U.S. patent application number 12/549525 was filed with the patent office on 2009-12-31 for cleaning and/or treatment compositions.
Invention is credited to Andre Cesar Baeck, Eva Maria Perez-Prat Vinuesa, Philip Frank Souter, Colin Ure.
Application Number | 20090325852 12/549525 |
Document ID | / |
Family ID | 38832195 |
Filed Date | 2009-12-31 |
United States Patent
Application |
20090325852 |
Kind Code |
A1 |
Perez-Prat Vinuesa; Eva Maria ;
et al. |
December 31, 2009 |
CLEANING AND/OR TREATMENT COMPOSITIONS
Abstract
This invention relates to compositions comprising certain
amylase variants and processes for making and using such
compositions including the use of such compositions to clean and/or
treat a situs.
Inventors: |
Perez-Prat Vinuesa; Eva Maria;
(Newcastle, GB) ; Ure; Colin; (Newcastle, GB)
; Baeck; Andre Cesar; (Bonheiden, BE) ; Souter;
Philip Frank; (Morpeth, GB) |
Correspondence
Address: |
THE PROCTER & GAMBLE COMPANY;Global Legal Department - IP
Sycamore Building - 4th Floor, 299 East Sixth Street
CINCINNATI
OH
45202
US
|
Family ID: |
38832195 |
Appl. No.: |
12/549525 |
Filed: |
August 28, 2009 |
Related U.S. Patent Documents
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Application
Number |
Filing Date |
Patent Number |
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11811129 |
Jun 8, 2007 |
|
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12549525 |
|
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60814442 |
Jun 16, 2006 |
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Current U.S.
Class: |
510/392 ;
435/7.94 |
Current CPC
Class: |
C11D 3/1253 20130101;
C11D 3/386 20130101; C11D 3/42 20130101; C12N 9/2417 20130101 |
Class at
Publication: |
510/392 ;
435/7.94 |
International
Class: |
C11D 3/386 20060101
C11D003/386; G01N 33/573 20060101 G01N033/573 |
Claims
1. A composition comprising an amylase having Seq. I.D. 1 and based
on total product weight, less than 15% builder.
2. The composition of claim 1, said composition comprising a
material selected from the group consisting of surfactants,
chelating agents, dye transfer inhibiting agents, dispersants,
additional enzymes, and enzyme stabilizers, catalytic materials,
bleaching agents, polymeric dispersing agents, clay soil
removal/anti-redeposition agents, brighteners, suds suppressors,
dyes, perfumes, structure elasticizing agents, fabric softeners,
carriers, hydrotropes, processing aids, solvents, pigments, hueing
agents, photobleaches, structurants, and mixtures thereof.
3. The composition of claim 2, said composition comprising an
additional enzyme.
4. The composition of claim 3, wherein said additional enzyme is
selected from the group consisting of hemicellulases, peroxidases,
proteases, cellulases, xylanases, lipases, phospholipases,
esterases, cutinases, pectinases, mannanases, pectate lyases,
keratinases, reductases, oxidases, phenoloxidases, lipoxygenases,
ligninases, pullulanases, tannases, pentosanases, glucanases,
arabinosidases, hyaluronidase, chondroitinase, laccase, amylases,
and mixtures thereof.
5. The composition of claim 4, wherein said additional enzyme is
selected from the group consisting of: a.) lipases; b.)
alpha-amylases; c.) serine proteases; d.) microbial-derived
endoglucanases; and e.) mixtures thereof.
6. The composition of claim 2, said composition comprising a
surfactant, selected from the group of: a.) anionic surfactants
selected from the group consisting of linear alkylbenzene-sulfonate
(LAS), alcohol ethoxysulfate (AES), mid-branched alkyl sulfates
(HSAS) and mixtures thereof; b.) non ionic alcohol ethoxylates,
said alcohol ethoxylates; c.) amine oxides; and d.) mixtures
thereof.
7. The composition of claim 2, said composition comprising a
polymer, selected from the group consisting of a.) polyacrylates;
b.) maleic/acrylic acid copolymers; c.) cellulose-derived polymers;
d.) polyethyleneimine polymer; and e.) mixtures thereof.
8. The composition of claim 2, said composition comprising a
material selected from the group consisting of a photobleach, a
fabric hueing agent and mixtures thereof, said photobleach being
selected from the group consisting of a.) xanthene dyes; b.)
sulfonated zinc phthalocyanine, sulfonated aluminum phthalocyanine,
Eosin Y, Phoxine B, Rose Bengal, C.I. Food Red 14 and mixtures
thereof; c.) water soluble phthalocyanine; and d.) mixtures thereof
and said fabric hueing agent being selected from the group
consisting of a.) dyes; b.) dye-clay conjugates comprising at least
one cationic/basic dye and a smectite clay; and c.) mixtures
thereof.
9. The composition of claim 8, said composition comprising, based
on total product weight, from about 0% to about 3% photobleach
and/or from about 0.00003% to about 0.3% hueing agent.
10. A composition comprising an amylase enzyme having E.C. 3.2.1.1,
and a material selected from the group consisting of surfactants,
chelating agents, dye transfer inhibiting agents, dispersants,
additional enzymes, and enzyme stabilizers, catalytic materials,
bleaching agents, polymeric dispersing agents, clay soil
removal/anti-redeposition agents, brighteners, suds suppressors,
dyes, perfumes, structure elasticizing agents, fabric softeners,
carriers, hydrotropes, processing aids, solvents, pigments, hueing
agents, photobleaches, structurants, and mixtures thereof, said
composition having an enzyme deposition index of at least 2.5.
11. The composition of claim 10, said composition comprising an
additional enzyme.
12. The composition of claim 11, wherein said additional enzyme is
selected from the group consisting of hemicellulases, peroxidases,
proteases, cellulases, xylanases, lipases, phospholipases,
esterases, cutinases, pectinases, mannanases, pectate lyases,
keratinases, reductases, oxidases, phenoloxidases, lipoxygenases,
ligninases, pullulanases, tannases, pentosanases, glucanases,
arabinosidases, hyaluronidase, chondroitinase, laccase, amylases,
or mixtures thereof.
13. The composition of claim 12, wherein said additional enzyme is
selected from the group consisting of: a.) lipases; b.)
alpha-amylases; c.) serine proteases; d.) microbial-derived
endoglucanases; and e.) mixtures thereof.
14. The composition of claim 10, said composition comprising a
surfactant, selected from the group of: a.) anionic surfactants
selected from the group consisting of linear alkylbenzene-sulfonate
(LAS), alcohol ethoxysulfate (AES), mid-branched alkyl sulfates
(HSAS) and mixtures thereof; b.) non ionic alcohol ethoxylates; c.)
amine oxides; and d.) mixtures thereof.
15. The composition of claim 10, said composition comprising a
polymer selected from the group consisting of: a.) polyacrylates;
b.) maleic/acrylic acid copolymers; c.) cellulose-derived polymers;
d.) polyethyleneimine polymer; and e.) mixtures thereof.
16. The composition of claim 10, said composition comprising a
builder selected from the group consisting of a.) citric acid; b.)
C.sub.12-C.sub.18 fatty acid; c.) aluminosilicates; d.) sodium
tripolyphosphate; and e.) mixtures thereof.
17. The composition of claim 16, said composition comprising, based
on total product weight, less than 15% builder.
18. The composition of claim 10, said composition comprising a
material selected from the group consisting of a photobleach, a
hueing agent and mixtures thereof, said photobleach being selected
from the group consisting of a.) xanthene dyes; b.) sulfonated zinc
phthalocyanine, sulfonated aluminum phthalocyanine, Eosin Y,
Phoxine B, Rose Bengal, C.I. Food Red 14 and mixtures thereof; c.)
water soluble phthalocyanine; and d.) mixtures thereof and said
fabric hueing agent being selected from the group consisting of a.)
dyes; b.) dye-clay conjugates comprising at least one
cationic/basic dye and a smectite clay; and c.) mixtures
thereof.
19. The composition of claim 18, said composition comprising, based
on total product weight, from about 0% to about 3% photobleach
and/or from about 0.00003% to about 0.3% hueing agent.
20. A composition comprising an amylase having Seq. I.D. 1 and a
sufficient amount of calcium to provide a wash liquor comprising
said composition with a free calcium concentration of from about
0.1 ppm to about 500 ppm.
21. A method of determining the deposition index of an enzyme, said
method comprising determining the enzyme deposition index of an
enzyme according to Test Method 2.
Description
CROSS-REFERENCES TO RELATED APPLICATIONS
[0001] This application claims priority under 35 U.S.C. .sctn. 120
to U.S. application Ser. No. 11/811,129 filed Jun. 8, 2007, which
in turn claims priority under 35 U.S.C. .sctn. 119(e) to U.S.
Provisional Application Ser. No. 60/814,442 filed Jun. 16,
2006.
FIELD OF INVENTION
[0002] Compositions comprising enzymes and processes for making and
using such compositions.
BACKGROUND OF THE INVENTION
[0003] The appearance of enzymes suitable for cleaning and/or
treatment applications gave the formulator a new approach to clean
and/or treat hard surfaces and fabrics. Unfortunately, even when
enzymes are employed, performance issues remain. For example, in
certain matrices and/or use conditions, enzymes do not deposit as
efficiently as required to provide the desired performance. Thus,
the use of this technology continues to be limited.
[0004] Surprisingly, when cleaning compositions that comprise
certain .alpha.-amylases are formulated in accordance with the
teachings of the present invention, such compositions can provide
improved cleaning.
SUMMARY OF THE INVENTION
[0005] This invention relates to compositions comprising certain
.alpha.-amylase enzymes and processes for making and using such
products.
DETAILED DESCRIPTION OF THE INVENTION
Definitions
[0006] As used herein, the term "cleaning composition" includes,
unless otherwise indicated, granular or powder-form all-purpose or
"heavy-duty" washing agents, especially laundry detergents; liquid,
gel or paste-form all-purpose washing agents, especially the
so-called heavy-duty liquid types; liquid fine-fabric detergents;
hand dishwashing agents or light duty dishwashing agents,
especially those of the high-foaming type; machine dishwashing
agents, including the various tablet, granular, liquid and
rinse-aid types for household and institutional use; liquid
cleaning and disinfecting agents, including antibacterial hand-wash
types, laundry bars, mouthwashes, denture cleaners, car or carpet
shampoos, bathroom cleaners; hair shampoos and hair-rinses; shower
gels and foam baths and metal cleaners; as well as cleaning
auxiliaries such as bleach additives and "stain-stick" or pre-treat
types.
[0007] As used herein, the phrase "is independently selected from
the group consisting of . . . " means that moieties or elements
that are selected from the referenced Markush group can be the
same, can be different or any mixture of elements.
[0008] As used herein, articles, for example, "a" and "an" when
used in a claim, are understood to mean one or more of what is
claimed or described.
[0009] As used herein, the terms "include", "includes" and
"including" are meant to be non-limiting.
[0010] The test methods disclosed in the Test Methods Section of
the present application must be used to determine the respective
values of the parameters of Applicants' inventions.
[0011] Unless otherwise noted, all component or composition levels
are in reference to the active level of that component or
composition, and are exclusive of impurities, for example, residual
solvents or by-products, which may be present in commercially
available sources.
[0012] Unless otherwise noted, the enzymes of the present invention
are expressed in terms of active protein level and are exclusive of
impurities, for example, residual solvents or by-products, which
may be present in commercially available sources.
[0013] All percentages and ratios are calculated by weight unless
otherwise indicated. All percentages and ratios are calculated
based on the total composition unless otherwise indicated.
[0014] 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.
Compositions
[0015] In one aspect, a composition comprising an amylase and:
[0016] a.) a sufficient amount of calcium to provide a wash liquor
comprising said composition with a free calcium concentration as
determined by Test Method 1 of from about 0.1 ppm to about 500 ppm,
from about 0.2 ppm to about 200 ppm, from about 1 ppm to about 150
ppm, or from about 2 ppm to about 100 ppm, or even from about 3 ppm
to about 50 ppm; [0017] b.) based on total product weight, less
than 15%, less than 10%, less than 8% or even from about 0.01% to
about 7% builder; and/or [0018] c.) having an enzyme deposition
index as defined in Test Method 2 of at least 2.5, at least 2.6, or
even from about 2.7 to about 50 is disclosed. Such composition may
comprise, based on total composition weight, from about 0.0001% to
about 2%, from about 0.0005% to about 1%, from about 0.001% to
about 0.5% or even from about 0.002% to about 0.25% of said enzyme.
Such compositions may be cleaning and/or treatment compositions.
Thus it is understood that they may be solids or fluids.
[0019] In one aspect, said amylase includes .alpha.-amylases
derived from Bacillus licheniformis having Sequence I.D. 5 or 6, or
an enzyme that is at least 65%, 70%, 75%, 80%, 85%, 90%, 95%, or
even 99% identical to said Sequence I.D. 5 or 6. Such
.alpha.-amylases having at least one of the following mutations at
positions corresponding to the positions corresponding to Sequence
I.D. 5 or 6: 15, 23, 133, 188, 209, 475 or combinations of said
positions.
[0020] In another aspect, said amylase enzymes include
.alpha.-amylases derived from Bacillus licheniformis having
Sequence I.D. 5 (SEQ ID No. 5 herein being equivalent to SEQ ID No
34 in U.S. Pat. No. 5,958,739) or an enzyme having at least 65%,
70%, 75%, 80%, 85%, 90%, 95%, or even 99% identity to said Sequence
I.D. 5. Such .alpha.-amylases having one or more of the following
mutations: M15T, H133Y, N188S or T, A209V or G475R.
[0021] In another aspect, said amylase enzymes include
.alpha.-amylases derived from Bacillus licheniformis having
Sequence 6 (SEQ ID No. 6 herein being equivalent to SEQ ID NO. 2 in
U.S. Pat. No. 6,436,888 B1) or an enzyme having at least 65%, 70%,
75%, 80%, 85%, 90%, 95%, or even 99% identity to said Sequence I.D.
6. Such .alpha.-amylases having one or more of the following
mutations: M15T, H133Y, N188S or T, A209V or G475R; and optionally
R23K.
[0022] In another aspect, said amylase enzymes include an amylase
selected from the group consisting of: [0023] a.) an amylase having
Seq. I.D. 5, said amylase having one of the following groups of
mutations: [0024] (i) M15T+H133Y+N188S+A209V; [0025] (ii)
M15T+H133Y+N188T+A209V; [0026] (iii) H133Y+N188S+G475R; or [0027]
(iv) H133Y+N188S; [0028] b.) an amylase having Seq. I.D. 6, said
amylase having one of the following groups of mutations: [0029] (i)
M15T+R23K+H133Y+N188S+A209V; [0030] (ii)
M15T+R23K+H133Y+N188T+A209V; [0031] (iii) R23K+H133Y+N188S+G475R;
[0032] (iv) R23K+H133Y+N188S; [0033] (v) M15T+H133Y+N188S+A209V
[0034] (vi) M15T+H133Y+N188T+A209V; [0035] (vii) H133Y+N188S+G475R;
or [0036] (viii) H133Y+N188S and combinations thereof.
[0037] In one aspect, a composition comprising an amylase belonging
to EC 3.2.1.1 such as an enzyme having Seq. I.D. 1 and: [0038] a.)
a sufficient amount of calcium to provide a wash liquor comprising
said composition with a free calcium concentration as determined by
Test Method 1 of from about 0.1 ppm to about 500 ppm, from about
0.2 ppm to about 200 ppm, from about 1 ppm to about 150 ppm, or
from about 2 ppm to about 100 ppm, or even from about 3 ppm to
about 50 ppm; [0039] b.) based on total product weight, less than
15%, less than 10%, less than 8% or even from about 0.01% to about
7% builder; and/or [0040] c.) having an enzyme deposition index as
defined in Test Method 2 of at least 2.5, at least 2.6, or even
from about 2.7 to about 50 is disclosed. Such composition may
comprise, based on total composition weight, from about 0.0001% to
about 2%, from about 0.0005% to about 1%, from about 0.001% to
about 0.5% or even from about 0.002% to about 0.25% of said enzyme.
Such compositions may be cleaning and/or treatment compositions.
Thus it is understood that they may be solids or fluids.
[0041] Any of the aspects of said compositions described in the
present specification may comprise a material selected from the
group consisting of surfactants, builders, chelating agents, dye
transfer inhibiting agents, dispersants, additional enzymes, and
enzyme stabilizers, catalytic materials, bleaching agents,
polymeric dispersing agents, clay soil removal/anti-redeposition
agents, brighteners, suds suppressors, dyes, perfumes, structure
elasticizing agents, fabric softeners, carriers, hydrotropes,
processing aids, solvents, pigments, hueing agents, structurants,
and mixtures thereof.
[0042] Any of the aspects of said compositions described in the
present specification may comprise an additional enzyme selected
from the group consisting of hemicellulases, peroxidases,
proteases, cellulases, xylanases, lipases, phospholipases,
esterases, cutinases, pectinases, mannanases, pectate lyases,
keratinases, reductases, oxidases, phenoloxidases, lipoxygenases,
ligninases, pullulanases, tannases, pentosanases, glucanases,
arabinosidases, hyaluronidase, chondroitinase, laccase, amylases,
or mixtures thereof.
[0043] In one aspect, such additional enzyme may be selected from
the group consisting of: lipases, including "first cycle lipases"
described in U.S. Pat. No. 6,939,702 B1 (SEQ ID No. 2 in the
present specification being equivalent to SEQ ID NO:1 in U.S. Pat.
No. 6,939,702 B1), a variant of SEQ ID No. 2, a variant of SEQ ID
No. 2 having at least 90% identity to SEQ ID No. 2 comprising a
substitution of an electrically neutral or negatively charged amino
acid with R or K at any of positions 3, 224, 229, 231 and 233, or
even a variant comprising T231R and N233R mutations, such variant
being sold under the tradename Lipex.RTM.; alpha-amylases,
including a variant of SEQ ID No. 3 (SEQ ID No. 3 corresponding to
SEQ ID No. 2 in U.S. Pat. No. 5,856,164), a variant of SEQ ID No. 3
having at least 90% identity to SEQ ID No. 3 (such variant
disclosed in U.S. Pat. No. 6,187,576) comprising two deletions at
positions 183 and 184 and sold under the tradename Natalase.RTM.;
serine proteases, including neutral or alkaline microbial serine
proteases, such as subtilisins (EC 3.4.21.62), including those
derived from Bacillus lentus, B. alkalophilus, B. subtilis, B.
amyloliquefaciens described in U.S. Pat. No. 6,312,936 B1, U.S.
Pat. No. 5,679,630, U.S. Pat. No. 4,760,025; 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 of SEQ ID No.
4 (SEQ ID No. 4 herein being equivalent to SEQ ID NO:2 in US
2005/0112749 A1)--such an enzyme being commercially available under
the tradename Celluclean.TM. by Novozymes A/S, and mixtures
thereof.
[0044] Any of the aspects of the compositions described in the
present specification may comprise a surfactant, including a
surfactant selected from the group of anionic surfactants including
anionic surfactants selected from the group consisting of linear
alkylbenzene-sulfonate (LAS), alcohol ethoxysulfate (AES),
mid-branched alkyl sulfates (HSAS) and mixtures thereof; non-ionic
surfactants including alcohol ethoxylates, for example alcohol
ethoxylates having a chain length of from 1 to 14 carbons, or 12 to
14 carbons; amine oxides and mixtures thereof.
[0045] Any of the aspects of the compositions described in the
present specification may comprise a polymer, including polymers
selected from the group consisting of polyacrylates, maleic/acrylic
acid copolymers, cellulose-derived polymers, including
carboxymethylcellulose and methyl hydroxyethylcellulose,
polyethyleneimine polymers and mixtures thereof.
[0046] Any of the aspects of said compositions described in the
present specification may comprise a builder selected from the
group consisting of citric acid, C.sub.12-C.sub.18 fatty acid,
aluminosilicates, including zeolites A, X and/or Y, sodium
tripolyphosphate and mixtures thereof.
[0047] Any of the aspects of the compositions described in the
present specification may comprise a material selected from the
group consisting of a photobleach, a fabric hueing agent and
mixtures thereof.
[0048] Any of the aspects of the compositions described in the
present specification may comprise a photobleach being selected
from the group consisting of xanthene dyes and mixtures thereof;
sulfonated zinc phthalocyanine, sulfonated aluminum phthalocyanine,
Eosin Y, Phoxine B, Rose Bengal, C.I. Food Red 14 and mixtures
thereof; water soluble phthalocyanine; and/or a fabric hueing agent
selected from the group consisting of dyes, including small
molecule dyes such as small molecule dyes selected from the group
consisting of Colour Index (Society of Dyers and Colourists,
Bradford, UK) numbers Direct Violet 9, Direct Violet 35, Direct
Violet 48, Direct Violet 51, Direct Violet 66, Direct Blue 1,
Direct Blue 71, Direct Blue 80, Direct Blue 279, Acid Red 17, Acid
Red 73, Acid Red 88, Acid Red 150, Acid Violet 15, Acid Violet 17,
Acid Violet 24, Acid Violet 43, Acid Violet 49, Acid Blue 15, Acid
Blue 17, Acid Blue 25, Acid Blue 29, Acid Blue 40, Acid Blue 45,
Acid Blue 75, Acid Blue 80, Acid Blue 83, Acid Blue 90 and Acid
Blue 113, Acid Black 1, Basic Violet 1, Basic Violet 3, Basic
Violet 4, Basic Violet 10, Basic Violet 35, Basic Blue 3, Basic
Blue 16, Basic Blue 22, Basic Blue 47, Basic Blue 66, Basic Blue
75, Basic Blue 159 and mixtures thereof, polymeric dyes and
mixtures thereof, dye-clay conjugates comprising at least one
cationic/basic dye and a smectite clay and mixtures thereof.
[0049] Any of the aspects of the compositions described in the
present specification may comprise, based on total product weight,
from about 0% to about 3%, from about 0.0001% to about 0.5%, or
even from about 0.0005% to about 0.3% photobleach and/or from about
0.00003% to about 0.3%, from about 0.00008% to about 0.05%, or even
from about 0.0001% to about 0.04% hueing agent.
[0050] Enzymes suitable for use in the present compositions can be
obtained from Genencor International, Palo Alto, Calif., U.S.A;
Novozymes A/S, Bagsvaerd, Denmark; Amersham Pharmacia Biotech.,
Piscataway, N.J., U.S.A; Sigma-Aldrich Company Ltd, Dorset, UK.
[0051] An enzyme having Seq. ID 1 is sold under the tradename
Optisize.RTM. HT Plus by Genencor International, Palo Alto, Calif.,
U.S.A. An enzyme having at least 90% identity to Seq. ID 2 is sold
under the tradename Lipex.RTM. by Novozymes A/S, Bagsvaerd,
Denmark. An enzyme having at least 90% identity with Seq. ID 3 is
sold under the tradename Natalase.RTM. by Novozymes A/S, Bagsvaerd,
Denmark. An enzyme having at least 90% identity to Seq. ID 4 is
sold under the tradename Celluclean.TM. by Novozymes A/S,
Bagsvaerd, Denmark. An enzyme having Seq. ID 5 is sold under the
tradename of Purastar.RTM. by Genencor International, Palo Alto,
Calif., U.S.A. An enzyme having Seq. ID 6 is sold under the
tradename of Termamyl.RTM. by Novozymes A/S, Bagsvaerd,
Denmark.
[0052] Surfactants suitable for use in the present compositions can
be obtained from Stepan, Northfield, Ill., USA; Huntsman, Salt Lake
City, Utah, USA; Procter & Gamble Chemicals, Cincinnati, Ohio,
USA.
[0053] Builders suitable for use in the present compositions can be
obtained from Rhodia, Paris, France; Industrial Zeolite (UK) Ltd,
Grays, Essex, UK; Koma, Nestemica, Czech Republic.
[0054] Polymers suitable for use in the present compositions can be
obtained from BASF, Ludwigshafen, Germany, CP Kelco, Arnhem,
Netherlands.
[0055] Photobleaches suitable for use in the present compositions
can be obtained from Aldrich, Milwaukee, Wis., USA; Frontier
Scientific, Logan, Utah, USA; Ciba Specialty Chemicals, Basel,
Switzerland; BASF, Ludwigshafen, Germany; Lamberti S.p.A,
Gallarate, Italy; Dayglo Color Corporation, Mumbai, India; Organic
Dyestuffs Corp., East Providence, R.I., USA.
[0056] Hueing agents suitable for use in the present compositions
can be obtained from Aldrich, Milwaukee, Wis., USA; Ciba Specialty
Chemicals, Basel, Switzerland; BASF, Ludwigshafen, Germany; Dayglo
Color Corporation, Mumbai, India; Organic Dyestuffs Corp., East
Providence, R.I., USA; Dystar, Frankfurt, Germany; Lanxess,
Leverkusen, Germany; Megazyme, Wicklow, Ireland; Clariant, Muttenz,
Switzerland.
Adjunct Materials
[0057] While not essential for the purposes of the present
invention, the non-limiting list of adjuncts illustrated
hereinafter are suitable for use in the instant compositions and
may be desirably incorporated in certain embodiments of the
invention, for example to assist or enhance cleaning performance,
for treatment of the substrate to be cleaned, or to modify the
aesthetics of the cleaning composition as is the case with
perfumes, colorants, dyes or the like. The precise nature of these
additional components, and levels of incorporation thereof, will
depend on the physical form of the composition and the nature of
the cleaning operation for which it is to be used. Suitable adjunct
materials include, but are not limited to, additional surfactants,
additional builders, additional polymers, additional hueing agents,
additional photobleaches, chelating agents, dye transfer inhibiting
agents, dispersants, additional enzymes, and enzyme stabilizers,
catalytic materials, bleach activators, hydrogen peroxide, sources
of hydrogen peroxide, preformed peracids, polymeric dispersing
agents, clay soil removal/anti-redeposition agents, brighteners,
suds suppressors, dyes, perfumes, structure elasticizing agents,
fabric softeners, carriers, hydrotropes, processing aids, solvents,
additional hueing agents, structurants and/or pigments. In addition
to the disclosure below, suitable examples of such other adjuncts
and levels of use are found in U.S. Pat. Nos. 5,576,282, 6,306,812
B1 and 6,326,348 B1 that are incorporated by reference.
[0058] As stated, the adjunct ingredients are not essential to
Applicants' compositions. Thus, certain embodiments of Applicants'
compositions do not contain one or more of the following adjuncts
materials: additional surfactants, additional builders, additional
polymers, additional photobleaches, chelating agents, dye transfer
inhibiting agents, dispersants, additional enzymes, and enzyme
stabilizers, catalytic materials, bleach activators, hydrogen
peroxide, sources of hydrogen peroxide, preformed peracids,
polymeric dispersing agents, clay soil removal/anti-redeposition
agents, brighteners, suds suppressors, dyes, perfumes, structure
elasticizing agents, fabric softeners, carriers, hydrotropes,
processing aids, solvents, additional hueing agents, structurants
and/or pigments. However, when one or more adjuncts are present,
such one or more adjuncts may be present as detailed below:
[0059] Bleaching Agents--The cleaning compositions of the present
invention may comprise one or more bleaching agents. Suitable
bleaching agents other than bleaching catalysts include
photobleaches, bleach activators, hydrogen peroxide, sources of
hydrogen peroxide, pre-formed peracids and mixtures thereof. In
general, when a bleaching agent is used, the compositions of the
present invention may comprise from about 0.1% to about 50% or even
from about 0.1% to about 25% bleaching agent by weight of the
subject cleaning composition. Examples of suitable bleaching agents
include:
[0060] (1) photobleaches
[0061] (2) preformed peracids: Suitable preformed peracids include,
but are not limited to, compounds selected from the group
consisting of percarboxylic acids and salts, percarbonic acids and
salts, perimidic acids and salts, peroxymonosulfuric acids and
salts, for example, Oxone.RTM., and mixtures thereof. Suitable
percarboxylic acids include hydrophobic and hydrophilic peracids
having the formula R--(C.dbd.O)O--O-M wherein R is an alkyl group,
optionally branched, having, when the peracid is hydrophobic, from
6 to 14 carbon atoms, or from 8 to 12 carbon atoms and, when the
peracid is hydrophilic, less than 6 carbon atoms or even less than
4 carbon atoms; and M is a counter ion, for example, sodium,
potassium or hydrogen;
[0062] (3) sources of hydrogen peroxide, for example, inorganic
perhydrate salts, including alkali metal salts such as sodium salts
of perborate (usually mono- or tetra-hydrate), percarbonate,
persulphate, perphosphate, persilicate salts and mixtures thereof.
In one aspect of the invention the inorganic perhydrate salts are
selected from the group consisting of sodium salts of perborate,
percarbonate and mixtures thereof. When employed, inorganic
perhydrate salts are typically present in amounts of from 0.05 to
40 wt %, or 1 to 30 wt % of the overall composition and are
typically incorporated into such compositions as a crystalline
solid that may be coated. Suitable coatings include, inorganic
salts such as alkali metal silicate, carbonate or borate salts or
mixtures thereof, or organic materials such as water-soluble or
dispersible polymers, waxes, oils or fatty soaps; and
[0063] (4) bleach activators having R--(C.dbd.O)-L wherein R is an
alkyl group, optionally branched, having, when the bleach activator
is hydrophobic, from 6 to 14 carbon atoms, or from 8 to 12 carbon
atoms and, when the bleach activator is hydrophilic, less than 6
carbon atoms or even less than 4 carbon atoms; and L is leaving
group. Examples of suitable leaving groups are benzoic acid and
derivatives thereof--especially benzene sulphonate. Suitable bleach
activators include dodecanoyl oxybenzene sulphonate, decanoyl
oxybenzene sulphonate, decanoyl oxybenzoic acid or salts thereof,
3,5,5-trimethyl hexanoyloxybenzene sulphonate, tetraacetyl ethylene
diamine (TAED) and nonanoyloxybenzene sulphonate (NOBS). Suitable
bleach activators are also disclosed in WO 98/17767. While any
suitable bleach activator may be employed, in one aspect of the
invention the subject cleaning composition may comprise NOBS, TAED
or mixtures thereof.
[0064] When present, the peracid and/or bleach activator is
generally present in the composition in an amount of from about 0.1
to about 60 wt %, from about 0.5 to about 40 wt % or even from
about 0.6 to about 10 wt % based on the composition. One or more
hydrophobic peracids or precursors thereof may be used in
combination with one or more hydrophilic peracid or precursor
thereof.
[0065] The amounts of hydrogen peroxide source and peracid or
bleach activator may be selected such that the molar ratio of
available oxygen (from the peroxide source) to peracid is from 1:1
to 35:1, or even 2:1 to 10:1.
[0066] Surfactants--The cleaning compositions according to the
present invention may comprise a surfactant or surfactant system
wherein the surfactant can be selected from nonionic surfactants,
anionic surfactants, cationic surfactants, ampholytic surfactants,
zwitterionic surfactants, semi-polar nonionic surfactants and
mixtures thereof. When present, surfactant is typically present at
a level of from about 0.1% to about 60%, from about 1% to about 50%
or even from about 5% to about 40% by weight of the subject
composition.
[0067] Builders--The cleaning compositions of the present invention
may comprise one or more detergent builders or builder systems.
Builders include, but are not limited to, the alkali metal,
ammonium and alkanolammonium salts of polyphosphates, alkali metal
silicates, alkaline earth and alkali metal carbonates,
aluminosilicate builders and polycarboxylate compounds, ether
hydroxypolycarboxylates, copolymers of maleic anhydride with
ethylene or vinyl methyl ether, 1,3,5-trihydroxy
benzene-2,4,6-trisulphonic acid, and carboxymethyloxysuccinic acid,
the various alkali metal, ammonium and substituted ammonium salts
of polyacetic acids such as ethylenediamine tetraacetic acid and
nitrilotriacetic acid, as well as polycarboxylates such as mellitic
acid, succinic acid, citric acid, oxydisuccinic acid, polymaleic
acid, benzene 1,3,5-tricarboxylic acid, carboxymethyloxysuccinic
acid, and soluble salts thereof.
[0068] Chelating Agents--The cleaning compositions herein may
contain a chelating agent. Suitable chelating agents include
copper, iron and/or manganese chelating agents and mixtures
thereof. When a chelating agent is used, the subject composition
may comprise from about 0.005% to about 15% or even from about 3.0%
to about 10% chelating agent by weight of the subject
composition.
[0069] Dye Transfer Inhibiting Agents--The cleaning compositions of
the present invention may also include one or more dye transfer
inhibiting agents. Suitable polymeric dye transfer inhibiting
agents include, but are not limited to, polyvinylpyrrolidone
polymers, polyamine N-oxide polymers, copolymers of
N-vinylpyrrolidone and N-vinylimidazole, polyvinyloxazolidones and
polyvinylimidazoles or mixtures thereof. When present in a subject
composition, the dye transfer inhibiting agents may be present at
levels from about 0.0001% to about 10%, from about 0.01% to about
5% or even from about 0.1% to about 3% by weight of the
composition.
[0070] Brighteners--The cleaning compositions of the present
invention can also contain additional components that may tint
articles being cleaned, such as fluorescent brighteners. Suitable
fluorescent brightener levels include lower levels of from about
0.01, from about 0.05, from about 0.1 or even from about 0.2 wt %
to upper levels of 0.5 or even 0.75 wt %.
[0071] Dispersants--The compositions of the present invention can
also contain dispersants. Suitable water-soluble organic materials
include the homo- or co-polymeric acids or their salts, in which
the polycarboxylic acid comprises at least two carboxyl radicals
separated from each other by not more than two carbon atoms.
[0072] Enzymes--The cleaning compositions can comprise one or more
enzymes which provide cleaning performance and/or fabric care
benefits. Examples of suitable enzymes include, but are not limited
to, hemicellulases, peroxidases, proteases, cellulases, xylanases,
lipases, phospholipases, esterases, cutinases, pectinases,
mannanases, pectate lyases, keratinases, reductases, oxidases,
phenoloxidases, lipoxygenases, ligninases, pullulanases, tannases,
pentosanases, glucanases, arabinosidases, hyaluronidase,
chondroitinase, laccase, amylases, or mixtures thereof. A typical
combination is an enzyme cocktail that may comprise, for example, a
protease and lipase in conjunction with amylase. When present in a
cleaning composition, the aforementioned additional enzymes may be
present at levels from about 0.00001% to about 2%, from about
0.0001% to about 1% or even from about 0.001% to about 0.5% enzyme
protein by weight of the composition.
[0073] Enzyme Stabilizers--Enzymes for use in detergents can be
stabilized by various techniques. The enzymes employed herein can
be stabilized by the presence of water-soluble sources of calcium
and/or magnesium ions in the finished compositions that provide
such ions to the enzymes. In case of aqueous compositions
comprising protease, a reversible protease inhibitor, such as a
boron compound, can be added to further improve stability.
[0074] Catalytic Metal Complexes--Applicants' cleaning compositions
may include catalytic metal complexes. One type of metal-containing
bleach catalyst is a catalyst system comprising a transition metal
cation of defined bleach catalytic activity, such as copper, iron,
titanium, ruthenium, tungsten, molybdenum, or manganese cations, an
auxiliary metal cation having little or no bleach catalytic
activity, such as zinc or aluminum cations, and a sequestrate
having defined stability constants for the catalytic and auxiliary
metal cations, particularly ethylenediaminetetraacetic acid,
ethylenediaminetetra(methylenephosphonic acid) and water-soluble
salts thereof. Such catalysts are disclosed in U.S. Pat. No.
4,430,243.
[0075] If desired, the compositions herein can be catalyzed by
means of a manganese compound. Such compounds and levels of use are
well known in the art and include, for example, the manganese-based
catalysts disclosed in U.S. Pat. No. 5,576,282.
[0076] Cobalt bleach catalysts useful herein are known, and are
described, for example, in U.S. Pat. No. 5,597,936; U.S. Pat. No.
5,595,967. Such cobalt catalysts are readily prepared by known
procedures, such as taught for example in U.S. Pat. No. 5,597,936,
and U.S. Pat. No. 5,595,967.
[0077] Compositions herein may also suitably include a transition
metal complex of ligands such as bispidones (WO 05/042532 A1)
and/or macropolycyclic rigid ligands--abbreviated as "MRLs". As a
practical matter, and not by way of limitation, the compositions
and processes herein can be adjusted to provide on the order of at
least one part per hundred million of the active MRL species in the
aqueous washing medium, and will typically provide from about 0.005
ppm to about 25 ppm, from about 0.05 ppm to about 10 ppm, or even
from about 0.1 ppm to about 5 ppm, of the MRL in the wash
liquor.
[0078] Suitable transition-metals in the instant transition-metal
bleach catalyst include, for example, manganese, iron and chromium.
Suitable MRLs include
5,12-diethyl-1,5,8,12-tetraazabicyclo[6.6.2]hexadecane.
[0079] Suitable transition metal MRLs are readily prepared by known
procedures, such as taught for example in WO 00/32601, and U.S.
Pat. No. 6,225,464.
[0080] Solvents--Suitable solvents include water and other solvents
such as lipophilic fluids. Examples of suitable lipophilic fluids
include siloxanes, other silicones, hydrocarbons, glycol ethers,
glycerine derivatives such as glycerine ethers, perfluorinated
amines, perfluorinated and hydrofluoroether solvents,
low-volatility nonfluorinated organic solvents, diol solvents,
other environmentally-friendly solvents and mixtures thereof.
Processes of Making Compositions
[0081] The compositions of the present invention can be formulated
into any suitable form and prepared by any process chosen by the
formulator, non-limiting examples of which are described in
Applicants' examples and in U.S. Pat. No. 4,990,280; U.S.
20030087791A1; U.S. 20030087790A1; U.S. 20050003983A1; U.S.
20040048764A1; U.S. Pat. No. 4,762,636; U.S. Pat. No. 6,291,412;
U.S. 20050227891A1; EP 1070115A2; U.S. Pat. No. 5,879,584; U.S.
Pat. No. 5,691,297; U.S. Pat. No. 5,574,005; U.S. Pat. No.
5,569,645; U.S. Pat. No. 5,565,422; U.S. Pat. No. 5,516,448; U.S.
Pat. No. 5,489,392; U.S. Pat. No. 5,486,303.
Method of Use
[0082] The present invention includes a method for cleaning and/or
treating a situs inter alia a surface or fabric. Such method
includes the steps of optionally washing and/or rinsing said
surface or fabric, contacting said surface or fabric with a
composition of the present invention in neat or diluted form such
as in a wash liquor and then optionally washing and/or rinsing said
surface or fabric. For purposes of the present invention, washing
includes but is not limited to, scrubbing, and mechanical
agitation. As will be appreciated by one skilled in the art, the
cleaning compositions of the present invention are ideally suited
for use in laundry applications. Accordingly, the present invention
includes a method for laundering a fabric. The method may comprise
the steps of contacting a fabric to be laundered with a said
cleaning laundry solution comprising at least one embodiment of
Applicants' cleaning composition, cleaning additive or mixture
thereof. The fabric may comprise most any fabric capable of being
laundered in normal consumer use conditions. The solution may have
in one aspect a pH of from about 7.5 to about
[0083] 10.5 or even a pH of from about 8 to about 10.5. The
compositions may be employed at
[0084] concentrations of from about 500 ppm to about 15,000 ppm in
solution. The water temperatures typically range from about
5.degree. C. to about 90.degree. C. The water to fabric ratio is
typically from about 1:1 to about 30:1.
Test Methods
Test Method 1
Procedure for Determining the Concentration of Free CALCIUM
(Ca.sup.++)
Basis of Method
[0085] Free calcium is assayed by using an ion specific electrode
that is specific for calcium. This measurement technique is well
known and is exemplified in many literature references, such as
Analytical Chemistry, Vol 46, No 1, 1974, p. 12-15, and manuals
exemplifying the use of such electrodes are broadly known and
available (e.g. from Metrohm of Buckinghamshire, UK and from HACH
LANGE LTD, Manchester, UK). The description below shows how such a
technique may be applied to measurements of free calcium for
detergents.
Calibration:
[0086] Before use, the electrodes must be calibrated. This may be
done by measuring a series of known standard solutions, made by
serial dilution of the 1000 ppm Calcium standard solution. For a
full calibration, prepare 100 ml of solutions containing 1000, 100,
10, 1, and 0.1 ppm Ca.sup.2+.
[0087] Add 2 ml of Ionic Strength Adjustment Buffer (ISAB) solution
to each standard and mix. Prepare a calibration graph.
Sample Preparation
[0088] a. To 6 separate IL volumetric flasks add, 0, 20, 30, 40,
50, 100 and 200 ml of 1000 ppm calcium standard solution and add
deionised water to make the volume to 1 liter to make solutions
containing 0, 20, 30, 40, 50, 100 & 200 ppm of calcium.
Transfer each 1 liter calcium solution to a 1 liter tergotometer
pot and stir for 10 mins on a standard tergotometer. [0089] b. To
50 ml of each solution from Step a. above, add 1 ml of ISAB buffer
and measure calcium. This serves to check that the initial solution
contains the level of calcium expected. [0090] c. To each
tergotometer pot from Step a. above add sufficient detergent to
give a detergent solution having the same concentration as would be
realized by adding the detergent manufacturer's recommended dose of
detergent to the standard volume within a washing machine or median
hand-wash practices. (For example formulations 1-6, typical
detergent concentration would be 1.5-3 g/liter; for example
formulations 7-12, typical detergent concentration would be 8-9
g/liter; for example formulations 13-16, typical detergent
concentration would be 1.5 g/liter; and for examples 17 & 18,
typical detergent concentrations would be 8-9 g/liter). Stir for 10
mins. [0091] d. To 50 ml of each solution from Step c., add 1 ml of
ISAB buffer, immerse the electrode and take the calcium reading,
once equilibrated (typically takes several seconds). This is the
free calcium reading for the detergent composition.
Apparatus Used:
[0092] Ion-Selective Calcium Electrode: Ion-selective calcium
electrodes are broadly available. The one used for this test is
sourced from VWR International Ltd., Leicestershire, UK and
comprises the following parts: Ion-Selective Electrode for calcium
ion (such as ELIT 8041 PVC membrane); Reference electrode: single
junction silver chloride (such as ELIT 001); Dual electrode head
(such as ELIT 201); ELIT Computer Interface/Ion Analyzer attached
to a Dell PC.
[0093] Standard solutions: The 1000 ppm calcium chloride solution
can be made by dissolving calcium chloride (sourced from Sigma
Aldrich of Milwaukee, US) in deionized water, and the buffer
solution (ISAB) comprising 4 Molar KCl can be sourced from VWR
International Ltd., Leicestershire, UK.
[0094] Standard Tergotometer: (e.g. models available from Copley
Scientific, Nottingham, UK such as that sold under catalogue number
Dissolution Tester DIS 8000).
Test Method 2
Procedure for Determining Enzyme Deposition Index
Basis of Method:
[0095] This method compares the residual enzyme concentration of
various amylases detectable by standard Double Antibody Sandwich
ELISA (DAS-ELISA) methods, well known to those skilled in the art,
by reaction with the appropriate antibodies (DAS-ELISA technique is
exemplified in various patents, e.g. U.S. Pat. No. 5,188,937 &
U.S. Pat. No. 6,818,804, and in various literature articles, e.g.
L. S. Miller, "A robotic immunoassay system for detergent enzymes."
Laboratory Information Management, 1994, Vol 26, pgs 79-87; Butler,
J. E. "The immunochemistry of sandwich ELISA's: principles and
applications for the quantitative determination of
immunoglobulins." In "ELISA and Other Solid Phase Immunoassays.
Theoretical and Practical Aspects" Eds Kemeny, D. M. and
Challacombe, S. J. John Wiley and Sons, NY. 1988, pgs. 155-180 and
references incorporated therein.) Standard calibration methods are
used.
[0096] The enzyme deposition index (EDI) is the ratio of the (mass
of test alpha-amylase protein extracted/g fabric) and the (mass of
Termamyl.RTM. protein extracted/g fabric). Thus, the equation for
cotton fabric is Equation 1. This method may be used, for example,
to determine the suitability of an enzyme for use as a detergent
ingredient and/or predict the performance of an enzyme in, for
example, a detergent application.
EDI=(Mass of test alpha-amylase protein extracted per g
cotton)/(Mass of Termamyl.RTM. extracted per g cotton) Equation
1
Sample Preparation
[0097] 1. To separate tergotometer pots add 980 ml of water
containing 145.+-.10 ppm calcium and 2.0 g of sodium carbonate
(sourced from SigmaAldrich of Milwaukee, USA). Stir for 10 minutes
to dissolve. Allow to equilibrate to 40.degree. C. [0098] 2. Add
0.69 g of LAS (Linear alkylbenzenesulfonate having an average
aliphatic carbon chain length C.sub.11-C.sub.12) and 0.38 g of
AE3S(C.sub.12-15 alkyl ethoxy (3) sulfate), both supplied by
Stepan, Northfield, Ill., USA. Stir to dissolve. [0099] 3. Add
liquid samples of the various enzymes to be studied to the
different tergotometer pots to ensure 0.2 mg of amylase are present
in each pot. One pot should contain 0.2 mg Termamyl.RTM. (available
from Novozymes of Denmark) to act as the reference versus which the
other enzymes are to be indexed. [0100] 4. Adjust the water volume
in each pot to 1 liter, if needed, using water containing 145.+-.10
ppm calcium. The resultant solution should contain 690 ppm of LAS,
380 ppm AE3S, 2000 ppm of sodium carbonate and 0.2 ppm of the
enzyme. [0101] 5. To each tergotometer pot, add three standard
cotton swatches (sourced ex. Center for Test Materials (CFT) B.V.
of Holland) with fabric code CN03, each weighing 3.5.+-.0.3 g. The
total weight of cotton should be 10.5.+-.0.5 g per tergotometer
pot. [0102] 6. Start the tergotometer run (conditions are
40.+-.2.degree. C., 150 rpm and run time is 20 minutes). [0103] 7.
After 20 minutes the fabrics are removed, hand squeezed until not
excess liquid is visible and then rinsed for 5 minutes in a
tergotometer in 1 liter of water containing 145.+-.10 ppm calcium
(conditions are 150 rpm agitation, with a water temperature of
25.+-.2.degree. C.). [0104] 8. The swatches are removed and hand
squeezed to remove excess liquor and then allowed to air dry at
room temperature for 3-5 hours. [0105] 9. An extraction buffer is
prepared comprising of: [0106] a. 0.93 g/L
2-Amino-2-(hydroxymethyl)-1,3-propanediol (otherwise known as
Trizma base); [0107] b. 4.96 g/L Sodium Thiosulphate pentahydrate;
[0108] c. 0.147 g/L Calcium Chloride dehydrate; [0109] d. 29.22 g/L
sodium Chloride; [0110] e. 1.0 g Sodium Azide; and [0111] f. 1.0
g/L Polyethylene glycol sorbitan monolaurate (otherwise known as
Tween 20 with CAS #9005-64-5) [0112] The pH of the buffer is
adjusted to pH=8 using 0.1N hydrochloric acid prior to use. [0113]
All reagents are available from Sigma Aldrich Company Ltd. Dorset,
UK. [0114] 10. Each swatch of known weight is placed in a separate
50 ml extraction tube and 25 ml of extraction buffer is added. The
tube is hand shaken vigorously for 1 minute (+/-10 s) then left to
stand for 15 minutes (+/-1 minute) then shaken vigorously again for
1 minute (+/-10 s). The tube is allowed to stand for a further 15
minutes (+/-1 minute) before given a final vigorous shaking for 1
minute (+/-10 s). [0115] 11. The resultant solution is assayed via
standard ELISA methods using a Rosys Plato 7381 analyzer (Supplier
Rosys Anthos GmbH Feldbachstr CH-8634 Hombrechtikon Switzerland or
equivalent ELISA equipment such as those supplied by Dynex
Technologies of Virginia, USA or Biotech of Vermont, USA). [0116]
12. From this assay by comparing to the standard calibration curve,
the mass of amylase protein detected can be determined and the mass
of enzyme extracted/g of fabric can be calculated. [0117] 13. The
whole process (Steps 1-12) is repeated 3 more times to generate
further sets of data. [0118] 14. The enzyme deposition index is
then calculated by taking the average of 12 readings expressed in
ng amylase protein/g fabric (these twelve readings come from the
three pieces of cloth per pot from each of the four runs) for each
enzyme and indexing such value to that observed for Termamyl.RTM.
protein as shown in Equation 1.
Equipment Used
[0119] Standard Tergotometer (e.g. models available from Copley
Scientific, Nottingham, UK such as that sold under catalogue number
Dissolution Tester DIS 8000).
EXAMPLES
[0120] Unless otherwise indicated, materials can be obtained from
Aldrich, P.O. Box 2060, Milwaukee, Wis. 53201, USA.
Examples 1-6
[0121] Granular laundry detergent compositions designed for hand
washing or top-loading washing machines.
TABLE-US-00001 1 2 3 4 5 6 (wt %) (wt %) (wt %) (wt %) (wt %) (wt
%) Linear alkylbenzenesulfonate 20 22 20 15 20 20 C.sub.12-14
Dimethylhydroxyethyl 0.7 0.2 1 0.6 0.0 0 ammonium chloride AE3S 0.9
1 0.9 0.0 0.5 0.9 AE7 0.0 0.0 0.0 1 0.0 3 Sodium tripolyphosphate 5
0.0 4 9 2 0.0 Zeolite A 0.0 1 0.0 1 4 1 1.6R Silicate
(SiO.sub.2:Na.sub.2O at 7 5 2 3 3 5 ratio 1.6:1) Sodium Carbonate
25 20 25 17 18 19 Polyacrylate MW 4500 1 0.6 1 1 1.5 1 Carboxy
Methyl Cellulose 1 0.3 1 1 1 1 Amylase* (20 mg active/g) 0.1 0.2
0.1 0.2 0.1 0.1 Savinase .RTM. (32.89 mg active/g) 0.1 0.1 0.1 0.1
0.1 0.1 Natalase .RTM. (8.65 mg active/g) 0.1 0.0 0.1 0.0 0.1 0.1
Lipex .RTM. (18 mg active/g) 0.03 0.07 0.3 0.1 0.07 0.4 Fluorescent
Brightener 1 0.06 0.0 0.06 0.18 0.06 0.06 Fluorescent Brightener 2
0.1 0.06 0.1 0.0 0.1 0.1 DTPA 0.6 0.8 0.6 0.25 0.6 0.6 MgSO.sub.4 1
1 1 0.5 1 1 Sodium Percarbonate 0.0 5.2 0.1 0.0 0.0 0.0 Sodium
Perborate 4.4 0.0 3.85 2.09 0.78 3.63 Monohydrate NOBS 1.9 0.0 1.66
0.0 0.33 0.75 TAED 0.58 1.2 0.51 0.0 0.015 0.28 Sulphonated zinc
0.0030 0.0 0.0012 0.0030 0.0021 0.0 phthalocyanine S-ACMC 0.1 0.0
0.0 0.0 0.06 0.0 Direct Violet 9 0.0 0.0 0.0003 0.0005 0.0003 0.0
Acid Blue 29 0.0 0.0 0.0 0.0 0.0 0.0003 Sulfate/Moisture* *Balance
to 100% for Examples 1-6
Examples 7-12
[0122] Granular laundry detergent compositions designed for
front-loading automatic washing machines.
TABLE-US-00002 7 8 9 10 11 12 (wt %) (wt %) (wt %) (wt %) (wt %)
(wt %) Linear alkylbenzenesulfonate 8 7.1 7 6.5 7.5 7.5 AE3S 0 4.8
0 5.2 4 4 Alkylsulfate 1 0 1 0 0 0 AE7 2.2 0 3.2 0 0 0 C.sub.10-12
Dimethyl 0.75 0.94 0.98 0.98 0 0 hydroxyethylammonium chloride
Crystalline layered silicate (.delta.- 4.1 0 4.8 0 0 0
Na.sub.2Si.sub.2O.sub.5) Zeolite A 5 0 5 0 2 2 Citric Acid 3 5 3 4
2.5 3 Sodium Carbonate 15 20 14 20 23 23 Silicate 2R
(SiO.sub.2:Na.sub.2O at ratio 0.08 0 0.11 0 0 0 2:1) Soil release
agent 0.75 0.72 0.71 0.72 0 0 Acrylic Acid/Maleic Acid 1.1 3.7 1.0
3.7 2.6 3.8 Copolymer Carboxymethylcellulose 0.15 1.4 0.2 1.4 1 0.5
Protease (84 mg active/g) 0.2 0.2 0.3 0.15 0.12 0.13 Amylase* (20
mg active/g) 0.2 0.15 0.2 0.3 0.15 0.15 Lipex .RTM. (18.00 mg
active/g) 0.05 0.15 0.1 0 0 0 Natalase .RTM. (8.65 mg active/g) 0.1
0.2 0 0 0.15 0.15 Celluclean .TM. (15.6 mg active/g) 0 0 0 0 0.1
0.1 TAED 3.6 4.0 3.6 4.0 2.2 1.4 Percarbonate 13 13.2 13 13.2 16 14
Na salt of Ethylenediamine-N,N'- 0.2 0.2 0.2 0.2 0.2 0.2 disuccinic
acid, (S,S) isomer (EDDS) Hydroxyethane di phosphonate 0.2 0.2 0.2
0.2 0.2 0.2 (HEDP) MgSO.sub.4 0.42 0.42 0.42 0.42 0.4 0.4 Perfume
0.5 0.6 0.5 0.6 0.6 0.6 Suds suppressor agglomerate 0.05 0.1 0.05
0.1 0.06 0.05 Soap 0.45 0.45 0.45 0.45 0 0 Sulphonated zinc
phthalocyanine 0.0007 0.0012 0.0007 0 0 0 (active) S-ACMC 0.01 0.01
0 0.01 0 0 Direct Violet 9 (active) 0 0 0.0001 0.0001 0 0
Sulfate/Water & Miscellaneous* *Balance to 100% for Examples
7-12
[0123] Any of the above compositions is used to launder fabrics at
a concentration of 7000 to 10000 ppm in water, 20-90.degree. C.,
and a 5:1 water:cloth ratio. The typical pH is about 10.
Examples 13-18
Heavy Duty Liquid Laundry Detergent Compositions
Raw Materials and Notes For Composition Examples 1-18
TABLE-US-00003 [0124] 13 14 15 16 17 18 (wt %) (wt %) (wt %) (wt %)
(wt %) (wt %) AES C.sub.12-15 alkyl 11 10 4 6.32 0 0 ethoxy (1.8)
sulfate AE3S 0 0 0 0 2.4 0 Linear alkyl 1.4 4 8 3.3 5 8 benzene
sulfonate HSAS 3 5.1 3 0 0 0 Sodium formate 1.6 0.09 1.2 0.04 1.6
1.2 Sodium hydroxide 2.3 3.8 1.7 1.9 1.7 2.5 Monoethanolamine 1.4
1.49 1.0 0.7 0 0 Diethylene glycol 5.5 0.0 4.1 0.0 0 0 Nonionic
23.9 0.4 0.6 0.3 0.3 0 0 Nonionic 24.7 0 0 0 0 2.4 6 Chelant 0.15
0.15 0.11 0.07 0.5 0.11 Citric Acid 2.5 3.96 1.88 1.98 0.9 2.5
C.sub.12-14 dimethyl 0.3 0.73 0.23 0.37 0 0 Amine Oxide C.sub.12-18
Fatty Acid 0.8 1.9 0.6 0.99 3.5 2.5 Borax 1.43 1.5 1.1 0.75 1 1.07
Ethanol 1.54 1.77 1.15 0.89 0 3 Ethoxylated (EO.sub.15) 0.3 0.33
0.23 0.17 0.0 0.0 tetraethylene pentaimine.sup.1 Ethoxylated 0.8
0.81 0.6 0.4 1 1 hexamethylene diamine.sup.2 1,2-Propanediol 0.0
6.6 0.0 3.3 0.5 2 Protease (40.6 mg active/g) 0.8 0.6 0.7 0.9 0.7
0.6 Mannaway .RTM. (25 mg active/g) 0.07 0.05 0.045 0.06 0.04 0.045
Amylase* (15 mg active/g) 0.3 0.2 0.3 0.1 0.2 0.4 Natalase .RTM.
(29 mg 0 0.2 0.1 0.15 0.07 0 active/g) Lipex .RTM. (18 mg active/g)
0.4 0.2 0.3 0.1 0.2 0 Liquitint .RTM. Violet 0.006 0.002 0 0 0
0.002 CT (active) S-ACMC -- -- 0.01 0.05 0.01 0.02 Water, perfume,
dyes & Balance Balance Balance Balance Balance Balance other
components
Raw Materials and Notes For Composition Examples 1-18
[0125] Linear alkylbenzenesulfonate having an average aliphatic
carbon chain length C.sub.11-C.sub.12 supplied by Stepan,
Northfield, Ill., USA
[0126] C.sub.12-14 Dimethylhydroxyethyl ammonium chloride, supplied
by Clariant GmbH, Sulzbach, Germany [0127] AE3S is C.sub.12-15
alkyl ethoxy (3) sulfate supplied by Stepan, Northfield, Ill.,
USA
[0128] AE7 is C.sub.12-15 alcohol ethoxylate, with an average
degree of ethoxylation of 7, supplied by Huntsman, Salt Lake City,
Utah, USA
[0129] Sodium tripolyphosphate is supplied by Rhodia, Paris,
France
[0130] Zeolite A is supplied by Industrial Zeolite (UK) Ltd, Grays,
Essex, UK
[0131] 1.6R Silicate is supplied by Koma, Nestemica, Czech
Republic
[0132] Sodium Carbonate is supplied by Solvay, Houston, Tex.,
USA
[0133] Polyacrylate MW 4500 is supplied by BASF, Ludwigshafen,
Germany
[0134] Carboxy Methyl Cellulose is Finnfix.RTM. BDA supplied by CP
Kelco, Arnhem, Netherlands
[0135] Suitable chelants are, for example, diethylenetetraamine
pentaacetic acid (DTPA) supplied by Dow Chemical, Midland, Mich.,
USA or Hydroxyethane di phosphonate (HEDP) supplied by Solutia, St
Louis, Mo., USA Bagsvaerd, Denmark
[0136] Protease (examples 7-12) described in U.S. Pat. No.
6,312,936 B1 supplied by Genencor International, Palo Alto, Calif.,
USA
[0137] Protease (examples 13-18) described in U.S. Pat. No.
4,760,025 is supplied by Genencor International, Palo Alto, Calif.,
USA [0138] A suitable amylase is, for example, Optisize.RTM. HT
Plus supplied by Genencor International, Palo Alto, Calif., USA, or
any of the other amylases specifically described in the present
specification.
[0139] Fluorescent Brightener 1 is Tinopal.RTM. AMS, Fluorescent
Brightener 2 is Tinopal.RTM. CBS-X, Sulphonated zinc phthalocyanine
and Direct Violet 9 is Pergasol.RTM. Violet BN-Z all supplied by
Ciba Specialty Chemicals, Basel, Switzerland
[0140] Sodium percarbonate supplied by Solvay, Houston, Tex.,
USA
[0141] Sodium perborate is supplied by Degussa, Hanau, Germany
[0142] NOBS is sodium nonanoyloxybenzenesulfonate, supplied by
Eastman, Batesville, Ark., USA
[0143] TAED is tetraacetylethylenediamine, supplied under the
Peractive.RTM. brand name by Clariant GmbH, Sulzbach, Germany
[0144] S-ACMC is carboxymethylcellulose conjugated with C.I.
Reactive Blue 19, sold by Megazyme, Wicklow, Ireland under the
product name AZO-CM-CELLULOSE, product code S-ACMC.
[0145] Soil release agent is Repel-o-tex.RTM. PF, supplied by
Rhodia, Paris, France
[0146] Acrylic Acid/Maleic Acid Copolymer is molecular weight
70,000 and acrylate:maleate ratio 70:30, supplied by BASF,
Ludwigshafen, Germany
[0147] Na salt of Ethylenediamine-N,N'-disuccinic acid, (S,S)
isomer (EDDS) is supplied by Octel, Ellesmere Port, UK
[0148] Hydroxyethane di phosphonate (HEDP) is supplied by Dow
Chemical, Midland, Mich., USA
[0149] Suds suppressor agglomerate is supplied by Dow Corning,
Midland, Mich., USA
[0150] HSAS is mid-branched alkyl sulfate as disclosed in U.S. Pat.
No. 6,020,303 and U.S. Pat. No. 6,060,443
[0151] C.sub.12-14 dimethyl Amine Oxide is supplied by Procter
& Gamble Chemicals, Cincinnati, Ohio, USA
[0152] Liquitint(Violet CT is supplied by Milliken, Spartanburg,
S.C., USA)
[0153] .sup.1 as described in U.S. Pat. No. 4,597,898.
[0154] .sup.2 available under the tradename LUTENSIT.RTM. from BASF
and such as those described in WO 01/05874
[0155] 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".
[0156] All documents cited in the Detailed Description of the
Invention are, in relevant part, incorporated herein by reference;
the citation of any document is not to be construed as an admission
that it is prior art with respect to the present invention. To the
extent that any meaning or definition of a term in this document
conflicts with any meaning or definition of the same term in a
document incorporated by reference, the meaning or definition
assigned to that term in this document shall govern.
[0157] While particular embodiments of the present invention have
been illustrated and described, it would be obvious to those
skilled in the art that various other changes and modifications can
be made without departing from the spirit and scope of the
invention. It is therefore intended to cover in the appended claims
all such changes and modifications that are within the scope of
this invention.
Sequence CWU 1
1
61483PRTBacillus licheniformis 1Ala Asn Leu Asn Gly Thr Leu Met Gln
Tyr Phe Glu Trp Tyr Thr Pro1 5 10 15Asn Asp Gly Gln His Trp Lys Arg
Leu Gln Asn Asp Ser Ala Tyr Leu 20 25 30Ala Glu His Gly Ile Thr Ala
Val Trp Ile Pro Pro Ala Tyr Lys Gly 35 40 45Thr Ser Gln Ala Asp Val
Gly Tyr Gly Ala Tyr Asp Leu Tyr Asp Leu 50 55 60Gly Glu Phe His Gln
Lys Gly Thr Val Arg Thr Lys Tyr Gly Thr Lys65 70 75 80Gly Glu Leu
Gln Ser Ala Ile Lys Ser Leu His Ser Arg Asp Ile Asn 85 90 95Val Tyr
Gly Asp Val Val Ile Asn His Lys Gly Gly Ala Asp Ala Thr 100 105
110Glu Asp Val Thr Ala Val Glu Val Asp Pro Ala Asp Arg Asn Arg Val
115 120 125Ile Ser Gly Glu Tyr Leu Ile Lys Ala Trp Thr His Phe His
Phe Pro 130 135 140Gly Arg Gly Ser Thr Tyr Ser Asp Phe Lys Trp His
Trp Tyr His Phe145 150 155 160Asp Gly Thr Asp Trp Asp Glu Ser Arg
Lys Leu Asn Arg Ile Tyr Lys 165 170 175Phe Gln Gly Lys Ala Trp Asp
Trp Glu Val Ser Ser Glu Asn Gly Asn 180 185 190Tyr Asp Tyr Leu Met
Tyr Ala Asp Ile Asp Tyr Asp His Pro Asp Val 195 200 205Val Ala Glu
Ile Lys Arg Trp Gly Thr Trp Tyr Ala Asn Glu Leu Gln 210 215 220Leu
Asp Gly Phe Arg Leu Asp Ala Val Lys His Ile Lys Phe Ser Phe225 230
235 240Leu Arg Asp Trp Val Asn His Val Arg Glu Lys Thr Gly Lys Glu
Met 245 250 255Phe Thr Val Ala Glu Tyr Trp Gln Asn Asp Leu Gly Ala
Leu Glu Asn 260 265 270Tyr Leu Asn Lys Thr Asn Phe Asn His Ser Val
Phe Asp Val Pro Leu 275 280 285His Tyr Gln Phe His Ala Ala Ser Thr
Gln Gly Gly Gly Tyr Asp Met 290 295 300Arg Lys Leu Leu Asn Gly Thr
Val Val Ser Lys His Pro Leu Lys Ser305 310 315 320Val Thr Phe Val
Asp Asn His Asp Thr Gln Pro Gly Gln Ser Leu Glu 325 330 335Ser Thr
Val Gln Thr Trp Phe Lys Pro Leu Ala Tyr Ala Phe Ile Leu 340 345
350Thr Arg Glu Ser Gly Tyr Pro Gln Val Phe Tyr Gly Asp Met Tyr Gly
355 360 365Thr Lys Gly Asp Ser Gln Arg Glu Ile Pro Ala Leu Lys His
Lys Ile 370 375 380Glu Pro Ile Leu Lys Ala Arg Lys Gln Tyr Ala Tyr
Gly Ala Gln His385 390 395 400Asp Tyr Phe Asp His His Asp Ile Val
Gly Trp Thr Arg Glu Gly Asp 405 410 415Ser Ser Val Ala Asn Ser Gly
Leu Ala Ala Leu Ile Thr Asp Gly Pro 420 425 430Gly Gly Ala Lys Arg
Met Tyr Val Gly Arg Gln Asn Ala Gly Glu Thr 435 440 445Trp His Asp
Ile Thr Gly Asn Arg Ser Glu Pro Val Val Ile Asn Ser 450 455 460Glu
Gly Trp Gly Glu Phe His Val Asn Gly Gly Ser Val Ser Ile Tyr465 470
475 480Val Gln Arg2269PRTHumicola lanuginosa 2Glu Val Ser Gln Asp
Leu Phe Asn Gln Phe Asn Leu Phe Ala Gln Tyr1 5 10 15Ser Ala Ala Ala
Tyr Cys Gly Lys Asn Asn Asp Ala Pro Ala Gly Thr 20 25 30Asn Ile Thr
Cys Thr Gly Asn Ala Cys Pro Glu Val Glu Lys Ala Asp 35 40 45Ala Thr
Phe Leu Tyr Ser Phe Glu Asp Ser Gly Val Gly Asp Val Thr 50 55 60Gly
Phe Leu Ala Leu Asp Asn Thr Asn Lys Leu Ile Val Leu Ser Phe65 70 75
80Arg Gly Ser Arg Ser Ile Glu Asn Trp Ile Gly Asn Leu Asn Phe Asp
85 90 95Leu Lys Glu Ile Asn Asp Ile Cys Ser Gly Cys Arg Gly His Asp
Gly 100 105 110Phe Thr Ser Ser Trp Arg Ser Val Ala Asp Thr Leu Arg
Gln Lys Val 115 120 125Glu Asp Ala Val Arg Glu His Pro Asp Tyr Arg
Val Val Phe Thr Gly 130 135 140His Ser Leu Gly Gly Ala Leu Ala Thr
Val Ala Gly Ala Asp Leu Arg145 150 155 160Gly Asn Gly Tyr Asp Ile
Asp Val Phe Ser Tyr Gly Ala Pro Arg Val 165 170 175Gly Asn Arg Ala
Phe Ala Glu Phe Leu Thr Val Gln Thr Gly Gly Thr 180 185 190Leu Tyr
Arg Ile Thr His Thr Asn Asp Ile Val Pro Arg Leu Pro Pro 195 200
205Arg Glu Phe Gly Tyr Ser His Ser Ser Pro Glu Tyr Trp Ile Lys Ser
210 215 220Gly Thr Leu Val Pro Val Thr Arg Asn Asp Ile Val Lys Ile
Glu Gly225 230 235 240Ile Asp Ala Thr Gly Gly Asn Asn Gln Pro Asn
Ile Pro Asp Ile Pro 245 250 255Ala His Leu Trp Tyr Phe Gly Leu Ile
Gly Thr Cys Leu 260 2653485PRTBacillus strain NCIB 12513 3His His
Asn Gly Thr Asn Gly Thr Met Met Gln Tyr Phe Glu Trp His1 5 10 15Leu
Pro Asn Asp Gly Asn His Trp Asn Arg Leu Arg Asp Asp Ala Ser 20 25
30Asn Leu Arg Asn Arg Gly Ile Thr Ala Ile Trp Ile Pro Pro Ala Trp
35 40 45Lys Gly Thr Ser Gln Asn Asp Val Gly Tyr Gly Ala Tyr Asp Leu
Tyr 50 55 60Asp Leu Gly Glu Phe Asn Gln Lys Gly Thr Val Arg Thr Lys
Tyr Gly65 70 75 80Thr Arg Ser Gln Leu Glu Ser Ala Ile His Ala Leu
Lys Asn Asn Gly 85 90 95Val Gln Val Tyr Gly Asp Val Val Met Asn His
Lys Gly Gly Ala Asp 100 105 110Ala Thr Glu Asn Val Leu Ala Val Glu
Val Asn Pro Asn Asn Arg Asn 115 120 125Gln Glu Ile Ser Gly Asp Tyr
Thr Ile Glu Ala Trp Thr Lys Phe Asp 130 135 140Phe Pro Gly Arg Gly
Asn Thr Tyr Ser Asp Phe Lys Trp Arg Trp Tyr145 150 155 160His Phe
Asp Gly Val Asp Trp Asp Gln Ser Arg Gln Phe Gln Asn Arg 165 170
175Ile Tyr Lys Phe Arg Gly Asp Gly Lys Ala Trp Asp Trp Glu Val Asp
180 185 190Ser Glu Asn Gly Asn Tyr Asp Tyr Leu Met Tyr Ala Asp Val
Asp Met 195 200 205Asp His Pro Glu Val Val Asn Glu Leu Arg Arg Trp
Gly Glu Trp Tyr 210 215 220Thr Asn Thr Leu Asn Leu Asp Gly Phe Arg
Ile Asp Ala Val Lys His225 230 235 240Ile Lys Tyr Ser Phe Thr Arg
Asp Trp Leu Thr His Val Arg Asn Ala 245 250 255Thr Gly Lys Glu Met
Phe Ala Val Ala Glu Phe Trp Lys Asn Asp Leu 260 265 270Gly Ala Leu
Glu Asn Tyr Leu Asn Lys Thr Asn Trp Asn His Ser Val 275 280 285Phe
Asp Val Pro Leu His Tyr Asn Leu Tyr Asn Ala Ser Asn Ser Gly 290 295
300Gly Asn Tyr Asp Met Ala Lys Leu Leu Asn Gly Thr Val Val Gln
Lys305 310 315 320His Pro Met His Ala Val Thr Phe Val Asp Asn His
Asp Ser Gln Pro 325 330 335Gly Glu Ser Leu Glu Ser Phe Val Gln Glu
Trp Phe Lys Pro Leu Ala 340 345 350Tyr Ala Leu Ile Leu Thr Arg Glu
Gln Gly Tyr Pro Ser Val Phe Tyr 355 360 365Gly Asp Tyr Tyr Gly Ile
Pro Thr His Ser Val Pro Ala Met Lys Ala 370 375 380Lys Ile Asp Pro
Ile Leu Glu Ala Arg Gln Asn Phe Ala Tyr Gly Thr385 390 395 400Gln
His Asp Tyr Phe Asp His His Asn Ile Ile Gly Trp Thr Arg Glu 405 410
415Gly Asn Thr Thr His Pro Asn Ser Gly Leu Ala Thr Ile Met Ser Asp
420 425 430Gly Pro Gly Gly Glu Lys Trp Met Tyr Val Gly Gln Asn Lys
Ala Gly 435 440 445Gln Val Trp His Asp Ile Thr Gly Asn Lys Pro Gly
Thr Val Thr Ile 450 455 460Asn Ala Asp Gly Trp Ala Asn Phe Ser Val
Asn Gly Gly Ser Val Ser465 470 475 480Ile Trp Val Lys Arg
4854773PRTBacillus sp 4Ala Glu Gly Asn Thr Arg Glu Asp Asn Phe Lys
His Leu Leu Gly Asn1 5 10 15Asp Asn Val Lys Arg Pro Ser Glu Ala Gly
Ala Leu Gln Leu Gln Glu 20 25 30Val Asp Gly Gln Met Thr Leu Val Asp
Gln His Gly Glu Lys Ile Gln 35 40 45Leu Arg Gly Met Ser Thr His Gly
Leu Gln Trp Phe Pro Glu Ile Leu 50 55 60Asn Asp Asn Ala Tyr Lys Ala
Leu Ala Asn Asp Trp Glu Ser Asn Met65 70 75 80Ile Arg Leu Ala Met
Tyr Val Gly Glu Asn Gly Tyr Ala Ser Asn Pro 85 90 95Glu Leu Ile Lys
Ser Arg Val Ile Lys Gly Ile Asp Leu Ala Ile Glu 100 105 110Asn Asp
Met Tyr Val Ile Val Asp Trp His Val His Ala Pro Gly Asp 115 120
125Pro Arg Asp Pro Val Tyr Ala Gly Ala Glu Asp Phe Phe Arg Asp Ile
130 135 140Ala Ala Leu Tyr Pro Asn Asn Pro His Ile Ile Tyr Glu Leu
Ala Asn145 150 155 160Glu Pro Ser Ser Asn Asn Asn Gly Gly Ala Gly
Ile Pro Asn Asn Glu 165 170 175Glu Gly Trp Asn Ala Val Lys Glu Tyr
Ala Asp Pro Ile Val Glu Met 180 185 190Leu Arg Asp Ser Gly Asn Ala
Asp Asp Asn Ile Ile Ile Val Gly Ser 195 200 205Pro Asn Trp Ser Gln
Arg Pro Asp Leu Ala Ala Asp Asn Pro Ile Asn 210 215 220Asp His His
Thr Met Tyr Thr Val His Phe Tyr Thr Gly Ser His Ala225 230 235
240Ala Ser Thr Glu Ser Tyr Pro Pro Glu Thr Pro Asn Ser Glu Arg Gly
245 250 255Asn Val Met Ser Asn Thr Arg Tyr Ala Leu Glu Asn Gly Val
Ala Val 260 265 270Phe Ala Thr Glu Trp Gly Thr Ser Gln Ala Asn Gly
Asp Gly Gly Pro 275 280 285Tyr Phe Asp Glu Ala Asp Val Trp Ile Glu
Phe Leu Asn Glu Asn Asn 290 295 300Ile Ser Trp Ala Asn Trp Ser Leu
Thr Asn Lys Asn Glu Val Ser Gly305 310 315 320Ala Phe Thr Pro Phe
Glu Leu Gly Lys Ser Asn Ala Thr Asn Leu Asp 325 330 335Pro Gly Pro
Asp His Val Trp Ala Pro Glu Glu Leu Ser Leu Ser Gly 340 345 350Glu
Tyr Val Arg Ala Arg Ile Lys Gly Val Asn Tyr Glu Pro Ile Asp 355 360
365Arg Thr Lys Tyr Thr Lys Val Leu Trp Asp Phe Asn Asp Gly Thr Lys
370 375 380Gln Gly Phe Gly Val Asn Ser Asp Ser Pro Asn Lys Glu Leu
Ile Ala385 390 395 400Val Asp Asn Glu Asn Asn Thr Leu Lys Val Ser
Gly Leu Asp Val Ser 405 410 415Asn Asp Val Ser Asp Gly Asn Phe Trp
Ala Asn Ala Arg Leu Ser Ala 420 425 430Asp Gly Trp Gly Lys Ser Val
Asp Ile Leu Gly Ala Glu Lys Leu Thr 435 440 445Met Asp Val Ile Val
Asp Glu Pro Thr Thr Val Ala Ile Ala Ala Ile 450 455 460Pro Gln Ser
Ser Lys Ser Gly Trp Ala Asn Pro Glu Arg Ala Val Arg465 470 475
480Val Asn Ala Glu Asp Phe Val Gln Gln Thr Asp Gly Lys Tyr Lys Ala
485 490 495Gly Leu Thr Ile Thr Gly Glu Asp Ala Pro Asn Leu Lys Asn
Ile Ala 500 505 510Phe His Glu Glu Asp Asn Asn Met Asn Asn Ile Ile
Leu Phe Val Gly 515 520 525Thr Asp Ala Ala Asp Val Ile Tyr Leu Asp
Asn Ile Lys Val Ile Gly 530 535 540Thr Glu Val Glu Ile Pro Val Val
His Asp Pro Lys Gly Glu Ala Val545 550 555 560Leu Pro Ser Val Phe
Glu Asp Gly Thr Arg Gln Gly Trp Asp Trp Ala 565 570 575Gly Glu Ser
Gly Val Lys Thr Ala Leu Thr Ile Glu Glu Ala Asn Gly 580 585 590Ser
Asn Ala Leu Ser Trp Glu Phe Gly Tyr Pro Glu Val Lys Pro Ser 595 600
605Asp Asn Trp Ala Thr Ala Pro Arg Leu Asp Phe Trp Lys Ser Asp Leu
610 615 620Val Arg Gly Glu Asn Asp Tyr Val Ala Phe Asp Phe Tyr Leu
Asp Pro625 630 635 640Val Arg Ala Thr Glu Gly Ala Met Asn Ile Asn
Leu Val Phe Gln Pro 645 650 655Pro Thr Asn Gly Tyr Trp Val Gln Ala
Pro Lys Thr Tyr Thr Ile Asn 660 665 670Phe Asp Glu Leu Glu Glu Ala
Asn Gln Val Asn Gly Leu Tyr His Tyr 675 680 685Glu Val Lys Ile Asn
Val Arg Asp Ile Thr Asn Ile Gln Asp Asp Thr 690 695 700Leu Leu Arg
Asn Met Met Ile Ile Phe Ala Asp Val Glu Ser Asp Phe705 710 715
720Ala Gly Arg Val Phe Val Asp Asn Val Arg Phe Glu Gly Ala Ala Thr
725 730 735Thr Glu Pro Val Glu Pro Glu Pro Val Asp Pro Gly Glu Glu
Thr Pro 740 745 750Pro Val Asp Glu Lys Glu Ala Lys Lys Glu Gln Lys
Glu Ala Glu Lys 755 760 765Glu Glu Lys Glu Glu 7705483PRTBacillus
licheniformis 5Ala Asn Leu Asn Gly Thr Leu Met Gln Tyr Phe Glu Trp
Tyr Met Pro1 5 10 15Asn Asp Gly Gln His Trp Lys Arg Leu Gln Asn Asp
Ser Ala Tyr Leu 20 25 30Ala Glu His Gly Ile Thr Ala Val Trp Ile Pro
Pro Ala Tyr Lys Gly 35 40 45Thr Ser Gln Ala Asp Val Gly Tyr Gly Ala
Tyr Asp Leu Tyr Asp Leu 50 55 60Gly Glu Phe His Gln Lys Gly Thr Val
Arg Thr Lys Tyr Gly Thr Lys65 70 75 80Gly Glu Leu Gln Ser Ala Ile
Lys Ser Leu His Ser Arg Asp Ile Asn 85 90 95Val Tyr Gly Asp Val Val
Ile Asn His Lys Gly Gly Ala Asp Ala Thr 100 105 110Glu Asp Val Thr
Ala Val Glu Val Asp Pro Ala Asp Arg Asn Arg Val 115 120 125Ile Ser
Gly Glu His Leu Ile Lys Ala Trp Thr His Phe His Phe Pro 130 135
140Gly Arg Gly Ser Thr Tyr Ser Asp Phe Lys Trp His Trp Tyr His
Phe145 150 155 160Asp Gly Thr Asp Trp Asp Glu Ser Arg Lys Leu Asn
Arg Ile Tyr Lys 165 170 175Phe Gln Gly Lys Ala Trp Asp Trp Glu Val
Ser Asn Glu Asn Gly Asn 180 185 190Tyr Asp Tyr Leu Met Tyr Ala Asp
Ile Asp Tyr Asp His Pro Asp Val 195 200 205Ala Ala Glu Ile Lys Arg
Trp Gly Thr Trp Tyr Ala Asn Glu Leu Gln 210 215 220Leu Asp Gly Phe
Arg Leu Asp Ala Val Lys His Ile Lys Phe Ser Phe225 230 235 240Leu
Arg Asp Trp Val Asn His Val Arg Glu Lys Thr Gly Lys Glu Met 245 250
255Phe Thr Val Ala Glu Tyr Trp Gln Asn Asp Leu Gly Ala Leu Glu Asn
260 265 270Tyr Leu Asn Lys Thr Asn Phe Asn His Ser Val Phe Asp Val
Pro Leu 275 280 285His Tyr Gln Phe His Ala Ala Ser Thr Gln Gly Gly
Gly Tyr Asp Met 290 295 300Arg Lys Leu Leu Asn Gly Thr Val Val Ser
Lys His Pro Leu Lys Ser305 310 315 320Val Thr Phe Val Asp Asn His
Asp Thr Gln Pro Gly Gln Ser Leu Glu 325 330 335Ser Thr Val Gln Thr
Trp Phe Lys Pro Leu Ala Tyr Ala Phe Ile Leu 340 345 350Thr Arg Glu
Ser Gly Tyr Pro Gln Val Phe Tyr Gly Asp Met Tyr Gly 355 360 365Thr
Lys Gly Asp Ser Gln Arg Glu Ile Pro Ala Leu Lys His Lys Ile 370 375
380Glu Pro Ile Leu Lys Ala Arg Lys Gln Tyr Ala Tyr Gly Ala Gln
His385 390 395 400Asp Tyr Phe Asp His His Asp Ile Val Gly Trp Thr
Arg Glu Gly Asp 405 410 415Ser Ser Val Ala Asn Ser Gly Leu Ala Ala
Leu Ile Thr Asp Gly Pro 420 425 430Gly Gly Ala Lys Arg Met Tyr Val
Gly Arg Gln Asn Ala Gly Glu Thr 435 440 445Trp His
Asp Ile Thr Gly Asn Arg Ser Glu Pro Val Val Ile Asn Ser 450 455
460Glu Gly Trp Gly Glu Phe His Val Asn Gly Gly Ser Val Ser Ile
Tyr465 470 475 480Val Gln Arg6483PRTBacillus licheniformis 6Ala Asn
Leu Asn Gly Thr Leu Met Gln Tyr Phe Glu Trp Tyr Met Pro1 5 10 15Asn
Asp Gly Gln His Trp Arg Arg Leu Gln Asn Asp Ser Ala Tyr Leu 20 25
30Ala Glu His Gly Ile Thr Ala Val Trp Ile Pro Pro Ala Tyr Lys Gly
35 40 45Thr Ser Gln Ala Asp Val Gly Tyr Gly Ala Tyr Asp Leu Tyr Asp
Leu 50 55 60Gly Glu Phe His Gln Lys Gly Thr Val Arg Thr Lys Tyr Gly
Thr Lys65 70 75 80Gly Glu Leu Gln Ser Ala Ile Lys Ser Leu His Ser
Arg Asp Ile Asn 85 90 95Val Tyr Gly Asp Val Val Ile Asn His Lys Gly
Gly Ala Asp Ala Thr 100 105 110Glu Asp Val Thr Ala Val Glu Val Asp
Pro Ala Asp Arg Asn Arg Val 115 120 125Ile Ser Gly Glu His Leu Ile
Lys Ala Trp Thr His Phe His Phe Pro 130 135 140Gly Arg Gly Ser Thr
Tyr Ser Asp Phe Lys Trp His Trp Tyr His Phe145 150 155 160Asp Gly
Thr Asp Trp Asp Glu Ser Arg Lys Leu Asn Arg Ile Tyr Lys 165 170
175Phe Gln Gly Lys Ala Trp Asp Trp Glu Val Ser Asn Glu Asn Gly Asn
180 185 190Tyr Asp Tyr Leu Met Tyr Ala Asp Ile Asp Tyr Asp His Pro
Asp Val 195 200 205Ala Ala Glu Ile Lys Arg Trp Gly Thr Trp Tyr Ala
Asn Glu Leu Gln 210 215 220Leu Asp Gly Phe Arg Leu Asp Ala Val Lys
His Ile Lys Phe Ser Phe225 230 235 240Leu Arg Asp Trp Val Asn His
Val Arg Glu Lys Thr Gly Lys Glu Met 245 250 255Phe Thr Val Ala Glu
Tyr Trp Gln Asn Asp Leu Gly Ala Leu Glu Asn 260 265 270Tyr Leu Asn
Lys Thr Asn Phe Asn His Ser Val Phe Asp Val Pro Leu 275 280 285His
Tyr Gln Phe His Ala Ala Ser Thr Gln Gly Gly Gly Tyr Asp Met 290 295
300Arg Lys Leu Leu Asn Gly Thr Val Val Ser Lys His Pro Leu Lys
Ser305 310 315 320Val Thr Phe Val Asp Asn His Asp Thr Gln Pro Gly
Gln Ser Leu Glu 325 330 335Ser Thr Val Gln Thr Trp Phe Lys Pro Leu
Ala Tyr Ala Phe Ile Leu 340 345 350Thr Arg Glu Ser Gly Tyr Pro Gln
Val Phe Tyr Gly Asp Met Tyr Gly 355 360 365Thr Lys Gly Asp Ser Gln
Arg Glu Ile Pro Ala Leu Lys His Lys Ile 370 375 380Glu Pro Ile Leu
Lys Ala Arg Lys Gln Tyr Ala Tyr Gly Ala Gln His385 390 395 400Asp
Tyr Phe Asp His His Asp Ile Val Gly Trp Thr Arg Glu Gly Asp 405 410
415Ser Ser Val Ala Asn Ser Gly Leu Ala Ala Leu Ile Thr Asp Gly Pro
420 425 430Gly Gly Ala Lys Arg Met Tyr Val Gly Arg Gln Asn Ala Gly
Glu Thr 435 440 445Trp His Asp Ile Thr Gly Asn Arg Ser Glu Pro Val
Val Ile Asn Ser 450 455 460Glu Gly Trp Gly Glu Phe His Val Asn Gly
Gly Ser Val Ser Ile Tyr465 470 475 480Val Gln Arg
* * * * *