CN101432411A - Detergent compositions - Google Patents

Abstract

This invention relates to compositions comprising certain lipase variants and a photobleach and processes for making and using such compositions. Including the use of such compositions to clean and/or treat a situs.

Description

Detergent composition

Invention field

The present invention relates to comprise the preparation and the using method of composition and the said products of lipase and optical white.

Background of invention

The formulator that appears as that is applicable to the lipase of washing composition provides a kind of novel method that grease is removed of improving.The hydrolysis of these enzyme catalysis Witepsol W-S 55s, Witepsol W-S 55 are many common greasy dirts, such as the main ingredient of sebum, Tallow, beef (for example lard, butter, butter) and vegetables oil (for example sweet oil, sunflower oil, peanut oil).Yet these enzymes are poor effect in first cycles of washing usually, and is accompanied by stench usually, it is believed that described stench is by the milk preparation dirt, causes as the fat splitting that exists in milk, cream, butter and the sour milk.Be not bound by theory, it is believed that these dirts are easy to produce the stench that is caused by lipase, because they comprise and have short chain (C for example ₄) the functionalized Witepsol W-S 55 of fatty acyl unit, fatty acyl can discharge malodorous voltaile fatty acid after steatolysis.Even improved the performance of these enzymes, the stench problem still exists.Therefore, the purposes of this technology has been subjected to serious restriction.

We have found that the combination of optical white and some lipase Variant can produce the cleaning beneficial effect of improvement, the stench that will make us unhappy reduces to minimum simultaneously.Be not bound by theory, it is believed that following mechanism may produce these beneficial effects: cause having the clean effect of improvement by the synergism between lipase and the optical white, comprise carotenoid, anthocyanidin, porphyrin, tannic acid and flavine material, for example curry, pepper food flavouring, tomato system pasta sauce, coffee ﹠ tea; And washing back optical white is to the oxygenizement of lipase, the oxygenizement that between the dry epoch of cleaning or into treatment sites, takes place for example, thus cause stench to reduce.

Summary of the invention

The present invention relates to comprise the composition of optical white and lipase Variant, the smell that described lipase Variant has minimizing produces trend and good relative performance, and does not have the terminal extension sequence of C-.Lipase Variant is introduced sudden change by one or more zones of determining and is obtained in parent lipase.Thus obtained variant must have and is not less than 80% the active lipase activity of parent lipase, represents with relative performance.

Description of drawings

Fig. 1 represents the lipase sequence alignment.

Sequence list

Sequence identification number: the dna sequence dna of 1 presentation code thermophilic fungus lipase.

Sequence identification number: the aminoacid sequence of 2 expression thermophilic fungus lipase.

Sequence identification number: the aminoacid sequence of the mould lipase of 3 expression colters.

Sequence identification number: the aminoacid sequence of 4 expression absidia corymbifera lipase.

Sequence identification number: the aminoacid sequence of 5 expression rhizomucor miehei lipases.

Sequence identification number: the aminoacid sequence of 6 expression Rhizopus oryzae lipase.

Sequence identification number: the aminoacid sequence of 7 expression aspergillus niger lipase.

Sequence identification number: the aminoacid sequence of 8 expression Tabin aspergillus lipase.

Sequence identification number: the aminoacid sequence of 9 expression Fusarium oxysporum lipase.

Sequence identification number: the aminoacid sequence of 10 expression fusarium heterosporium lipase.

Sequence identification number: the aminoacid sequence of 11 expression aspergillus oryzae lipase.

Sequence identification number: the aminoacid sequence of 12 expression penicillium camembertii lipase.

Sequence identification number: the aminoacid sequence of the smelly aspergillus niger lipase enzyme of 13 expressions.

Sequence identification number: the aminoacid sequence of 14 expression aspergillus niger lipase.

Sequence identification number: the aminoacid sequence of 15 expression aspergillus oryzae lipase.

Sequence identification number: the aminoacid sequence of 16 expression Landerina penisapora lipase.

Detailed Description Of The Invention

Definition

Except as otherwise noted, term used herein " cleaning compositions " comprises particulate state or powdery multifunctional detergent or " heavy duty type " washing composition, especially laundry detergent; Liquid, gel or pasty state multifunctional detergent, especially common described heavy duty type liquid type; Liquid high-count fabric washing composition; Detergent for washing dishware with hand or light-duty dishwashing agent, those of especially high alveolitoid; The machine washing dish washing detergent comprises various sheet, particulate state, liquid and rinse aid type washing composition in family and public place use; Liquid cleaner and sterilant comprise antibiotic hand washing type sanitising agent, washing soap, collutory, denture cleanser, automobile or carpet cleaner, bathroom detergent; Shampoo and profit hair-cream; Bath gels and bubble bath and metal cleaner; And cleaning additive, as bleaching assistant and " decontamination rod " or pre-treatment type auxiliary agent.

As used herein, phrase " be independently selected from the group of forming by following " and be meant be selected from reference to the part of Markush group or element can be identical, can difference maybe can be the arbitrary combination of element.

Must use disclosed testing method in the Test Methods section among the application to measure each parameter value of applicant's invention.

Except as otherwise noted, all components or composition levels all based on the activity substance content of this component or composition, do not comprise the impurity that may be present in the commercial sources, for example residual solvent or byproduct.

Except as otherwise noted, all per-cents and ratio are all calculated by weight.Except as otherwise noted, all per-cents and ratio all calculate based on total composition.

Should be appreciated that each higher limit that provides in this manual comprises each lower value, is also clearly represented in this article as described lower value.Each lower value that provides in this specification will comprise each higher limit, also clearly be represented at this paper as described higher limit.Each numerical range that provides in this specification will comprise all narrower numerical ranges that are contained in this broader numerical, also clearly be represented at this paper as described narrower numerical range.

The relevant part of all references all is incorporated herein with way of reference.Quoting of any document may not be interpreted as its approval as prior art of the present invention.

Composition

Composition of the present invention comprises about 0.0001% to about 1% usually, about 0.0002% to about 0.5%, or about 0.0005% to about 0.3% optical white and about 0.0005% to about 0.1%, about 0.001% is to about 0.05%, or about 0.002% to about 0.03% lipase.

These compositions can be any form, for example, and the form of cleaning compositions and/or the form of treatment compositions.

The surplus of any aspect of above-mentioned cleaning compositions is made up of one or more auxiliary substances.

The lipase Variant that is suitable for

The lipase of composition of the present invention is a kind of lipase Variant, the terminal extension sequence of its no C-, but introduce sudden change in some zone of parent lipase, thus the trend that produces smell reduced.

Parent lipase

Parent lipase can be a fungal lipase, and described in " homology and sequence alignment " part, its aminoacid sequence has and sequence identification number: the homology of the thermophilic fungus lipase sequence at least 50% that shows in 2.

Parent lipase can be a yeast polypeptides, for example candiyeast, kluyveromyces, pichia spp, yeast, fission yeast or Ye Shi yeast polypeptides; Or filamentous fungus polypeptide more preferably, for example top spore mould, aspergillus tubigensis, short stalk mould, cryptococcus, line black powder yeast, sickle mycete, humic mould, Pyricularia oryzae, mucormycosis, ruin a mould, Xin Kaoma fat mould, neurospora, paecilomycerol, Penicillium notatum, cud fungi, Split-gill, yellow silk aspergillus tubigensis, thermophilic ascomycete, grass roots mould, Trichoderma or Trichoderma polypeptide.

One preferred aspect, parent lipase is Ka Ersibai yeast, cereuisiae fermentum, saccharomyces diastaticus, Douglas yeast, kluyveromyces, Nuo Shi yeast or the ellipsoideus yeast polypeptide with lipase activity.

Another preferred aspect, parent lipase is a microorganism Aspergillus aculeatus, Aspergillus awamori, Aspergillus fumigatus, smelly aspergillus, aspergillus japonicus, Aspergillus nidulans, aspergillus niger, aspergillus oryzae, Tabin aspergillus, sickle spore bacterioide, the wheat wilt, sickle spore bacterium, fusarium culmorum, Fusarium graminearum, the red sickle spore of standing grain, fusarium heterosporium, the five-leaved chaste tree sickle-like bacteria, Fusarium oxysporum, netted sickle-like bacteria, the moniliform sickle-like bacteria, fusarium sambucinum, colour of skin sickle spore, Fusarium sporotrichioides, fusarium sulphureum, bunch capsule sickle-like bacteria, fusarium trichothecioides, fusarium, special humicola lanuginosa, thermophilic fungus (synonym: the high temperature chactomium globosum), the rice black wool is mould, thermophilic ruin the silk mould, Neurospora, penicillium purpurogenum, trichoderma harziarum, healthy and free from worry wood is mould, long shoot wood is mould, Trichodermareesei, or viride polypeptide.

Another preferred aspect, parent lipase is that thermophilic fungus belongs to lipase.

One preferred aspect, parent lipase is a thermophilic fungus lipase.In a preferred embodiment, parent lipase is a sequence identification number: 2 lipase.

Zone identification and replacement.

The area I of hereinafter mentioning to the site of area I V is a sequence identification number: the amino-acid residue site in 2.Use the described method of " homology and sequence alignment " part to find (or homologous) site corresponding in the different lipase.

Replacement in the area I

Area I is made up of the amino-acid residue around N-terminal residue E1.Preferably in this zone replace amino acid in the parent lipase with amino acid with more positive electricity.Area I comprises the amino-acid residue in corresponding following site: 1 to 11 and 223-239.Following site has special significance: 1,2,4,8,11,223,227,229,231,233,234 and 236.Specifically, confirmed following replacement: X1N/ ^*, X4V, X227G, X231R and X233R.

In a preferred embodiment, parent lipase and sequence identification number: 2 have at least 80%, such as 85% or 90%, and the identity such as at least 95% or 96% or 97% or 98% or 99%.In a preferred embodiment, parent lipase and sequence identification number: 2 is identical.

Replacement among the area I I

Area I I by on the one side of acyl chain with one side at alcohol moiety on contact substrate amino-acid residue form.Preferred in this zone with the amino acid that replaces with the amino acid of more positive electricity or low hydrophobic amino acid in the parent lipase.Area I I comprises the amino-acid residue in corresponding following site: 202 to 211 and 249 to 269.Following site has special significance: 202,210,211,253,254,255,256,259.Specifically, following replacement: X202G, X210K/W/A, X255Y/V/A, X256K/R and X259G/M/Q/V have been confirmed.

In a preferred embodiment, parent lipase and sequence identification number: 2 have at least 80%, such as 85% or 90%, and the identity such as at least 95% or 96% or 97% or 98% or 99%.In a preferred embodiment, parent lipase and sequence identification number: 2 is identical.

Replacement among the area I II

Thereby area I II forms by forming the amino-acid residue that flexible structure allows substrate to enter avtive spot.Preferred in this zone with the amino acid that replaces with the amino acid of more positive electricity or low hydrophobic amino acid in the parent lipase.Area I II comprises the amino-acid residue in corresponding following site: 82 to 102.Following site has special significance: 83,86,87,90,91,95,96,99.Specifically, following replacement: X83T, X86V and X90A/R have been confirmed.

In a preferred embodiment, parent lipase and sequence identification number: 2 have at least 80%, such as 85% or 90%, and the identity such as at least 95% or 96% or 97% or 98% or 99%.In a preferred embodiment, parent lipase and sequence identification number: 2 is identical.

Replacement among the area I V

Area I V is made up of the amino-acid residue that static is bonded to the surface.Preferably in this zone replace amino acid in the parent lipase with amino acid with more positive electricity.Area I V comprises the amino-acid residue in corresponding following site: 27 and 54 to 62.Following site has special significance: 27,56,57,58,60.Following replacement: X27R, X58N/AG/T/P and X60V/S/G/N/R/K/A/L have been confirmed specifically.

In a preferred embodiment, parent lipase and sequence identification number: 2 have at least 80%, such as 85% or 90%, and the identity such as at least 95% or 96% or 97% or 98% or 99%.In a preferred embodiment, parent lipase and sequence identification number: 2 is identical.

The amino acid in other site

Parent lipase can randomly comprise other amino acid whose replacement, especially is less than 10 or be less than 5 such replacements.Embodiment is the replacement corresponding to the one or more sites in parent lipase 24,37,38,46,74,81,83,115,127,131,137,143,147,150,199,200,203,206,211,263,264,265,267 and 269.In a particular embodiment, replacement occurs in corresponding to wherein at least one site in 81,143,147,150 and 249 sites.In a preferred embodiment, at least one replacement is selected from the group of being made up of following: X81Q/E, X143S/C/N/D/A, X147M/Y, X150G/K and X249R/I/L.

Variant can be included in the replacement outside the I to IV of localized area, replacement quantity outside the I to IV of localized area preferably is less than six or be less than five or be less than four or be less than three or be less than two, such as five or four or three or two or one.Alternatively, variant does not comprise any replacement outside the I to IV of localized area.

For example, can more replace the replacement described in WO92/05249, WO94/25577, WO95/22615, WO97/04079 and WO97/07202 according to rule known in the art.

Parent's fat variant

In one aspect, when comparing with described parent, described variant comprises at least three replacements of total, and described replacement is selected from one or more by the following group of forming:

A) at least two in the area I or at least three or at least four or at least five or at least six, such as two, three, four, five or six replacements,

B) at least one among the area I I, at least two or at least three or at least four or at least five or at least six, such as one, two, three, four, five or six replacements,

C) at least one among the area I II, at least two or at least three or at least four or at least five or at least six, such as one, two, three, four, five or six replacements,

D) at least one and/or among the area I V, at least two or at least three or at least four or at least five or at least six, such as one, two, three, four, five or six replacements.

Variant is compared with the parent of variant can comprise replacement, and described replacement is corresponding to those replacements of listing in the following table 1.

Area I	Area I I	Area I II	Area I V	Outside the zone
					X4V+X227G+ X231R+X233R	X210K+X256K	X83T+X86V	X58A+X60S	X150G
X227G+X231R+ X233R	X256K	X86V	X58N+X60S	X150G
					X231R+X233R	X255Y
X231R+X233R	X202G
					X227G+X231R+ X233R	X256K	X86V
X4V+X231R+ X233R			X58N+X60S
					X231R+X233R		X90R	X58N+X60S
X231R+X233R	X255V	X90A
					X227G+X231R+ X233R	X256K	X86V	X58N+X60S	X150G
X231R+X233R	X211L		X58N+X60S	X147M
					X231R+X233R				X150K

Table 1: some special variants

Parent lipase and sequence identification number: 2 is identical more in the certain embodiments at one, and therefore the variant of table 1 will be:

Area I	Area I I	Area I II	Area I V	Outside the zone
					Q4V+L227G+ T231R+N233R	E210K+P256K	S83T+I86V	S58A+V60S	A150G
L227G+T231R+ N233R	P256K	I86V	S58N+V60S	A150G
					T231R+N233R	I255Y
T231R+N233R	I202G
					L227G+T231R+ N233R	P256K	I86V
Q4V+T231R+ N233R			S58N+V60S
					T231R+N233R		I90R	S58N+V60S
T231R+N233R	I255V	I90A
					L227G+T231R+ N233R	P256K	I86V	S58N+V60S	A150G
T231R+N233R	F211L		S58N+V60S	L147M
					T231R+N233R				A150K

Table 2: sequence identification number: some specific variants of 2

Amino acid modified name

When describing as described in the present invention lipase Variant, use following nomenclature to be beneficial to reference: initial amino acid: site: substituted amino acid

According to this nomenclature, for example the L-glutamic acid with 195 places, site is substituted by glycine, is expressed as G195E.Words at identical site disappearance glycine are expressed as G195 ^*, and insert additional amino-acid residue such as Methionin is expressed as G195GK.Compare with other lipase for one, comprise one in the site " disappearance " amino acid of 36, the specific lipase that inserts an aspartic acid simultaneously in this site is expressed as ^*36D.A plurality of sudden changes are separated with plus sige, that is: R170Y+G195E is illustrated in site 170 and 195 places and respectively tyrosine and L-glutamic acid is substituted by arginine and glycine.

When using described sequence alignment method, X231 is illustrated in parent's polypeptide the amino acid corresponding to site 231.X231R represents that this amino acid replaces with R.Concerning sequence identification number: 2 X are T, and therefore be illustrated in 231 places, site replaces T with R to X231R.When the amino acid of a site (for example 231) can be selected from one group of amino acid whose aminoacid replacement with another, for example, form by R and P and Y for described group, represent with X231R/P/Y.

In all cases, use the IUPAC single-letter or the trigram amino acid abbreviations of generally acknowledging.

The amino acid grouping

In this manual, amino acid is divided into electronegative, positively charged or electroneutral amino acid according to its electric charge under the pH10 condition.Therefore, electronegative amino acid is E, D, C (halfcystine) and Y, especially E and D.The amino acid of positively charged is R, K and H, especially R and K.When forming disulfide linkage, neutral amino acids is G, A, V, L, I, P, F, W, S, T, M, N, Q and C.By the another kind of aminoacid replacement in same group (electronegative, positively charged or electric neutrality), be called as conservative the replacement.

That neutral amino acids can be divided into is hydrophobic or nonpolar (G, A, V, L, I, P, F, W and as the C of the part of disulfide linkage) and hydrophilic or polar (S, T, M, N, Q).

Amino acid identity

With parameter " identity " dependency between two aminoacid sequences or two nucleotide sequences is described.

For purposes of the invention, by using comparison from two aminoacid sequences of Needle program determination of EMBOSS package (http://emboss.org) 2.8.0 version.The Needle program is used the overall comparison algorithm, and this arthmetic statement is in Needleman, S.B. and Wunsch, and C.D. (1970) J.Mol.Biol.48, the substitution matrix that 443-453. uses is BLOSUM62, and the open point penalty in room is 10, and it is 0.5 that point penalty is expanded in the room.

Aminoacid sequence of the present invention (" invention sequence "; Sequence identification number for example: 2 amino acid/11 to 269) and the identity degree between the difference aminoacid sequence (" external sequence ") calculate by the following method: the accurate matching number of two sequence alignments is divided by the length of " invention sequence " or the length of " external sequence ", and the length of whichever sequence is the shortest.The result is expressed as identity per-cent.

When " invention sequence " had identical amino-acid residue with " external sequence " in the identity site of lap, accurate coupling can take place.Sequence length is the number (for example sequence identification number: 2 length is 269) of the amino-acid residue in the sequence.

Parent lipase have with thermophilic fungus lipase (sequence identification number: 2) at least 50%, especially at least 55%, at least 60%, at least 75%, at least 85%, at least 90%, surpass 95% or surpass 98% homology.In a particular embodiment, parent lipase is identical with thermophilic fungus lipase (sequence identification number 2).

Can use aforesaid method calculating identity and homology and be used for sequence alignment.Under situation of the present invention, homology and sequence alignment are calculated as follows.

Homology and sequence alignment

For purposes of the invention, by computer program known in the art, as GAP (Program Manual for the Wisconsin Package, the 8th edition, in the August, 1994 that is provided in the GCG routine package, Genetics Computer Group, 575 Science Drive, Madison, Wisconsin, USA 53711) (Needleman, S.B. and Wunsch, C.D., (1970), " Journal of Molecular Biology ", 48,443-45), use to have the GAP that following peptide sequence contrast is provided with, measuring homology degree: GAP generation point penalty aptly is 3.0, and GAP extension point penalty is 0.1.

In the present invention, (synonym: corresponding (or homologous) site is determined by the sequence alignment that shows among Fig. 1 the high temperature chactomium globosum) and in the Landerina penisapora lipase sequence for mould, the absidia corymbifera of colter, rice black root Mucor, Dai Shi head mold, aspergillus niger, Tabin aspergillus, Fusarium oxysporum, fusarium heterosporium, aspergillus oryzae, penicillium camembertii, smelly aspergillus, aspergillus niger, thermophilic fungus.

In order to find the homologous site that is not presented in the lipase sequence in the sequence alignment, the sequence that shows among the sequence paid close attention to and Fig. 1 is compared.Carry out the GAP sequence alignment by the highest sequence of homology that the GAP program is found, the existing sequence among new sequence and Fig. 1 is compared.(August 1994 for Program Manual for the Wisconsin Package, Version8 for the GCG routine package, Genetics Computer Group, 575 Science Drive, Madison, Wisconsin, USA 53711) (Needleman, S.B. and Wunsch, C.D., (1970), Journal of Molecular Biology, 48,443-45) provide GAP.It is 3.0 that peptide sequence relatively uses following setting: GAP to produce point penalty, and it is 0.1 that GAP extends point penalty.

Parent lipase have with thermophilic fungus lipase (sequence identification number: 2) at least 50%, especially at least 55%, at least 60%, at least 75%, at least 85%, at least 90%, surpass 95% or surpass 98% amino acid identity.In a particular embodiment, parent lipase and thermophilic fungus lipase (sequence identification number: 2) identical.

Hybridization

The present invention also relates to by polynucleotide encoding, isolated polypeptide with lipase activity, described polynucleotide are under low-down preciseness condition, under the preferred low preciseness condition, more preferably under the preciseness condition, more preferably in-Gao preciseness condition under, even under the more preferably high preciseness condition, under the most preferably very high preciseness condition, hybridize with following nucleotide sequences: (i) Nucleotide 178 to 660, sequence identification number: 1, (ii) be included in the cDNA sequence of Nucleotide 178 to 660, sequence identification number: 1, (iii) (i) or sequence (ii), or (iv) (i), (ii) or complementary strand (J.Sambrook (iii), E.F.Fritsch, and T.Maniatus, 1989, Molecular Cloning, ALaboratory Manual, 2d edition, Cold Spring Harbor, New York).Sequence identification number: 1 subsequence comprise at least 100 in abutting connection with Nucleotide or preferably at least 200 in abutting connection with Nucleotide.In addition, the subsequence codified has the polypeptide fragment of lipase activity.

Concerning length is the long probe of at least 100 Nucleotide, prehybridization and the hybridization of very high preciseness conditional definition for carrying out under the following conditions will be low to moderate very much: 42 ℃, 5X SSPE, 0.3%SDS, that 200ug/mL has sheared and the milt DNA of sex change, perhaps 25% formyl ammonia is used for very low and low preciseness condition, 35% formyl ammonia is used for neutralization-Gao preciseness condition, perhaps 50% formyl ammonia is used for high and very high preciseness condition, standard Southern hybridization program hybridization most preferably 12 to 24 hours.

Concerning length is the long probe of at least 100 Nucleotide, use 2X SSC, 0.2%SDS is preferably at least 45 ℃ (low-down preciseness), more preferably at least 50 ℃ (low preciseness), more preferably at least 55 ℃ (middle preciseness), more preferably at least 60 ℃ (in-Gao preciseness), even more preferably at least 65 ℃ (high preciseness), most preferably at least 70 ℃ (very high preciseness), last wash vehicle material three times, each 15 minutes.

Dna sequence dna, expression vector, host cell, lipase production

The invention provides code book invention lipase dna sequence dna, comprise the expression vector of described dna sequence dna and comprise the transformed host cell of described dna sequence dna or described expression vector.They can obtain by methods known in the art.

The present invention also provides the method for producing lipase, and this method is by cultivating transformant and regain lipase yielding lipase in next life from the gained broth culture under being of value to the condition of producing lipase.Described method is carried out according to principle known in the art.

Lipase activity

-under neutral pH (LU) condition to the lipase activity of tributyrin

Use Sudan Gum-arabic as emulsifying agent, emulsification tributyrin (tributyrin) prepares the lipase substrate.Then in the constant burette test of pH-, at 30 ℃, hydrolysis tributyrin under pH7 or the pH9 condition.One unit lipase activity (1LU) is equivalent to can be under the pH7 condition, and per minute discharges the butyro-enzyme amount of 1 micromole.

-imitate dangerous

With describe performance and smell reduce risks than effect danger coefficient be defined as: BR=RP _Avg/ R.Lipase Variant as herein described can have greater than 1, greater than 1.1, or even greater than the dangerous coefficient of 1 to about 1000 effect.

-average relative performance

The program of calculating average relative performance (RPavg) is present among the embodiment 5 of this specification sheets.Lipase Variant as herein described can have at least 0.8, at least 1.1, at least 1.5, or even at least 2 to about 1000 average relative performance (RPavg).

The optical white that is suitable for

The optical white that is suitable for comprises catalysis optical white and light trigger.The catalysis optical white that is suitable for is selected from the group of being made up of the water soluble metal phthalocyanine with following chemical formula:

Or

Wherein:

PC is the phthalocyanine ring system;

Me is Zn; Fe (II); Ca; Mg; Na; K; Al-Z ₁Si (IV); P (V); Ti (IV); Ge (IV); Cr (VI); Ga (III); Zr (IV); In (III); Sn (IV) or Hf (VI);

Z ₁Be halogenide; Vitriol; Nitrate; Carboxylate; Alkanol; Or hydroxide ion;

Q is 0; 1 or 2;

R is 1 to 4;

Q ₁, be sulfo group or carboxylic group; Or chemical formula group

-SO ₂X ₂-R ₁-X ₃ ⁺-O-R ₁-X ₃ ⁺Or-(CH ₂) ,-Y ₁ ⁺

Wherein

R ₁Be C collateralization or non-collateralization ₁-C ₈Alkylidene group; Or 1,3-or 1,4-phenylene;

X ₂Be-NH-; Or-N-C ₁-C ₅Alkyl;

X ₃ ⁺It is the following formula group

Perhaps, at R ₁=C ₁-C ₈Under the situation of alkylidene group, also be the following formula group

Or

Y ₁ ⁺It is the following formula group

Or

T is 0 or 1

Wherein in following formula

R ₂And R ₃Be C independently of one another ₁-C ₆Alkyl

R ₄Be C ₁-C ₅Alkyl; C ₅-C ₇Cycloalkyl or NR ₇R ₈

R ₅And R ₆Be C independently of one another ₁-C ₅Alkyl;

R ₇And R ₈Be hydrogen or C independently of one another ₁-C ₅Alkyl;

R ₉And R ₁₀Be not replace C independently of one another ₁-C ₆Alkyl or replacement C ₁-C ₆Alkyl, substituted alkyl is by hydroxyl, cyano group, carboxyl, carb-C ₁-C ₆Alkoxyl group, C ₁-C ₆Alkoxyl group, phenyl, naphthyl or pyridyl replace;

U is 1 to 6;

A ₁Be the unit that constitutes aromatics 5-to 7-unit nitrogen heterocyclic, in the ring suitable position also can comprise again one or two nitrogen-atoms as ring members and

B ₁Be the unit that constitutes the first nitrogen heterocyclic of saturated 5-to 7-, suitable position also can comprise 1 to 2 nitrogen, oxygen and/or sulphur atom as ring members in the ring;

Q ₂It is hydroxyl; C ₁-C ₂₂Alkyl; Side chain C ₃-C ₂₂Alkyl; C ₂-C ₂₂Thiazolinyl; Side chain C ₃-C ₂₂Thiazolinyl and their mixture; C ₁-C ₂₂Alkoxyl group; Sulfo group or carboxyl; The following formula group

-SO ₂(CH ₂) _V-OSO ₃M；-SO ₂(CH ₂) _V-SO ₃M；

The branched alkoxy group of following formula

The vinyloxy group alkyl unit of following formula

-(T ₁)d-(CH ₂) _b(OCH ₂CH ₂) _a-B ₃

Or the ester of following formula

COOR ₁₈

Wherein

B ₂Be hydrogen; Hydroxyl; C ₁-C ₃₀Alkyl; C ₁-C ₃₀Alkoxyl group;-CO ₂H;-CH ₂COOH;-SO ₃-M ₁-OSO ₃-M ₁-PO ₃ ^2-M ₁-OPO ₃ ^2-M ₁And their mixture;

B ₃Be hydrogen; Hydroxyl;-COOH;-SO ₃-M ₁-OSO ₃M ₁Or C ₁-C ₆Alkoxyl group;

M ₁It is water-soluble cationic;

T ₁Be-O-; Or-NH-;

X ₁And X ₄Be independently of one another-O-;-NH-or-N-C ₁-C ₅Alkyl;

R ₁₁And R ₁₂Be hydrogen independently of one another; Sulfo group and salt thereof; Carboxyl and salt thereof or hydroxyl; R ₁₁And R ₁₂In the base at least one is sulfo group or carboxyl or their salt,

Y ₂Be-O-;-S-;-NH-or-N-C ₁-C ₅Alkyl;

R ₁₃And R ₁₄Be hydrogen independently of one another; C ₁-C ₆Alkyl; Hydroxyl-C ₁-C ₆Alkyl; Cyano group-C ₁-C ₆Alkyl; Sulfo group-C ₁-C ₆Alkyl; Carboxyl or halogen-C ₁-C ₆Alkyl; The phenyl that unsubstituted phenyl or halogen replace, C ₁-C ₄Alkyl or C ₁-C ₄Alkoxyl group; Sulfo group or carboxyl or R ₁₃And R ₁₄And nitrogen-atoms, they are incorporated on the nitrogen-atoms to form saturated 5-or 6-unit heterocycle, and heterocycle also can additionally comprise nitrogen-atoms or the Sauerstoffatom member as ring;

R ₁₅And R ₁₆Be C independently of one another ₁-C ₆Alkyl or aryl-C ₁-C ₆Alkyl;

R ₁₇Be hydrogen; Unsubstituted C ₁-C ₆The C of alkyl or replacement ₁-C ₆Alkyl, substituted alkyl is by halogen, hydroxyl, cyano group, phenyl, carboxyl, carb-C ₁-C ₆Alkoxyl group or C ₁-C ₆Alkoxyl group replaces;

R ₁₈Be C ₁-C ₂₂Alkyl; Side chain C ₃-C ₂₂Alkyl; C ₁-C ₂₂Thiazolinyl or side chain C ₃-C ₂₂Thiazolinyl; C ₃-C ₂₂Ethylene glycol; C ₁-C ₂₂Alkoxyl group; Side chain C ₃-C ₂₂Alkoxyl group; And their mixture;

M is a hydrogen; Or alkalimetal ion or ammonium ion,

Z ₂ ^-Be chlorine; Bromine; Alkyl-sulphate or aromatic sulfuric acid salt ion;

A is 0 or 1;

B is 0 to 6;

C is 0 to 100;

D is 0; Or 1;

E is 0 to 22;

V is 2 to 12 integer;

W is 0 or 1; With

A ^-Be organic or inorganic ion and

S is at monovalent anion A ^-Situation under equal r, under the situation of multivalent anions, be less than or equal to r, A _s ^-For the compensation positive charge is essential; If wherein r is not equal to 1, Q ₁Base can be identical or different,

And wherein the phthalocyanine ring system also can comprise solubilizing group in addition;

Other suitable catalysis optical white comprises xanthene dyestuff and their mixture.On the other hand, suitable catalysis optical white is selected from the group of being made up of following: sulfonation phthalocyanine phthalocyanine zinc, aluminum phthalocyanine, Eosin Y, Phoxine B, Rose Bengal, C.I. Food Red 14 and their mixture.But on the other hand, suitable catalysis optical white can be the mixture of sulfonation phthalocyanine phthalocyanine zinc and aluminum phthalocyanine, and the sulfonation phthalocyanine phthalocyanine zinc of described mixture and the weight ratio of aluminum phthalocyanine be greater than 1, greater than 1 less than about 100, perhaps even from about 1 to about 4.

Suitable light trigger is selected from the group of being made up of following: aromatics 1, and the 4-quinone is anthraquinone and naphthoquinones for example; The α keto-amine, especially those comprise the keto-amine of benzoyl part, are called alpha-aminoacetophenone in addition; α hydroxyketone, especially Alpha-hydroxy methyl phenyl ketone; The phosphorated light trigger comprises monoacyl, two acyl group and three acyl group phosphine oxide and sulfide; The dialkoxy methyl phenyl ketone; Alpha-halo acetophenone; Three acyl group phosphine oxides; Bitter almond oil camphor and bitter almond oil camphor base light trigger and their mixture.On the other hand, suitable light trigger is selected from the group of being made up of following: 2-ethyl-anthraquinone; Vitamin K3; 2-sulfuric acid-anthraquinone; 2-methyl 1-[4-phenyl]-2-morpholinyl-1-ketone (

907); (2-benzyl-2-dimethylamino-1-(4-morpholinyl phenyl)-Ding-1-ketone (

369); (1-[4-(2-hydroxy ethoxy)-phenyl]-2 hydroxy-2-methyls-1-third-1-ketone) (

2959); 1-hydroxy-cyclohexyl phenyl-ketone (

184); Oligomerization [2-hydroxyl 2-methyl isophthalic acid-[4 (1-methyl)-phenyl] acetone (

KIP 150); 2-4-6-(Three methyl Benzene formyl) phenylbenzene-phosphine oxide, two (2,4,6-Three methyl Benzene formyl)-phenyl-phosphine oxides (

819); (2,4,6 Three methyl Benzene formyl) phosphenylic acid ethyl ester (

TPO-L); And their mixture.

Can be used in combination above-mentioned optical white (can use the mixture of any optical white).Suitable optical white can be available from Aldrich, Milwaukee, Wisconsin, USA; FrontierScientific, 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, Rhode Island, USA; And/or the optical white made of the embodiment that comprises according to this paper.

Promoter material

Though it is optional for the present invention, but hereinafter the non-limiting tabulation of illustrational auxiliary substance be applicable to the present composition, and can expect it is merged among some embodiment of the present invention, for example helping or to improve the clean-up performance of handling substrate to be cleaned, or under the situation that contains spices, tinting material, dyestuff etc., regulate the aesthetic property of cleaning compositions.The physical form that the clear and definite character of these annexing ingredients and incorporation thereof will depend on composition with and the character of the clean operation used.Suitable promoter material includes but not limited to tensio-active agent, washing assistant, sequestrant, dye transfer inhibitor, dispersion agent, additional enzyme and enzyme stabilizers, catalytic specie, bleach-activating agent, hydrogen peroxide, hydrogen peroxide cource, preformed peracid, the dispersion agent of polymkeric substance, clay soil removes/anti-redeposition agent, whitening agent, suds suppressor, dyestuff, fabric hueing agent, spices, the structural elasticity agent, fabric softener, carrier, hydrotropic agent, processing aid, solvent and/or pigment.Except the following discloses content, the suitable embodiment and the consumption of these other auxiliary agents also are present in United States Patent (USP) 5,576, and among 282,6,306,812 B1 and 6,326,348 B1, described document is introduced for your guidance.

Such as statement, ancillary component is not that applicant's composition is necessary.Therefore, some embodiment of applicant's composition does not comprise one or more following promoter materials: tensio-active agent, washing assistant, sequestrant, dye transfer inhibitor, dispersion agent, additional enzyme and enzyme stabilizers, catalytic specie, bleach-activating agent, hydrogen peroxide, hydrogen peroxide cource, preliminary shaping peracid, polymeric dispersant, clay soil remove/and anti-redeposition agent, whitening agent, suds suppressor, dyestuff, spices, structural elasticity agent, fabric softener, carrier, hydrotropic agent, processing aid, solvent and/or pigment.Yet when having one or more auxiliary agents, these one or more auxiliary agents can exist as detailed below:

SYNTHETIC OPTICAL WHITNER-cleaning compositions of the present invention can comprise one or more SYNTHETIC OPTICAL WHITNER.The suitable SYNTHETIC OPTICAL WHITNER that is different from bleaching catalyst comprises optical white, bleach-activating agent, hydrogen peroxide, hydrogen peroxide cource, preliminary shaping peracid and their mixture.Usually, when using SYNTHETIC OPTICAL WHITNER, composition of the present invention can comprise by the weight of this theme cleaning compositions about 0.1% to about 50%, or even about 0.1% to about 25% SYNTHETIC OPTICAL WHITNER.The example of suitable SYNTHETIC OPTICAL WHITNER comprises:

(1) preliminary shaping peracid: suitable preliminary shaping peracid includes but not limited to be selected from the compound of being made up of following: percarboxylic acids and salt thereof, percarbonic acid and salt thereof, mistake imidic acid and salt, permonosulphuric acid and salt thereof are (for example ) and their mixture.Suitable percarboxylic acids comprises the hydrophobic and hydrophilic peracid with molecular formula R-(C=O) O-O-M, and wherein R is an alkyl, optional branched-chain alkyl.When peracid when being hydrophobic, it has 6 to 14 carbon atoms or 8 to 12 carbon atoms.When peracid when being hydrophilic, its have less than 6 carbon atoms or even less than 4 carbon atoms; And M is counter ion, for example sodium, potassium or hydrogen;

(2) hydrogen peroxide cource, for example inorganic over hydrogenation adduct salt comprises following an alkali metal salt such as sodium salt: perborate (being generally monohydrate or tetrahydrate), percarbonate, persulphate, superphosphate, persilicate and their mixture.In one aspect of the invention, inorganic over hydrogenation adduct salt is selected from the group of being made up of following: peroxyboric acid sodium salt, percarbonic acid sodium salt and their mixture.If be used, inorganic over hydrogenation adduct salt exists with 0.05 to 40% weight of total composition or the content of 1 to 30% weight usually, and usually as can coated crystalline solid being incorporated in this composition.Suitable coating compounds comprises: inorganic salt such as alkalimetal silicate, carbonate or borate or their mixture, or organism such as water-soluble or dispersible polymer, wax, oil or fatty soap; With

(3) have the bleach-activating agent of R-(C=O)-L, wherein R is an alkyl, optional branched-chain alkyl.When bleach-activating agent when being hydrophobic, it has 6 to 14 carbon atoms or 8 to 12 carbon atoms.When bleach-activating agent when being hydrophilic, its have less than 6 carbon atoms or even less than 4 carbon atoms; And L is a leavings group.The example of suitable leavings group is phenylformic acid and derivative thereof, especially benzene sulfonate.Suitable bleach-activating agent comprises dodecane acyl-oxygen base benzene sulfonate, last of the ten Heavenly stems acyloxy benzene sulfonate, caprinoyl aminobenzoic acid and salt, 3 thereof; 5,5-trimethyl acetyl oxygen base benzene sulfonate, tetra acetyl ethylene diamine (TAED) and nonanoly acyloxy benzene sulfonate (NOBS).Suitable bleach-activating agent also is disclosed among the WO 98/17767.Although can adopt any suitable bleach-activating agent, in one aspect of the invention, the cleaning compositions of this theme can comprise NOBS, TAED or their mixture.

If present, peracid and/or bleach-activating agent usually with based on described composition about 0.1 to about 60% weight, about 0.5 to about 40% weight, perhaps in addition about 0.6 content to about 10% weight be present in the described composition.One or more hydrophobic peracids or its precursor can be united use with one or more hydrophilic peracid or its precursor.

Can select the amount of hydrogen peroxide cource and peracid or bleach-activating agent, make that the mol ratio of available oxygen (from peroxide source) and peracid is 1:1 to 35:1, perhaps even 2:1 to 10:1.

Tensio-active agent-cleaning compositions can comprise tensio-active agent or surfactant system as described in the present invention, and wherein said tensio-active agent can be selected from nonionogenic tenside, anion surfactant, cats product, amphoterics, zwitterionics, semi-polar nonionic surfactants and their mixture.If present, tensio-active agent usually in by the weight of this theme composition about 0.1% to about 60%, about 1% to about 50% or even about 5% to about 40% content exist.

Washing assistant-cleaning compositions of the present invention can comprise one or more detergent builder or builder system.When using washing assistant, this theme composition will comprise weight by this theme composition usually at least about 1%, and about 5% to about 60%, perhaps even about 10% to about 40% washing assistant.Washing assistant includes but not limited to: basic metal, the poly-phosphate of ammonium and alkanol ammonium, alkalimetal silicate, alkaline-earth metal and alkaline carbonate, silico-aluminate washing assistant and polycarboxylic acid salt compound, the ether hydroxy-polycarboxylate, the multipolymer of maleic anhydride and ethene or vinyl methyl ether, 1,3,5-trihydroxybenzene-2,4, the 6-trisulfonic acid, with the carboxymethyl oxysuccinic acid, polynary acetate (as ethylenediamine tetraacetic acid (EDTA) and nitrilotriacetic acid(NTA)) and polycarboxylic acid are (as mellitic acid, succsinic acid, citric acid, oxygen di-succsinic acid, polynary toxilic acid, 1,3,5-three phenylformic acid, the carboxymethyl oxysuccinic acid) various an alkali metal salts, ammonium salt and substituted ammonium salt, and their soluble salt.

Sequestrant-this paper cleaning compositions can comprise sequestrant.Suitable sequestrant comprises copper, iron and/or manganese sequestrant and their mixture.When using sequestrant, this theme composition can comprise by the weight of this theme composition about 0.005% to about 15%, perhaps even about 3.0% to about 10% sequestrant.

Dye transfer inhibitor-cleaning compositions of the present invention also can comprise one or more dye transfer inhibitors.Suitable polymeric dye transfer inhibitor includes but not limited to: the multipolymer of polyvinyl pyrrolidone polymers, polyamine N-oxide pllymers, N-vinyl pyrrolidone and N-vinyl imidazole, Ju Yi Xi oxazolidinone and polyvinyl imidazol or their mixture.In the time of in being present in this theme composition, dye transfer inhibitor can be by the weight of described composition about 0.0001% to about 10%, about 0.01% to about 5%, perhaps in addition about 0.1% to about 3% content exist.

Whitening agent-cleaning compositions of the present invention also can comprise the annexing ingredient that can be color articles to be cleaned, as white dyes.Suitable fluorescent brightener levels comprises from about 0.01 weight, about 0.05 weight, about 0.1 weight, or even lower aq to 0.5% weight of about 0.2% weight or even the high level of 0.75% weight.

Dispersion agent-composition of the present invention also can comprise dispersion agent.Suitable water soluble organic substance comprises homopolymerization or co-polymeric acids or its salt, and wherein polycarboxylic acid comprises at least two and is separated by and is no more than the carboxyl of two carbon atoms.

Additional enzyme-cleaning compositions can comprise one or more enzymes, and this enzyme provides clean-up performance and/or fabric care benefit effect.The embodiment of suitable enzyme includes but not limited to: hemicellulase, peroxidase, proteolytic enzyme, cellulase, zytase, lipase, Phospholipid hydrolase, esterase, at, polygalacturonase, mannase, pectin lyase, M-Zyme, reductase enzyme, oxydase, phenol oxidase, lipoxygenase, ligninase, Starch debranching enzyme, tannase, pentosanase, malanases, beta-glucanase, arabinase, Unidasa, chondroitinase, laccase and amylase or their mixture.Typical combination is the enzyme combination that for example can comprise with amylase bonded proteolytic enzyme and lipase.In the time of in being present in cleaning compositions, above-mentioned additional enzymes can be by the weight of described composition about 0.00001% to about 2%, about 0.0001% to about 1%, perhaps in addition about 0.001% content to about 0.5% zymoprotein exist.

The enzyme of enzyme stabilizers-be used for washing composition can use multiple technologies to stablize.The enzyme that the present invention uses can be stablized by calcium that exists in the final composition and/or magnesium ion water-soluble sources, and final product offers enzyme with this ion.Comprising under the aqueous composition situation of proteolytic enzyme, can add reversible protease inhibitors (for example boron compound) with further improvement stability.

Catalytic metal complexes-applicant's cleaning compositions can comprise catalytic metal complexes.The metallic bleaching catalyst of one class is such catalyst system, this system comprises and has the active transition-metal cation of definite bleach catalyst, as copper positively charged ion, iron positively charged ion, titanium positively charged ion, ruthenium positively charged ion, tungsten positively charged ion, molybdenum positively charged ion or manganese positively charged ion; Comprise and have very low or do not have the active assistant metal positively charged ion of bleach catalyst, as zinc cation or aluminium cations; And comprise sequestrant, especially ethylenediamine tetraacetic acid (EDTA), ethylenediamine tetraacetic (methylene phosphonic acid) and their water-soluble salt that definite stability constant is arranged for catalytic and auxiliary metallic cation.This type of catalyzer is disclosed in U.S.4, in 430,243.

If desired, the present composition can carry out catalysis by manganic compound.These compounds and consumption are well known in the art, and comprise and for example be disclosed in United States Patent (USP) 5,576, the manganese-based catalyst in 282.

It is known being used for cobalt bleaching catalyst of the present invention, and is described in for example United States Patent (USP) 5,597,936; United States Patent (USP) 5,595 is in 967.Above-mentioned cobalt catalyst is easy to by the preparation of known method, and for example United States Patent (USP) 5,597,936 and United States Patent (USP) 5,595,967 in the method that proposed.

The composition of this paper also can comprise the transition metal complex of part aptly, and described part is bispidones (WO 05/042532A1) and/or encircle rigid ligand (being abbreviated as " MRL ") mostly for example.As practical matter, and it is unrestricted, the composition of adjustable abridged edition literary composition and method, make approximately at least one 1/100000000th active MRL material is provided in the aqueous cleaning medium, and in washing liq, will be provided as about 0.005ppm usually to about 25ppm, about 0.05ppm is to about 10ppm, or even about 0.1ppm MRL of about 5ppm extremely.

Suitable transition metal comprises for example manganese, iron and chromium in the transition metal bleach catalyzer of the present invention.Suitable MRL comprises 5,12-diethyl-1,5,8,12-four azabicyclos [6.6.2] n-Hexadecane.

Be easy to prepare suitable transition metal M RL by known procedure, for example the program that in WO00/32601 and United States Patent (USP) 6,225,464, is proposed.

Solvent-suitable solvent comprises water and other solvent such as lipophilic fluid.The example of suitable lipophilic fluid comprises siloxanes, other siloxanes, hydrocarbon, glycol ether, glycerol derivative such as glyceryl ether, perfluoroamine, perfluorination and hydrogen fluorine ether solvents, the floride-free organic solvent of low volatility, diol solvent, other environment amenable solvent and their mixture.

The preparation method for compositions

Composition of the present invention can be formulated into any suitable form and adopt any method of preparation personnel selection to prepare, at United States Patent (USP) 4,990,280, and United States Patent (USP) 20030087791A1; United States Patent (USP) 20030087790A1; United States Patent (USP) 20050003983A1; United States Patent (USP) 20040048764A1; United States Patent (USP) 4,762,636; United States Patent (USP) 6,291,412; United States Patent (USP) 20050227891A1; EP1070115A2; United States Patent (USP) 5,879,584; United States Patent (USP) 5,691,297; United States Patent (USP) 5,574,005; United States Patent (USP) 5,569,645; United States Patent (USP) 5,565,422; United States Patent (USP) 5,516,448; United States Patent (USP) 5,489,392; United States Patent (USP) 5,486 has been narrated these applicants' non-limiting example in 303, and these patents are all incorporated this paper into way of reference.

Using method

The present invention includes a kind of method that cleans and/or handle a certain position, particularly surface or fabric.Aforesaid method may further comprise the steps: applicant's cleaning compositions embodiment (with the pure substance form or be diluted in the washing liq) is contacted with part surface or fabric at least, then randomly above-mentioned surface of rinsing or fabric.Can before above-mentioned rinse step, carry out washing step to described surface or fabric.For the purpose of the present invention, washing includes but not limited to clean and mechanical stirring.Understand as those skilled in the art, cleaning compositions of the present invention is ideally suited for the purposes of doing washing.Therefore, the present invention includes a kind of method that is used for laundering of textile fabrics, said method comprising the steps of: fabric that will be to be washed contacts with described cleaning washing soln, and described washing soln comprises at least one embodiment of applicant's cleaning compositions, cleaning additive or their mixture.Fabric can comprise any most of any fabric that can wash under the normal consumer working conditions.Described solution preferably has about 8 to about 10 pH5.Described composition can solution in about 500ppm to about 15, the concentration of 000ppm is used.Water temperature is generally about 5 ℃ to about 90 ℃.The ratio of water and fabric is generally about 1:1 to about 30:1.

Embodiment

The lipase Variant example

As the chemical substance of buffer reagent and substrate is the commerical prod of SILVER REAGENT at least.

-substratum and solution: LAS (Surfac PS ^TM) and zeolite A (Wessalith P ^TM).Other used composition is a standard laboratory reagent.

-material: EMPA221, from EMPA St.Gallen, Lerchfeldstrasse 5, CH-9014, St.Gallen, Switzerland

Example 1: enzyme production

Use the standard method of this area, make up the plasmid of a gene that comprises the lipase of encoding and its transfection is entered proper host cell.

Use 34 ℃ of constant temperature, the substratum that initial volume is 1.2 liters carries out fed-batch fermentation.The initial pH of substratum is made as 6.5.In case pH rises to 7.0, keep this value constant by adding 10% H3PO4.Dissolved oxygen levels in the substratum is by changing stir speed (S.S.) and using the fixedly rate of venting of every liter of substratum per minute 1.0 litres of air to control.In the whole fed-batch fermentation stage, feeding rate maintains a constant level.The batch culture base comprises malt syrup as carbon source, and urea and yeast extract are as nitrogenous source, and the mixture of trace-metal and salt.The charging that adds continuously in the fed-batch fermentation stage comprises malt syrup as carbon source, yet adding urea and yeast extract are in order to ensure competent nitrogenous source supply.

Use standard method known in the art to carry out the purifying of lipase, for example by filtering fermented supernatant fluid and follow-up hydrophobic chromatography and anionresin liquid, for example described method of EP0851913 among the embodiment 3.

Example 2:AMSA-automation stress check and analysis method-be used to calculate relative performance (RP)

Use the enzyme variants of automation stress check and analysis methods (AMSA) test present patent application.By the AMSA test, can detect the scourability of a large amount of small volume enzyme detergent solution.The AMSA plate has a plurality of slits that are used for test soln, and one firmly choke fabric sample, so that its capping that is washed at all slotted opening places.During washing, acutely shake described plate, test soln, fabric and capping so that the test soln contact fabric, and apply mechanical stress.More detailed description can be referring to WO 02/42740, especially 23 to 24 pages paragraph " Specialmethod embodiments ".The container that comprises the washing composition test soln is made up of the cylindrical cavity in a metal sheet (diameter 6mm, dark 10mm).Dirty fabric (test substances) is positioned at the top of metal sheet, as capping and the sealing member on container.Another metal sheet is positioned at the top of dirty fabric to avoid overflowing any liquid from any one vessel.Two metal sheets together with dirty fabric with the frequency of 30Hz and the amplitude up-down vibration of 2mm.

Carry out under the specified hereinafter test conditions of described check and analysis method:

Test soln	0.5g/L LAS 0.52g/L Na2CO3 1.07g/L zeolite A 0.52g/L trisodium citrate
		The test soln volume	160micro L
PH value	As is(≈9.9.
		Washing time	20 minutes
Temperature	30℃
		Water hardness
	15°dH Ca 2+/Mg 2+/ NaHCO3 ratio is: 4: 1: 7.5
		Enzyme concn in the test soln	0.125,0.25,0.50, the 1.0mg zymoprotein/liter
Dry	Performance: pieces of fabric is in rinsing in tap water immediately after the washing, and at 85 ℃ of following air-dry 5 minutes smells: pieces of fabric is in rinsing in tap water immediately after the washing, and room temperature (20 ℃) dry 2 hours down
		Test substances	White cream turmeric sample as described below (as the EMPA221 of cotton-spinning fabric)

Table 3

By mixing 5g (Santa Maria down at 50 ℃, Denmark) turmeric and 100g (38% fat, Arla, Denmark) white cream prepares white cream turmeric sample, and mixture kept under this temperature about 20 minutes and filtration (50 ℃) removes any undissolved particle.Mixture is cooled to 20 ℃, and with the cotton spinning sample, EMPA221 immerses this white cream turmeric mixture, and at room temperature dried overnight is also freezing until use then.The preparation method of white cream turmeric sample is disclosed in the patent application PA200500775 that submitted on May 27th, 2005.

The performance of enzyme variants can be measured by the colour brightness with the fabric sample of certain enzyme variant washing.Represent from the light intensity of fabric sample reflection during the also available white-light illuminating of brightness.When fabric was dirty, the intensity of reflected light of its catoptrical strength ratio clean textile was low, and therefore catoptrical intensity can be used for measuring the scourability of enzyme variants.

Use a kind of plane scanner (PFU DL2400pro) of specialty to carry out color measuring, this scanning device is used to obtain the image of laundering of textile fabrics sample.Scanning resolution is 200dpi, 24 of output color depths.In order to obtain accurate result, with Kodak reflection IT8 colour atla frequent calibration scanner.

Use a specially designed application software (Novozymes Color Vector Analyzer) to come from scanning image, to extract light intensity value.Described program is retrieved 24 pixel values and is converted it into red, green and blue (RGB) value from image.By with the rgb value addition as carrier, extract the length of gained carrier then and come computed strength value (Int):

$\mathrm{Int}=\sqrt{{\mathrm{<figure-callout\; id="2"\; label="r"\; filenames="A200780002820E00701.png,A200780002820E00711.png"\; state="\{\{state\}\}">r</figure-callout>}}^2+{\mathrm{<figure-callout\; id="2"\; label="g"\; filenames="A200780002820E00701.png,A200780002820E00711.png"\; state="\{\{state\}\}">g</figure-callout>}}^2+{\mathrm{<figure-callout\; id="2"\; label="b"\; filenames="A200780002820E00701.png,A200780002820E00711.png"\; state="\{\{state\}\}">b</figure-callout>}}^2}$

The scourability of variant (P) is calculated according to following formula:

P=Int (v)-Int (r) is wherein

(v) be the light intensity value with the fabric face of tested enzyme washing, Int (r) is the light intensity value without the fabric face of tested enzyme washing to Int.

According to definition, regulation relative performance score is the result of AMSA washing: relative performance score (RP) is performance (P) sum and the ratio of reference enzyme performance: RP=P (the tested enzyme)/P (reference enzyme) of tested enzyme variant.

RPavg is meant under all four kinds of enzyme concns the average relative performance that compare with reference enzyme (0.125,0.25,0.5,1.0mg ep/l)

RPavg＝avg(RP(0.125)，RP(0.25)RP(0.5)，RP(1.0))

If the variant performance is better than reference enzyme, think that then it shows the scourability of improvement.Under situation of the present invention, reference enzyme is a sequence identification number: 2 lipase, it has the replacement of T231R+N233R.

Example 3: be used to calculate the GC-gas-chromatography of imitating the danger

By solid-phase microextraction vapor-phase chromatography (SPME-GC), the butyric acid that uses following method to measure in the lipase washing sample discharges.To specify four pieces of fabric (diameter 5mm) of washing in the solution to be transferred to gas-chromatography (GC) bottle at the table 3 that comprises 1mg/L lipase.Analytic sample on a Varian3800 GC who is furnished with a Stabilwax-DA w/Integra-Guard post (30m, 0.32mm internal diameter and 0.25micro-m df) and a Carboxen PDMS SPME fiber (75micro-m).Each sample is 40 ℃ of pre-cultivations 10 minutes, then with sampling in the headspace of SPME fiber on pieces of fabric 20 minutes.Subsequently sample is injected chromatographic column (injector temperature=250 ℃).Post flow=2mL helium/minute.The column oven thermograde: 0 minute=40 ℃, 2 minutes=40 ℃, 22 minutes=240 ℃, 32 minutes=240 ℃.Detect butyric acid with fid detector, and calculate butyro-amount based on the butyric acid typical curve.

The risk performance smell of lipase Variant, R, be the butyric acid that discharges from the lipase Variant washing sample with from sequence identification number: the ratio between the butyric acid amount of 2 lipase washing sample release, sequence identification number: 2 lipase has the replacement of T231R+N233R (reference enzyme), and two values all use the butyric acid amount that discharges from the washing sample of fat-free enzyme to proofread and correct.Calculate the risk (R) of variant according to following formula:

The microgram butyric acid that smell=1mg zymoprotein records/1 blank correction

α _{Tested enzyme}=smell _{Tested enzyme}-blank

α _{Reference enzyme}=smell _{Reference enzyme}-blank

R=α _{Tested enzyme}/ α _{Reference enzyme}

If the R coefficient of a variant, thinks promptly that it shows the smell of comparing minimizing with reference less than 1.

Example 4: with respect to activity (LU) in the absorbancy of 280nm

Measure lipase with respect to activity by following check and analysis method LU/A280 in the absorbancy of 280nm:

The method that use is partly described at lipase activity is above measured lipase activity.Measure lipase in the absorbancy (A280) of 280nm and calculate the LU/A280 ratio.The LU/A280 of variant calculates relative LU/A280 divided by the LU/A280 of reference enzyme.Under situation of the present invention, reference enzyme is a sequence identification number: 2 lipase, it has the replacement of T231R+N233R.

Example 5:BR-is imitated the danger

With describe performance and smell reduce risks than effect danger coefficient therefore be defined as: BR=RP _Avg/ R

If the BR coefficient of a variant is higher than 1, think that promptly it shows the scourability of improvement and the smell of minimizing.

The result who uses above method acquisition is as follows:

Variant	In sequence identification number: 2	Average RP (RP avg)	BR	LU/A280
					1	I202G+T231R+N233R	0.84	1.41	Do not determine
2	I86V+L227G+T231R+N233R+ P256K	1.08	1.52	1700
					3	Q4V+S58N+V60S+T231R+N233R	0.87	1.73	1950
4	S58N+V60S+I90R+T231R+N233R	1.06	1.27	2250
					5	I255Y+T231R+N233R	1.19	1.17	3600
6	I90A+T231R+N233R+I255V	1.13	1.14	2700
					Reference	T231R+N233R	1.00	1.00	3650

7	G91A+E99K+T231R+N233R+ Q249R+270H+271T+272P+273S+ 274S+275G+276R+277G+278G+ 279H+280R	0.43	Do not determine	850
					8	G91A+E99K+T231R，N233R+ Q249R+270H+271T+272P+273S+ 274S+275G+276R+277G+278G	0.13	Do not determine	500

Table 4

WO 2000/060063 has described reference lipase and variant 7 and 8 in the table 4.

Example 6

BR-is imitated the danger

The effect danger of the variant of listing in the meter 5.Measure the dangerous coefficient of effect with the method identical with the method described in the embodiment 5, it imitates dangerous coefficient all greater than 1 all variants of listing.

Variant	In sequence identification number: the sudden change in 2
		Reference	T231R+N233R
9	L97V+T231R+N233R
		10	A150G+T231R+N233R
11	I90R+T231R+N233R
		12	I202V+T231R+N233R
13	L227G+T231R+N233R+P256K
		14	I90A+T231R+N233R
15	T231R+N233R+I255P
		16	I90V+I255V+T231R+N233R
17	F211L+L227G+T231R+N233R+I255L+P256K
		18	S58N+V60S+T231R+N233R+Q249L
19	S58N+V60S+T231R+N233R+Q249I

20	A150G+L227G+T231R+N233R+P256K
		21	K46L+S58N+V60S+T231R+N233R+Q249L+D254I
22	Q4L+E43T+K46I+S58N+V60S+T231R+N233R+ Q249L+D254I
		23	Q4L+S58N+V60S+T231R+N233R+Q249L+D254I
24	K46I+S58N+V60S+T231R+N233R+Q249L+D254L
		25	K46L+S58N+V60S+K223I+T231R+N233R+D254I
26	E43T+K46I+S58N+V60S+T231R+N233R+Q249L+ D254I
		27	S58N+V60S+I86V+A150G+L227G+T231R+N233R+ P256K
28	K24R+K46R+K74R+I86V+K98R+K127R+D137K+ A150G+K223R+T231R+N233R
		29	S58A+V60A+I86V+T231R+N233R
30	K24R+K46R+S58N+V60S+K74R+I86V+K98R+ K127R+D137K+K223R+T231R+N233R
		31	S58A+V60A+I86V+A150G+T231R+N233R
32	S58N+V60V+D62G+T231R+N233R
		33	Q4V+S58N+V60S+I86V+T231R+N233R+Q249L
34	Q4V+S58N+V60S+I86V+A150G+T231R+N233R+ I255V
		35	Q4V+S58N+V60S+I90A+A150G+T231R+N233R+ I255V
36	Y53A+S58N+V60S+T231R+N233R+P256L
		37	I202L+T231R+N233R+I255A
38	S58A+V60S+I86V+A150G+L227G+T231R+N233R+ P256K
		39	D27R+S58N+V60S+I86V+A150G+L227G+T231R+ N233R+P256K
40	V60K+I86V+A150G+L227G+T231R+N233R+P256K
		41	Q4V+S58A+V60S+S83T+I86V+A150G+E210K+

	L227G+T231R+N233R+P256K
		42	Q4V+V60K+S83T+I86V+A150G+L227G+T231R+ N233R+P256K
43	D27R+V60K+I86V+A150G+L227G+T231R+N233R+ P256K
		44	Q4N+L6S+S58N+V60S+I86V+A150G+L227G+ T231R+N233R+P256K
45	E1N+V60K+I86V+A150G+L227G+T231R+N233R+ P256K
		46	V60K+I86V+A150G+K223N+G225S+T231R+N233R+ P256K
47	E210V+T231R+N233R+Q249R
		48	S58N+V60S+E210V+T231R+N233R+Q249R
49	Q4V+V60K+I90R+T231R+N233R+I255V
		50	Q4V+V60K+A150G+T231R+N233R
51	V60K+S83T+T231R+N233R
		52	V60K+A150G+T231R+N233R+I255V
53	T231R+N233G+D234G
		54	S58N+V60S+I86V+A150G+E210K+L227G+T231R+ N233R+Q249R+P256K
55	S58N+V60S+I86V+A150G+E210K+L227G+T231R+ N233R+I255A+P256K
		56	S58N+V60S+I86V+A150G+G156R+E210K+L227G+ T231R+N233R+I255A+P256K
57	S58T+V60K+I86V+N94K+A150G+E210V+L227G+ T231R+N233R+P256K
		58	S58T+V60K+I86V+D102A+A150G+L227G+T231R+ N233R+P256K
59	S58T+V60K+I86V+D102A+A150G+E210V+L227G+ T231R+N233R+P256K
		60	S58T+V60K+S83T+I86V+N94K+A150G+E210V+

	L227G+T231R+N233R+P256K
		61	S58A+V60S+I86V+T143S+A150G+L227G+T231R+ N233R+P256K
62	G91S+D96V+D254R
		63	V60L+G91M+T231W+Q249L
64	T37A+D96A+T231R+N233R+Q249G
		65	E56G+E87D+T231R+N233R+D254A
66	E210K+T231R+N233R
		67	D27H+E87Q+D96N+T231R+N233R+D254V
68	F181L+E210V+T231R+N233R
		69	D27N+D96G+T231R+N233R
70	D96N+T231R+N233R
		71	T231R+N233I+D234G
72	S58K+V60L+E210V+Q249R
		73	S58H+V60L+E210V+Q249R
74	Q4V+F55V+I86V+T231R+N233R+I255V
		75	Q4V+S58T+V60K+T199L+N200A+E210K+T231R+ N233R+I255A+P256K
76	Q4V+D27N+V60K+T231R+N233R
		77	I90F+I202P+T231R+N233R+I255L
78	S58N+V60S+D158N+T231R+N233R
		79	S58N+V60S+S115K+T231R+N233R
80	S58N+V60S+L147M+A150G+F211L+T231R+N233R
		81	V60K+A150G+T231R+N233R
82	I90V+L227G+T231R+N233R+P256K
		83	T231R+N233R+I255S
84	I86G+T231R+N233R
		85	V60K+I202V+E210K+T231R+N233R+I255A+P256K
86	I90G+I202L+T231R+N233R+I255S
		87	S58G+V60G+T231R+N233R

Table 5

In WO 2000/060063, described with reference to lipase.

The composition example

Except as otherwise noted, raw material can be available from Al drich, and P.O.Box 2060, Milwaukee, and WI 53201, USA.

Example 1 to 6

The granular laundry cleaning composition is designed for the washing machine of hand washing or top-loaded.

Under 25 ℃, any above-mentioned composition that is used for laundering of textile fabrics is 600ppm to 10 in the concentration of water, 000ppm, and typical intermediate conditions is 2500ppm, and the ratio of water and fabric is 25:1.

Example 7 to 10

The granular laundry cleaning composition is designed for the anterior automatic washing machine that loads.

Under 20 ℃ to 90 ℃ temperature, any above-mentioned composition that is used for laundering of textile fabrics is 10 in the concentration of water, 000ppm, and the ratio of water and fabric is 5:1.Typical pH is about 10.

Example 11 to 16The heavy duty type liquid laundry detergent composition

Be used for starting material and the explanation of composition embodiment 1 to 16

Linear alkyl benzene sulfonate, its average fatty carbon chain length is C ₁₁-C ₁₂, by Stepan, Northfield, Illinois, USA supply

C _12-14Dimethyl hydroxyethyl ammonium chloride, by Clariant GmbH, Sulzbach, Germany supply

AE3S is C _12-15Alkyl ethoxy (3) sulfuric ester, by Stepan, Northfield, Illinois, USA supply

AE7 is C _12-15Alcohol ethoxylate, its average degree of ethoxylation is 7, by Huntsman, Salt Lake City, Utah, USA supply

Tripoly phosphate sodium STPP, by Rhodia, Paris, France supply

Zeolite A, by Industrial Zeolite (UK) Ltd, Grays, Essex, UK provides

1.6R silicate, by Koma, Nestemica, Czech Republic supply

Yellow soda ash, by Solvay, Houston, Texas, USA supply

The polyacrylic ester of molecular weight 4500, by BASF, Ludwigshafen, Germany supply Walocel MT 20.000PV is

BDA, by CPKelco, Arnhem, Netherlands supply

By Novozymes, Bagsvaerd, Denmark supply

Lipase Variant 1 to 5 and their combination have been described in the embodiment 5 of table 4.

White dyes 1 is AMS, white dyes 2 is

CBS-X, sulfonation phthalocyanine phthalocyanine zinc and direct purple 9 is

Violet BN-Z, they are all by Ciba Specialty Chemicals, Basel, Switzerland supply

Diethylene triaminepentaacetic acid(DTPA), by Dow Chemical, Midland, Michigan, USA provides

SPC-D, by Solvay, Houston, Texas, USA supply

Sodium peroxoborate, by Degussa, Hanau, Germany supply

NOBS is an acyloxy benzene sulfonic acid sodium salt in the ninth of the ten Heavenly Stems, by Eastman, and Batesville, Arkansas, USA supply

TAED is a tetra acetyl ethylene diamine, trade(brand)name

By Clariant GmbH, Sulzbach, Germany supply

Stain remover is

PF, by Rhodia, Paris, France provides

The molecular weight of vinylformic acid/maleic acid is 70,000, and the ratio of acrylate and maleate is 70:30, by BASF, and Ludwigshafen, Germany supply

Proteolytic enzyme is FN3, by Genencor International, and Palo Alto, California, USA supply

1-N, the sodium salt of N '-disuccinic acid, (S, S) isomer (EDDS), by Octel, Ellesmere Port, UK supply

Hydroxyl ethane diphosphonates (HEDP), by Dow Chemical, Midland, Michigan, USA supply

The suds suppressor aggregate, by Dow Corning, Midland, Michigan, USA provides

HSAS be in the middle of the alkyl-sulphate of branching, be disclosed in US 6,020, in 303 and US6,060,443

C _12-14Dimethyl oxidation amine is by Procter; Gamble Chemicals, Cincinnati, Ohio, USA supply

Nonionic is C preferably ₁₂-C ₁₃The ethyl oxide compound, preferably average degree of ethoxylation is 9.

Proteolytic enzyme, by Genencor International, Palo Alto, California, USA supply

^*Numerical value in mg enzyme/100g

¹As US 4,597, described in 898.

²With trade(brand)name

Available from BASF, and described in WO 01/05874 those

Described in this specification sheets

Lipase.

Although illustrated and described the present invention with specific embodiment, it will be apparent to those skilled in the art that many other variations and modifications may be made in the case of without departing from the spirit and scope of protection of the present invention.Therefore, in additional claims, comprise all such changes and modifications that belong in the scope of the invention consciously.

Sequence table

<110>Procter & Gamble Company

＜120〉detergent composition

<130>10280M

<160>16

<170>PatentIn version 3.3

<210>1

<211>807

<212>DNA

＜213〉thermophilic fungus (Thermomyces lanuginosus)

<220>

<221>CDS

<222>(1)..(807)

<220>

<221>mat_peptide

<222>(1)..()

<400>1

<210>2

<211>269

<212>PRT

＜213〉thermophilic fungus (Thermomyces lanuginosus)

<400>2

<210>3

<211>265

<212>PRT

＜213〉colter mould (Absidia reflexa)

<400>3

<210>4

<211>264

<212>PRT

＜213〉absidia corymbifera (Absidia corymbifera)

<400>4

<210>5

<211>269

<212>PRT

＜213〉rice black root Mucor (Rhizomucor miehei)

<400>5

<210>6

<211>271

<212>PRT

＜213〉Dai Shi head mold (Rhizopus oryzae)

<400>6

<210>7

<211>267

<212>PRT

＜213〉aspergillus niger (Aspergi1lus niger)

<400>7

<210>8

<211>266

<212>PRT

＜213〉Tabin aspergillus (Aspergillus tubingensis)

<400>8

<210>9

<211>276

<212>PRT

＜213〉Fusarium oxysporum (Fusarium oxysporum)

<400>9

<210>10

<211>273

<212>PRT

＜213〉fusarium heterosporium (Fusarium heterosporum)

<400>10

<210>11

<211>278

<212>PRT

＜213〉aspergillus oryzae (Aspergillus oryzae)

<400>11

<210>12

<211>278

<212>PRT

＜213〉penicillium camembertii (Penicillium camemberti)

<400>12

<210>13

<211>270

<212>PRT

＜213〉smelly aspergillus (Aspergillus foetidus)

<400>13

<210>14

<211>270

<212>PRT

＜213〉aspergillus niger (Aspergillus niger)

<400>14

<210>15

<211>269

<212>PRT

＜213〉aspergillus oryzae (Aspergi1lus oryzae)

<400>15

<210>16

<211>251

<212>PRT

<213>Landerina penisapora

<400>16

Claims (35)

1. composition, described composition comprises the variant of optical white and parent lipase, and when comparing with described parent, described variant comprises at least three kinds of replacements of total, and described replacement is selected from one or more following replacement groups:

A.) at least two kinds of replacements in area I,

B) at least a replacement in area I I,

C) at least a replacement in area I II, and/or

D) at least a replacement in area I V.

2. detergent composition as claimed in claim 1, wherein the described replacement in area I is included in the replacement corresponding to the site of described site 231 and 233.

3. detergent composition as claimed in claim 2, wherein 231 and 233 described replacement is replaced by R in the site.

4. detergent composition as claimed in claim 2, wherein said variant are included in corresponding to sequence identification number: the replacement in 2 site 4.

5. detergent composition as claimed in claim 4, wherein corresponding to sequence identification number: the described replacement in 2 site 4 is V.

6. detergent composition as claimed in claim 2, wherein said variant are included in corresponding to sequence identification number: the replacement in 2 site 227.

7. detergent composition as claimed in claim 6, wherein corresponding to sequence identification number: the described replacement in 2 site 227 is G.

8. detergent composition as claimed in claim 1, wherein the described at least a replacement in area I I is selected from the group of being made up of following: in the replacement corresponding to described site 202,211,255 and 256.

9. detergent composition as claimed in claim 8, wherein the described at least a replacement in area I I is selected from the group of being made up of following: X202G, X211L, X255Y/V and X256K.

10. detergent composition as claimed in claim 1, wherein the described at least a replacement in area I I is included in the replacement corresponding to the site in described site 210.

11. detergent composition as claimed in claim 10 wherein comprises X210K in the replacement corresponding to the site in site 210.

12. detergent composition as claimed in claim 1, wherein the described at least a replacement in area I II is selected from the group of being made up of following: in the replacement corresponding to the site of described site 86 and 90.

13. detergent composition as claimed in claim 12, wherein the described at least a replacement in area I II is selected from the group of being made up of following: X86V and X90A/R.

14. detergent composition as claimed in claim 1, wherein the described at least a replacement in area I II is included in the replacement corresponding to the site in described site 83.

15. detergent composition as claimed in claim 14 wherein comprises X83T in the replacement corresponding to the site in described site 83.

16. detergent composition as claimed in claim 1, wherein the described at least a replacement in area I V is selected from the group of being made up of following: in the replacement corresponding to the site of described site 27,58 and 60.

17. detergent composition as claimed in claim 15, wherein the described at least a replacement in area I V is selected from the group of being made up of following: X27R, X58N/A/G/P/T and X60S/V/G/N/R/K/A/L.

18. detergent composition as claimed in claim 1, described composition are included at least two kinds of replacements corresponding to described site 27,58 and 60 among the area I V.

19. detergent composition as claimed in claim 1, described composition are included at least two kinds of replacements among the area I V, described replacement is selected from the group of being made up of following: X27R, X58N/A/G/P/T and X60S/V/G/N/R/K/A/L.

20. detergent composition as claimed in claim 1, wherein said variant comprise at least a replacement outside described localized area I to IV.

21. detergent composition as claimed in claim 20, wherein the described at least a replacement outside described localized area I to IV is selected from the group of being made up of following: in the replacement corresponding to the site of site 81,147,150 and 249.

22. detergent composition as claimed in claim 20, wherein at least a replacement outside described localized area I to IV is selected from the group of being made up of following: X81Q/E, X147M/Y, X150G and X249R/I/L.

23. detergent composition as claimed in claim 2, wherein said parent lipase and sequence identification number: 2 have at least 90% identity.

24. detergent composition as claimed in claim 1, wherein said parent lipase and sequence identification number: 2 is identical, and described variant comprises one of following replacement group:

a)T231R+N233R+I255Y

b)I202G+T231R+N233R

c)I86V+L227G+T231R+N233R+P256K

d)Q4V+S58N+V60S+T231R+N233R

e)S58N+V60S+I90R+T231R+N233R

f)I90A+T231R+N233R+I255V

g)S58N+V60S+I86V+A150G+L227G+T231R+N233R+P256K

h)S58N+V60S+L147M+F211L+T231R+N233R

i)Q4V+S58A+V60S+S83T+I86V+A150G+E210K+L227G+T231R+N233R+P256K

j)S58N+V60S+I86V+A150G+L227G+T231R+N233R+P256K。

25. detergent composition as claimed in claim 1, wherein said parent lipase and sequence identification number: 2 is identical, and described variant comprises one of following replacement group:

a)Q4V+S58A+V60S+S83T+I86V+A150G+E210K+L227G+T231R+N233R+P256K

b)S58N+V60S+I86V+A150G+L227G+T231R+N233R+P256K。

26. detergent composition as claimed in claim 1, wherein said lipase Variant be characterised in that described imitate the danger in described specification sheets during given method measurement greater than 1.

27. a detergent composition, described composition comprises optical white and polypeptide, and described polypeptide has lipase activity, and also has at least 0.8 average relative performance and at least 1.1 effect danger in described specification sheets under the given test condition.

28. will remove 1 described composition as right, wherein said composition comprises 0.1% to 40% anion surfactant.

29. composition as claimed in claim 28, wherein said composition are a kind of cleaning and/or treatment compositions.

30. composition as claimed in claim 1, wherein said composition comprises sulfonation phthalocyanine phthalocyanine zinc.

31. composition as claimed in claim 25, wherein said composition comprises the mixture of sulfonation phthalocyanine phthalocyanine zinc and aluminum phthalocyanine, and the sulfonation phthalocyanine phthalocyanine zinc that described mixture has and the weight ratio of aluminum phthalocyanine are greater than 1.

32. composition as claimed in claim 1, wherein said composition comprises aluminum phthalocyanine.

33. composition as claimed in claim 1, wherein said optical white comprises xanthene dyestuff, anthraquinone or naphthoquinones.

34. the method for a cleaning and/or treat surface or fabric said method comprising the steps of: described surface or fabric are contacted with the composition of claim 1, then randomly washing and/or described surface of rinsing or fabric.

35. composition as claimed in claim 1, wherein said lipase Variant is a sequence identification number: 2 variant, described variant comprises at least one in the following sudden change: Q4V, S58N/A/G/P/T, I90R or Q249I/L.

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