Note: Descriptions are shown in the official language in which they were submitted.
1
CLEANING COMPOSITIONS INCLUDING ENZYMES
REFERENCE TO A SEQUENCE LISTING
This application contains a Sequence Listing in computer readable form.
FIELD OF THE INVENTION
The present disclosure relates to cleaning compositions that include a
glycoside hydrolase
enzyme. The present disclosure also relates to methods of making and using
such cleaning
compositions. The present disclosure also relates to the use of the glycoside
hydrolase enzyme.
BACKGROUND OF THE INVENTION
The detergent formulator is constantly aiming to improve the performance of
detergent
compositions. One particular challenge is the removal of certain soils of
microbial origin from
surfaces such as textiles. Such soils can be sticky and difficult to remove.
Furthermore, because
they are sticky they tend to adhere body soils and/or particulate soils to the
surface, making soil
removal difficult and tending to build up over time. This may be particularly
noticeable for
example on collars and cuffs where incomplete cleaning may occur.
There is a need for improved cleaning compositions which provide cleaning of
such
soils. The present inventors have found that this problem may be ameliorated
by cleaning
compositions comprising certain glycoside hydrolases. Glycosyl hydrolases are
enzymes that
catalyze the hydrolysis of the glycosyl bond to release smaller sugars. There
are over 100 classes
of glycosyl hydrolase and many different enzymes fall within the class of
glycosyl hydrolases, for
example cellulases and xyloglucanases which can be used in cleaning
compositions. Surprisingly,
certain specific glycosyl hydrolases can provide particularly improved
cleaning.
Glycoside hydrolases are described by Coutinho, P.M. and Henrissat, B., 1999,
Carbohydrate-active enzymes: an integrated database approach, in "Recent
Advances In
Carbohydrate Bioengineering", H.J. Gilbert, G. Davies, B. Henrissat and B.
Svensson eds., The
Royal Society of Chemistry, Cambridge, pp. 3-12.
SUMMARY OF THE INVENTION
The present invention provides a cleaning and/or treatment composition
comprising an
amylase enzyme and an enzyme having glycoside hydrolase activity, wherein the
enzyme is a
member of a glycoside hydrolase family GH 39.
A preferred glycoside hydrolase enzyme having glycoside hydrolase activity is
a variant
having at least 60% identity or at least 65% or at least 70% or at least 75%
or at least 80% or at
Date Recue/Date Received 2020-11-04
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least 85% or at least 90% or at least 95% identity to SEQ ID NO:1, and less
than, or up to 100%
identity with SEQ ID NO:1.
The present invention provides a method of cleaning a surface, such as a
textile, that
comprises mixing a cleaning composition as described herein with water to form
an aqueous liquor
and contacting a surface with the aqueous liquor in a laundering step.
Preferably the glycoside
hydrolase enzyme is present in the aqueous wash liquor in an amount of from
0.01ppm to 1000
ppm enzyme, based on active protein.
The present invention also relates to the use of a composition comprising an
amylase
enzyme and an enzyme having glycoside hydrolase activity selected from
glycoside hydrolases
from family GH 39 to enhance soil and/or stain removal from a surface,
preferably a fabric, and/or
for malodour reduction from a surface, preferably the glycoside hydrolase
having at least 60% or
at least 65% or at least 70% or at least 75% or at least 80% or at least 85%
or at least 90% or at
least 95% identity to less than or up to 100% identity with SEQ ID NO:1, to
enhance soil and/or
stain removal from a surface, preferably a fabric, and/or for malodour
reduction from a surface.
A preferred composition comprises a second glycosyl hydrolase from the endo-
alpha-1,4-
polygalactosminidase class (EC 3.2.1.109) of enzymes.
DETAILED DESCRIPTION OF THE INVENTION
The components of the compositions and processes of the present disclosure are
described in more detail below.
As used herein, the articles "a" and "an" when used in a claim, are understood
to mean one
or more of what is claimed or described. As used herein, the terms -include," -
includes," and
"including" are meant to be non-limiting. The compositions of the present
disclosure can
comprise, consist essentially of, or consist of, the components of the present
disclosure.
The terms "substantially free of' or "substantially free from" may be used
herein. This
means that the indicated material is at the very minimum not deliberately
added to the composition
to form part of it, or, preferably, is not present at analytically detectable
levels. It is meant to
include compositions whereby the indicated material is present only as an
impurity in one of the
other materials deliberately included. The indicated material may be present,
if at all, at a level of
less than 1%, or less than 0.1%, or less than 0.01%, or even 0%, by weight of
the composition.
As used herein, the term "etheramine" includes the term "poly etheramine" and
includes
amines that have one or more ether groups.
Unless otherwise noted, all component or composition levels are in reference
to the active
portion of that component or composition, and are exclusive of impurities, for
example, residual
Date Recue/Date Received 2020-11-04
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solvents or by-products, which may be present in commercially available
sources of such
components or compositions.
All temperatures herein are in degrees Celsius ( C) unless otherwise
indicated. Unless
otherwise specified, all measurements herein are conducted at 20 C and under
atmospheric
pressure.
In all embodiments of the present disclosure, all percentages are by weight of
the total
composition, unless specifically stated otherwise. All ratios are weight
ratios, unless specifically
stated otherwise.
It should be understood that every maximum numerical limitation given
throughout this
specification includes every lower numerical limitation, as if such lower
numerical limitations
were expressly written herein. Every minimum numerical limitation given
throughout this
specification will include every higher numerical limitation, as if such
higher numerical limitations
were expressly written herein. Every numerical range given throughout this
specification will
include every narrower numerical range that falls within such broader
numerical range, as if such
narrower numerical ranges were all expressly written herein.
As used herein, the term "alkoxy" is intended to include C1-C8 alkoxy and C1-
C8 alkoxy
derivatives of polyols having repeating units such as butylene oxide, glycidol
oxide, ethylene oxide
or propylene oxide.
As used herein, unless otherwise specified, the terms "alkyl" and "alkyl
capped" are
intended to include C1-C18 alkyl groups, or even C1-C6 alkyl groups.
As used herein, unless otherwise specified, the term -aryl" is intended to
include C3-12
aryl groups.
As used herein, unless otherwise specified, the term "ary lalky 1" and
"alkaryl" are
equivalent and are each intended to include groups comprising an alkyl moiety
bound to an
aromatic moiety, typically having C1-C18 alkyl groups and, in one aspect, C1-
C6 alkyl groups.
The terms "ethylene oxide," "propylene oxide" and "butylene oxide" may be
shown herein
by their typical designation of "E0," "PO" and "BO," respectively.
As used herein, the term "cleaning and/or treatment composition" includes,
unless
otherwise indicated, granular, powder, liquid, gel, paste, unit dose, bar form
and/or flake type
washing agents and/or fabric treatment compositions, including but not limited
to products for
laundering fabrics, fabric softening compositions, fabric enhancing
compositions, fabric
freshening compositions, and other products for the care and maintenance of
fabrics, and
combinations thereof. Such compositions may be pre-treatment compositions for
use prior to a
Date Recue/Date Received 2020-11-04
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washing step or may be rinse added compositions, as well as cleaning
auxiliaries, such as bleach
additives and/or "stain-stick" or pre-treat compositions or substrate-laden
products such as dryer
added sheets.
As used herein, "cellulosic substrates" are intended to include any substrate
which
comprises cellulose, either 100% by weight cellulose or at least 20% by
weight, or at least 30 %
by weight or at least 40 or at least 50 % by weight or even at least 60 % by
weight cellulose.
Cellulose may be found in wood, cotton, linen, jute, and hemp. Cellulosic
substrates may be in
the form of powders, fibers, pulp and articles formed from powders, fibers and
pulp. Cellulosic
fibers, include, without limitation, cotton, rayon (regenerated cellulose),
acetate (cellulose acetate),
triacetate (cellulose triacetate), and mixtures thereof. Typically cellulosic
substrates comprise
cotton. Articles formed from cellulosic fibers include textile articles such
as fabrics. Articles
formed from pulp include paper.
As used herein, the term "maximum extinction coefficient" is intended to
describe the
molar extinction coefficient at the wavelength of maximum absorption (also
referred to herein as
the maximum wavelength), in the range of 400 nanometers to 750 nanometers.
As used herein "average molecular weight" is reported as a weight average
molecular
weight, as determined by its molecular weight distribution; as a consequence
of their
manufacturing process, polymers disclosed herein may contain a distribution of
repeating units in
their polymeric moiety.
As used herein the term "variant" refers to a polypeptide that contains an
amino acid
sequence that differs from a wild type or reference sequence. A variant
polypeptide can differ from
the wild type or reference sequence due to a deletion, insertion, or
substitution of a nucleotide(s)
relative to said reference or wild type nucleotide sequence. The reference or
wild type sequence
can be a full-length native polypeptide sequence or any other fragment of a
full- length polypeptide
sequence. A polypeptide variant generally has at least about 70% amino acid
sequence identity
with the reference sequence, but may include 75% amino acid sequence identity
within the
reference sequence, 80% amino acid sequence identity within the reference
sequence, 85% amino
acid sequence identity with the reference sequence, 86% amino acid sequence
identity with the
reference sequence, 87% amino acid sequence identity with the reference
sequence, 88% amino
acid sequence identity with the reference sequence, 89% amino acid sequence
identity with the
reference sequence, 90% amino acid sequence identity with the reference
sequence, 91% amino
acid sequence identity with the reference sequence, 92% amino acid sequence
identity with the
reference sequence, 93% amino acid sequence identity with the reference
sequence, 94% amino
Date Recue/Date Received 2020-11-04
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acid sequence identity with the reference sequence, 95% amino acid sequence
identity with the
reference sequence, 96% amino acid sequence identity with the reference
sequence, 97% amino
acid sequence identity with the reference sequence, 98% amino acid sequence
identity with the
reference sequence, 98.5% amino acid sequence identity with the reference
sequence or 99%
amino acid sequence identity with the reference sequence.
As used herein, the term "solid" includes granular, powder, bar and tablet
product forms.
As used herein, the term "fluid" includes liquid, gel, paste, and gas product
forms.
Cleaning Composition
The present disclosure relates to cleaning and/or treatment compositions. The
cleaning
composition may be selected from the group of light duty liquid detergents
compositions, heavy
duty liquid detergent compositions, solid, for example powder detergent, hard
surface cleaning
compositions, detergent gels commonly used for laundry, bleaching
compositions, laundry
additives, fabric enhancer compositions, shampoos, body washes, other personal
care
compositions, and mixtures thereof. The cleaning composition may be a hard
surface cleaning
composition (such as a dishwashing composition) or a laundry composition (such
as a heavy duty
liquid detergent composition).
The cleaning compositions may be in any suitable form. The composition can be
selected
from a liquid, solid, or combination thereof. As used herein, "liquid"
includes free-flowing liquids,
as well as pastes, gels, foams and mousses. Non-limiting examples of liquids
include light duty
.. and heavy duty liquid detergent compositions, fabric enhancers, detergent
gels commonly used for
laundry, bleach and laundry additives. Gases, e.g., suspended bubbles, or
solids, e.g. particles,
may be included within the liquids. A "solid" as used herein includes, but is
not limited to,
powders, agglomerates, and mixtures thereof. Non-limiting examples of solids
include: granules,
micro-capsules, beads, noodles, and pearlised balls. Solid compositions may
provide a technical
benefit including, but not limited to, through-the-wash benefits, pre-
treatment benefits, and/or
aesthetic effects.
The cleaning composition may be in the form of a unitized dose article, such
as a tablet or
in the form of a pouch. Such pouches typically include a water-soluble film,
such as a polyvinyl
alcohol water-soluble film, that at least partially encapsulates a
composition. Suitable films are
available from MonoSol, LLC (Indiana, USA). The composition can be
encapsulated in a single
or multi-compai __ intent pouch. A multi-compai ____________________________
intent pouch may have at least two, at least three,
or at least four compartments. A multi-compai ______________________________
iniented pouch may include compartments that are
Date Recue/Date Received 2020-11-04
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side-by-side and/or superposed. The composition contained in the pouch may be
liquid, solid
(such as powders), or combinations thereof.
Glycoside Hydrolase Enzyme
The composition comprises a glycoside hydrolase enzyme having glycoside
hydrolase
.. activity and selected from GH family 39 glycoside hydrolases. The enzyme
essential to the
present invention preferably comprises glycoside hydrolase enzyme having at
least 60% or at least
65% or at least 70% or at least 75% or at least 80% or at least 85% or at
least 90% or at least 95%,
and less than or up to 100% identity to SEQ ID NO:l.
Preferably the glycoside hydrolase is from GH family 39.
Preferably, the glycoside hydrolase enzyme comprises a microbial enzyme. The
glycoside
hydrolase enzyme may be fungal or bacterial in origin. Bacterial glycoside
hydrolases may be
most preferred. Fungal glycoside hydrolases may be most preferred.
The glycoside hydrolase may be obtainable from Pseudomonas, such as a
Pseudomonas
aeruginosa. Suitable examples are described in Baker et al., (2016) Sci Adv,
2, such as the mature
polypeptide SEQ ID NO: 1 of the present invention from Pseudomonas aeruginosa.
Preferably
the glycoside hydrolase is Ps1Gh, optionally in addition to further glycoside
hydrolases.
Preferably the glycoside hydrolase is an isolated glycoside hydrolase.
Preferably the or each glycoside hydrolase enzyme is present in the cleaning
composition
in an amount from 0.001 to 1 wt%, or from 0.005 to 0.5 wt% or from 0.01 to
0.25 wt% based on
active protein.
Preferably the glycoside hydrolase enzyme is present in a laundering aqueous
liquor in an
amount of from 0.01ppm to 1000 ppm enzyme, based on active protein or from
0.05 or from
0.1ppm to 750 or 500ppm.
The composition comprising the glycoside hydrolase described herein may also
give rise
to/be useful for biofilm-disrupting effects or soil anti-redeposition effects.
Amylase Enzyme
The composition comprises an amylase enzyme. Suitable alpha-amylases include
those of
bacterial or fungal origin. Chemically or genetically modified mutants
(variants) are included. A
preferred alkaline alpha-amylase is derived from a strain of Bacillus, such as
Bacillus
licheniformis, Bacillus amyloliquefaciens, Bacillus stearothermophilus,
Bacillus subtilis, or other
Bacillus sp., such as Bacillus sp. NCIB 12289, NCIB 12512, NCIB 12513, DSM
9375 (USP
7,153,818) DSM 12368, DSMZ no. 12649, KSM AP1378 (WO 97/00324), KSM K36 or KSM
K38 (EP 1,022,334). Preferred amylases include:
Date Recue/Date Received 2020-11-04
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(a) the variants described in WO 94/02597, WO 94/18314, W096/23874 and WO
97/43424, especially the variants with substitutions in one or more of the
following positions
versus the enzyme listed as SEQ ID NO: 2 herein (SEQ ID No. 2 in WO 96/23874):
15, 23, 105,
106, 124, 128, 133, 154, 156, 181 , 188, 190, 197, 202, 208, 209, 243, 264,
304, 305, 391, 408,
and 444.
(b) the variants described in USP 5,856,164 and W099/23211, WO 96/23873,
W000/60060 and WO 06/002643, especially the variants with one or more
substitutions in the
following positions versus the AA560 enzyme listed as SEQ ID NO: 3 herein (SEQ
ID No. 12 in
WO 06/002643):
26, 30, 33, 82, 37, 106, 118, 128, 133, 149, 150, 160, 178, 182, 186, 193,
203, 214, 231, 256, 257,
258, 269, 270, 272, 283, 295, 296, 298, 299, 303, 304, 305, 311, 314, 315,
318, 319, 339, 345,
361, 378, 383, 419, 421, 437, 441, 444, 445, 446, 447, 450, 461, 471, 482,
484, preferably that
also contain the deletions of D183* and G184*.
(c) variants exhibiting at least 90% identity with as SEQ ID NO: 4 herein
(SEQ ID No.
4 in W006/002643), the wild-type enzyme from Bacillus 5P722, especially
variants with deletions
in the 183 and 184 positions and variants described in WO 00/60060.
(d) variants exhibiting at least 95% identity with as SEQ ID NO:5 herein,
the wild-type
enzyme from Bacillus sp.707 (SEQ ID NO:7 in US 6,093, 562), especially those
comprising one
or more of the following mutations M202, M208, S255, R172, and/or M261.
Preferably said
amylase comprises one or more of M202L, M202V, M2025, M202T, M202I, M202Q,
M202W,
S255N and/or R172Q. Particularly preferred are those comprising the M202L or
M202T
mutations.
(e) variants described in WO 09/149130, preferably those exhibiting at
least 90%
identity with SEQ ID NO: 6 or SEQ ID NO:7 herein (SEQ ID NOS: 1 and 2 from WO
09/149130),
the wild-type enzyme from Geobacillus Stearophermophilus or a truncated
version thereof;
(0 variants as described in EP2540825 and EP2357220, EP2534233;
(g) variants as described in W02009100102 and W02010115028;
(h) variants exhibiting at least 89% identity with as SEQ ID NO: 8 herein (SEQ
ID NO:1
in W02016091688), especially those comprising deletions at positions H183+G184
and
additionally one or more mutations at positions 405, 421, 422 and/or 428.
(i) variants exhibiting at least 60% amino acid sequence identity with the
"PcuAmyl a-
amylase" from Paenibacillus curdlanolyticus YK9 as SEQ ID NO: 9 herein (SEQ ID
NO:3 in
W02014099523).
Date Recue/Date Received 2020-11-04
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(j) variants exhibiting at least 60% amino acid sequence identity with the
"CspAmy2
amylase- from Cytophaga sp., as SEQ ID NO: 10 herein (SEQ ID NO:1 in
W02014164777).
(k) variants exhibiting at least 85% identity with AmyE from Bacillus subtilis
as SEQ ID
NO: 11 herein (SEQ ID NO:1 in W02009149271).
(1) Variants exhibiting at least 90% identity variant with the wild-type
amylase from
Bacillus sp. KSM-K38 with accession number AB051102.
Suitable commercially available alpha-amylases include DURAMYLO, LIQUEZYMEO,
TERMAMYLO, TERMAMYL ULTRA , NATALASEO, SUPRAMYLO, STAINZYMEO,
STAINZYME PLUS , FUNGAMYLO and BAN (Novozymes A/S, Bagsvaerd, Denmark),
.. KEMZYMO AT 9000 Biozym Biotech Trading GmbH Wehlistrasse 27b A-1200 Wien
Austria,
RAPIDASEO , PURASTARO, ENZYSIZEO, OPTISIZE HT PLUS , POWERASEO and
PURASTAR OXAMO (Genencor International Inc., Palo Alto, California) and KAMO
(Kao, 14-
10 Nihonbashi Kayabacho, 1-chome, Chuo-ku Tokyo 103-8210, Japan). In one
aspect, suitable
amylases include NATALASEO, STAINZYMEO and STAINZYME PLUS and mixtures
thereof. The amylase is preferably present in an amount 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
Optional Additional Glycosyl Hydrolase
The composition of the invention preferably comprises an additional glycosyl
hydrolase.
A preferred additional glycosyl hydrolase comprises a glycosyl hydrolase from
the endo-alpha-
1,4-polygalactosminidase class (EC 3.2.1.109) of enzymes. preferably having at
least 60% or 65%
or more preferably at least 70% or 75% or 80% or 85% or 90% or 95% up to 100%
identity to
SEQ ID NO:12. Preferably the additional glycoside hydrolase is from GH family
114.
Preferably, the additional glycoside hydrolase enzyme is a microbial enzyme,
it may be
fungal or bacterial in origin, though bacterial glycoside hydrolases are most
preferred. Fungal
glycoside hydrolases may be most preferred. Such additional glycoside
hydrolase may be
obtainable from Pseudomonas, such as a Pseudomonas aeruginosa. Suitable
examples from class
EC 3.2.1.109 are described in Baker et al., (2016) Sci Adv, 2, such as the
mature polypeptide SEQ
ID NO: 12 of the present invention from Pseudomonas aeruginosa. Preferably
such additional
glycoside hydrolase in the cleaning composition of the invention is PelAh.
Adjuncts
The cleaning compositions described herein may optionally include other
adjunct
components, for example fabric care benefit agent; additional enzyme;
surfactant system; fabric
Date Recue/Date Received 2020-11-04
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shading dye; deposition aid; rheology modifier; builder; chelant; bleach;
bleach activator,
bleaching agent; bleach precursor; bleach booster; bleach catalyst; perfume
and/or perfume
microcapsules; perfume loaded zeolite; starch encapsulated accord;
polyglycerol esters; whitening
agent; pearlescent agent; enzyme stabilizing systems; scavenging agents
including fixing agents
for anionic dyes, complexing agents for anionic surfactants, and mixtures
thereof; optical
brighteners or fluorescers; polymer including but not limited to soil release
polymer and/or soil
suspension polymer; dispersants; antifoam agents; non-aqueous solvent; fatty
acid; suds
suppressors, e.g., silicone suds suppressors; cationic starches; scum
dispersants; substantive dyes;
colorants; opacifier; antioxidant; hydrotropes such as toluenesulfonates,
cumenesulfonates and
naphthalenesulfonates; color speckles; colored beads, spheres or extrudates;
clay softening agents;
anti-bacterial agents, quaternary ammonium compounds. In particular quaternary
ammonium
compounds may be present in particular for fabric enhancer compositions, such
as fabric softeners,
and comprise quaternary ammonium cations that are positively charged
polyatomic ions of the
structure NR4+, where R is an alkyl group or an aryl group.
Additional Enzymes
Preferably the composition of the invention comprises additional enzyme, for
example
selected from lipases, proteases, nucleases, galactanases, mannanases, pectate
lyases, cellulases,
cutinases, and mixtures thereof. The cleaning composition preferably comprises
one or more
additional enzymes from the group selected from nucleases, galactanases,
mannanases and
mixtures thereof. The cleaning composition preferably comprises one or more
additional enzymes
selected from the group lipases, proteases, pectate lyases, cellulases,
cutinases, and mixtures
thereof. Preferably in addition, the cleaning composition comprises one or
more additional
enzymes selected from proteases. Preferably the cleaning composition comprises
one or more
additional enzymes selected from lipases. The composition may also comprise
hemicellulases,
peroxidases, xylanases, pectinases, keratinases, reductases, oxidases,
phenoloxidases,
lipoxygenases, ligninases, pullulanases, tannases, pentosanases, malanases, B-
glucanases,
arabinosidases, hyaluronidase, chondroitinase, laccase and mixtures thereof.
When present in the
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.
Nucleases
In a preferred composition, the composition additionally comprises a nuclease
enzyme.
The nuclease enzyme is an enzyme capable of cleaving the phosphodiester bonds
between the
Date Recue/Date Received 2020-11-04
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nucleotide sub-units of nucleic acids. Suitable nuclease enzymes may be
deoxyribonuclease or
ribonuclease enzyme or a functional fragment thereof. By functional fragment
or part is meant the
portion of the nuclease enzyme that catalyzes the cleavage of phosphodiester
linkages in the DNA
backbone and so is a region of said nuclease protein that retains catalytic
activity. Thus it includes
.. truncated, but functional versions, of the enzyme and/or variants and/or
derivatives and/or
homologues whose functionality is maintained.
Preferably the nuclease enzyme is a deoxyribonuclease, preferably selected
from any of
the classes E.C. 3.1.21.x, where x=1, 2, 3, 4, 5, 6, 7, 8 or 9, E.C. 3.1.22.y
where y=1, 2, 4 or 5,
E.C. 3.1.30.z where z= 1 or 2, E.C. 3.1.31.1 and mixtures thereof. Nuclease
enzymes from class
E.C. 3.1.21.x and especially where x=1 are particularly preferred. Nucleases
in class E.C. 3.1.22.y
cleave at the 5' hydroxyl to liberate 3' phosphomonoesters. Enzymes in class
E.C. 3.1.30.z may
be preferred as they act on both DNA and RNA and liberate 5'-
phosphomonoesters. Suitable
examples from class E.C. 3.1.31.2 are described in U52012/0135498A, such as
SEQ ID NO:3
therein. Such enzymes are commercially available as DENARASEO enzyme from c-
LECTA.
Nuclease enzymes from class E.C. 3.1.31.1 produce 3 'phosphomonoesters.
Preferably, the nuclease enzyme comprises a microbial enzyme. The nuclease
enzyme
may be fungal or bacterial in origin. Bacterial nucleases may be most
preferred. Fungal nucleases
may be most preferred.
The microbial nuclease is obtainable from Bacillus, such as a Bacillus
licheniformis or
.. Bacillus subtilis bacterial nucleases. A preferred nuclease is obtainable
from Bacillus
licheniformis, preferably from strain El-34-6. A preferred deoxyribonuclease
is a variant of
Bacillus licheniformis, from strain EI-34-6 nucB deoxyribonuclease defined in
SEQ ID NO:13
herein, or variant thereof, for example having at least 70% or 75% or 80% or
85% or 90% or 95%,
96%, 97%, 98%, 99% or 100% identical thereto. Other suitable nucleases are
defined in SEQ ID
NO:14 herein, or variant thereof, for example having at least 70% or 75% or
80% or 85% or 90%
or 95%, 96%, 97%, 98%, 99% or 100% identical thereto. Other suitable nucleases
are defined in
SEQ ID NO:15 herein, or variant thereof, for example having at least 70% or
75% or 80% or 85%
or 90% or 95%, 96%, 97%, 98%, 99% or 100% identical thereto.
A fungal nuclease is obtainable from Aspergillus, for example Aspergillus
oryzae. A
.. preferred nuclease is obtainable from Aspergillus oryzae defined in SEQ ID
NO: 16 herein, or
variant thereof, for example having at least 60% or 70% or75% or 80% or 85% or
90% or 95%,
96%, 97%, 98%, 99% or 100% identical thereto.
Date Recue/Date Received 2020-11-04
11
Another suitable fungal nuclease is obtainable from Trichoderma, for example
Trichoderma harzianum . A preferred nuclease is obtainable from Trichoderma
harzianum defined
in SEQ ID NO: 17 herein, or variant thereof, for example having at least 60%
or 70% or75% or
80% or 85% or 90% or 95%, 96%, 97%, 98%, 99% or 100% identical thereto.
Other fungal nucleases include those encoded by the DNA sequences of
Aspergillus oryzae
RIB40, Aspergillus oryzae 3.042, Aspergillus flavus NRRL3357, Aspergillus
parasiticus SU-1,
Aspergillus nomius NRRL13137, Trichoderma reesei QM6a, Trichoderma virens Gy29-
8,
Oidiodendron maius Zn, Metarhizium guizhouense ARSEF 977, Metarhizium majus
ARSEF 297,
Metarhizium robertsii ARSEF 23, Metarhizium acridum CQMa 102, Metarhizium
brunneum
ARSEF 3297, Metarhizium anisopliae, Colletotrichum fioriniae PJ7,
Colletotrichum sublineola,
Trichoderma atroviride IMI 206040, Tolypocladium ophioglossoides CBS 100239,
Beauveria
bassiana ARSEF 2860, Colletotrichum higginsianum, Hirsutella minnesotensis
3608,
Scedosporium apiospermum, Phaeomoniella chlamydospora, Fusarium
verticillioides 7600,
Fusarium oxysporum f. sp. cubense race 4, Colletotrichum graminicola M1.001,
Fusarium
oxysporum FOSC 3-a, Fusarium avenaceum, Fusarium langsethiae, Grosmannia
clavigera
kw1407, Claviceps purpurea 20.1, Verticillium longisporum, Fusarium oxysporum
f. sp. cubense
race 1, Magnaporthe oryzae 70-15, Beauveria bassiana D1-5, Fusarium
pseudograminearum
CS3096, Neonectria ditissima, Magnaporthiopsis poae ATCC 64411, Cordyceps
militaris CM01,
Marssonina brunnea f. sp. 'multigermtubi' MB ml, Diaporthe ampelina,
Metarhizium album
ARSEF 1941, Colletotrichum gloeosporioides Nara gc5, Madurella mycetomatis,
Metarhizium
brunneum ARSEF 3297, Verticillium alfalfae VaMs.102, Gaeumannomyces grarninis
var. tritici
R3-111a-1, Nectria haematococca mpVI 77-13-4, Verticillium longisporum,
Verticillium dahliae
VdLs.17, Torrubiella hemipterigena, Verticillium longisporum, Verticillium
dahliae VdLs.17,
Botrytis cinerea B05.10, Chaetomium globosum CBS 148.51, Metarhizium
anisopliae,
Stemphylium lycopersici, Sclerotinia borealis F-4157, Metarhizium robertsii
ARSEF 23,
Myceliophthora thermophila ATCC 42464, Phaeosphaeria nodorum 5N15, Phialophora
attae,
Ustilaginoidea virens, Diplodia seriata, Ophiostoma piceae UAMH 11346,
Pseudogymnoascus
pannorum VKM F-4515 (FW-2607), Bipolaris oryzae ATCC 44560, Metarhizium
guizhouense
ARSEF 977, Chaetomium thermophilum var. thermophilum DSM 1495, Pestalotiopsis
fici W106-
1, Bipolaris zeicola 26-R-13, Setosphaeria turcica Et28A, Arthroderma otae CBS
113480 and
Pyrenophora tritici-repentis Pt-1C-BFP.
Preferably the nuclease is an isolated nuclease.
Date Recue/Date Received 2020-11-04
12
Preferably the nuclease enzyme is present in the aqueous solution in an amount
from
0.01ppm to 1000 ppm of the nuclease enzyme, or from 0.05 or from 0.1ppm to 750
or 500ppm.
Galactanases
Preferably as an additional enzyme, the composition comprises a galactanase.
Particularly
preferred are the endo-beta-1,6-galactanase extracellular polymer-degrading
enzyme. The term
"endo-beta-1,6-galactanase" or "a polypeptide having endo-beta-1,6-galactanase
activity" means
an endo-beta-1,6-galactanase (EC 3.2.1.164) from the glycoside hydrolase
family 30 that catalyzes
the hydrolytic cleavage of 1,6-3-D-galactooligosaccharides with a degree of
polymerization (DP)
higher than 3, and their acidic derivatives with 4-0-methylglucosyluronate or
glucosyluronate
groups at the non-reducing terminals. For purposes of the present disclosure,
endo-beta-1,6-
galactanase activity is determined according to the procedure described in WO
2015185689 in
Assay I. Suitable examples from class EC 3.2.1.164 are described in WO
2015185689, such as
the mature polypeptide SEQ ID NO: 2 described therein.
Preferably the galactanase enzyme is s selected from Glycoside Hydrolase
Family 30.
Preferably, the endo-beta-1,6-galactanase is a microbial enzyme. The endo-beta-
1,6-
galactanase may be fungal or bacterial in origin. Bacterial endo-beta-1,6-
galactanase may be most
preferred. Fungal endo-beta-1,6-galactanase may be most preferred.
A bacterial endo-beta-1,6-galactanase is obtainable from Streptomyces, for
example
Streptomyces davawensis. A preferred endo-beta-1,6-galactanase is obtainable
from Streptomyces
davawensis JCM 4913 defined in SEQ ID NO: 18 herein, or variant thereof, for
example having
at least 40% or 50% or 60% or 70% or 75% or 80% or 85% or 90% or 95%, 96%,
97%, 98%, 99%
or 100% identical thereto.
Other bacterial endo-beta-1,6-galactanase include those encoded by the DNA
sequences of
Streptomyces avermitilis MA-4680 with amino acid sequence defined in SEQ ID
NO: 19 herein,
or variant thereof, for example having at least 40% or 50% or 60% or 70% or
75% or 80% or 85%
or 90% or 95%, 96%, 97%, 98%, 99% or 100% identical thereto.
A fungal endo-beta-1,6-galactanase is obtainable from Trichoderma, for example
Trichoderma harzianum. A preferred endo-beta-1,6-galactanase is obtainable
from Trichoderma
harzianum defined in SEQ ID NO: 20 herein, or variant thereof, for example
having at least 40%
or 50% or 60% or 70% or 75% or 80% or 85% or 90% or 95%, 96%, 97%, 98%, 99% or
100%
identical thereto.
Date Recue/Date Received 2020-11-04
13
Other fungal endo-beta-1,6-galactanase include those encoded by the DNA
sequences of
Ceratocystis fimbriata f. sp. Platani, Muscodor strobelii WG-2009a,
Oculimacula yallundae,
Trichoderma viride GD36A, Thermomyces stellatus, Myceliophthora thermophilia.
Preferably the galactanase has an amino acid sequence having at least 60%, or
at least 80%, or at
least 90% or at least 95% identity with the amino acid sequence shown in SEQ
ID NO: 18, SEQ
ID NO: 19 or SEQ ID NO: 20.
Preferably the galactanase is an isolated galactanase.
Preferably the galactanase enzyme is present in the composition in an amount
from 0.001
to 1 wt% based on active protein in the composition, or from 0.005 to 0.5 wt%
or from 0.01 to
0.25 wt% based on the weight of the composition. Preferably the galactanase
enzyme is present
in the laundering aqueous solution in an amount of from 0.01ppm to 1000 ppm of
the galactanase
enzyme, or from 0.05 or from 0.1ppm to 750 or 500ppm.
Mannanases
Preferably the composition comprises a mannanase. Particularly preferred are
mannanases
having mannan endo-1,4- beta-mannosidase activity (EC 3.2.1 .78) from the
glycoside hydrolase
family 26 that catalyzes the hydrolysis of 1 ,4-3-D-mannosidic linkages in
mannans,
galactomannans and glucomannans. Alternative names of mannan endo-1,4-beta-
mannosidase are
1,4-3 -D-mannan mannanohy drolase; endo- 1,4-3 -mannanase; endo- (3- 1,4-
mannas e; 13-mannanase
B; 3-1,4-mannan 4-mannanohydrolase; endo-3-mannanase; and 13-D-mannanase.
Preferred
mannanases are members of the glycoside hydrolase family 26.
For purposes of the present disclosure, mannanase activity may be detelinined
using the
Reducing End Assay as described in the experimental section of WO 2015040159.
Suitable examples from class EC 3.2.1.78 are described in WO 2015040159, such
as the mature
polypeptide SEQ ID NO: 2 described therein.
Preferred mannanases are variants having at least 60%, at least 65%, at least
70%, at least
75%, at least 80%, at least 81 %, at least 82%, at least 83%, at least 84%, at
least 85%, at least
86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at
least 92%, at least
93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at
least 99% or 100%
sequence identity to the mature polypeptide SEQ ID NO: 21 from Ascobolus
stictoideus;
Preferred mannanases are variants having at least 81 %, at least 82%, at least
83%, at least
84%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at
least 90%, at least 91
%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at
least 97%, at least 98%,
Date Recue/Date Received 2020-11-04
14
at least 99% or 100% sequence identity to the mature polypeptide SEQ ID NO: 22
from
Chaetomium virescens.
Preferred mannanases are variants having at least 75%, at least 76%, at least
77%, at least
78%, at least 79%, at least 80%, at least 81%, at least 82%, at least 83%, at
least 84%, at least 85%,
at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least
91 %, at least 92%, at
least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least
98%, at least 99% or
100% sequence identity to the mature polypeptide SEQ ID NO: 23 from Preussia
aemulans.
Preferred mannanases are variants having at least at least 65%, at least 66%,
at least 67%,
at least 68%, at least 69%, at least 70%, at least 71%, at least 72%, at least
73%, at least 74%, at
least 75%, at least 76%, at least 77%, at least 78%, at least 79%, at least
80%, at least 81%, at least
82%, at least 83%, at least 84%, at least 85%, at least 86%, at least 87%, at
least 88%, at least 89%,
at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at
least 95%, at least 96%, at
least 97%, at least 98%, at least 99% or 100% sequence identity to the mature
polypeptide SEQ
ID NO: 24 from Yunnania penicillata.
Preferred mannanases are variants having at least at least 75%, at least 76%,
at least 77%,
at least 78%, at least 79%, at least 80%, at least 81%, at least 82%, at least
83%, at least 84%, at
least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least
90%, at least 91 %, at
least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least
97%, at least 98%, at least
99% or 100% sequence identity to the mature polypeptide SEQ ID NO: 25 from
Myrothecium
roridum.
Preferably the mannanase is an isolated mannanase.
Preferably the mannanase enzyme is present in the composition in an amount
from 0.001
to 1 wt% based on active protein in the composition, or from 0.005 to 0.5 wt%
or from 0.01 to
0.25 wt% based on the weight of the composition. Preferably the mannanase
enzyme is present in
the laundering aqueous solution in an amount of from 0.01ppm to 1000 ppm of
the mannanase
enzyme, or from 0.05 or from 0.1ppm to 750 or 500ppm.
Xanthan-degrading enzyme
The composition preferably comprises a xanthan-degrading enzyme. Xanthan gum
is a
polysaccharide secreted by the bacterium Xanthomonas campestris. Xanthan is
composed of
pentasaccharide subunits, forming a cellulose backbone with trisaccharide side
chains composed
of mannose-(beta 1, 4)-glucuronic-acid-(beta 1, 2)-mannose attached to
alternate glucose residues
in the backbone by alphal ,3 linkages. The cleaning composition preferably
includes a xanthan
degrading polypetide having xanthan lyase activity and/or endo-beta-1,4-
glucanase activity.
Date Recue/Date Received 2020-11-04
15
Xanthan lyases are enzymes that cleave the beta-D-mannosylalpha-beta-D-1 ,4-
glucuronosyl bond
of xanthan, preferably xanthan lyases isolated from Paenibacillus
alginolyticus XL-1. Preferred
xanthan-degrading enzymes are selected from the glycosyl hydrolase family 5
(GH5).
Acety lglucosaminidases
In a preferred composition, the composition may additionally comprise an
acetylglucosaminidase enzyme, preferably a 13-N-acetylglucosaminidase enzyme
from E.C.
3.2.1.52, preferably an enzyme having at least 70%, or at least 75% or at
least 80% or at least 85%
or at least 90% or at least 95% or at least 96% or at least 97% or at least
98% or at least 99% or at
least or 100% identity to SEQ ID NO:26.
Proteases
Preferably the composition comprises one or more proteases. Suitable proteases
include
metalloproteases and serine proteases, including neutral or alkaline microbial
serine proteases,
such as subtilisins (EC 3.4.21.62). Suitable proteases include those of
animal, vegetable or
microbial origin. In one aspect, such suitable protease may be of microbial
origin. The suitable
proteases include chemically or genetically modified mutants of the
aforementioned suitable
proteases. In one aspect, the suitable protease may be a serine protease, such
as an alkaline
microbial protease or/and a trypsin-type protease. Examples of suitable
neutral or alkaline
proteases include:
(a)
subtilisins (EC 3.4.21.62), preferably those derived from Bacillus sp., such
as B.
lent us, B. alkalophilus, B. subtilis, B. amyloliquefaciens, B. pumilus and B.
gibsonii and B. akibaii
described in W02004067737, W02015091989, W02015091990, W02015024739,
W02015143360, US 6,312,936 B 1, US 5,679,630, US 4,760,025, US7,262,042 and
W009/021867, DE102006022216A1, DE102006022224A1, W02015089447, W02015089441,
W02016066756, W02016066757, W02016069557, W02016069563, W02016069569. .
(b) trypsin-
type or chymotrypsin-type proteases, such as trypsin (e.g., of porcine or
bovine origin), including the Fusarium protease described in WO 89/06270 and
the chymotrypsin
proteases derived from Cellumonas described in WO 05/052161 and WO 05/052146.
(c)
metalloproteases, preferably those derived from Bacillus amyloliquefaciens
described in WO 07/044993A2; from Bacillus, Brevibacillus, Thermoactinomyces,
Geobacillus,
Paenibacillus, Lysinibacillus or Streptomyces spp. Described in W02014194032,
W02014194054 and W02014194117; from Kribella alluminosa described in
W02015193488;
and from Streptomyces and Lysobacter described in W02016075078.
Date Recue/Date Received 2020-11-04
16
(d) Protease having at least 90% identity to the subtilase from Bacillus sp.
TY145, NCIMB
40339, described in W092/17577 (Novozymes A/S), including the variants of this
Bacillus sp
TY145 subtilase described in W02015024739, and W02016066757.
Preferred proteases include those derived from Bacillus gibsonii or Bacillus
Lent us.
Suitable commercially available protease enzymes include those sold under the
trade
names Alcalase0, Savinase0, Primase0, DurazymO, Polarzymet, Kannase0,
Liquanase0,
Liquanase Ultra , Savinase Ultra , Ovozyme0, Neutraset, Everlase and
Esperase0 by
Novozymes A/S (Denmark), those sold under the tradename Maxataset, Maxacal0,
Maxapem0,
Properase0, Purafect , Purafect Prime , Purafect Ox , FN30 , FN40, Excellase
and Purafect
OXPO by Genencor International, those sold under the tradename Opticlean and
Optimase0 by
Solvay Enzymes, those available from Henkel/ Kemira, namely BLAP (sequence
shown in Figure
29 of US 5,352,604 with the following mutations 599D + S101 R + 5103A + V1041
+ G1595,
hereinafter referred to as BLAP), BLAP R (BLAP with 53T + V4I + V199M + V2051
+ L217D),
BLAP X (BLAP with 53T + V4I + V2051) and BLAP F49 (BLAP with 53T + V4I + A194P
+
V199M + V2051 + L217D) - all from Henkel/Kemira; and KAP (Bacillus
alkalophilus subtilisin
with mutations A230V + 5256G + 5259N) from Kao, or as disclosed in
W02009/149144,
W02009/149145, W02010/56653, W02010/56640, W02011/072117, US2011/0237487,
W02011/140316, W02012/151480, EP2510092, EP2566960 OR EP2705145.
Lipases
Preferably the composition comprises one or more lipases, including "first
cycle lipases"
such as those described in U.S. Patent 6,939,702 B1 and US PA 2009/0217464.
Preferred lipases
are first-wash lipases. In one embodiment of the invention the composition
comprises a first wash
lipase. First wash lipases includes a lipase which is a polypeptide having an
amino acid sequence
which: (a) has at least 90% identity with the wild-type lipase derived from
Humicola lanuginosa
strain DSM 4109; (b) compared to said wild-type lipase, comprises a
substitution of an electrically
neutral or negatively charged amino acid at the surface of the three-
dimensional structure within
15A of El or Q249 with a positively charged amino acid; and (c) comprises a
peptide addition at
the C-terminal; and/or (d) comprises a peptide addition at the N-terminal
and/or (e) meets the
following limitations: i) comprises a negative amino acid in position E210 of
said wild-type lipase;
ii) comprises a negatively charged amino acid in the region corresponding to
positions 90-101 of
said wild-type lipase; and iii) comprises a neutral or negative amino acid at
a position
corresponding to N94 or said wild-type lipase and/or has a negative or neutral
net electric charge
in the region corresponding to positions 90-101 of said wild-type lipase.
Preferred are variants of
Date Recue/Date Received 2020-11-04
17
the wild-type lipase from Thermomyces lanuginosus comprising one or more of
the T231R and
N233R mutations. The wild-type sequence is the 269 amino acids (amino acids 23
¨ 291) of the
Swissprot accession number Swiss-Prot 059952 (derived from Thermomyces
lanuginosus
(Humicola lanuginosa)). Preferred lipases would include those sold under the
tradenames Lipex0
and Lipolex0 and Lipocleana Other suitable lipases include those described in
European Patent
Application No. 12001034.3 or EP2623586.
Endoglucanases
Other preferred enzymes include microbial-derived endoglucanases exhibiting
endo-beta-
1,4-glucanase activity (E.C. 3.2.1.4), including a bacterial polypeptide
endogenous to a member
of the genus Bacillus which has a sequence of at least 90%, 94%, 97% and even
99% identity to
the amino acid sequence SEQ ID NO:2 in US7,141,403B2) and mixtures thereof.
Suitable
endoglucanases are sold under the tradenames Celluclean0 and Whitezyme0
(Novozymes A/S,
Bagsvaerd, Denmark).
Pectate Lyases
Other preferred enzymes include pectate lyases sold under the tradenames
PectawashO,
Pectaway0, XpectO and mannanases sold under the tradenames Mannaway0 (all from
Novozymes A/S, Bagsvaerd, Denmark), and Purabrite0 (Genencor International
Inc., Palo Alto,
California).
Surfactant system
The cleaning composition may comprise a surfactant system. The cleaning
composition
may comprise from about 1% to about 80%, or from 1% to about 60%, preferably
from about 5%
to about 50% more preferably from about 8% to about 40%, by weight of the
cleaning composition,
of a surfactant system.
Surfactants suitable for use in the surfactant system may be derived from
natural and/or
renewable sources.
The surfactant system may comprise an anionic surfactant, more preferably an
anionic
surfactant selected from the group consisting of, alkyl benzene sulfonate,
alkyl sulfate, alkyl
alkoxy sulfate. Alkyl ethoxy sulfate, paraffin sulfonate and mixtures thereof
may be preferred
however, alkyl benzene sulfonates are particularly preferred. The surfactant
system may further
comprise a surfactant selected from the group consisting of nonionic
surfactant, cationic surfactant,
amphoteric surfactant, zwitterionic surfactant, and mixtures thereof. The
surfactant system
preferably comprises a nonionic surfactant, for example an ethoxylated
nonionic surfactant. The
surfactant system may comprise an amphoteric surfactant, for example an amine
oxide surfactant,
Date Recue/Date Received 2020-11-04
18
such as an alkyl dimethyl amine oxide. The surfactant system may comprise a
zwitterionic
surfactant, such as a betaine.
The most preferred surfactant system for the detergent composition of the
present invention
comprises from 1% to 40%, preferably 6% to 35%, more preferably 8% to 30%
weight of the total
composition of an anionic surfactant, preferably comprising an alkyl benzene
sulphonate. The
preferred surfactant system may optionally in addition comprise an alkyl
alkoxy sulfate surfactant,
more preferably an alkyl ethoxy sulfate, optionally combined with 0.5% to 15%,
preferably from
1% to 12%, more preferably from 2% to 10% by weight of the composition of
amphoteric and/or
zwitterionic surfactant, more preferably an amphoteric and even more
preferably an amine oxide
surfactant, especially an alkyl dimethyl amine oxide.
Preferably the composition further comprises a nonionic surfactant, especially
an alcohol
alkoxylate in particular an alcohol ethoxylate nonionic surfactant. Most
preferably the surfactant
system comprises an anionic and a nonionic surfactant, preferably the weight
ratio of the anionic
to nonionic surfactant is from 25:1 to 1:2.
Anionic surfactant
Anionic surfactants may be in salt form or acid form, typically in the form of
a water-
soluble sodium, potassium, ammonium, magnesium or mono-, di- or tri- C2-C3
alkanolammonium
salt, with the sodium cation being the usual one chosen.
Sulfonate Surfactant
Suitable anionic sulfonate surfactants for use herein include water-soluble
salts of C8-C18
alkyl or hydroxyalkyl sulfonates; C11-C18 alkyl benzene sulfonates (LAS),
modified
alkylbenzene sulfonate (MLAS) as discussed in WO 99/05243, WO 99/05242, WO
99/05244, WO
99/05082, WO 99/05084, WO 99/05241, WO 99/07656, WO 00/23549, and WO 00/23548;
methyl
ester sulfonate (MES); and alpha-olefin sulfonate (AOS). Those also include
the paraffin
sulfonates which may be monosulfonates and/or disulfonates, obtained by
sulfonating paraffins of
10 to 20 carbon atoms. The sulfonate surfactant may also include the alkyl
glyceryl sulfonate
surfactants.
Sulfated anionic surfactant
Preferably the sulfated anionic surfactant is alkoxylated, more preferably, an
alkoxylated
branched sulfated anionic surfactant having an alkoxylation degree of from
about 0.2 to about 4,
even more preferably from about 0.3 to about 3, even more preferably from
about 0.4 to about 1.5
and especially from about 0.4 to about 1. Preferably, the alkoxy group is
ethoxy. When the
sulfated anionic surfactant is a mixture of sulfated anionic surfactants, the
alkoxylation degree is
Date Recue/Date Received 2020-11-04
19
the weight average alkoxylation degree of all the components of the mixture
(weight average
alkoxylation degree). In the weight average alkoxylation degree calculation
the weight of sulfated
anionic surfactant components not having alkoxylated groups should also be
included.
Weight average alkoxylation degree = (xl * alkoxylation degree of surfactant 1
+ x2 *
alkoxylation degree of surfactant 2 + ....) / (x1 + x2 + ....)
wherein xl, x2, ... are the weights in grams of each sulfated anionic
surfactant of the
mixture and alkoxylation degree is the number of alkoxy groups in each
sulfated anionic surfactant.
Preferably, the branching group is an alkyl. Typically, the alkyl is selected
from methyl,
ethyl, propyl, butyl, pentyl, cyclic alkyl groups and mixtures thereof. Single
or multiple alkyl
branches could be present on the main hydrocarbyl chain of the starting
alcohol(s) used to produce
the sulfated anionic surfactant used in the detergent of the invention. Most
preferably the branched
sulfated anionic surfactant is selected from alkyl sulfates, alkyl ethoxy
sulfates, and mixtures
thereof.
The branched sulfated anionic surfactant can be a single anionic surfactant or
a mixture of
anionic surfactants. In the case of a single surfactant the percentage of
branching refers to the
weight percentage of the hydrocarbyl chains that are branched in the original
alcohol from which
the surfactant is derived.
In the case of a surfactant mixture the percentage of branching is the weight
average and it
is defined according to the following folinula:
Weight average of branching (%)= [(xl * wt% branched alcohol 1 in alcohol 1 +
x2 * wt%
branched alcohol 2 in alcohol 2 + ....) / (x1 + x2 + ....)] * 100
wherein xl, x2, ... are the weight in grams of each alcohol in the total
alcohol mixture of
the alcohols which were used as starting material for the anionic surfactant
for the detergent of the
invention. In the weight average branching degree calculation the weight of
anionic surfactant
components not having branched groups should also be included.
Suitable sulfate surfactants for use herein include water-soluble salts of C8-
C18 alkyl or
hydroxyalkyl, sulfate and/or ether sulfate. Suitable counterions include
alkali metal cation or
ammonium or substituted ammonium, but preferably sodium.
The sulfate surfactants may be selected from C8-C18 primary, branched chain
and random
alkyl sulfates (AS); C8-C18 secondary (2,3) alkyl sulfates; C8-C18 alkyl
alkoxy sulfates (AExS)
wherein preferably x is from 1-30 in which the alkoxy group could be selected
from ethoxy,
propoxy, butoxy or even higher alkoxy groups and mixtures thereof
Date Recue/Date Received 2020-11-04
20
Alkyl sulfates and alkyl alkoxy sulfates are commercially available with a
variety of chain
lengths, ethoxylation and branching degrees. Commercially available sulfates
include, those based
on NeodolTM alcohols ex the Shell company, LialTM ¨ IsalchemTM and SafolTM ex
the Sasol
company, natural alcohols ex The Procter & Gamble Chemicals company.
Preferred alkyl sulfates are those in which the anionic surfactant is an alkyl
ethoxy sulfate
with a degree of ethoxylation of from about 0.2 to about 3, more preferably
from about 0.3 to about
2, even more preferably from about 0.4 to about 1.5, and especially from about
0.4 to about 1.
They are also preferred anionic surfactant having a level of branching of from
about 5% to about
40%, even more preferably from about 10% to 35% and especially from about 20%
to 30%.
Nonionic surfactant
Preferably the surfactant system comprises a nonionic surfactant, in an amount
of from
0.1% to 40%, preferably 0.2% to 20%, most preferably 0.5% to 10% by weight of
the composition.
Suitable nonionic surfactants include the condensation products of aliphatic
alcohols with from 1
to 25 moles of ethylene oxide. The alkyl chain of the aliphatic alcohol can
either be straight or
branched, primary or secondary, and generally contains from 8 to 22 carbon
atoms. Particularly
preferred are the condensation products of alcohols having an alkyl group
containing from 10 to
18 carbon atoms, preferably from 10 to 15 carbon atoms with from 2 to 18
moles, preferably 2 to
15, more preferably 5-12 of ethylene oxide per mole of alcohol. Highly
preferred nonionic
surfactants are the condensation products of guerbet alcohols with from 2 to
18 moles, preferably
2 to 15, more preferably 5-12 of ethylene oxide per mole of alcohol.
Other suitable non-ionic surfactants for use herein include fatty alcohol
polyglycol ethers,
alkylpolyglucosides and fatty acid glucamides.
Amphoteric surfactant
The surfactant system may include amphoteric surfactant, such as amine oxide.
Preferred
amine oxides are alkyl dimethyl amine oxide or alkyl amido propyl dimethyl
amine oxide, more
preferably alkyl dimethyl amine oxide and especially coco dimethyl amino
oxide. Amine oxide
may have a linear or mid-branched alkyl moiety. Typical linear amine oxides
include water-
soluble amine oxides containing one R1 C8-18 alkyl moiety and 2 R2 and R3
moieties selected
from the group consisting of CI-3 alkyl groups and CI-3 hydroxyalkyl groups.
Preferably amine
oxide is characterized by the formula R1 ¨ N(R2)(R3) 0 wherein RI is a C8-18
alkyl and R2 and
R3 are selected from the group consisting of methyl, ethyl, propyl, isopropyl,
2-hydroxethyl, 2-
hydroxypropyl and 3-hydroxypropyl. The linear amine oxide surfactants in
particular may include
linear C10-C18 alkyl dimethyl amine oxides and linear C8-C12 alkoxy ethyl
dihydroxy ethyl
Date Recue/Date Received 2020-11-04
21
amine oxides. Preferred amine oxides include linear C10, linear C10-C12, and
linear C12-C14
alkyl dimethyl amine oxides. As used herein "mid-branched- means that the
amine oxide has one
alkyl moiety having n1 carbon atoms with one alkyl branch on the alkyl moiety
having n2 carbon
atoms. The alkyl branch is located on the a carbon from the nitrogen on t he
alkyl moiety. This
type of branching for the amine oxide is also known in the art as an internal
amine oxide. The
total sum of n1 and n2 is from 10 to 24 carbon atoms, preferably from 12 to
20, and more preferably
from 10 to 16. The number of carbon atoms for the one alkyl moiety (n1) should
be approximately
the same number of carbon atoms as the one alkyl branch (n2) such that the one
alkyl moiety and
the one alkyl branch are symmetric. As used herein "symmetric" means thatInl ¨
n21 is less than
or equal to 5, preferably 4, most preferably from 0 to 4 carbon atoms in at
least 50 wt%, more
preferably at least 75 wt% to 100 wt% of the mid-branched amine oxides for use
herein.
The amine oxide may further comprise two moieties, independently selected from
a C1-3
alkyl, a C1-3 hydroxyalkyl group, or a polyethylene oxide group containing an
average of from
about 1 to about 3 ethylene oxide groups. Preferably the two moieties are
selected from a C1-3
alkyl, more preferably both are selected as a Cl alkyl.
Zwitterionic surfactant
Other suitable surfactants include betaines, such as alkyl betaines,
alkylamidobetaine,
amidazoliniumbetaine, sulfobetaine (INCI Sultaines) as well as the
Phosphobetaine and preferably
meets formula (I):
R1-[CO-X (CH2)dx-N (R2)(R3)-(CH2)m-[CH(OH)-CH21y-Y- (I)
wherein
R1 is a saturated or unsaturated C6-22 alkyl residue, preferably C8-18 alkyl
residue, in
particular a saturated C10-16 alkyl residue, for example a saturated C12-14
alkyl residue;
X is NH, NR4 with C1-4 Alkyl residue R4, 0 or S,
n a number from 1 to 10, preferably 2 to 5, in particular 3,
x 0 or 1, preferably 1,
R2, R3 are independently a C1-4 alkyl residue, potentially hydroxy substituted
such as a
hydroxy ethyl, preferably a methyl.
m a number from 1 to 4, in particular 1, 2 or 3,
y 0 or 1 and
Y is COO, S03, OPO(0R5)0 or P(0)(0R5)0, whereby R5 is a hydrogen atom H or a
C1-4 alkyl residue.
Date Recue/Date Received 2020-11-04
22
Preferred betaines are the alkyl betaines of the formula (Ia), the alkyl amido
propyl betaine
of the formula (Ib), the Sulfo betaines of the formula (Ic) and the Amido
sulfobetaine of the
formula (Id);
le-N (CH3)2-CH2C00- (Ia)
IV-CO-NH(CH2)3-1\1- (CH3)2-CH2C00- (Ib)
1V-1\r(CH3)2-CH2CH(OH)CH2S03- (Ic)
le-CO-NH-(CH2)34\1 (CH3)2-CH2CH(OH)CH2S03- (Id) in which le-1 as the same
meaning as in formula I. Particularly preferred betaines are the Carbobetaine
[wherein r=C00-
1, in particular the Carbobetaine of the formula (Ia) and (Ib), more preferred
are the
Alkylamidobetaine of the formula (Ib).
Examples of suitable betaines and sulfobetaine are the following [designated
in accordance
with INCI]: Almondamidopropyl of betaines, Apricotam idopropyl betaines,
Avocadamidopropyl
of betaines, Babassuamidopropyl of betaines, Behenam idopropyl betaines,
Behenyl of betaines,
betaines, Canolam idopropyl betaines, Capryl/Capram idopropyl betaines,
Carnitine, Cetyl of
betaines, Cocamidoethyl of betaines, Cocam idopropyl betaines, Cocam idopropyl
Hydroxysultaine, Coco betaines, Coco Hydroxysultaine, Coco/Oleam idopropyl
betaines, Coco
Sultaine, Decyl of betaines, Dihydroxyethyl Oleyl Glycinate, Dihydroxyethyl
Soy Glycinate,
Dihydroxyethyl Stearyl Glycinate, Dihydroxyethyl Tallow Glycinate, Dimethicone
Propyl of PG-
betaines, Erucam idopropyl Hydroxysultaine, Hydrogenated Tallow of betaines,
Isostearam
idopropyl betaines, Lauram idopropyl betaines, Lauryl of betaines, Lauryl
Hydroxysultaine,
Lauryl Sultaine, Milkam idopropyl betaines, Minkamidopropyl of betaines,
Myristam idopropyl
betaines, Myristyl of betaines, Oleam idopropyl betaines, Oleam idopropyl
Hydroxysultaine, Oleyl
of betaines, Olivamidopropyl of betaines, Palmam idopropyl betaines, Palm itam
idopropyl
betaines, Palmitoyl Camitine, Palm Kemelam idopropyl betaines,
Polytetrafluoroethylene
Acetoxypropyl of betaines, Ricinoleam idopropyl betaines, Sesam idopropyl
betaines, Soyam
idopropyl betaines, Stearam idopropyl betaines, Stearyl of betaines, Tallowam
idopropyl betaines,
Tallowam idopropyl Hydroxysultaine, Tallow of betaines, Tallow Dihydroxyethyl
of betaines,
Undecylenam idopropyl betaines and Wheat Germam idopropyl betaines. A
preferred betaine is,
for example, Cocoamidopropylbetaine.
Fatty Acid
Especially when in liquid form, preferably, the detergent composition
comprises between
1.5% and 20%, more preferably between 2% and 15%, even more preferably between
3% and
10%, most preferably between 4% and 8% by weight of the liquid detergent
composition of soap,
Date Recue/Date Received 2020-11-04
23
preferably a fatty acid salt, more preferably an amine neutralized fatty acid
salt, wherein preferably
the amine is an alkanolamine more preferably selected from monoethanolamine,
diethanolamine,
triethanolamine or a mixture thereof, more preferably monoethanolamine.
Perfume
Preferred compositions of the invention comprise perfume. Typically the
composition
comprises a perfume that comprises one or more perfume raw materials, selected
from the group
as described in W008/87497. However, any perfume useful in a detergent may be
used. A
preferred method of incorporating perfume into the compositions of the
invention is via an
encapsulated perfume particle comprising either a water-soluble hydroxylic
compound or
melamine-formaldehyde or modified polyvinyl alcohol. In one aspect the
encapsulate comprises
(a) an at least partially water-soluble solid matrix comprising one or more
water-soluble hydroxylic
compounds, preferably starch; and (b) a perfume oil encapsulated by the solid
matrix. In a further
aspect the perfume may be pre-complexed with a polyamine, preferably a
polyethylenimine so as
to form a Schiff base.
Polymers
The detergent composition may comprise one or more polymers for example for
cleaning
and/or care. Examples are optionally modified carboxymethylcellulose, poly
(ethylene glycol),
poly(vinyl alcohol), polycarboxylates such as polyacrylates, maleic/acrylic
acid copolymers and
lauryl methacrylate/acrylic acid co-polymers and carboxylate polymers.
Suitable carboxylate polymers include maleate/acrylate random copolymer or
polyacrylate
homopolymer. The carboxylate polymer may be a polyacrylate homopolymer having
a molecular
weight of from 4,000 Da to 9,000 Da, or from 6,000 Da to 9,000 Da. Other
suitable carboxylate
polymers are co-polymers of maleic acid and acrylic acid, and may have a
molecular weight in the
range of from 4,000 Da to 90,000 Da.
Other suitable carboxylate polymers are co-polymers comprising: (i) from 50 to
less than 98
wt% structural units derived from one or more monomers comprising carboxyl
groups; (ii) from 1
to less than 49 wt% structural units derived from one or more monomers
comprising sulfonate
moieties; and (iii) from 1 to 49 wt% structural units derived from one or more
types of monomers
selected from ether bond-containing monomers represented by formulas (I) and
(II):
Date Recue/Date Received 2020-11-04
24
formula (I):
Ro
H2C=C
0
CH2
CH2
x-
0¨R1
wherein in formula (I), Ro represents a hydrogen atom or CH3 group, R
represents a CH2 group,
CH2CH2 group or single bond, X represents a number 0-5 provided X represents a
number 1-5
when R is a single bond, and Ri is a hydrogen atom or Cl to C20 organic group;
formula (II)
Ro
H2C=C
0
HC¨OH
H2O¨CH2CH2)-0¨R1
in formula (II), Ro represents a hydrogen atom or CH3 group, R represents a
CH2 group, CH2CH2
group or single bond, X represents a number 0-5, and Ri is a hydrogen atom or
Cl to C20 organic
group.
The composition may comprise one or more amphiphilic cleaning polymers such as
the
compound having the following general structure: bis((C2H50)(C21-140)n)(CH3)-
1\1+-CxH2x-1\r-
(CH3)-bis((C2H50)(C21-140)n), wherein n = from 20 to 30, and x = from 3 to 8,
or sulphated or
sulphonated variants thereof. In one aspect, this polymer is sulphated or
sulphonated to provide a
zwitterionic soil suspension polymer.
The composition preferably comprises amphiphilic alkoxylated grease cleaning
polymers
which have balanced hydrophilic and properties such that they remove grease
particles from
.. fabrics and surfaces. Preferred amphiphilic alkoxylated grease cleaning
polymers comprise a core
structure and a plurality of alkoxylate groups attached to that core
structure. These may comprise
alkoxylated polyalkylenimines, preferably having an inner polyethylene oxide
block and an outer
Date Recue/Date Received 2020-11-04
25
polypropylene oxide block. Typically these may be incorporated into the
compositions of the
invention in amounts of from 0.005 to 10 wt%, generally from 0.5 to 8 wt%.
Alkoxylated polycarboxylates such as those prepared from polyacrylates are
useful herein
to provide additional grease removal performance. Such materials are described
in WO 91/08281
and PCT 90/01815. Chemically, these materials comprise polyacrylates having
one ethoxy side-
chain per every 7-8 acrylate units. The side-chains are of the formula -
(CH2CH20). (CH2)nCH3
wherein m is 2-3 and n is 6-12. The side-chains are ester-linked to the
polyacrylate "backbone" to
provide a "comb" polymer type structure. The molecular weight can vary, but is
typically in the
range of about 2000 to about 50,000. Such alkoxylated polycarboxylates can
comprise from about
0.05% to about 10%, by weight, of the compositions herein.
The composition may comprise polyethylene glycol polymers and these may be
particularly
preferred in compositions comprising mixed surfactant systems. Suitable
polyethylene glycol
polymers include random graft co-polymers comprising: (i) hydrophilic backbone
comprising
polyethylene glycol; and (ii) side chain(s) selected from the group consisting
of: C4-C25 alkyl
group, polypropylene, polybutylene, vinyl ester of a saturated C1-C6 mono-
carboxylic acid, Cl-
C 6 alkyl ester of acrylic or methacrylic acid, and mixtures thereof. Suitable
polyethylene glycol
polymers have a polyethylene glycol backbone with random grafted polyvinyl
acetate side chains.
The average molecular weight of the polyethylene glycol backbone can be in the
range of from
2,000 Da to 20,000 Da, or from 4,000 Da to 8,000 Da. The molecular weight
ratio of the
polyethylene glycol backbone to the polyvinyl acetate side chains can be in
the range of from 1:1
to 1:5, or from 1:1.2 to 1:2. The average number of graft sites per ethylene
oxide units can be less
than 1, or less than 0.8, the average number of graft sites per ethylene oxide
units can be in the
range of from 0.5 to 0.9, or the average number of graft sites per ethylene
oxide units can be in the
range of from 0.1 to 0.5, or from 0.2 to 0.4. A suitable polyethylene glycol
polymer is Sokalan
HP22.
Typically these polymers when present are each incorporated into the
compositions of the
invention in amounts from 0.005 to 10 wt%, more usually from 0.05 to 8 wt%.
Preferably the composition comprises one or more carboxylate polymer, such as
a
maleate/acry late random copolymer or polyacrylate homopolymer. In one aspect,
the carboxylate
polymer is a polyacrylate homopolymer having a molecular weight of from 4,000
Da to 9,000 Da,
or from 6,000 Da to 9,000 Da. Typically these are incorporated into the
compositions of the
invention in amounts from 0.005 to 10 wt%, or from 0.05 to 8 wt%.
Preferably the composition comprises one or more soil release polymers.
Date Recue/Date Received 2020-11-04
26
Suitable soil release polymers are polyester soil release polymers such as
Repel-o-texTm
polymers, including Repel-o-texTM SF, SF-2 and SRP6 supplied by Rhodia. Other
suitable soil
release polymers include TexcareTm polymers, including TexcareTm SRA100,
SRA300, SRN100,
SRN170, 5RN240, 5RN260, SRN300 and 5RN325 supplied by Clariant. Other suitable
soil
release polymers are MarloquestTM polymers, such as MarloquestTM SL supplied
by Sasol.
Preferably the composition comprises one or more cellulosic polymer, including
those
selected from alkyl cellulose, alkyl alkoxyalkyl cellulose, carboxyalkyl
cellulose, alkyl
carboxyalkyl cellulose. Preferred cellulosic polymers are selected from the
group comprising
carboxymethyl cellulose, methyl cellulose, methyl hydroxyethyl cellulose,
methyl carboxymethyl
cellulose, and mixtures thereof. In one aspect, the carboxymethyl cellulose
has a degree of
carboxymethyl substitution from 0.5 to 0.9 and a molecular weight from 100,000
Da to 300,000
Da.
The composition preferably comprises a cationically-modified polysaccharide
polymer.
Preferably, the cationic polysaccharide polymer is selected from cationically
modified
hydroxyethyl cellulose, cationically modified hydroxypropyl cellulose,
cationically and
hydrophobically modified hydroxyethyl cellulose, cationically and
hydrophobically modified
hydroxypropyl cellulose, or a mixture thereof, more preferably cationically
modified hydroxyethyl
cellulose, cationically and hydrophobically modified hydroxyethyl cellulose,
or a mixture thereof.
Amines
The cleaning compositions described herein may contain an amine. The cleaning
compositions may include from about 0.1% to about 10%, or from about 0.2% to
about 5%, or
from about 0.5% to about 4%, or from about 0.1% to about 4%, or from about
0.1% to about 2%,
by weight of the composition, of an amine. The amine can be subjected to
protonation depending
on the pH of the cleaning medium in which it is used. Non-limiting examples of
amines include,
but are not limited to, etheramines, cyclic amines, polyamines, oligoamines
(e.g., triamines,
diamines, pentamines, tetraamines), or combinations thereof. The compositions
described herein
may comprise an amine selected from the group consisting of oligoamines,
etheramines, cyclic
amines, and combinations thereof. In some aspects, the amine is not an
alkanolamine. In some
aspects, the amine is not a polyalkyleneimine. Examples of suitable
oligoamines include
tetraethylenepentamine, triethylenetetraamine, diethylenetri amine, and
mixtures thereof.
Etheramines and cyclic amines may be particularly preferred.
Date Recue/Date Received 2020-11-04
27
Fabric Shading Dye
The composition may comprise a fabric shading agent. Suitable fabric shading
agents
include dyes, dye-clay conjugates, and 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. Preferred dyes include alkoxylated azothiophenes, Solvent
Violet 13, Acid
Violet 50 and Direct Violet 9. Particularly preferred dyes are polymeric dyes,
particularly
comprising polyalkoxy, most preferably polyethoxy groups, for example:
H3C (CH2CH20)x-H
H3CCN
N =N
I \ \
NC
(CH2CH20)y-H
S
wherein the index values x and y are independently selected from 1 to 10.
Dye Transfer Inhibitors
Suitable dye transfer inhibitors include polyamine N-oxide polymers,
copolymers of N-
vinylpyrrolidone and N-vinylimidazole, polyvinylpyrrolidone,
polyvinyloxazolidone,
polyvinylimidazole and mixtures thereof. Preferred are poly(vinyl
pyrrolidone),
poly(vinylpyridine betaine), poly(vinylpyridine N-oxide), poly(vinyl
pyrrolidone-vinyl imidazole)
and mixtures thereof. Suitable commercially available dye transfer inhibitors
include PVP-K15
and K30 (Ashland), Sokalan0 HP165, HP50, HP53, HP59, HP56K, HP56, HP66 (BASF),
Chromabond0 S-400, 5403E and S-100 (Ashland).
Chelant
The composition may comprise chelant for example selected from phosphonic,
sulphonic,
succinic and acetic chelants or mixtures thereof. Suitable examples include
HEDP, DTPA, EDTA,
MGDA, GLDA, EDDS and 4,5-dihydroxy-1,3-benzenedisulfonic acids and salts
thereof.
Methods of Making the Composition
The present disclosure relates to methods of making the compositions described
herein.
The compositions of the invention may be solid (for example granules or
tablets) or liquid form.
Date Recue/Date Received 2020-11-04
28
It may be preferred for the compositions to be in liquid form. They may be
made by any process
chosen by the formulator, including by a batch process, a continuous loop
process, or
combinations thereof.
When in the form of a liquid, the compositions of the invention may be aqueous
(typically
above 2 wt% or even above 5 or 10 wt% total water, up to 90 or up to 80wt% or
70 wt% total
water) or non-aqueous (typically below 2 wt% total water content). Typically
the compositions of
the invention will be in the form of an aqueous solution or uniform dispersion
or suspension of
optical brightener, DTI and optional additional adjunct materials, some of
which may normally be
in solid form, that have been combined with the normally liquid components of
the composition,
such as the liquid alcohol ethoxylate nonionic, the aqueous liquid carrier,
and any other normally
liquid optional ingredients. Such a solution, dispersion or suspension will be
acceptably phase
stable. When in the form of a liquid, the detergents of the invention
preferably have viscosity from
1 to 1500 centipoises (1-1500 mPa*s), more preferably from 100 to 1000
centipoises (100-1000
mPa*s), and most preferably from 200 to 500 centipoises (200-500 mPa*s) at 20s-
1 and
21 C. Viscosity can be determined by conventional methods. Viscosity may be
measured using
an AR 550 rheometer from TA instruments using a plate steel spindle at 40 mm
diameter and a
gap size of 500 gm. The high shear viscosity at 20s-1 and low shear viscosity
at 0.05-1 can be
obtained from a logarithmic shear rate sweep from 0.1-1 to 25-1 in 3 minutes
time at 21C. The
preferred rheology described therein may be achieved using internal existing
structuring with
detergent ingredients or by employing an external rheology modifier. More
preferably the
detergents, such as detergent liquid compositions have a high shear rate
viscosity of from about
100 centipoise to 1500 centipoise, more preferably from 100 to 1000 cps. Unit
Dose detergents,
such as detergent liquid compositions have high shear rate viscosity of from
400 to
1000cps. Detergents such as laundry softening compositions typically have high
shear rate
.. viscosity of from 10 to 1000, more preferably from 10 to 800 cps, most
preferably from 10 to 500
cps. Hand dishwashing compositions have high shear rate viscosity of from 300
to 4000 cps, more
preferably 300 to 1000 cps.
The cleaning and/or treatment compositions in the form of a liquid herein can
be prepared
by combining the components thereof in any convenient order and by mixing,
e.g., agitating, the
resulting component combination to form a phase stable liquid detergent
composition. In a process
for preparing such compositions, a liquid matrix is formed containing at least
a major proportion,
or even substantially all, of the liquid components, e.g., nonionic
surfactant, the non-surface active
liquid carriers and other optional liquid components, with the liquid
components being thoroughly
Date Recue/Date Received 2020-11-04
29
admixed by imparting shear agitation to this liquid combination. For example,
rapid stirring with
a mechanical stirrer may usefully be employed. While shear agitation is
maintained, substantially
all of any anionic surfactants and the solid form ingredients can be added.
Agitation of the mixture
is continued, and if necessary, can be increased at this point to form a
solution or a uniform
dispersion of insoluble solid phase particulates within the liquid phase.
After some or all of the
solid-form materials have been added to this agitated mixture, particles of
any enzyme material to
be included, e.g., enzyme granulates, are incorporated. As a variation of the
composition
preparation procedure hereinbefore described, one or more of the solid
components may be added
to the agitated mixture as a solution or slurry of particles premixed with a
minor portion of one or
more of the liquid components. After addition of all of the composition
components, agitation of
the mixture is continued for a period of time sufficient to form compositions
having the requisite
viscosity and phase stability characteristics. Frequently this will involve
agitation for a period of
from about 30 to 60 minutes.
The adjunct ingredients in the compositions of this invention may be
incorporated into the
composition as the product of the synthesis generating such components, either
with or without an
intermediate purification step. Where there is no purification step, commonly
the mixture used
will comprise the desired component or mixtures thereof (and percentages given
herein relate to
the weight percent of the component itself unless otherwise specified) and in
addition unreacted
starting materials and impurities formed from side reactions and/or incomplete
reaction. For
example, for an ethoxylated or substituted component, the mixture will likely
comprise different
degrees of ethoxylation/substitution.
Method of Use
The present disclosure relates to methods of using the cleaning compositions
of the present
disclosure to clean a surface, such as a textile. In general, the method
includes mixing the cleaning
composition as described herein with water to form an aqueous liquor and
contacting a surface,
preferably a textile, with the aqueous liquor in a laundering step. The target
surface may include
a greasy soil or body soil.
The present invention also provides use of a composition comprising an amylase
enzyme
and an enzyme having glycoside hydrolase activity, wherein the enzyme is a
member of a
glycoside hydrolase family GH 39 for enhanced stain removal from a surface,
preferably a fabric
surface, particularly greasy stain or body soil removal and/or for reducing
malodour. Preferably
the glycoside hydrolase enzyme has at least 60% identity or 65% or at least
70% or at least 75%
or at least 80% or at least 85% or at least 90% or at least 95% identity and
up to less than or 100%
Date Recue/Date Received 2020-11-04
30
identity to SEQ ID NO:l. Typically contact of the glycoside hydrolase enzyme
with the surface
will be in a laundering process in which the glycoside hydrolase enzyme or
composition
comprising the glycoside hydrolase enzyme is mixed with water to provide an
aqueous (wash)
liquor which is contacted with the surface.
The compositions of this invention, typically prepared as hereinbefore
described, can be
used to form aqueous (washing/treatment) liquor for use in the
laundering/treatment of fabrics
and/or hard surfaces. Generally, an effective amount of such a composition is
added to water, for
example in a conventional fabric automatic washing machine, to form such
aqueous laundering
solutions. The aqueous liquor so formed is then contacted, typically under
agitation, with the
fabrics to be laundered/treated therewith. An effective amount of the cleaning
composition herein
added to water to form aqueous liquor laundering solutions can comprise
amounts sufficient to
form from about 500 to 25,000 ppm, or from 500 to 15,000 ppm of composition in
aqueous liquor,
or from about 1,000 to 5,000 ppm or 3000ppm of the cleaning compositions
herein will be provided
in aqueous liquor.
Typically, the aqueous liquor is formed by contacting the detergent with wash
water in
such an amount so that the concentration of the detergent in the aqueous
liquor is from above 0.1g/1
to 5g/1, or from 1g/1, and to 4.5g/1, or to 4.0g/1, or to 3.5g/1, or to
3.0g/1, or to 2.5g/1, or even to
2.0g/1, or even to 1.5g/1. The method of laundering fabric or textile may be
carried out in a top-
loading or front-loading automatic washing machine, or can be used in a hand-
wash laundry
application. In these applications, the aqueous liquor formed and
concentration of laundry
detergent composition in the aqueous liquor is that of the main wash cycle.
Any input of water
during any optional rinsing step(s) is not included when determining the
volume of the aqueous
liquor.
The aqueous liquor may comprise 40 litres or less of water, or 30 litres or
less, or 20 litres
or less, or 10 litres or less, or 8 litres or less, or even 6 litres or less
of water. The aqueous liquor
may comprise from above 0 to 15 litres, or from 2 litres, and to 12 litres, or
even to 8 litres of
water. Typically from 0.0 lkg to 2kg of fabric per litre of aqueous liquor is
dosed into said liquor.
Typically from 0.0 lkg, or from 0.05kg, or from 0.07kg, or from 0.10kg, or
from 0.15kg, or from
0.20kg, or from 0.25kg fabric per litre of aqueous liquor is dosed into said
wash liquor. Optionally,
50g or less, or 45g or less, or 40g or less, or 35g or less, or 30g or less,
or 25g or less, or 20g or
less, or even 15g or less, or even lOg or less of the composition is contacted
to water to form the
aqueous liquor. Such compositions are typically employed at concentrations of
from about 500
ppm to about 15,000 ppm in solution. The water temperature typically ranges
from about 5 C to
Date Recue/Date Received 2020-11-04
31
about 90 C, for example from 20 C to 60 C, preferably up to 40 C or 30 C
and, when laundering
a fabric, the water to fabric ratio is typically from about 1:1 to about 30:1.
Typically the wash
liquor comprising the cleaning composition of the invention has a pH of from 3
to 11.5, typically
from 7 to 11, more usually 8 to 10.5.
In one aspect, such method comprises the steps of optionally washing and/or
rinsing said
surface or fabric, contacting said surface or fabric with any composition
disclosed in this
specification then optionally washing and/or rinsing said surface or fabric
with an optional drying
step.
Drying of such surfaces or fabrics may be accomplished by any one of the
common means
employed either in domestic or industrial settings: machine drying or open-air
drying. The fabric
may comprise any fabric capable of being laundered in normal consumer or
institutional use
conditions, and the invention is particularly suitable for synthetic textiles
such as polyester and
nylon and especially for treatment of mixed fabrics and/or fibres comprising
synthetic and
cellulosic fabrics and/or fibres. As examples of synthetic fabrics are
polyester, nylon, these may
be present in mixtures with cellulosic fibres, for example, polycotton
fabrics.
EXAMPLES
The following are illustrative examples of cleaning compositions according to
the present
disclosure and are not intended to be limiting.
Examples 1 to 18: Unit Dose Compositions.
These examples provide various formulations for unit dose laundry detergents
and
comprise double compai __ anent unit dose products comprising one powder and
one liquid
compai __ anent. The film used to encapsulate the compositions in PVA. Each
example is prepared
by combining a liquid compartment composition selected from compositions A-E
with a powder
__ compai anent composition selected from compositions F-K.
Example 1 2 3 4 5 6
Liquid 20g A 25g A 20g A 15g A 20g B 20g B
composition
Solid 15g F 12g G 12g H 12g1 15g J 15g K
composition
Date Recue/Date Received 2020-11-04
32
Example 7 8 9 10 11 12
Liquid 15g B 17g B 20g C 19g C 15g C 25g C
composition
Solid 15g L 14g F 15g G 18g H 15g1 12g J
composition
Example 13 14 15 16 17 18
Liquid 20g D 18g D 22g D 32g E 32g E 27g E
composition
Solid 20g K 13g L 15g F 17g G 12g H 18g1
composition
A B C D E
Ingredients
% weight of compai anent
LAS 19.09 16.76 8.59 6.56 3.44
AE3S 1.91 0.74 0.18 0.46 0.07
AE7 14.00 17.50 26.33 28.08 31.59
Citric Acid 0.6 0.6 0.6 0.6 0.6
C12-15 Fatty Acid 14.8 14.8 14.8 14.8 14.8
Polymer 3 4.0 4.0 4.0 4.0 4.0
Chelant 2 1.2 1.2 1.2 1.2 1.2
Optical Brightener 1 0.20 0.25 0.01 0.01 0.50
Optical Brightener 2 0.20 - 0.25 0.03 0.01
Optical Brightener 3 0.18 0.09 0.30 0.01 -
DTI 1 0.10 - 0.20 0.01 0.05
DTI 2 - 0.10 0.20 0.25 0.05
Glycerol 6.1 6.1 6.1 6.1 6.1
Monoethanol amine 8.0 8.0 8.0 8.0 8.0
Tri-isopropanol amine - - 2.0 - -
Tri-ethanol amine - 2.0 - - -
Cumene sulfonate - - - - 2.0
Protease 0.80 0.60 0.07 1.00 1.50
Date Recue/Date Received 2020-11-04
33
Mannanase 0.07 0.05 0.05 0.10 0.01
Amylase 1 0.20 0.11 0.30 0.50 0.05
Amylase 2 0.11 0.20 0.10 - 0.50
Hydrolase of SEQ ID
0.005 0.05 0.005 0.010 0.01
NO:1(active protein)
Polishing enzyme 0.005 0.05 - - -
Nuclease 0.005 - - - 0.005
Dispersin B 0.010 0.05 0.005 0.005 -
Cyclohexyl dimethanol - - - 2.0 -
Acid violet 50 0.03 0.02
Violet DD 0.01 0.05 0.02
Structurant 0.14 0.14 0.14 0.14 0.14
Perfume 1.9 1.9 1.9 1.9 1.9
Water, solvents and
To 100%
miscellaneous
pH 7.5-8.2
F G H I J K
Ingredient
% weight
Sodium carbonate 20.0 35.0 30.0 29.0 28.0
18.0
Carboxymethyl cellulose 2.0 1.0 - - 2.5 0.6
Sodium silicate 2R 5.0 - 5.0 3.2 20.0 -
Tetraacetyl ethylenediamine 20.0 15.0 18.0 15.0 - 25.0
Sodium percarbonate 50.0 44.0 45.0 45.0 29.0
50.0
Polyetheramine 0.5 2 0.5 1 0.5 4
Sulfate/ Water & Balance
Miscellaneous
Based on total cleaning and/or treatment composition/compartment weight.
Enzyme
levels are reported as raw material.
Date Recue/Date Received 2020-11-04
34
Examples 19 to 24
Granular laundry detergent compositions for hand washing or washing machines,
typically top-loading washing machines.
19 20 21 22 23 24
Ingredient
% weight
LAS 11.33 10.81 7.04 4.20 3.92
2.29
Quaternary ammonium 0.70 0.20 1.00 0.60 - -
AE3S 0.51 0.49 0.32 - 0.08 0.10
AE7 8.36 11.50 12.54 11.20 16.00
21.51
Sodium Tripolyphosphate 5.0 - 4.0 9.0 2.0 -
Zeolite A - 1.0 - 1.0 4.0 1.0
Sodium silicate 1.6R 7.0 5.0 2.0 3.0 3.0 5.0
Sodium carbonate 20.0 17.0 23.0 14.0 14.0 16.0
Polyacrylate MW 4500 1.0 0.6 1.0 1.0 1.5 1.0
Polymer 6 0.1 0.2 - - 0.1 -
Carboxymethyl cellulose 1.0 0.3 1.0 1.0 1.0 1.0
Acid Violet 50 0.05 - 0.02 - 0.04 -
Violet DD - 0.03 - 0.03 - 0.03
Protease 2 0.10 0.10 0.10 0.10 - 0.10
Amylase 0.03 0.007 0.03 0.03 0.03 0.03
Lipase 0.03 0.07 0.30 0.10 0.07 0.40
Polishing enzyme 0.002 - 0.05 - 0.02 -
Hydrolase of SEQ ID
0.001 0.001 0.01 0.05 0.002 0.02
NO:1(active protein)
Nuclease (as active protein) 0.001 - - - 0.001 -
Dispersin B 0.001 0.001 0.05 - 0.001 -
Optical Brightener 1 0.200 0.001 0.300 0.650 0.050
0.001
Optical Brightener 2 0.060 - 0.650 0.180 0.200
0.060
Optical Brightener 3 0.100 0.060 0.050 - 0.030
0.300
Chelant 1 0.60 0.80 0.60 0.25 0.60 0.60
Date Recue/Date Received 2020-11-04
35
DTI 1 0.32 0.15 0.15 - 0.10 0.10
DTI 2 0.32 0.15 0.30 0.30 0.10 0.20
Sodium Percarbonate 4.6 5.2 5.0 5.7 4.5 7.3
Nonanoyloxybenzensulfonate 1.9 0.0 1.66 0.0 0.33 0.75
Tetraacetylethylenediamine 0.58 1.2 0.51 0.0 0.015 0.28
Photobleach 0.0030 0.0 0.0012
0.0030 0.0021 -
S-ACMC 0.1 0.0 0.0 0.0 0.06 0.0
Polyetheramine 0.5 2 0.5 1 0.5 4
Sulfate/Moisture Balance
Examples 25-30
Granular laundry detergent compositions typically for front-loading automatic
washing
machines.
25 26 27 28 29 30
Ingredient
% weight
LAS 6.08 5.05 4.27 3.24 2.30 1.09
AE3S - 0.90 0.21 0.18 - 0.06
AS 0.34 - - - - -
AE7 4.28 5.95 6.72 7.98 9.20 10.35
Quaternary ammonium 0.5 - - 0.3 - -
Crystalline layered silicate 4.1 - 4.8 - - -
Zeolite A 5.0 - 2.0 - 2.0 2.0
Citric acid 3.0 4.0 3.0 4.0 2.5 3.0
Sodium carbonate 11.0 17.0 12.0 15.0 18.0 18.0
Sodium silicate 2R 0.08 - 0.11 - - -
Optical Brightener 1 - 0.25 0.05 0.01 0.10 0.02
Optical Brightener 2 - - 0.25 0.20 0.01 0.08
Optical Brightener 3 - 0.06 0.04 0.15 - 0.05
DTI 1 0.08 - 0.04 - 0.10 0.01
DTI 2 0.08 - 0.04 0.10 0.10 0.02
Soil release agent 0.75 0.72 0.71 0.72 - -
Date Recue/Date Received 2020-11-04
36
Acrylic /maleic acid copolymer 1.1 3.7 1.0 3.7 2.6 3.8
Carboxymethyl cellulose 0.2 1.4 0.2 1.4 1.0 0.5
Protease 3 0.20 0.20 0.30 0.15 0.12 0.13
Amylase 3 0.20 0.15 0.20 0.30 0.15 0.15
Lipase 0.05 0.15 0.10 - - -
Amylase 2 0.03 0.07 - - 0.05 0.05
Cellulase 2 - - - - 0.10 0.10
Polishing enzyme 0.003 0.005 0.020 - - -
Hydrolase of SEQ ID
0.002 0.010 0.020 0.020 0.020 0.003
NO:1(active protein)
Nuclease - - - 0.005 0.005
Dispersin B 0.002 - 0.020 0.020 - -
Tetraacetylehtylenediamine 3.6 4.0 3.6 4.0 2.2 1.4
Sodium percabonate 110 112 110 112 16M 14M
Chelant 3 - 0.2 - 0.2 - 0.2
Chelant 2 0.2 - 0.2 - 0.2 0.2
MgSO4 - 0.42 - 0.42 - 0.4
Perfume 0.5 0.6 0.5 0.6 0.6 0.6
Suds suppressor agglomerate 0.05 0.10 0.05 0.10 0.06 0.05
Soap 0.45 0.45 0.45 0.45 - -
Acid Violet 50 0.04 - 0.05 - 0.04 -
Violet DD - 0.04 - 0.05 - 0.04
S-ACMC 0.01 0.01 - 0.01 - -
Direct Violet 9 (active) - - 0.0001 0.0001 - -
Polyetheramine 0.5 2 0.5 1 0.5 4
Sulfate/ Water & Balance
Miscellaneous
Date Recue/Date Received 2020-11-04
37
Examples 31-37: Heavy Duty Liquid laundry detergent compositions.
31 32 33 34 35 36 37
Ingredients
% weight
AE1.8S 6.77 5.16 1.36 1.30 - - -
AE3S - - - - 0.45 - -
LAS 0.86 2.06 2.72 0.68 0.95 1.56
3.55
HSAS 1.85 2.63 1.02 - - - -
AE9 6.32 9.85 10.20 7.92
AE8 35.45
AE7 8.40 12.44
C12-14 dimethyl Amine Oxide 0.30 0.73 0.23 0.37 - - -
C12-18 Fatty Acid 0.80 1.90 0.60 0.99 1.20 -
15.00
Citric Acid 2.50 3.96 1.88 1.98 0.90 2.50
0.60
Optical Brightener 1 LOO 0.80 0.10 0.30 0.05 0.50
0.001
Optical Brightener 3 0.001 0.05 0.01 0.20 0.50 -
1.00
Sodium formate 1.60 0.09 1.20 0.04 1.60 1.20
0.20
DTI 1 0.32 0.05 - 0.60 0.10 0.60
0.01
DTI 2 0.32 0.10 0.60 0.60 0.05 0.40
0.20
Sodium hydroxide 2.30 3.80 1.70 1.90 1.70 2.50
2.30
Monoethanolamine 1.40 1.49 1.00 0.70 - - -
Diethylene glycol 5.50 - 4.10 - - - -
Chelant 1 0.15 0.15 0.11 0.07 0.50 0.11
0.80
4-formyl-phenylboronic acid - - - - 0.05 0.02 0.01
Sodium tetraborate 1.43 1.50 1.10 0.75 - 1.07 -
Ethanol 1.54 1.77 1.15 0.89 - 3.00
7.00
Polymer 1 0.10 - - - - - 2.00
Polymer 2 0.30 0.33 0.23 0.17 - - -
Polymer 3 - - - - - - 0.80
Polymer 4 0.80 0.81 0.60 0.40 1.00 1.00
-
1,2-Propanediol - 6.60 - 3.30 0.50 2.00 8.00
Structurant 0.10 - - - - - 0.10
Perfume 1.60 1.10 1.00 0.80 0.90 1.50
1.60
Date Recue/Date Received 2020-11-04
38
Perfume encapsulate 0.10 0.05 0.01 0.02 0.10
0.05 0.10
Protease
0.80 0.60 0.70 0.90 0.70 0.60 1.50
Hydrolase of SEQ ID NO:1
0.07 0.05 0.045 0.06 0.04 0.045 0.10
(active protein)
Amylase 1 0.30 - 0.30 0.10 - 0.40
0.10
Amylase 2 - 0.20 0.10 0.15 0.07 -
0.10
Xyloglucanase 0.20 0.10 - -
0.05 0.05 0.20
Lipase 0.40 0.20 0.30
0.10 0.20
Polishing enzyme - 0.04 - - - 0.004
-
Nuclease
0.05 0.03 0.01 0.03 0.03 0.003 0.003
Dispersin B - - - 0.05 0.03 0.001
0.001
Acid Violet 50 0.05 - - - - -
0.005
Direct Violet 9 - - - - - 0.05 -
Violet DD - 0.035 0.02 0.037 0.04 -
-
Water insoluble plant fiber 0.2 - - - 1.2 - -
Dye control agent - 0.3 - 0.5 - 0.3 -
Alkoxylated poly aryl/
polyalkyl phenol
Water, dyes & minors Balance
pH 8.2
Based on total cleaning and/or treatment composition weight. Unless indicated
otherwise,
enzyme levels are reported as raw material.
AE1.85 is C12-15 alkyl ethoxy sulfate with an average degree
of ethoxylation of 1.8
AE3S is C12-15 alkyl ethoxy sulfate with an av degree of ethoxylation of 3
AE7 is C12-13 alcohol ethoxylate, with an average degree
of ethoxylation
of 7
AE8 is C12_13 alcohol ethoxylate, with an average degree
of ethoxylation
of 8
AE9 is C12-13 alcohol ethoxylate, with an average degree of ethoxylation
of 9
Date Recue/Date Received 2020-11-04
39
Alkoxylated polyaryl is alkoxylated polyaryl/polyalkyl phenol for example
Emulsogen0
TS160, Hostapale
/ polyalkyl phenol BY conc., SapogenatO T110 or SapogenatO T139, all
from Clariant
Amylase 1 is Stainzyme0, 15 mg active/g
Amylase 2 is Natalase , 29 mg active/g
Amylase 3 is Stainzyme0 Plus, 20 mg active/g,
AS is C12-14 alkylsulfate
Cellulase 2 is CellucleanTm , 15.6 mg active/g
Xyloglucanase is Whitezymet, 20mg active/g
Chelant 1 is diethylene triamine pentaacetic acid
Chelant 2 is 1-hydroxyethane 1,1-diphosphonic acid
Chelant 3 is sodium salt of ethylenediamine-N,N'-disuccinic
acid, (S,S) isomer
(EDDS)
Dispersin B is a glycoside hydrolase, reported as 1000mg active/g
DTI 1 is poly(4-vinylpyridine-l-oxide) (such as Chromabond
S-403E0),
DTI 2 is poly(1-vinylpyrrolidone-co-l-vinylimidazole) (such
as Sokalan
HP560 ).
Dye Control Agent is for example Suparexe 0.IN (M1), Nylofixang P (M2),
Nylofixang PM (M3),
or Nylofixang HF (M4)
HSAS is mid-branched alkyl sulfate as disclosed in US
6,020,303 and
U56,060,443
LAS is linear alkylbenzenesulfonate having an average
aliphatic carbon
chain length C9-C15 (HLAS is acid form).
Lipase is Lipex0, 18 mg active/g
Mannanase is Mannawaye, 25 mg active/g
Nuclease is a Phosphodiesterase according to any of SEQ ID
NOs: 2 to 6,
preferably SEQ ID NO: 2, 3 and/or 4, reported as active protein
Optical Brightener 1 is disodium 4,4'-bis {{4-anilino-6-morpholino-s-
triazin-2-y11-aminol -
2,T-stilbenedisulfonate
Optical Brightener 2 is disodium 4,4'-bis-(2-sulfostyryl)biphenyl (sodium
salt)
Optical Brightener 3 is Optiblanc SPL100 from 3V Sigma
Perfume encapsulate is a core¨shell melamine formaldehyde perfume
microcapsules
Date Recue/Date Received 2020-11-04
40
Photobleach is a sulfonated zinc phthalocyanine
Polishing enzyme is Para-nitrobenzyl esterase, reported as 1000mg
active/g
Polyetheramine as described in present disclosure.
Polymer 1 is bis((C2H50)(C21-140)n)(CH3)-1\1+-CxH2x-N -(CH3)-
bis((C2H50)(C21-140)n), wherein n = 20-30,x = 3 to 8 or sulphated or
sulfonated variants thereof
Polymer 2 is ethoxylated (E015) tetraethylene pentamine
Polymer 3 is ethoxylated polyethylenimine
Polymer 4 is ethoxylated hexamethylene diamine
Polymer 5 is Acusol 305, provided by Rohm&Haas
Polymer 6 is a polyethylene glycol polymer grafted with vinyl
acetate side
chains, provided by BASF.
Protease is Purafect Prime , 40.6 mg active/g
Protease 2 is Savinase , 32.89 mg active/g
Protease 3 is PurafectO, 84 mg active/g
Quaternary ammonium is C12-14 Dimethylhydroxyethyl ammonium chloride
S-ACMC is Reactive Blue 19 Azo-CM-Cellulose provided by
Megazyme
Soil release agent is Repel-o-tex0 SF2, supplied by Solvay
Structurant is Hydrogenated Castor Oil
Violet DD is a thiophene azo polymeric hueing dye provided by Milliken
The dimensions and values disclosed herein are not to be understood as being
strictly
limited to the exact numerical values recited. Instead, unless otherwise
specified, each such
dimension is intended to mean both the recited value and a functionally
equivalent range
surrounding that value. For example, a dimension disclosed as "40 mm" is
intended to mean
"about 40 mm."
Date Recue/Date Received 2020-11-04
