The resistance of the lipase formulation against the bleach
catalyst is calculated in accordance with the below formulation
Calculation of Residual Performance Score (ResP)
[0168] Residual performance score (ResP) is calculated as the
performance (P) of the tested lipase formulation with the bleach
catalyst relative to the tested lipase formulation without the
bleach catalyst:
ResP=P(invention formulation with bleach catalyst)/P(invention
formulation without bleach catalyst).
[0169] ResPavg indicates the average relative performance compared
to the conventional lipase formulation on each swatch type at all
repetitions (3 repeated washes with 2 stains in each wash).
[0170] An improvement factor was taken as ResPavg for the invention
formulation relative to the conventional formulation. A lipase
formulation exhibits improved resistance towards the bleach
catalyst if it has higher residual performance than the
conventional lipase formulation.
Results
TABLE-US-00003 [0171] Equest stains CFT Hamburger Bacon Avg stain
grease Lard Margarine grease Butter Equest CS67 % ResPavg Invention
22 47 60 58 38 45 59 with 2.5 ppm formulation Bleach catalyst
Conventional 0 25 20 8 26 16 37 formulation Improvement NA 1.9 2.9
7.0 1.4 3.3 1.6 factor with 2.5 ppm Bleach catalyst RPavg (%) Lipex
DR/ 117 95 120 68 80 96 106 Lipex 100T
[0172] The results for ResPavg for the conventional formulation are
all 37% or less, indicating that the lipase is sensitive to the
bleach catalyst.
[0173] The results for the improvement factor demonstrate that the
lipase in the form of granules with a delayed-release coating is
markedly less inhibited by the organic non-metal bleach catalyst
than conventional granules. On average, the lipase with
delayed-release coating was inhibited by 49-56% while the
conventional granules were inhibited by 65-85%.
[0174] The results for RPavg demonstrate that the lipase
performance of granules with delayedrelease coating broadly matches
that of conventional lipase granules although there is high
variation in the performance values on the individual stains for
both of the lipase samples.
Example 3: Release Profile
[0175] A lipase variant was granulated and coated as described in
Example 1, and the release profile was determined according to Test
Method 2 (Dissolution test), described above.
[0176] The time for release of 50% activity and 90% activity (T50
and T90) was found to be well above 4 ?seconds and well above 800
seconds, respectively.
[0177] For comparison, a conventional T-granulate of the same
lipase variant coated with PEG (polyethylene glycol) and
CaCO.sub.3/kaolin was also tested. T50 and T90 of the conventional
granulate were found to be 112 seconds and 242 seconds,
respectively.
* * * * *