CN1336953A

CN1336953A - Enzymatic cleaning compositions

Info

Publication number: CN1336953A
Application number: CN98810047A
Authority: CN
Inventors: J·L·P·贝蒂奥尔; C·E·A·约斯
Original assignee: Procter and Gamble Co
Current assignee: Procter and Gamble Co
Priority date: 1997-08-14
Filing date: 1998-06-10
Publication date: 2002-02-20
Also published as: BR9811187A; DE69837850T2; JP2001515129A; TR200000339T2; CZ2000506A3; JP2001515132A; JP2001515128A; CN1306566A; JP2001515131A; HUP0003670A2; ES2185172T3; BR9811189A; WO1999009128A1; MXPA00001618A; KR20010022908A; DE69826294D1; AU7958198A; MXPA00001617A; JP4090688B2; BR9811191A

Abstract

The present invention relates to cleaning compositions comprising a mannanase and a carbohydrase selected from cellulases, amylases, pectin degrading enzimes and/or xyloglucanases, providing superior cleaning performance.

Description

Enzymatic cleaning compositions

Invention field

The present invention relates to comprise mannase and a kind of cleaning compositions that is selected from the carbohydrase of cellulase, amylase, pectin degrading enzyme and/or xyloglucanase enzymes.

Background of invention

Be familiar with this area carbohydrase using to people in washing composition, for example amylase is used to remove starch food products residue or starch film and understanding considerable time has been provided providing to the cleaning performance of the common dirt of starch soil and other laundry by people from tableware or crust in detergent composition.

In addition, the purposes of cellulase or relevant xyloglucanase enzymes also is familiar with by this area people.This specifically to the activity of fabric provide the woven fabric structure cleaning, recovered, hand feel characteristic softening and that improve usually.The activity of cellulase is meant cellulosic fibre or substrate by the activity of cellulase effect, and it depends on the concrete function of cellulase, and described cellulase can be plain enzyme of inner cellulose enzyme or outer fiber and hemicellulase separately.Cellulosic structure is by depolymerization or be cracked into less and more solvable according to this or dispersible composition.

Known pectin degrading enzyme provides stain to remove usefulness when being used for washing and cleaning, and plant and the removal of fruit based spot and the real project cleaning scope that strengthens detergent composition of wide region particularly is provided.Really, the removal that comes from the spot of plant, timber, farming soil matrix dirt and fruit is the clean up task of a current arduousness; Particularly washing just develops towards cryogenic direction.The food dirt is difficult to usually from removing with dirty dirt-carrying body material.Highly coloured dirt or " mummification " dirt of coming from fruit juice and/or dish juice are difficult to remove especially.The object lesson of this dirt comprises orange juice, tomato juice, banana, mango or sprouting broccoli dirt.

Yet above-mentioned carbohydrase has the specific activity at its given substrate, and its enzymic activity may limited (IndustrialEnzymology for the substrate of other type and/or composite substrate, 2.13 chapter, second edition, T.Godffey work, ISBN 0-333-59464-9).

The foods and cosmetics stain is the stain that most consumers is often met, and generally includes foodstuff additive such as viscosifying agent/stablizer.Really, hydro-colloid natural gum and emulsifying agent are the foodstuff additive of using always.Described term " natural gum " is meant industrial available polysaccharide (long chain polymer) or derivatives thereof, and its hydration in hot water or cold water forms viscous soln, dispersion or gel.Natural gum is classified as natural gum and modification natural gum.Natural gum comprises Seaweed Extract, plant extrudate, from the natural gum of seed or root and the natural gum that obtains by microbial fermentation.(semi-synthetic) natural gum of modification comprises Mierocrystalline cellulose and starch derivative and some synthetic gum such as low-methoxy pectin, propylene glycol alginate and carboxymethyl and Rhoximat RH 148 (referring to J.Baird, the Gums chapters and sections during the 4th edition Encyclopedia ChemicalTechnology the 12nd of Kelco division of Merck rolls up 842 to 862 pages).Also referring to Carbohydrate Chemistry for Food Scientists (the Eagan press of R.L.Whistler and J.N.BeMiller, 1997), Direct FoodAdditivesin Fruit Processing (the Technomie press of 63 to 89 pages in the 4th chapter and P.Laslo, 1996), Bioprinciplesand Applications, 313 to 325 pages in the 1st volume 11 chapters.Some these class natural gum such as guar gums (E412), Viscogum BE (E410) extensively are used alone or are used in combination (referring to the Gums chapters and sections in 842 to 862 pages of the 4th edition EncyclopediaChemical Technology the 12nd volumes of J.Baird.Kelco divison of Merck) in numerous food product processing.

Used guar gum obtains from the seed endosperm of leguminous plants guanidine ear beans (Cyamopsis tetragonoloba) in these foods and cosmetics spots.The guar gum (being also referred to as guaran) that extracts from described dicotyledonous seed comprises 1-4 b-D-pyran-mannose glycosylation unit skeleton, and in seasonings and frozen product and makeup, be used as viscosifying agent (H.D.Belitz, FoodChemistry, 243 pages, the English edition of second edition, Springer-verlag, 1987, ISBN 0-387-15043-9, the U.S.) and (Carbohydrate Chemistry for Food Scientists, R.LWilstler, Eagan Press, 1997, ISBN 0-913250-92-9) and (Industrial Gum, second edition, R.L.Whistler, 308 pages, Academic Press, 1973, ISBN 0-12-74-6252-x).Viscogum BE (being also referred to as tragon or St Jon ' s bread) also is used in the foodstuffs industry, and extracts from the seed of a kind of evergreen plant of Mediterranean Zone plantation.The structural difference of Viscogum BE and guar gum may be the number of its less D-galactosyl side chain, and Viscogum BE has same 1-4 b-D-pyran-mannose glycosylation skeleton.In seeds of leguminous plant, water miscible polygalactomannan is main storage carbohydrate, and it is up to 20% of gross dry weight in some cases.Polygalactomannan has a α-semi-lactosi that links to each other with the O-6 of mannose residue, and can be on the O-2 of mannose residue and O-3 acetylize to various degree.

From as seen last, exist the lasting needs that preparation provided the cleaning compositions of excellent clean-up performance.This target comprises that by preparation mannase and a kind of cleaning compositions that is selected from the carbohydrase of cellulase, amylase, pectin degrading enzyme and/or xyloglucanase enzymes reach.

The synergism that is used in combination owing to this mixed enzyme system of now finding mannase and one or more selected carbohydrases unexpectedly provides excellent clean-up performance, instant food greasiness removal, booty cleaning and retention of whiteness energy.Specifically, have now found that being used in combination of mannase and one or more selected carbohydrases provides in addition under low-down wash temperature and/or low washing composition level to the outstanding removing effect of crucial spot.

The performance of also having found cleaning compositions of the present invention is enhanced by adding selected tensio-active agent, auxiliary agent and/or bleach system.

Alleged occurrence mannase in several genus bacillus biologies.For example people such as Talbot to have described molecular weight 3505 to 3510 pages of the Appl.Environ.Microbiol. of 56 11 phases of volume of nineteen ninety be that 162 kDa and best pH are the 'beta '-mannase that comes from bacstearothermophilus (Bacillu stearothermophilus) of the dipolymer form of 5.5-7.5.People such as Mendoza 551 to 555 pages of WorldJ.Microbiol.Biotech. of 1994 10 5 phases of volume described a kind of molecular weight with 38 kDa, under pH5.0 and 55 ℃ optimum activity and 4.8 pI, come from the 'beta '-mannase of bacillus subtilis Pseudomonas (Bacillus subtilisis).JP-0304706 disclose the best pH of molecular weight that a kind of gel-filtration with 37 ± 3kDa records, 8-10 and 5.3-5.4 pI, come from the 'beta '-mannase of bacillus bacterial classification.JP-63056289 has described for example β of mannosans-1 of a kind of hydrolysis, the 4-D-mannopyranose glycosidic bond and the alkalescence of generation manna oligosaccharide, the production of thermally-stabilised 'beta '-mannase.JP-63036774 relates to the bacillus micro-organism FERM P-8856 that produces 'beta '-mannase and beta-Mannosidase under alkaline pH.Mannase of a kind of purifying that comes from bacillus amyloliquefaciens (Bacillus amyloliquefaciens) that can be used for bleached pulp and paper and preparation method thereof is disclosed among the WO 97/11164.WO91/18974 has described under extreme pH and temperature has active hemicellulase such as dextranase, zytase or mannase and production thereof.WO94/25576 discloses and a kind ofly demonstrated the mannosans enzymic activity, the enzyme of (Aspergillus aculeatus) CBS 101.43 that comes from microorganism Aspergillus aculeatus, and it can be used for the degraded or the modification of plant or alga cells wall material.WO 93/24622 disclose can be used for the bleaching lignin cellulose pulp, from the isolating mannase of Trichoderma (Trichoderma reseei).

Amylase and cellulase are commonly used for the washing enzyme.Be described among patent application PCT/US96/12963, PCT/US96/12962, PCT/US96/12959, PCT/US96/12960 and the PCT/US96/12691 of EP-A-751990 and while pending trial as the pectin degrading enzyme of washing with enzyme, all these patent applications are all submitted on August 9th, 1996.WO95/35362 discloses the cleaning compositions that comprises plant cell-wall degrading enzymes, and described plant cell-wall degrading enzymes has the activity of the polygalacturonase and/or hemicellulase and the optional cellulase that are used to remove the plant-sourced spot.

But, the clean-up performance in cleaning compositions of the described mannase and the excellence that synergistic composition had of the carbohydrase that is selected from cellulase, amylase, pectin degrading enzyme and/or xyloglucanase enzymes, promptly superior detergency ability, dirty clean-up performance and retention of whiteness can before not have to be familiar with by the people.

The present invention's summary

The present invention relates to comprise mannase and a kind of cleaning compositions that is selected from the carbohydrase of cellulase, amylase, pectin degrading enzyme and/or xyloglucanase enzymes.These cleaning compositions provide excellent clean-up performance, promptly superior detergency ability, dirty clean-up performance and retention of whiteness energy.

Detailed description of the present invention

Now find uncannily since the synergism mannase of mixed enzyme system and one or more selected carbohydrases be used in combination the clean-up performance that provides excellent, promptly superior detergency ability, dirty clean-up performance and retention of whiteness energy.Specifically, find uncannily now that being used in combination of mannase and one or more selected carbohydrases provides in addition under low-down wash temperature and/or low washing composition level to the outstanding removing effect of crucial spot.

Be not wishing to be bound by theory, believe the more substrate of wide spectrum of more effectively having degraded that is used in combination of mannase and a kind of carbohydrase that is selected from amylase, cellulase, pectin degrading enzyme and/or xyloglucanase enzymes.This causes superior cleaning, and is particularly respond well for the feel aspect of the removing of foods and cosmetics spot and fabric.

Mannase

A kind of basal component of cleaning compositions of the present invention is a mannase.

Comprise following three kinds of mannosans degrading enzyme: the E.C.3.2.1.25 that have in the present invention: beta-Mannosidase, E.C.3.2.1.78: interior-1,4-beta-Mannosidase (hereinafter being called " mannase ") and E.C.3.2.1.100:1,4-β-mannobiose Glycosylase (mannobiosidase) (IUPAC classification-enzyme nomenclature, 1992ISBN 0-12-227165-3 Academic Press).

More preferably, cleaning compositions of the present invention comprises the β-1 that is called mannase, 4-mannosidase (E.C.3.2.1.78).Term " mannase " or " polygalactomannan enzyme " are meant a kind of mannase according to this art definition, formal name is called mannosans interior-1, the 4-beta-Mannosidase, and have can for the name 'beta '-mannase and interior-1, the following reaction of 4-mannase and catalysis: in mannosans, polygalactomannan, glucomannan and galactoglucomannan 1, the random hydrolysis of 4-β-D-seminose glycosidic bond.

Specifically, mannase (E.C.3.2.1.78) comprises that one group of degraded mannosans refers to that also the energy cracking contains the polysaccharidase of the unitary polysaccharide chain of seminose, polysaccharidase that can the glycosidic link of cracking in mannosans, glucomannan, polygalactomannan and galactoglucomannan.Therefore mannase comprises the interior mannase of inner cracking mannosans polymkeric substance and from the outer mannase of the terminal cracking mannosans polymkeric substance of chain.Mannosans is meant to have the β of comprising-1, the polysaccharide of the skeleton of the seminose that 4-connects; Glucomannan is meant to have such skeleton, i.e. alternative β-1 regularly to a certain extent, the seminose that 4-connects and the polysaccharide of glucose; Polygalactomannan and galactoglucomannan are meant tool α-1, the mannosans and the glucomannan of the galactose side that 6-connects.These compounds can be acetylation.

Remove the degraded that galactose side helps polygalactomannan and galactoglucomannan by all or part of.In addition by the deacetylated degraded that helps acetylizad mannosans, glucomannan, polygalactomannan and galactoglucomannan wholly or in part.Ethanoyl can be removed by alkali or by the mannosans acetylase.The oligopolymer that is discharged by mannase or the composition by mannase and alpha-galactosidase and/or mannosans acetyl esterase can further disengage free maltose by beta-Mannosidase and/or beta-glucosidase enzyme degraded.

Alleged occurrence mannase in several genus bacillus biologies.For example people such as Talbot to have described molecular weight 3505 to 3510 pages of the Appl.Environ.Microbiol. of 56 11 phases of volume of nineteen ninety be that 162kDa and best pH are the 'beta '-mannase that comes from bacstearothermophilus of the dipolymer form of 5.5-7.5.People such as Mendoza have described the molecular weight of a kind of 38kDa of having and at the 'beta '-mannase that comes from subtilis of the pI of the optimum activity of pH5.0 and 55 ℃ and 4.8 at 551 to 555 pages of WorldJ.Microbiol.Biotech. of 1994 10 5 phases of volume.JP-0304706 discloses the 'beta '-mannase that comes from the bacillus bacterial classification of the pI of the best pH of molecular weight that the gel-filtration of a kind of 373kDa of having records, 8-10 and 5.3-5.4.JP-63056289 has described for example β of mannosans-1 of a kind of hydrolysis, the 4-D-mannopyranose glycosidic bond and the alkalescence of generation manna oligosaccharide, the production of thermally-stabilised 'beta '-mannase.JP-63036774 relates to the bacillus micro-organism FERM P-8856 that produces 'beta '-mannase and beta-Mannosidase under alkaline pH.JP-08051975 discloses the alkaline ' beta '-mannase that comes from the bacillus bacterial classification AM-001 that has a liking for alkali.Mannase of a kind of purifying that comes from bacillus amyloliquefaciens that can be used for bleached pulp and paper and preparation method thereof is disclosed among the WO 97/11164.WO91/18974 has described under extreme pH and temperature has active hemicellulase such as dextranase, zytase or mannase.WO 94/25576 discloses a kind of enzyme that demonstrates the mannosans enzymic activity, comes from microorganism Aspergillus aculeatus CBS 101.43, and it can be used for the degraded or the modification of plant or alga cells wall material.WO 93/24622 disclose can be used for the bleaching lignin cellulose pulp, from the isolating mannase of Trichoderma.A kind of hemicellulase that contains the mannosans hemicellulose of degrading is described among the WO91/18974, and a kind of mannase that comes from bacillus amyloliquefaciens of purifying is disclosed among the WO97/11164.

Specifically, this mannase will be as the alkali mannanase of giving a definition, and most preferably be the mannase that comes from bacterial origin.Particularly, cleaning compositions of the present invention will comprise being selected from and come from bacterial strain bacillus Bacillus agaradherens and/or bacillus subtilis strain 168, the alkali mannanase of the mannase of gene yght.

Term " alkali mannanase " is meant and is included in the enzyme that specified 7 to 12, preferred 7.5 to 10.5 pH scope has at least 10%, preferred at least 25%, more preferably at least 40% enzymic activity of its maximum activity.

Cleaning compositions most preferably of the present invention comprises the alkali mannanase that comes from bacillus Bacillusagaradherens.Described mannase is:

I) polypeptide a kind of by Bacillus agaradherens, that NCIMB 40482 produces, or

The polypeptide of the aminoacid sequence shown in ii) a kind of position 32-343 that is included in SEQID NO:2, or

Iii) a kind of at i) or ii) in the analogue of polypeptide of definition, its at least 70% with described homologous peptide; Or come from described polypeptide by one or several amino acid whose displacement, disappearance or interpolation; Or can play immune response with the polyclonal antibody that produces by polypeptide at described purified form.

The present invention also comprises having the active following separated polypeptide that is selected from of mannase:

(a) coding has the active polypeptide of mannase and comprises as the polynucleotide molecule of Nucleotide among the SEQ ID NO:1 97 to the nucleotide sequence shown in the Nucleotide 1029;

(b) species homologue (a);

(c) a kind of polynucleotide molecule of coding with mannosans enzymic activity, its at least 70% polypeptide identical with the aminoacid sequence of amino-acid residue 32 to 343 among the SEQ ID NO:2;

(d) with (a) and (b) or (c) complementary molecule; With

(e) (a) and (b), (c) or degenerate core nucleotide sequence (d).

Comprise that the plasmid pSJ1678 of the polynucleotide molecule (dna sequence dna) of the mannase of the present invention of encoding has been converted to the bacterial strain of a kind of intestinal bacteria (Escherichia coli), the present inventor is used for the microbial preservation budapest treaty of patented procedure according to international recognition, in (the Federal Republic of Germany of Germany microbial preservation center (DSM), Mascheroder Weg1b, D-38124 Braunschweig), on May 18th, 1998 this bacterial strain has been carried out preservation, preserving number is DSM 12180.

Second kind of most preferred enzyme is the mannase that comes from bacillus subtilis strain 168, this mannase:

I) analogue of encoding part by the dna sequence dna shown in the SEQID NO:5 or described sequence be encoded and/or

Ii) comprise the aminoacid sequence shown in SEQID NO:6 polypeptide or

Iii) a kind of at the ii) analogue of polypeptide of definition, its at least 70% with described homologous peptide; Or come from described polypeptide, or can play immune response with the polyclonal antibody that produces by polypeptide at described purified form by one or several amino acid whose displacement, disappearance or interpolation.

(a) polynucleotide molecule of encoding and having the active polypeptide of mannase and comprising the nucleotide sequence as shown in SEQ ID NO:5;

(b) species homologue (a);

(c) a kind of polynucleotide molecule of coding with mannosans enzymic activity, its at least 70% polypeptide identical with aminoacid sequence among the SEQ ID NO:6;

(d) with (a) and (b) or (c) complementary molecule; With

(e) (a) and (b), (c) or degenerate core nucleotide sequence (d).

Definition

Before discussing the present invention in more detail, at first define following term:

Term " directly to homologue (ortholog) " (or " species homologue ") is meant polypeptide or the protein that obtains from species, have homology with similar polypeptide or protein from different plant species.

Term " symbiosis homologue (paralog) " is meant from one specifies polypeptide or protein that species obtain, that have homology with not homopolypeptide or protein from same species.

Term " expression vector " is meant linearity or Circular DNA molecular structure, and it comprises that a coding operability is connected to the fragment that another provides the target polypeptides on its fragment of transcribing.This other fragment can comprise promotor and terminator sequence, and can choose wantonly and comprise one or more replication orgin, one or more selected marker, an enhanser, a polyadenylation signal etc.Expression vector generally comes from plasmid or viral DNA maybe can comprise both key elements.Expression vector of the present invention can be any expression vector that carries out recombinant DNA method easily, and the host cell that carrier is imported into is depended in the selection of carrier usually.Therefore, described carrier can be an autonomously replicationg vector, and promptly as the carrier of extrachromosomal entity existence, it duplicates and is independent of chromosome duplication, as plasmid.Perhaps, described carrier can be the carrier that is integrated into the host cell gene group and duplicates with the karyomit(e) that has been integrated when being directed into host cell.

The term that uses together with polypeptide or protein expression in this " recombinant chou is expressed " or " recombinant expressed " adopt the standard definition of this area to define.Recombinant expression of proteins is generally by using just described expression vector to carry out in the above.

Therefore when being used for polynucleotide molecule, term " isolating " is meant that polynucleotide shift out from its natural genotypic environment, and does not contain other external or unwanted encoding sequence and for being applicable to the form in the engineered protein production system.This isolating molecule is the molecule that separates and comprise cDNA and genomic clone from its physical environment.Isolated DNA molecule of the present invention does not have the gene of other and its normally associate, but may comprise 5 ' and 3 ' non-translational region such as promotor and terminator that nature exists.Those skilled in the art all are familiar with the evaluation (referring to for example Dynan and the Tijan article at Nature 316:774-778 in 1985) in relevant district.

Term " isolating polynucleotide " also can be described as " clone's polynucleotide ".When being applied to protein/polypeptide, term " isolating " is meant the protein of finding under the non-natural environment condition.In a kind of preferred form, isolating protein does not have other protein, particularly other homologous protein (i.e. " homology impurity " (referring to following content)) on substantially.40% above purity form, the more preferably protein of 60% above purity form preferably are provided.Even more preferably preferably provide the protein of high-purity forms, i.e. 80% above purity, more preferably 95% above purity even the more preferably protein of 99% above purity (purity is measured by SDS-PAGE).

Term " isolating protein/polypeptide " also can be described as " protein/polypeptide of purifying ".

Term " homology impurity " is meant any impurity (the another kind of polypeptide beyond the polypeptide for example of the present invention) of the homologous cell that derives from initial acquisition polypeptide of the present invention.

Used term in this relevant with concrete microbial source " obtain from " is meant cell polynucleotide and/or the polypeptide that is produced by concrete source or be inserted into from the gene in described source.

When relating to dna fragmentation, term " can be operatively connected " and be meant described arrangement of fragments is become to work by desired purpose, for example carries out up to terminator from the promotor transcriptional start and by encode fragment.

Term " polynucleotide " is meant a kind of deoxynucleotide of reading to 3 ' end from 5 ' end or the strand or the dichain polymer of nucleotide base.Polynucleotide comprise RNA and DNA, and can separate from natural source, external synthetic or prepare from the combination of natural and synthetic molecules.

Term " complement of polynucleotide molecule " is meant polynucleotide molecule with complementary base sequence and becomes reverse paired polynucleotide molecule with the sequence of reference.For example sequence 5 ' ATGCACGGG3 ' and 5 ' CCCGTGCAT3 ' complementation.

Term " nucleotide sequence of degeneracy " is meant the nucleotide sequence (with comparing with reference to polynucleotide molecule of coded polypeptide) that comprises one or more degenerate codons.Degenerate codon comprises different nucleotide triplets, but the same amino-acid residue of encoding (being each own coding Asp of GAU and GAC triplet).

Term " promotor " is meant that a part comprises the combination that RNA polymerase is provided and the part of the gene of the initial dna sequence dna of transcribing.Promoter sequence common (but not always) appears at 5 ' non-coding region of gene.

Term " secretory signal sequence " is meant the dna sequence dna of a coded polypeptide (" secretion peptide "), and it is as passing through its synthetic emiocytosis approach than the macromole polypeptide than a component guiding of macromole polypeptide is described.In by the Secretory Pathway transhipment, the common cleaved described secretion peptide of removing of macromole peptide.

How to use sequence of the present invention to obtain relevant in addition sequence

Disclosed sequence data that relates to the polynucleotide sequence of the mannase of the present invention of encoding can be used as the instrument of verifying other homology mannase in this.For example, polymerase chain reaction (PCR) can be used for the sequence of amplification coding from other homology mannase of various microbial sources, particularly different genus bacillus bacterial classifications.

Active testing is analyzed

Have the active polypeptide of the present invention of mannase and can carry out the mannosans enzyme assay according to standard determination method known in the art, for example solution to be measured is placed in the hole of 4 mm dias that get out on the agar plate that contains 0.2%AZCL polygalactomannan (caroubier), promptly place for measure can with 110.00 dollars of per 3 grams from Megazyme company purchase interior-1, (interconnected network address of Megazyme is: http: ∥ www.megazyme.com/Purchase/index.htmI) in the substrate of 4-β-D-mannase (Cat NO.I-AZGMA).

Polynucleotide

The isolating polynucleotide of the present invention can under the condition of moderate strictness at least, hybridize to SEQID No:1 similar size the zone or be complementary to this regional sequence.

Polynucleotide of the present invention can under under the condition of moderate strictness at least but preferred condition, specifically hybridize on the denatured double stranded dna probe of the full length sequence shown in the 97-1029 position that is included in SEQ ID NO:1 in as detailed below height strictness or any probe that comprises at least about the subsequence of the SEQ ID NO:1 of the length of 100 base pairs in.The suitable experiment condition that is determined at the hybridization between the nucleotide probe and homologous dna or RNA sequence under moderate or the highly strict condition comprises the pre-soaking of the filter membrane that contains dna fragmentation or RNA, so that in 5 * SSC (sodium chloride/sodium citrate, people such as Sambrook, 1989) hybridization 10 minutes and filter membrane are at 5 * SSC in, 5 * Denhardt ' s solution (people such as Sambrook, 1989), 0.5%SDS and the ultransonic salmon sperm DNA of 100 mcg/ml sex change (people such as Sambrook, 1989) prehybridization in the solution, then under about 45 ℃, comprise 10 nanograms/milliliter random primers (Feinberg.A.P. and Vogelstein.B. (1983), Anal.Biochem.132:6-13), hybridization is 12 hours in the same solution of (specific activity is higher than 1 * 109cpm/ μ g) probe of 32P-dCTP-mark.Then with filter membrane in 2 * SSC, 0.5%SDS at least 60 ℃ (moderate strictnesses), more preferably at least 65 ℃ (in/highly strict) even more preferably at least 70 ℃ (highly strict) and more preferably at least 75 ℃ (very highly strict) washed twice 30 minutes down also.

The molecule of oligonucleotide probe hybridization adopts the X-ray sheet to detect under these conditions.

As noted earlier, the isolating polynucleotide of the present invention comprise DNA and RNA.The method of DNA isolation and RNA is familiar with by those skilled in the art.The DNA and the RNA of coding target gene can clone in gene pool or DNA library by the known method of those skilled in the art.

The polynucleotide that then coding had the active polypeptide of mannase of the present invention are identified and are separated by for example hybridization or PCR.

The present invention also provides from the corresponding polypeptide of different bacterial isolateses and polynucleotide (directly to homologue or symbiosis homologue).Special meaningfully from Gram-positive bite the alkali bacterial strain, comprise the mannosans enzyme polypeptide of genus bacillus bacterial classification.

Species homologue with the active polypeptide of mannase of the present invention can use by the clone technology of data provided by the invention and composition and routine clones.For example, dna sequence dna of the present invention can use the chromosomal DNA clone who obtains from the cell type of marking protein.The DNA source that is fit to can be surveyed the RNA trace by the probe of disclosed sequences Design in thus and identify.Chromosomal DNA from positive cell line prepares the library then.Can separate coding by the whole bag of tricks then and have the active polypeptide of mannase dna sequence dna of the present invention, such as surveying or survey with one or more sets degeneracy probes based on disclosed sequence by using by the probe of disclosed sequences Design in this specification sheets and claims.It is the primer clone of disclosed sequences Design in PCR (Mullis, United States Patent (USP) 4683202), the use thus that dna sequence dna of the present invention also can use polymerase chain reaction.In other method, the DNA library can be used for transforming or transfection host cell, and the expression of target dna detects as the available antibody (mono-clonal or polyclone) that produces at the mannase from B.agaradherens NCIMB40482 clone, expression and purifying described in material and method and the embodiment 1, perhaps detects by relating to the active testing with the active polypeptide of mannase.

Encoding part be cloned into the dna sequence dna of the plasmid pSJ1678 that is present among the intestinal bacteria DSM 12180 and/or similar DNA sequence of the present invention mannase can from generation have the mannosans degrading activity enzyme bacteria culture Bacillus agaradherens the bacterial strain clone, preferably from bacterial strain NCIMB 40482 clones, or from described other or relevant biological cloning in this.

Perhaps; similarly sequence can make up on the basis of the dna sequence dna (believing that it is identical with appended SEQ ID NO:1) that obtains from the plasmid that is present in intestinal bacteria DSM 12180; it for example is the one subsequence; and/or can not produce by another aminoacid sequence of the mannase of dna sequence encoding but its nucleotide subsitution of codon purposes that is equivalent to carry out the host living beings of described enzyme production makes up, or make up by importing the nucleotide subsitution that can produce different aminoacids sequence (being the variant of mannosans degrading enzyme of the present invention) by importing.

Polypeptide

32 to 343 the aminoacid sequence of SEQ ID NO:2 is a sophisticated mannosans enzyme sequence.

The present invention also provides basically and the polypeptide of SEQ ID NO:2 and its species homologue (symbiosis homologue or directly to homologue) homologous mannosans enzyme polypeptide.Term " homologous basically " is used to refer to the sequence shown in 32 to 343 in the amino acid with 70%, preferred at least 80%, more preferably at least 85% even more preferably at least 90% sequence and SEQ ID NO:2 in this or it is directly to homologue or the identical polypeptide of symbiosis homologue.These polypeptide more preferably at least 95%, most preferably 98% or 32 to 343 in the amino acid of above and SEQ ID NO:2 shown in sequence or it is directly identical to homologue or symbiosis homologue.Sequence identity property per-cent is measured by ordinary method by means of computer program known in the art, such as by means of intactly incorporating the Needleman of this paper by reference into as it, S.B. and Wunsch, C.D. at Joumal of Molecu1ar Biology in 1970,48, disclosed in the 443-453 page or leaf, at GCG routine package (Program Manual for the Wisconsin Package, Version 8, and August 1994, Genetics Computer Group, 575 Science Drive, Madison, Wisconsin, USA 53711) in the GAP that provides carry out.Adopt following setting to carry out peptide sequence relatively when using GAP: 3.0 GAP generates the GAP expansion compensation (extension penalty) of compensation (creation penalty) and 0.1.

The sequence identity property of polynucleotide molecule uses GAP to measure by similar approach, and its GAP adopts following setting to carry out dna sequence dna relatively: 5.0 GAP generates the GAP expansion compensation of compensation and 0.3.

Zymin of the present invention preferably derives from microorganism, preferably derive from bacterium, archea or fungi, particularly derive from bacterium such as the bacterium that belongs to bacillus, preferably belong to the bacterium of basophilic Bacillus strain, described basophilic Bacillus strain is selected from the Bacillus strain of Bacillusagaradherens bacterial classification and height correlation, in the genus bacillus bacterial classification of described height correlation all bacterial classifications preferably at least 95% even more preferably at least 98% on wire 16SrDNA sequence with Bacillus agaradherens homology.

Basically homologous protein and polypeptide are characterised in that and have one or more amino-acid substitutions, disappearance or interpolation.These variations are preferably the variation of small character, and it is folding or active other displacement of conservative amino acid displacement (referring to table 2) and not remarkably influenced protein or polypeptide; Little disappearance (general about 30 the amino acid whose disappearances of 1-) and little amino or the extension of C-terminal, such as the little connection peptides of aminoterminal methionine residue, about 20 to 25 residues of as many as or little extension (a kind of affinity tag) such as the polyhistidyl section of being convenient to purify, a-protein (people such as Nilsson, EMBOJ.4:1075,1985; People such as Nilsson, Methods Enzymol.198:3,1991).Generally speaking referring to the people such as Ford that incorporate this paper by reference at ProteinExpression and Purification 2:95-107, the article in 1991.The DNA of coding affinity tag can be from supplier (Pharmacia Biotech for example, Piscataway, NJ; New England Biolabs, Beverly MA) locates to buy.

But even above-mentioned variation is preferably the variation of little character, this variation also may be the variation of big character, such as extending to 300 amino acid or the above fusion than big polypeptide and mannosans enzyme polypeptide of the present invention as amino or C-terminal.

Table 1

The displacement of conservative amino acid

Alkalescence arginine, Methionin, Histidine

Acid L-glutamic acid, aspartic acid

Polarity glutamine, l-asparagine

Hydrophobicity leucine, Isoleucine, Xie Ansuan

Aromatics phenylalanine, tryptophane, tyrosine

Small molecules glycine, L-Ala, Serine, Threonine, methionine(Met)

Except 20 standard amino acids, the also replaceable amino-acid residue of non-standard amino acid (such as 4-oxyproline, 6-N-methyllysine, 2-aminoisobutyric acid, isovaline and a-methyl Serine) according to polypeptide of the present invention.The non-conservation amino acid of limited quantity, not by genetic code amino acids coding and the replaceable amino-acid residue of alpha-non-natural amino acid." alpha-non-natural amino acid " modified behind protein synthesis, and/or has the chemical structure different with standard amino acid on its side chain.But alpha-non-natural amino acid chemosynthesis or preferably can buy comprises pipecolinic acid, thiazolidine carboxylic acid, dehydroproline, 3-and 4-methylproline and 3,3-dimethyl proline(Pro).

Indispensable amino acid in mannosans enzyme polypeptide of the present invention can identify according to the known method of those skilled in the art, such as with site-directed mutagenesis or alanine scanning mutagenesis (Cunningham and Wells, Science 244:1081-1085,1989).In a kind of technology in back, the single alanine sudden change imports in each residue of molecule, and the mutating molecule that obtains carries out biological activity (being the mannosans enzymic activity) test to identify amino-acid residue, and it is important to molecular activity.Also referring to the article of people such as Hilton in J.Biol.Chem.271:4699-4708 in 1996.The avtive spot of described enzyme or other biological interaction also can be measured by the physical analysis of the structure of carrying out together with the amino acid whose sudden change in contact site of inferring, such as by measuring as technology such as nucleus magnetic resonance, crystallography, electron diffraction or photoaffinity labeling.Also referring to people such as for example de Vos at Science 255:306-312 in 1992,1992 article; People such as Smith are at the article of J.Mol.Biol.224:899-904 in 1992; People such as Wlodaver are at FEBS Lett in 1992, the article among the 309:59-64.The evaluation of indispensable amino acid also can be by adopting and analysis deduction according to the homologue of the relevant polypeptide of polypeptide of the present invention.

Can carry out a plurality of amino-acid substitutions and use the method for known mutagenesis, reorganization and/or reorganization and then relevant screening method such as by Reidhaar-Olson and Sauer (Science241:53-57,1988), Bowie and Sauer (Proc.Natl.Acad.Sci.USA 86:2152-2156,1989), WO95/17413 or WO95/22625 disclosed method are tested.In brief, these authors disclose the reorganization/reorganization (WO95/17413, WO95/22625) of the position that is used for selecting at random simultaneously on two or more polypeptide or different sudden changes and have then selected the function of polypeptide, also check order polypeptide through mutagenesis then to measure the method for each position tolerable metathetical scope.Other available method comprises phage display (people such as Lowman for example, Biochem.30:10832-10837,1991; People's such as Ladner U.S. Patent number 5223409; Huse, WIPO Publication WO 92/06204) and zone (region-directed) mutagenesis (people such as Derbyshire, Gene 46:145,1986; People such as Ner, DNA 7:127,1988).

As above disclosed mutagenesis/reorganization method can combine with high throughput, automatic screening method and measure the activity of polypeptide that clone in the host cell, mutagenic treatment.The dna molecular of the mutagenic treatment of coding active polypeptide can reclaim from host cell, and uses modern instrument equipment to check order fast.These methods can determine fast the single amino acids residue in target polypeptides importance and can be applicable to the polypeptide of unknown structure.

Use method discussed above, those skilled in the art can identify and/or prepare various basically with residue 32 to 343 homologies of SEQ ID NO:2 and keep the active polypeptide of mannase of wild-type protein.

Protein production

Protein of the present invention and polypeptide (comprising full length protein, its fragment and fusion rotein) can be produced in host cell in genetic engineering according to the technology of routine.The host cell that is fit to is available foreign DNA conversion or transfection and the cell type of growing in substratum, and comprises the higher eukaryotic cell of bacterium, fungal cell and cultivation.Preferred bacterium cell, the particularly culturing cell of Gram-positive biology.Preferred especially gram-positive cell from bacillus, such as from subtilis, bacillus lentus (Bacillus lentus), bacillus brevis (Bacillus brevis), bacstearothermophilus, Alkaliphilic bacillus (Bacillus alkalophilus), bacillus amyloliquefaciens, Bacillus coagulans (Bacilluscoagulans), Bacillus circulans (Bacillus circulans), bacillus lautus (Bacilluslautus), bacillus thuringiensis (Bacillus thuringiensis), the cell of Bacillus licheniformis (Bacillus licheniformis) and Bacillus agaradherens is particularly from the cell of Bacillus agaradherens.

Operation clone's dna molecular and the technology that foreign DNA imports various host cells is disclosed in the people's such as Sambrook that incorporate this paper by reference into molecular cloning: test guide, second edition, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, 1989; People such as Ausubel (editor), Current Protocols in Molecular Biology, JohnWiley and Sons, Inc., NY, 1987; " subtilis and other gram-positive microorganism ", people such as Sonensheim, 1993, American Society for Microbiology is among the Washington D.C.

In general, the dna sequence dna operability of the mannase of the present invention of encoding is connected to it and expresses on other required genetic constitution, and this genetic constitution generally comprises transcripting promoter and the terminator in expression vector.Described carrier also comprises one or more selected markers and one or more replication orgin usually, although one skilled in the art will realize that selected marker can provide in some system on the carrier that separates, and duplicating of foreign DNA can be provided to the host cell gene group by integration.The selection of promotor, terminator, selected marker, carrier and other composition is the thing of the conventional design in those skilled in the art's level.Many this compositions are described in the document and can obtain by supplier.

For polypeptide being imported to the Secretory Pathway of host cell, secretory signal sequence (being also referred to as leader sequence, presequence or pre-sequence) provides in expression vector.Described secretory signal sequence can be the sequence of described polypeptide or can come from another secretory protein or de novo synthesis.Various suitable secretory signal sequences are familiar with by those skilled in the art, and can be with reference to " subtilis and other gram-positive microorganism ", people such as Sonensheim, 1993, American Societyfor Microbiology, Washington D.C. and Cutting.S.M. (editor) " MolecularBiological Methods for Bacillus ", John WileyandSons, the 1990 relevant secretory signal sequences that are fit to, particularly relevant in Bacillus host cell excretory further describe.Secretory signal sequence is attached in the dna sequence dna with correct frame.Although some signal sequence can be positioned at other position of target dna sequence, secretory signal sequence usually by 5 ' be positioned at the coding target polypeptides dna sequence dna in (referring to people's such as for example Welch U.S. Patent number 5037743; People's such as Holland U.S. Patent number 5143830) in.

The host cell of conversion or transfection is cultivated in the substratum that comprises other required component of nutrient and selected host cell growth according to the method for routine.Various suitable substratum (comprising defined substratum and complex medium) are familiar with by those skilled in the art, and generally comprise carbon source, nitrogenous source, indispensable amino acid, VITAMIN and mineral substance.As needs, substratum also can comprise such as components such as somatomedin or serum.General described growth medium selects to comprise the cell of the DNA that external source adds, and for example by medicament selection or the shortage by basic nutrient, described basic nutrient replenishes to host cell by selected marker or the cotransfection that carries on expression vector.

Protein separation

When expressed recombinant polypeptide was secreted, described polypeptide can be purified from growth medium.Preferably before purifying, described polypeptide removes expression host cell (for example by centrifugal) from substratum.

When expressed recombinant polypeptide during not from secretory host cell, preferably host cell is broken and polypeptide is discharged in the water " extract ", this is the fs of this purification techniques.Preferably before cell rupture, collect expression host cell (for example by centrifugal) from substratum.

Lysis can be by routine technology such as by N,O-Diacetylmuramidase digestion or cell is undertaken by high pressure.This cell rupture technology further describe can referring to (the Protein Purification of Robert K.Scobes, second edition, Springer-Verlag).

No matter whether expressed recombinant polypeptide (or chimeric polyeptides) is secreted, and it all can use fractional separation and/or conventional method of purification and medium to carry out purifying.

Ammonium sulfate precipitation and acid or chaotropic agent extract the fractional separation that can be used for sample.The example of purification step can comprise hydroxyapatite, size exclusion, FPLC and RPLC.The anionic exchange medium that is fit to comprises the dextran of deriving, agarose, Mierocrystalline cellulose, polyacrylamide, property silica etc.Preferred PEI, DEAE, QAE and Q derivative, and the preferred especially quick sepharose of DEAE (can be available from Pharmacia, Piscataway, NJ).Chromatography media comprises by phenyl, butyl or octyl group deutero-medium, such as phenyl-agarose FF (Pharmacia), Toyopearl butyl 650 (Toso Haas, Montgomeryville, PA), octyl group-agarose (Pharmacia) etc.; Or polyacrylic resin, such as Amberchrom CG 71 (Toso Haas) etc.The solid carrier that is fit to comprises granulated glass sphere, silica-based resin, celluosic resin, sepharose 4B, Sepharose pearl, polystyrene bead, cross-linked polyacrylamide resin etc., and they are insoluble under working conditions.Thereby these carriers can make that can pass through amino, carboxyl, sulfydryl, hydroxyl and/or sugar moieties is connected with protein with the active group modification.The example of coupling chemistry comprises cyanogen bromide-activated, N-hydroxy-succinamide activation, epoxide activation, sulfydryl activation, hydrazides activation and is used for the carboxyl and the aminoderivative of carbodiimide coupling chemistry.These and other solid dielectric is familiar with by people and is widely used in this area, and can purchase from suppliers.

The thing that is chosen as conventional design of concrete grammar and depend in part on the character of selected carrier.Referring to for example Pharmacia LKB Biotechnology (Sweden, " affinity chromatography: principle and method " book Uppsala) in 1988.

Polypeptide of the present invention or its fragment also can prepare by chemosynthesis.Polypeptide of the present invention can be monomer or polymer, glycosylation or non-glycosylated, pegylated or non-pegylated; And can comprise or not comprise initial methionine(Met) amino-acid residue.

Based on disclosed sequence data in this, but clones coding mannase of the present invention and comprise the full length DNA sequence of the dna sequence dna shown in the SEQ ID NO:1 is 97 to 1029 dna sequence dna at least.

The clone is undertaken by the standard method that those skilled in the art are familiar with, such as passing through:

-from Bacillus strain, particularly B.agaradherens, NCIMB 40482 bacterial strains prepare genomic library;

-this group of storehouse is seeded on the suitable substrate plate;

-use based on the probe of SEQ ID NO:1 and identify the clone who comprises polynucleotide sequence of the present invention by the standard hybridization technique; Or pass through

-use based on primer and pass through the clone of inverse PCR strategy evaluation from described Bacillus agaradherens NCIMB 40482 genomic libraries from SEQ ID NO:1 sequence data.The more detailed data of relevant inverse PCR can be with reference to people's such as M.J.MCPherson " PCR A Practicalapproach ", Information Press Ltd., Oxford England.

Based on disclosed sequence in this (SEQ ID NO:1, SEQ ID NO:2) data, those skilled in the art's a routine work is to use genomic library from related microorganisms, particularly uses the genomic library of having a liking for the alkali bacterial classification from other bacterial strain of bacillus such as bacillus, separates the homology polynucleotide sequence of coding homology mannase of the present invention by similar strategy.

Perhaps, encode synthetic oligonucleotide probe that the DNA of mannosans of the present invention or galactomannan degradation enzyme can be by using the dna sequence dna preparation that obtains based on the plasmid from be present in intestinal bacteria DSM 12180, clone such as above-mentioned any biology from the source that is fit to easily according to well-known method.

Therefore, polynucleotide molecule of the present invention can separate from intestinal bacteria DSM 12180, and wherein the plasmid by clone's acquisition as described above is deposited.The present invention also relates to the isolating pure substantially biological culture thing of bacterial strain intestinal bacteria DSM12180.

In specification sheets of the present invention, term " zymin " is used in reference to may be from single conventional enzymic fermentation product of planting microorganism through separation and purifying, and this preparation generally includes various different enzymic activity things; Perhaps be meant the mixture of single composition enzyme, preferably by using the mixture of the enzyme that conventional recombinant technology obtains from bacterium or fungi strain, described enzyme has fermented and may be through separating respectively and purifying, and it may come from different bacterial classifications, preferably come from fungi or bacterium; Perhaps be meant the tunning of the microorganism of the host cell that is used as reorganization mannosans expression of enzymes, but described microorganism produces simultaneously as other enzyme of the abiogenous tunning of described microorganism such as pectin degrading enzyme, proteolytic enzyme or cellulase, the promptly conventional enzyme complex that is produced by corresponding natural microbial.

Also relate to a kind of method for preparing zymin of the present invention in this, described method comprise cultivation can produce mannase under the condition that allows enzyme production microorganism reclaim as wild type strain and from substratum as described in enzyme.Cultivation can use conventional fermentation technique to carry out, and for example cultivates in shaking bottle or cultivates in tool stirs with the fermentor tank of guaranteeing to induce ventilation enough in the growth medium that produces mannase.Described growth medium can comprise conventional N source such as peptone, yeast extract or casamino acids, conventional C source such as the dextrose of decrement or sucrose and inductor such as guar gum or Viscogum BE.Described recovery can use routine techniques to carry out, for example by centrifugal or filter break (if target enzyme is in cell) of the recovery carry out the separating of biomass and supernatant liquor, supernatant liquor or cell, the perhaps then further purification as EP0406314 described in or follow crystallization described in WO 97/15660.

Immune cross-reactivity

The polyclonal antibody that is used to measure immune cross-reactivity can prepare by using the mannase through purifying.More precisely, the antiserum(antisera) of anti-mannase of the present invention can be produced by the described method immunization rabbit (or other rodent) among the Immunochemistry in Practice (more particularly at 27 to 31 pages) of Blackwell ScientificPublications publication in nineteen eighty-two by method described in the 23rd chapter of the A Manual of Quantitative Immunoelectrophoresis of Blackwell Scientific Publications publication or according to A.Johnstone and R.Thorpe in 1973 according to people such as N.Axelsen.The immunoglobulin (Ig) of purifying can be for example by salt precipitation ((NH ₄) ₂SO ₄), then dialysis and for example on the DEAE-dextrane gel ion exchange chromatography come from antiserum(antisera), to obtain.Proteinic immunochemistry is identified and can be analyzed [the Handbook ofExperimental Immunology (D.M.Weir edits) of O.Ouchterlony by the Outcherlony bidirectional diffusion, Blackwell ScientificPublications, 1967, the 655-706 page or leaf], by crossed immunoelectrophoresis (people such as N.Axelsen, the 3rd and 4 chapters above) or by rocket immunoelectrophoresis people such as (, chapter 2) N.Axelsen undertaken.

The example that can be used for producing the useful bacterium of enzyme of the present invention or zymin has gram positive bacterium, preferably from genus bacillus/Bacterium lacticum subphylum, preferably from the bacterial strain of bacillus, more preferably from the bacterial strain of Bacillus agaradherens, particularly bacterial strain Bacillusagaradherens, NCIMB 40482.

The present invention includes the isolating mannase with above-mentioned character, it does not have homology impurity and can use conventional recombinant technology production.

The mensuration of mannosans enzymatic activity (ManU)

Colorimetric method for determining: substrate: from 0.2% AZCL-polygalactomannan (Megazyme, the Australia) solution in the 0.1M glycine buffer, the pH of buffer 10.0 of caroubier.Being determined at a tool stirring and temperature control is carrying out in 1.5 milliliters of Eppendorf micro tubes on 40 ℃ the hot mixing tank.0.750 milliliter of substrate was hatched 20 minutes with 0.05 milliliter of enzyme, under 15000rpm, stopped in centrifugal 4 minutes then.With supernatant liquor in 1 centimetre of cuvette under 600 nano wave lengths colorimetric.A ManU (mannosans unit of enzyme) has 0.24 absorbancy in 1 centimetre of cuvette.

The obtention of Bacillus agaradherens mannase NCIMB 40482

Bacterial strain

Bacillus agaradherens NCIMB 40482 comprises the dna sequence dna of the mannase of encoding.

Coli strain: preparation intestinal bacteria SJ2 cell also uses a Gene Pulser available from BIO-RAD ^TMElectroporation apparatus transforms (Diderichsen, B., Wedsted by supplier is described by electroporation, U., Hedegaard, L., Jensen, B.R., Sjoholm, C. (1990) alpha-acetolactate decarboxylase of encoding--the clone of the aldB of-a kind of extracellular enzyme from bacillus brevis, J.Bacteriol., 172,4315 to 4321 pages).

Subtilis PL2306: this bacterial strain is the subtilis DN1885 (Diderichsen of tool disruptive apr and npr gene, B., Wedsted, U., Hedegaard, L., Jensen, B.R., Sjoholm, C. (1990) coding alpha-acetolactate decarboxylase--the clone of the aldB of-a kind of extracellular enzyme from bacillus brevis, J.Bacteriol., 172,4315 to 4321 pages), it breaks in the transcription unit of known subtilis cellulose enzyme gene, produces the cell of cellulase feminine gender.Described breaking basically according to A.L.Sonenshein, described carrying out among the Bacillus subtilis and other Gram-PositiveBacteria that J.A.Hoch and Richard Losick compiled in 1993,618 pages of American Society for Microbiology.

As Yasbin, R.E., Wilson, G.A and Young, described preparation and the transformed competence colibacillus cell of F.E in the article " Transformation and transfection in lysogenicstrains of Bacillus subtilis:evidence for selective induction of prophage incompetent cells " among the J.Bacteriol.121:296-304 in 1975.

Plasmid

PSJ1678 (incorporating in full elaborating among the WO 94/19454 of this paper by reference into) as it

PMOL944: this plasmid is a kind of pUB110 derivative, mainly comprises element, the kalamycin resistance gene that described plasmid can be bred and have strong promoter and from the signal peptide of the amyL gene clone of Bacillus licheniformis ATCC 14580 in subtilis.The sort signal peptide comprises a SacII site that makes it easy to the protein maturation DNA partly of clones coding and the fusion of this signal peptide.This causes a kind of expression of protein precursor of the cell appearance that leads.

Described plasmid makes up by means of the genetic engineering technique of routine, and it is summarized as follows:

The structure of pMOL944:

PUB110 plasmid (McKenzie, people such as T., 1986, Plasmid 15:93-103) is digested with single restriction enzyme NciI.Will be from the amyL promotor amplification PCR fragment that goes up coding at plasmid pDN1981 (people such as P.L.Jorgensen, 1990, Gene, 96,37-41 page or leaf) with NciI digestion and be inserted among the pUB110 of NciI digestion and form plasmid pSJ2624.

Two kinds of used PCR primers have following sequence: #LWN5494 5 '-GTCGCCGGGGCGGCCGCTATCAATTGGTAACTGTATCTCAGC-3 ' #LWN5495 5 '-GTCGCCCGGGAGCTCTGATCAGGTACCAAGCTTGTCGACCTGCAGAATGAGGCAGC AAGAAGAT-3 '

Described primer #LWN5494 is inserted into the NotI site of described plasmid.

Then plasmid pSJ2624 is digested with SacI and NotI, and a new PCR fragment of the amyL promotor that will encode on plasmid pDN1981 amplification is with SacI and NotI digestion, and this dna fragmentation is inserted among the pSJ2624 of SacI-NotI digestion and forms plasmid pSJ2670.

With identical promoters but oppositely to substitute first amyL promotor clone with this clone.Two kinds of primers that are used for pcr amplification have following sequence: #LWN5938 5 '-GTCGGCGGCCGCTGATCACGTACCAAGCTTGTCGACCTGCAGAATGAGGCAGCAAG AAGAT-3 ' #LWN5939 5 '-GTCGGAGCTCTATCAATTGGTAACTGTATCTCAGC-3 '

Then with plasmid pSJ2670 with restriction enzyme PstI and BclI digestion, and will be from a PCR fragment of the clone's of coding alkali starch enzyme SP722 (being disclosed in it incorporates into the International Patent Application WO 95/26397 of this paper in full by reference) dna sequence dna amplification with PstI and BclI digestion and insert and form plasmid pMOL944.Two kinds of primers that are used for pcr amplification have following sequence: #LWN7864 5 '-AACAGCTGATCACGACTGATCTTTTAGCTTGGCAC-3 ' #LWN7901 5 '-AACTGCAGCCGCGGCACATCATAATGGGACAAATGGG-3 '

Primer #LWN7901 is inserted into a SacII site of described plasmid.

Carry out the clone of mannase gene from Bacillus agaradherens

The preparation of genomic dna:

Press breeding bacterial strain Bacillusagaradherens NCIMB 40482 in the described liquid medium among the WO94/01532.After under 30 ℃ and 300rpm, hatching 16 hours, harvested cell and by the described method of people such as Pitcher (Pitcher, D.G., Saunders, N.A., Owen, R.J. (1989) are with guanidine thiocyanate rapid extraction bacterial genomes DNA, Lett.Appl.Microbiol., 8,151 to 156 pages) isolation of genomic DNA.

Make up genomic library:

Genomic dna partly digested with restriction enzyme Sau3A and on 0.7% sepharose by the electrophoresis size fractionation.Size is passed through electrophoretic separation (Dretzen.G., Bellard, M., Sassone-Corsi, P., Chambon, P. (1981) in the fragment between 2 to 7kb on the DEAE-cellulose paper.A kind of reliable method from agarose and acrylamide gel recovery dna fragmentation, Anal Biochem., 112,295-298 page or leaf).

The separated DNA fragment is connected on the pSJ1678 plasmid DNA of BamHI digestion, and will connects mixture and be used for transformed into escherichia coli SJ2.

The evaluation of positive colony

To in intestinal bacteria, on the LB agar plate that contains 0.2%AZCL-polygalactomannan (Megazyme) and 9 mcg/ml paraxin, screen in the DNA library as above-mentioned structure, and 37 ℃ of overnight incubation.Express the active clone of mannase and demonstrate the blue haloing that spreads.Separate plasmid DNA from one of these clones (shaking 37 ℃ of incubated cells time in TY) by Qiagen plasmid spin preps by 1 milliliter of incubated overnight liquid with 9 mcg/ml paraxin with at 250rpm.

This clone (MB525) further identifies by clone's the segmental dna sequencing of Sau3ADNA.Dna sequencing is undertaken by using Taq deoxidation termination cycle sequencing test kit (Perkin-Elmer, the U.S.), fluorescently-labeled terminator and the suitable oligonucleotide primer step as primer to move (primerwalking).

The analysis of sequence data is according to the Nucleic AcidsRes. of people such as Devereux in 1984, and the method described in 12,387 to 395 pages is carried out.The sequence of coding mannase shows in SEQ ID NO:1.The deutero-protein sequence is shown among the SEQ ID NO:2.

Subclone and the expression of mannase in subtilis:

The dna sequence dna of coding mannase of the present invention uses and comprises that the PCR primer sets of following two oligonucleotide carries out pcr amplification: mannase. upstream .SacII5 '-CAT TCT GCA G

CA GCA AGT ACA GGC TTT TATGTT GAT GG-3 ' mannase. downstream .NotI5 '-GAC GAC GTA CAA

G CTA TTT CCC TAA CATGAT GAT ATT TTC G-3 '.

Restriction site SacII and NotII rule in the bottom.

The PCR reaction of using Amplitaq archaeal dna polymerase (Perkin Elmer), be used as template according to manufacturer's explanation from aforesaid B.agaradherens NCIMB 40482 isolating chromosomal DNAs.Described PCR is reflected at the PCR damping fluid of every kind of primer of the every kind of dNTP, 2.5 AmpliTaq of unit polysaccharases (Pekin-Elmer, Cetus, the U.S.) and the 100pmol that comprise 200 μ M, and (10mM Tris-HCl, pH 8.3,50mM KCl, 1.5mM MgCl ₂, 0.01% (w/v) gelatin) in carry out.

Described PCR reaction uses DNA thermal cycler (Landgraf, Germany) to carry out.94 ℃ hatch 1 minute (once) after, carry out 30 94 ℃ of 30 seconds of following sex change, 60 ℃ of annealing 1 minute with 72 ℃ of PCR circulations of extending 2 minutes (circulation).The amplified production of getting 5 microlitre equal portions is by (NuSieve FMC) goes up electrophoresis and analyzes at 0.7% sepharose.1.4kb the suitable amplification of this gene fragment appears showing in the dna fragmentation of size.

The segmental subclone of PCR

PCR product as 45 microlitre equal portions of above-mentioned generation uses QIA fast PCR purification kit (Qiagen, the U.S.) purifying according to manufacturer's explanation.DNA elution in the 10mM Tris-HCl of 50 microlitre pH 8.5 through purifying.

PCR fragment through purifying digests, hangs down gelation temperature agarose (SeaPlaque GTG 0.8% with SacII and NotI with 5 microgram pMOL944 and 25 microlitres, FMC) electrophoresis in the gel, use the QIA PhastGel to extract test kit (Qiagen, the U.S.) purifying from the gel cutting-out and according to manufacturer's explanation associated clip.Then isolating PCR dna fragmentation is connected in the pMOL944 of SacII-NotI digestion and purification.Described connection uses every kind of dna fragmentation of 0.5 microgram, T4 dna ligase and the T4 ligase enzyme damping fluid (BoehringerMannheim, Germany) of 1U to spend the night at 16 ℃.

Connect mixture and be used to transformed competence colibacillus subtilis PL2306.Cell transformed is seeded on the LBPG-10 mcg/ml kantlex flat board.37 ℃ hatch 18 hours after, on flat board, see bacterium colony.By analyzing several clones from incubated overnight liquid isolated plasmid dna.

A this positive colony is heavily rule several times on as above used agar plate, and this clone is called as MB594.This clone MB594 in TY-10 mcg/ml kantlex 37 ℃ of grow overnight, suggestion according to the preparation of the relevant bacillus subtilis bacteria plasmid of manufacturer in second day uses Qiaprep Spin Plasmid Miniprep Kit#27106 with 1 ml cells separation quality grain from this cell.It is the dna sequence dna of the 94-1404 position of appended SEQ ID NO:3 with the maturing part that discloses corresponding to mannase that this DNA is carried out dna sequencing.The deutero-mature protein is shown among the SEQ ID NO:4.Because the design of used downstream primer in PCR, by 3 ' the terminal situation that as if is changed shown in SEQ ID NO:3 of the mannase of the sequence encoding of SEQ ID NO:1.The aminoacid sequence that obtains is shown among the SEQ ID NO:4, and the C-terminal (SHHVREIGVQFSAADNSSGQTALYVDNVTLR) of obvious SEQ ID NO:2 is changed into the C-terminal (IIMLGK) of SEQ IDNO:4.

Substratum:

TY (as Ausubel, people such as F.M (editor), John Wiley and Sons is described in " the Current protocols in Molecular Biology " of nineteen ninety-five publication);

LB agar (as Ausubel, people such as F.M (editor), John Wiley and Sons is described in " the Current protocols in Molecular Biology " of nineteen ninety-five publication);

LBPG is the LB agar (referring to top) that replenishes with 0.5% glucose and 0.05M potassiumphosphate (pH 7.0).

Described in BPX substratum such as the EP 0506780 (WO 9I/09129).

Expression, purification and evaluation from the mannase of Bacillus agaradherens

By the clone MB594 of as above material and the described acquisition of method part in the shaking in 25 * 200 milliliters of BPX substratum that have 10 mcg/ml kantlex in the bottle of 500 milliliters two band baffle plates, in 37 ℃ and 300rpm growth 5 days down.

Collect 6500 milliliters clone MB594 (lot number #9813) shake-flask culture liquid and with pH regulator to 5.5.Under agitation add 146 milliliters of cationics (C521) and 292 milliliters of anionic agent (A130) flocculate.By using a Sorval RC 3B whizzer under 6 ℃, to separate floss in centrifugal 20 minutes with 9000rpm.Supernatant liquor uses Whatman glass filter membrane GF/D and C clarification, concentrates on cutoff value is the filtron of 10kDa at last.

With sodium hydroxide 750 milliliters of these concentrated solutions are adjusted to 7.5 pH.Clear solution is splined on 900 milliliters of Q-Sepharose posts of Tris (pH 7.5) equilibrated with 50 mmoles carries out anion-exchange chromatography.Use sodium-chlor gradient elution mannosans enzymic activity binding substances.

Described pure enzyme has shown the simple spectrum band of 38kDa molecular weight on SDS-PAGE.The dna sequence dna that the aminoacid sequence of mannase is promptly translated is shown among the SEQ ID NO:2.

The mensuration of power constant:

Substrate: Viscogum BE (caroubier) and reducing sugar analysis (PHBAH).Viscogum BE is available from Sigma (G-0753).

Use the Viscogum BE of different concns and hatch for 10 times at pH and carried out power determination in 20 minutes at 40 ℃:

K _Catalysis: 467/ second

K _m：0.08g/l

MW：38kDa

PI (iso-electric point): 4.2

The optimum temps of finding mannase is 60 ℃.

The pH profile of activity shows that maximum activity is between pH 8 to 10.

Dsc (DSC) obtains that the fusing point under the pH 7.5 is 77 ℃ in the Tris damping fluid, and it is very thermally-stabilised to demonstrate this kind of enzyme.

Use 0.2% from the AZCL-polygalactomannan of caroubier as substrate, and as mentioned above 40 ℃ of washing composition compatiblenesies of hatching demonstrate with the good compatibleness of conventional liq washing composition and with the good compatibleness of conventional powdered detergent.

The obtention of subtilis mannase 168

The following evaluation and purification of carrying out the subtilis 'beta '-mannase: search for the subtilis genome identical (people such as Mendoza with known bacillus bacterial classification beta-mannase gene sequence, Biochemica et Biophysica Acta 1243:552-554,1995).The ydh T coding region of its product the unknown demonstrates the similarity with known genus bacillus 'beta '-mannase 58%.Design following oligonucleotide and come the sequence of the maturing part of the 'beta '-mannase that amplification coding infers: 5 '-GCT CAA TTG GCG CAT ACT GTG TCG CCTGTG-3 ' and 5 '-GAC GGA TCC CGG ATT CAC TCA ACG ATT GGCG-3 '.Total genomic dna from subtilis 1A95 bacterial strain is used as the template of using aforementioned primer amplification ydh T maturation zone.PCR makes the gene A MP PCR test kit of apparatus AMPLITAQ archaeal dna polymerase, and (FosterCity CA) carries out for Perkin Elmer, Applied Biosystems.Beginning is 95 ℃ of circulations of then carrying out 25 follow procedures after unwinding 5 minutes: 95 ℃ were unwind 1 minute, 55 ℃ of annealing 2 minutes and 72 ℃ of extensions 2 minutes.After last circulation, reactant keeps 10 minutes to finish extension at 72 ℃.Described PCR product uses QIA fast PCR purification test kit, and (Qiagen, Chatsworth CA) purify.

Will be from following being inserted into the expression vector pPG1524 (as described above) in ydh T maturation zone of subtilis 1A95 bacterial strain amplification.The 1028bp fragment of amplification is digested with MfeI and BamHI.Expression vector pPG1527 is digested with EcoRI and BamHI.The restriction product uses QIA fast PCR purification test kit, and (Qiagen, Chatsworth CA) purify.Described two fragments use the T4 dna ligase to connect (13 hours, 16 ℃), and are used for transformed competence colibacillus bacillus coli DH 5-α bacterial strain.Cultivate the amicillin resistance bacterium colony for preparation DNA.Then DNA is identified by restriction analysis.Plasmid pPG3200 comprises the maturation zone of ydh T gene.Use plasmid pPG3200 transformed competence colibacillus subtilis PG632 bacterial strain (people such as Saunders, 1992) then.

7 kinds of kalamycin resistance subtilis clones of picking and a kind of PG632 contrast clone, and make it replenish 1 milliliter of 25%maltrin, 120 microlitre 10mM MnCl ₂With the middle growth of 20 milliliter of 20/20/5 substratum (20g/L tryptone, 20g/L yeast extract, 5g/L NaCl) of 20 microlitre 50mg/ml kantlex.Be cloned in 250 milliliters of grow overnight marking proteins in the bottle that shake of being with baffle plates that shake under 37 ℃ of 250rpm.Go out cell with 14000rpm centrifugation in 15 minutes.Every kind of supernatant liquor of one microlitre dilutes with 99 microlitre 50mM sodium acetates (pH6.0).Get this diluent of 1 microlitre according to the manufacturer illustrate use in-1,4-'beta '-mannase β-Mannazyme Tabs (Megazyme, Ireland) measures.On Beckman DU640 spectrophotometer, read absorbancy in the 590nm place.Clone 7 demonstrates 1.67 high absorbance value.PG632 has not demonstrated absorbancy to impinging upon the 590nm place.

Supernatant liquor is by (Novex, San Diego Ca) go up through the SDS-PAGE analysis to confirm the protein of desired 38kDa size in the 10-20%Tris-glycine gels.Sample is according to being prepared as follows.With 500 microlitre ydh T clone 7 sample and PG632 supernatant liquor with 55.5 microlitres, 100% trichoroacetic acid(TCA)s (Sigma) precipitation, wash, be suspended in the 50 microlitre Tris-glycine SDS sample buffers (Novex) again and boiled 5 minutes with 100 microlitres, 5% trichoroacetic acid(TCA).Every kind of sample get a microlitre under 30 mA on described gel electrophoresis 90 minutes.Observe big protein belt the ydh T of 38kDa place clone 7.

Carry out 10 liters of subtilis ydh T clones' 7 fermentation at B.Braun Biostat C fermentor tank.Fermentation condition is as follows.At 37 ℃, cell growth 18 hours in being similar to 20/20/5 rich medium.During fermentation ends, remove cell and use the tangential flow filtration system supernatant concentration to 1 liter.The ultimate yield that records the 'beta '-mannase in concentrated supernatant is 3g/l.

The following purification of carrying out from the 'beta '-mannase of fermented supernatant fluid: at 4 ℃ with 500ml supernatant liquor centrifugal 10 minutes with 10000rpm.In 4 ℃ the centrifugal supernatant liquor is passed through Spectrapor 12000-14000mol.wt. mwco membrane (Spectrum) dialysed overnight in the 10mM potassiumphosphate (pH 7.2) of replacing twice (each 4 liters) then.Will be at 4 ℃ through the supernatant liquor of dialysis under 10000rpm centrifugal 10 minutes.With 200 milliliters of Q Sepharose fast flow (Pharmacia) anion-exchange column 20 ℃ down with 1 liter of 10mM potassiumphosphate (pH 7.2) balance, and with on 300 milliliters of supernatant liquors on post.Collect 210 milliliters (sample A) and 175 milliliters (sample B) two components that flow through.Except sample dilutes with 199 microlitre 50mM sodium acetates (pH 6.0), two components and front to be measured like that, they demonstrate 0.38 and 0.52 absorbancy respectively.Every kind of sample get 2 microlitres join 8 microlitre Tris-glycine SDS sample buffers (Novex, Ca) in and boiled 5 minutes.(Novex CA) went up electrophoresis 90 minutes in the 10-20%Tris-glycine gels with the sample that obtains under 30mA.In each sample, all exist and account for more than 95% of gross protein corresponding to the master tape of 38kDa.Use bovine serum albumin(BSA) two samples to be carried out BCA protein determination (Pierce) according to manufacturer's explanation as standard.Sample A and sample B comprise the 'beta '-mannase of 1.3mg/ml and 1.6mg/ml respectively.Confirm proteinic identity by ion injection mass spectrum and aminoterminal amino acid sequence analysis.

Be used to identify enzymic activity with the 'beta '-mannase sample of purifying is following.All measure all used foregoing in-1,4-'beta '-mannase Beta-Mannazyme Tabs (Megazyme, Ireland).Activity in the 3.0-9.0pH scope is carried out in 50mM Citrate trianion-phosphate buffered saline buffer, then uses 50mMCAPSO (Sigma) for the determination of activity under pH 9.5, then uses 50mM CAPS damping fluid for the activity in the pH10.0-11.0 scope.The best pH scope of finding the subtilis 'beta '-mannase is 6.0-6.5.Temperature activity distribution curve is measured in 50mM Citrate trianion-phosphate buffered saline buffer (pH 6.5).Described enzyme demonstrates optimum activity at 40-45 ℃.Described subtilis 'beta '-mannase is below 15 ℃ and kept tangible activity more than 80 ℃.In using according to manufacturer's explanation-1,4-'beta '-mannase Beta-Mannazyme Tabs (Megazyme, Ireland) records at β-1, and the specific activity of 4-polygalactomannan is 160000 micromoles/minute milligram 'beta '-mannase.The Nucleotide of subtilis 'beta '-mannase and aminoacid sequence are shown among SEQID NO:5 and the SEQ ID NO:6.

Described mannase preferably with account for composition 0.0001-2% (weight), more preferably 0.0005-0.1% (weight), most preferably the level of the pure enzyme of 0.001-0.02% (weight) joins in the cleaning compositions of the present invention.

Except the enzyme core that comprises catalytic domain, enzyme of the present invention also comprises cellulose binding domain (CBD), and the cellulose binding domain of described enzyme is connected with enzyme core (catalytic activity territory) operability.The integrated part that described cellulose binding domain (CBD) can be used as coded enzyme exists, and perhaps can import in the described enzyme from the CBD in another source and produces the enzyme hybrid.In this article, term " cellulose binding domain " can be by people such as Peter Tomme at John N.Saddler and MichaelH.Penner (editor) " Enzymatic Degradation of InsolubleCarbohydrates " (ACS SymposiumSeries, No.618,1996) definition in " cellulose binding domain: classification and character " in is understood.This definition is divided into 10 families (I-X) with the cellulose binding domain more than 120 kinds, and has verified that CBD is found in various enzymes such as cellulase, zytase, mannase, arabinofuranosidase, acetylase and the chitinase.Also in algae such as red algae Porphyra purpurea, find the CBD of non-Polysaccharides conjugated protein form, referring to people such as Tomme, in the book of being quoted.But most of CBD are from cellulase and zytase, and CBD is found in proteinic N and C-terminal or is inner.The enzyme hybrid is familiar with by those skilled in the art, referring to for example WO90/00609 and WO95/16782, and can be prepared as follows: a DNA construction that comprises the dna fragmentation of at least one coding cellulose binding domain is transformed into [described cellulose binding domain is connected on the dna sequence dna of (being with or without linker) coding mannase] in the host cell, and makes the host cell growth to express the gene that merges.The enzyme hybrid can illustrate by following formula:

CBD is N-end or the C-end region corresponding to the aminoacid sequence of described at least cellulose binding domain in the CBD-MR-X formula; MR is middle district (linker) and can be a key or one preferred about 2 to about 100 carbon atoms, the more preferably short linking group of 2 to 40 carbon atoms, or is preferably about 2 and arrives about 100 amino acid, more preferably 2 to 40 amino acid; X is the N-end region or the C-end region of enzyme of the present invention.

Cleaning compositions of the present invention also comprises the carbohydrase that is selected from cellulase, amylase, pectin degrading enzyme and/or xyloglucanase enzymes as basal component.Preferred cleaning compositions of the present invention will comprise mannase, amylase and the another kind of carbohydrase that is selected from cellulase, pectin degrading enzyme and/or xyloglucanase enzymes.

Cellulase

Can be used for cellulase of the present invention and comprise bacteria cellulose enzyme and fungal cellulase.Preferably they have the pH and the specific activity that is higher than 50CEVU/mg (Mierocrystalline cellulose viscosity unit) between 5 to 12.The plain enzyme of useful fiber is disclosed among people's such as Barbesgoard United States Patent (USP) 4435307, J61078384 and the WO96/02653, and it discloses the fungal cellulase that produces from Humicolainsolens, Trichoderma, Thielavia and Sporotrichum respectively.EP 739982 has described from the cellulase of new bacillus strain separating.The Mierocrystalline cellulose that is fit to is described in GB-A-2075028; GB-A-2095275; Among DE-OS-2247832 and the WO95/26398.

The example of this cellulase has the cellulase that produces by Humico insolens bacterial strain (Humicola griseavar.thermoidea), particularly Humicola strain DSM 1800.Other cellulase that is fit to have come from Humicola insolens, have about 50KDa molecular weight, 5.5 iso-electric point and contain 415 amino acid whose Mierocrystalline celluloses; With the 43Kd xyloglucanase enzymes that comes from Humicola insolensDSM 1800, the plain enzymic activity of display fibers; Preferred xyloglucanase enzymes component has the aminoacid sequence that is disclosed in PCT patent application WO91/17243.The plain enzyme of useful fiber also has the EGIII cellulase from the Trichodema longibrachiatum of the WO 94/21801 that is disclosed in the Genencor that delivered on September 29th, 1994.Particularly suitable cellulase is to have the cellulase that protects the look benefit.The example of this cellulase has the cellulase described in the european patent application 91202879.2 that is described in the Novo that submitted on November 6th, 1991.Carezyme and Celluzyme (Novo Nordisk A/S) are particularly useful.Also referring to WO 91/17244 and WO 91/21801.Other cellulase that is used for fabric nursing and/or clean-up performance is described in WO96/34092, WO96/17994 and WO95/24471.

Described cellulase is flat being incorporated in the described detergent composition of pure enzyme water gaging to account for described detergent composition 0.0001-2% generally.

Amylase

Amylase (α and/or β) can comprise the spot that wherein is used to remove carbohydrate-based.The WO94/02597 of disclosed Novo Nordisk A/S described and mixed the diastatic cleaning compositions of mutant on February 3rd, 1994.Also can be referring to the WO95/10603 of disclosed NovoNordisk A/S on the 20th in April nineteen ninety-five.Other amylase that becomes known for cleaning compositions comprises α and βDian Fenmei.α-Dian Fenmei is familiar with by those skilled in the art and is comprised United States Patent (USP) 5003257; EP 252666; WO91/00353; FR 2676456; EP 285123; EP525610; Disclosed amylase among EP 368341 and british patent specification number 1296839 (Novo).Other amylase that is suitable for be on August 18th, 1994 disclosed WO94/18314 and February in 1996 disclosed Genencor on the 22nd WO96/05295 described in enhancing stable amylase and by described in the April nineteen ninety-five disclosed WO 95/10603 and can available from Novo Nordisk A/S, middle parent add in addition modification amylase variant.The EP that is Novo Nordisk in addition 277216, WO95/26397 that is suitable for and the amylase described in the WO96/23873.

The example of commodity α-Dian Fenmei product has available from the Purafect Ox Am  of Genencor and can be available from the Termamyl of the Novo Nordisk A/S of Denmark ^, Fungamy ^And Duramy ^WO95/26397 has described other amylase that is suitable for: promptly descend, pass through Phadebas by 25-55 ℃ temperature and the pH value of 8-10 ^The specific activity that the alpha-amylase activity assay method records compares Termamyl ^At least high 25% α-Dian Fenmei.What be suitable for is the variant (Novo Nordisk) that is described in the above-mentioned enzyme of WO96/23873.Other is described among the WO95/35382 with the starch lyase that combining of greater activity level has the character of improvement with regard to activity level and thermostability.

The amylase that preferably is used for the object of the invention is for the amylase sold with Termamyl, Duramyl and Maxamyl or at the α-ease variants of the thermostability with raising described in the SEQ of the WO96/23873 ID NO 2.

The level that is incorporated into starch lyase in the detergent composition of the present invention is for accounting for described composition 0.0001-2% (weight), preferred 0.00018-0.06%, the level of the pure enzyme of 0.00024-0.048% more preferably from about.

Pectin degrading enzyme

Described pectin degrading enzyme has been meant the enzyme of degraded pectin substance and pectin related substances.Pectin substance can be found in the plant tissue and be the conventional ingredient of fruit juice such as orange juice, tomato juice and Sucus Vitis viniferae.Pectin substance comprises galacturonic acid and/or its derivative.

Term " pectin degrading enzyme " will comprise polygalacturonase (EC 3.2.1.15), polygalacturonic acid excision enzyme (EC 3.2.1.67), poly--α-galacturonic acid excision enzyme (EC3.2.1.82), pectin lyase (EC 4.2.2.10), Rohapect MPE (EC 3.2.1.11), pectate lyase (EC 4.2.2.2), outer ester of polygalacturonic acid lyase (EC 4.2.2.9) and hemicellulase are such as interior-1,3-xylosidase (EC 3.2.1.32), xylan-1,4-xylosidase (EC3.2.1.37) and α-L-A Labaifunantangganmei (EC 3.2.1.55).Described pectin degrading enzyme is the natural mixture of above-mentioned enzymic activity.Therefore polygalacturonase comprise hydrolysis of pectin methyl esters key pectin methylesterase, the glycosidic link between the cracking galacturonic acid molecule polygalacturonase with pectic acid is worked and makes the non-hydrolytic rupture of α-1 → 4 glycosidic link become the trans elimination enzyme of pectin or the lyase of the unsaturated derivative of galacturonic acid.

Pectin degrading enzyme with the 0.0001-2% that accounts for total composition, more preferably 0.0005-0.5%, most preferably the pure enzyme level of 0.001-0.1% is incorporated into according in the cleaning compositions of the present invention.

The concrete preferred pectin degrading enzyme that uses is an alkaline pectin degrading enzyme, promptly under 7-12, preferred 10.5 pH, have its maximum activity at least 10%, the enzyme of preferred at least 25%, more preferably at least 40% enzymic activity.More preferably described pectin degrading enzyme is for having the enzyme of its maximum activity under 7-12, preferred 10.5 pH.Alkaline pectin degrading enzyme by halophile for example bacterium, fungi and yeast microorganism such as bacillus bacterial classification produce.Preferred microorganism is bacillus firmus (Bacillus firmus), Bacillus circulans and the subtilis that is described in JP 56131376 and JP 56068393.Alkaline pectin degrading enzyme comprises galacturan-1, and 4-α-galacturonic acid enzyme (EC 3.2.1.67), polygalacturonase actives (EC 4.2.1.15), Rohapect MPE (EC 3.1.1.11), pectate lyase (EC 4.2.2.2) and its isozyme and they can be produced by the Erminia bacterial classification.Preferably as being described in JP59066588, JP 63042988 and being described in World J.Microbiol.Microbiotechnol. (8,2,115-120) chrysanthemum Erwinia (E.Chrysanthemi), the Radix Dauci Sativae Erwinia (E.Carotovora) in 1992, separate starch Erwinia (E.Amylovora), grass livings Erwinia (E.Herbicold), dissolve Erwinia (E.Dissolvens).Described alkaline pectase also can produce by the bacillus bacterial classification described in (2) 285 to 293 pages of the Agr.Biol.Chem.36 of JP 73006557 and 1972.

Xyloglucanase enzymes

The term xyloglucanase enzymes comprises people (1994) Plant Physiol.104 such as the Vincken of Wageningen University and Voragen[Vincken, 99-107] described enzyme family, and described xyloglucanase enzymes can be as people such as Hayashi at Plant Physiol.Plant Mol.Biol. in 1989, described degraded xyloglucan in 40,139 to 168 pages.People such as Vincken have confirmed by from the removal to the xyloglucan film (coating) of the cellulase that comes from isolating apple cell walls of the xyloglucanase enzymes (interior IV dextranase) of viride (Trichoderma viride) purifying.This kind of enzyme has strengthened the cellulosic enzyme liberating that is embedded in cell walls and polygalacturonase has been produced synergy.Rapidase LIQ+ available from Gist-Brocades comprises the xyloglucan enzymic activity.

U.S. Patent Application Serial SN60/045826 number of pending trial the endoglucanase that shows the xyloglucan specific activity has been described when submitting on May 5th, 1997.Used term " endoglucanase activity " is meant that enzymic hydrolysis is present in 1 of cellulosic material such as Mierocrystalline cellulose, derivatived cellulose, lichenstarch, callose or xyloglucan in this, the ability of 4-β-D-glycosidic link.Endoglucanase activity can be according to measuring in methods known in the art, and its example is described in WO94/14953 and hereinafter.One unit endoglucanase activity (for example CMCU, AVIU, XGU or BGU) is defined as the amount that the dextran substrate per minute produces 1 micromole's reducing sugar, and dextran substrate is for example CMC (CMCU), acid-swellable Avicell (AVIU), xyloglucan (XGU) or cereal beta-glucan (BGU).Reducing sugar is according to WO94/14953 and hereinafter described mensuration.Endoglucanase is to the specific activity unit of the being defined as/milligram protein of substrate.More particularly, the present invention relates to comprise and demonstrate with laundry composition and the cleaning compositions of XGU endoglucanase activity described enzyme as the enzyme of its high reactivity (after this referring to " special ") to xyloglucan:

(i) by at least one dna sequence encoding that contains or comprises in partial sequence SEQID No:1 to 18 (U.S. Patent application of pending trial series is SN60/045826 number when submitting on May 5th, 1997); Or coding tool endoglucanase activity is to the homologous sequence of the special polypeptide of xyloglucan,

(ii) have with at by highly purified, by i) immunoreactivity of the antibody that produces of the endoglucanase of the dna sequence encoding of definition and come from Aspergilus aculeatus, CBS 101.43 and special to xyloglucan.

More particularly, used term " special to xyloglucan " is meant that described endoglucanase shows its highest endoglucanase activity to the xyloglucan substrate in this, and other cellulose substrate such as carboxymethyl cellulose, Mierocrystalline cellulose or other dextran shown preferably be lower than 75% activity, more preferably less than 50% activity, most preferably be lower than about 25% activity.Preferred endoglucanase also is defined as by by described enzyme is carried out the relative reactivity that release that enzyme hatches reducing sugar under the top condition of acquisition records with xyloglucan and other substrate to be measured respectively the specificity of xyloglucan.For example, specificity can be defined as xyloglucan to beta-glucan activity (XGU/BGU), xyloglucan to carboxymethyl cellulose activity (XGU/CMCU) or xyloglucan to acid-swellable Avicell activity (XGU/AVIU), it is preferably greater than about 50, such as 75,90 or 100.

Described xyloglucanase enzymes with the 0.0001-2% that accounts for total composition, more preferably 0.0005-0.5%, most preferably the pure enzyme level of 0.001-0.1% is incorporated into according in the cleaning compositions of the present invention.

Above-mentioned enzyme can be from any source such as plant, animal, bacterium, fungi and yeast.Described source can further be mesopilous organisms or have a liking for extremely biological (psychrophilic organism, psychrophilic bacteria, thermophile, have a liking for press biological, have a liking for alkali biology, acidophils, have a liking for halogen biology etc.).Can use purified or these enzymes of purified form not.Now, in order to make the optimizing effect at cleaning compositions of the present invention, the enzyme of modifying agriotype through protein/genetic engineering technique is conventional practice.For example, thus can design the compatibleness that described variant improves the conventional ingredient of described enzyme and this composition.Perhaps described variant can be designed so that best pH, bleaching or sequestrant stability, the catalytic activity etc. of described enzyme variants are adjusted to suitable concrete cleaning purposes.

Specifically, concerning bleach stability, attention should be placed on the amino acid to oxidation-sensitive, concerning the tensio-active agent compatibleness, attention should be placed on the surface charge.The iso-electric point of this kind of enzyme can change by the displacement of some charge residues, and for example the raising of iso-electric point can help to improve the compatibleness with anion surfactant.The stability of described enzyme can be further by the generation of for example other salt bridge with strengthen the melts combine site and increase to improve sequestrant stability.

Detergent component

Cleaning compositions of the present invention also can comprise at least a other detergent component.The exact nature of these other components and its level of mixing will depend on the physical form of described composition and use the character of the clean operation of these compositions.

Cleaning compositions of the present invention also preferably includes the detergent ingredients that is selected from selected tensio-active agent, another kind of enzyme, a kind of auxiliary agent and/or a kind of bleach system.

According to cleaning compositions of the present invention can be liquid agent, paste, gelifying agent, medicated roll, tablet, sprays, foaming agent, pulvis or granule.Particulate composition also can be " high-density " form, and liquid composition also can be " concentrating " form.

In a kind of embodiment preferred, the present invention relates to a kind of laundry composition, it comprises a kind of mannase and a kind of carbohydrase (embodiment 1-18) that is selected from cellulase, amylase, pectin degrading enzyme and/or xyloglucanase enzymes.In second kind of embodiment, the present invention relates to dishwashing detergent or household cleaning composition (embodiment 19-25), and in the third embodiment, the present invention relates to oral cavity/dental care compositions (embodiment 26-28).The 4th kind of embodiment relates to personal cleaning compositions (embodiment 30-31).

Cleaning compositions of the present invention can for example be mixed with hand washing or machine washing tableware cleaning compositions, hand washing and machine washing laundry detergent composition and (comprise the laundry additive composition and be applicable to the immersion of band spot fabric and/or fabric softener composition that pretreated composition, rinsing add and be used for the cleaning compositions that conventional family hard-surface cleaning is handled.Comprise this mannase and also can be mixed with health care and aesthetic nursing product such as oral cavity/dental care and personal cleaning compositions with the cleaning compositions that is selected from the carbohydrase of cellulase, amylase, pectin degrading enzyme and/or xyloglucanase enzymes.

When being mixed with the composition that is used for the manual dishwashing method, composition of the present invention preferably comprises a kind of tensio-active agent and preferred other the detergent compound that is selected from organic polyhydroxyl compound, suds booster, II family metal ion, solvent, solubilizing agent and other enzyme.

When being mixed with the composition that is applicable to washing machine washing, composition of the present invention preferably comprises tensio-active agent and auxiliary compound and other one or more and is preferably selected from organic polyhydroxyl compound, SYNTHETIC OPTICAL WHITNER, other enzyme, suds suppressor, dispersion agent, lime soap dispersing agent, stain remover and anti redeposition agent and the scrubbed component of corrosion inhibitor.Laundry composition also can comprise tenderizer as other detergent component.When being mixed with laundry detergent composition, this composition that contains mannase and be selected from the carbohydrase of amylase, cellulase, pectin degrading enzyme and/or xyloglucanase enzymes can provide that clean fabric, greasiness removal, whiteness keep, the usefulness of softening and bright-coloured outward appearance.

The detergent additives product that composition of the present invention also can be used as solid or liquid form uses.This additive product is used for replenishing or strengthening the performance of conventional detergent composition, and can add in any stage of cleaning course.

If desired, the density of cleaning compositions of the present invention (20 ℃ of mensuration) scope is 400-1200g/l, preferred 500-950g/l.

" high-density " form of the present composition is subjected to having the greatest impact of density, is subjected to the influence of the amount of mineral filler salt simultaneously according to the particular case of composition, and mineral filler salt is the conventional ingredient of powder type detergent composition; In conventional detergent composition, described filling salt exists in a large number, is generally the 17-35% (weight) of total composition.In high-density composition, the amount of filling salt generally is no more than 15% (weight) of total composition weight, preferably is no more than 10%, is most preferably not exceeding 5% (weight).Be selected from the vitriol and the muriate of basic metal and alkaline-earth metal such as the mineral filler salt of indication in composition of the present invention.A kind of preferred filling salt is a sodium sulfate.

According to liquid detergent composition of the present invention also can be " concentrating " form, in this case, will comprise water than the lower amount of conventional liq washing composition according to liquid detergent composition of the present invention.The water-content of general concentrated liquid detergent preferably is less than 40% (weight) of detergent composition, more preferably less than 30%, most preferably be less than 20%.

Be applicable to that the detergent composition in this is selected from compound described below.

Surfactant system

Generally comprise a kind of surfactant system according to cleaning compositions of the present invention, wherein said tensio-active agent can be selected from nonionic and/or negatively charged ion and/or positively charged ion and/or both sexes and/or zwitter-ion and/or semi-polarity tensio-active agent.Preferred cleaning compositions of the present invention comprises a kind of nonionic, a kind of negatively charged ion and/or a kind of cats product.

Now find uncannily to comprise that also the cleaning compositions of the present invention of a kind of nonionic, a kind of negatively charged ion and/or a kind of cats product provides the enhanced cleaning, promptly superior greasiness removal, dirty thing cleaning and whiteness keep.

Be not wishing to be bound by theory, believe that enzymic hydrolysis has produced the small-particle that the nonionogenic tenside that is easier to be become known for particulate fouling is removed.Preferred nonionic is that alkylethoxylate AE3 is to AE7.Believe that also direct (substantive) cats product of fabric provides the performance of improving with the combining of enzymic hydrolysis of the enzyme of combination.

Described tensio-active agent generally exists with the level of 0.1-60% (weight).The level of more preferably mixing for according to the 1-35% (weight) of cleaning compositions of the present invention, most preferably be 1-30% (weight).

Described tensio-active agent preferably make can with the form that is present in the enzyme component compatibility in the composition.In liquid or gelatinous composition, described tensio-active agent is most preferably made the form that can promote or not be reduced at least the stability of enzyme in these compositions.

Nonionogenic tenside

The polyoxyethylene of alkylphenol, polyoxypropylene and polyoxy croton condensation thing are suitable as the nonionogenic tenside of surfactant system of the present invention, wherein preferred polyoxyethylene condenses.These compounds comprise that its alkyl has about 6 and is the alkylphenol of straight or branched configuration and the condensation product of oxyalkylene to about 14 carbon atoms, preferred about 8 to about 14 carbon atoms.In an embodiment preferred, oxygen ethene with every mole of alkylphenol about 2 to about 25 moles, more preferably from about 3 exist to about 15 moles amount.Such commodity ionic surfactant pack is drawn together the Igepal that is introduced to the market by GAF Corporation ^TMCO-630; With by Rohm ﹠amp; The Triton that HaasCompany introduces to the market ^TMX-45, X-114, X-100 and X-102.These tensio-active agents are commonly called alkyl phenolic alkoxy thing (for example alkylphenol ethoxylate).

Primary and secondary fatty alcohol and about 1 condensation product to about 25 mole oxygen ethene are suitable as the nonionogenic tenside of nonionic surfactant system of the present invention.The alkyl chain of fatty alcohol can be straight or branched, uncle or the second month in a season, and generally comprises about 8 to about 22 carbon atoms.Preferably its alkyl comprises about 8 to about 20 carbon atoms, more preferably from about 10 arrives the condensation product of about 10 mole oxygen ethene to the alcohol of about 18 carbon atoms and every mol of alcohol about 2.In described condensation product, exist every mol of alcohol about 2 to about 7 mole oxygen ethene and 2 to 5 mole oxygen ethene most preferably.The example of such commercialization nonionogenic tenside comprises the Tergitol that is introduced to the market by Union Carbide Corporation ^TM15-S-9 (C ₁₁-C ₁₅The condensation product of linear alcohol and 9 mole oxygen ethene) and Tergitol ^TM24-L-6 NMW (C ₁₂-C ₁₄The condensation product of the narrow molecular weight distributions of primary alconol and 6 mole oxygen ethene); The Neodol that introduces to the market by Shell ChemicalCompany ^TM45-9 (C ₁₄-C ₁₅The condensation product of linear alcohol and 9 mole oxygen ethene), Neodol ^TM23-3 (C ₁₂-C ₁₃The condensation product of linear alcohol and 3.0 mole oxygen ethene), Neodol ^TM45-7 (C ₁₄-C ₁₅The condensation product of linear alcohol and 7 mole oxygen ethene), Neodol ^TM45-5 (C ₁₄-C ₁₅The condensation product of linear alcohol and 5 mole oxygen ethene); By Procter﹠amp; The Kyro that Gamble Company introduces to the market ^TMEOB (C ₁₃-C ₁₅The alcohol and the condensation product of 9 mole oxygen ethene) and the Genapol LA O3O or the O5O (C that introduce to the market by Hoechst ₁₂-C ₁₄The condensation product of alcohol and 3 or 5 mole oxygen ethene.The preferable range of the preferred HLB of these products is 8 to 11, and most preferably is 8 to 10.

Also can be used as surfactant system of the present invention nonionogenic tenside be disclosed alkyl polysaccharide in the United States Patent (USP) 4565647 of the Llenado that authorized on January 21st, 1986, its have a kind of contain about 6 to about 30 carbon atoms, preferred about 10 to the hydrophobic grouping of about 16 carbon atoms and a kind of have contain about 1.3 to about 10, preferably about 1.3 to about 3, most preferably from about 1.3 polysaccharide such as the glycan glycosides that arrive the hydrophilic group of about 2.7 sugar units.Can use any reducing sugar that contains 5 or 6 carbon atoms for example glucose and semi-lactosi, and galactosyl can replace glucosyl (thereby optional hydrophobic grouping connect in positions such as 2-, 3-, 4-make glucose or the semi-lactosi relative with glucoside or galactoside).Key between sugar can be the key between 2-, 3-, 4-and/or the 6-position of position of for example other sugar unit and front sugar unit.

Preferred APG has following formula:

R ²O (C _nH _2nO) _t(glycosyl) _xR wherein ²Be selected from alkyl, alkyl phenyl, hydroxyalkyl, hydroxyalkyl phenyl and its mixture, wherein said alkyl comprises about 10 and arrives about 18, preferred about 12 to about 14 carbon atoms; N is 2 or 3 and be preferably 2; T is 0 to about 10, and is preferably 0; X is about 1.3 to about 10, and is preferably about 1.3 to about 3, most preferably is about 1.3 to about 2.7.Glycosyl preferably comes from glucose.For preparing these compounds, at first form described alcohol or alkyl polyethoxye alcohol, react and formation glucoside (being connected 1) with glucose or source of glucose then.Can between 2-, 3-, 4-and/or the 6-position (preferably mainly at 2) of its 1 and front glycosyl units, connect other glycosyl units then.

Oxygen ethene is also suitable as other nonionic surfactant system of the present invention with the condensation product of the hydrophobic group that condensation by oxypropylene and propylene glycol forms.The hydrophobic part of these compounds preferably has about 1500 to about 1800 molecular weight, and demonstrates water-insoluble.Polyoxyethylene is partly added this hydrophobic part help to improve the water-soluble of molecule integral body, the fluid characteristics of product is held the level that polyoxyethylene content reaches condensation product gross weight about 50%, and it is equivalent to last to about 40 moles oxygen ethene condensation.The example of such compound comprises the commodity Plurafac that some is introduced to the market by BASF ^TMLF 404 and Pluronic ^TMTensio-active agent.

Also be suitable for nonionogenic tenside aerobic ethene and the condensation product that comes from the product of oxypropylene and reacting ethylenediamine as nonionic surfactant system of the present invention.The hydrophobic part of these products comprises the reaction product of quadrol and excess of oxygen propylene, and generally has about 2500 to about 3000 molecular weight.This hydrophobic part and oxygen ethene are condensed to the degree that its condensation product comprises about 80% (weight) polyoxyethylene of about 40-and has about 5000 to about 11000 molecular weight.The example of such nonionogenic tenside comprises the commodity Tetronic that some is introduced to the market by BASF ^TMCompound.

The nonionogenic tenside that is preferably used as surfactant system of the present invention is the polyoxyethylene condenses of alkylphenol, primary and secondary fatty alcohol and about 1 condensation product, alkyl polysaccharide and its mixture to about 25 mole oxygen ethene.The C that most preferably has 3 to 15 oxyethyl groups ₈-C ₁₄Alkylphenol ethoxylate and C with 2 to 10 oxyethyl groups ₈-C ₁₈Alcohol ethoxylate (preferred average C ₁₀) and its mixture.

Highly preferred nonionogenic tenside is the polyhydroxy fatty acid amide surfactants of following formula

R in the formula ¹Be H, perhaps R ¹Be C _1-4Alkyl, 2-hydroxyethyl, 2-hydroxypropyl or its mixture, R ²Be C _5-31Alkyl, Z are to have at least 3 polyhydroxy alkyl or its alkoxy derivatives that are directly connected to the linear hydrocarbyl chain of the hydroxyl on the chain.Preferred R ¹Be methyl, R ²Be straight chain C _11-15Alkyl or C _16-18Alkyl or alkenyl such as cocounut oil alkyl or its mixture, and Z comes from a kind of reducing sugar such as glucose, fructose, maltose, lactose in reductive amination process.

Anion surfactant

Anion surfactant preferred for the present invention is alkyl sulfate and LINEAR ALKYL BENZENE (LAB) tensio-active agent.The anion surfactant that is suitable for is linear alkyl benzene sulfonate, alkyl sulfonate surfactants, comprise according to " The Joumal of the American OilChemists Society, 52 (1975), the method for 323-329 page or leaf is with C ₈-C ₂₀The ol ester gaseous state SO of carboxylic acid (being lipid acid) ₃The sulfonated alkyl sulfonate surfactants.The raw material that is suitable for will comprise such as the natural fat material that comes from tallow, palm wet goods.

Preferred alkyl sulfonate surfactants, comprise the alkyl sulfonate surfactants of following structural formula especially for the alkyl sulfonate surfactants of laundry purposes R wherein ³Be C ₈-C ₂₀Alkyl, preferred alkyl or its combination, R ⁴Be C ₁-C ₆Alkyl, be preferably alkyl, or its combination, M be the positively charged ion with alkyl ester sulfonic acid formation water-soluble salt.The salt-forming cation that is fit to comprises metal such as sodium, potassium and lithium, replaces or unsubstituted ammonium cation such as monoethanolamine, diethanolamine and trolamine.Preferred R ³Be C ₁₀-C ₁₆Alkyl, R ⁴Be methyl, ethyl or sec.-propyl.Particularly preferably be R ³Be C ₁₀-C ₁₆The methyl ester sulfonate of alkyl.

Other anion surfactant that is suitable for comprises formula ROSO ₃The alkyl sulfate surfactant of the water-soluble salt of M or acid, wherein R is preferably C ₁₀-C ₂₄Alkyl, preferably has a C ₁₀-C ₂₀The alkyl of alkyl component or hydroxyalkyl, C more preferably ₁₂-C ₁₈Alkyl or hydroxyalkyl, and M is a H or a positively charged ion, for example alkali metal cation (for example sodium, potassium, lithium) or ammonium or replace ammonium (for example first ammonium, dimethylammonium and TMA (TriMethylAmine) positively charged ion and quaternary ammonium cation such as tetramethylammonium and lupetidine positively charged ion and come from the quaternary ammonium cation etc. of alkylamine such as ethamine, diethylamine, triethylamine and its mixture).General for lower wash temperature (for example being lower than about 50 ℃), preferred C ₁₂-C ₁₆Alkyl chain, for higher wash temperature (for example about more than 50 ℃), preferred C ₁₆-C ₁₈Alkyl chain.

Other anion surfactant that can be used for the washing composition purpose also can be included in the cleaning compositions of the present invention.They can comprise soap salt (for example comprise sodium, potassium, ammonium and substituted ammonium salt such as list, two and triethanolamine salt), C ₈-C ₂₂Uncle or secondary sulfonated alkane, C ₈-C ₂₄Alkene sulfonate, the sulfonation polycarboxylic acid, the C that for example prepare by the sulfonation of passing through the alkaline earth metal citrate pyrolysis product described in the british patent specification 1082179 ₈-C ₂₄Monoesters (the particularly saturated and unsaturated C of alkyl polyglycol ether sulfate (comprising oxygen ethene), alkyl glycerol sulfonate, fatty acyl glycerol sulfonate, fatty oleoyl glycerine vitriol, alkylphenol oxygen Vinyl Ether vitriol, alkane sulfonate, alkylphosphonic, isethionate such as acyl isethinate, N-acyl taurine salt, amber alkyl amide salts and sulfosuccinate, sulfosuccinate to 10 moles ₁₂-C ₁₈Monoesters) and the diester of sulfosuccinate (particularly saturated and unsaturated C ₆-C ₁₂Diester), the vitriol of the vitriol of acyl sarcosinate, alkyl polysaccharide such as alkyl polyglucoside (compound of nonionic non-sulfuric acidization is described below), ramose primary alkyl sulphates and the many ethoxy carboxylates of alkyl are such as having formula RO (CH ₂CH ₂O) _k-CH ₂COO-M ⁺Carboxylate salt, R is C in the formula ₈-C ₂₂Alkyl, k are 1 to 10 integer, and M is into the positively charged ion of soluble salt.Resinous acid and hydrogenated resin acid also are suitable for, such as rosin, staybelite with have or come from the resinous acid and the hydrogenated resin acid of Yatall MA in Yatall MA.

" Surface Active Agents andDetergents " I and II volume at Schwartz, Perry and Berch have been described other example.Various these class tensio-active agents also are disclosed in the people's such as Laughlin that authorized on December 30th, 1975 the 23rd hurdle 58 row of United States Patent (USP) 3929678 synoptically in 29 hurdles, 23 row (incorporating this paper by reference into).

When this anion surfactant existed, cleaning compositions of the present invention generally comprised about 40% (weight) of about 1-, preferred this analog anion surfactants of about 20% (weight) of about 3-.

Highly preferred anion surfactant comprises alkyl alkoxylated sulfate surfactant, and here it is formula RO (A) _mSO ₃The water-soluble salt of M or acid, R is unsubstituted C in the formula ₁₀-C ₂₄Alkyl or have C ₁₀-C ₂₄The hydroxyalkyl of alkyl component is preferably C ₁₂-C ₂₀Alkyl or hydroxyalkyl, more preferably C ₁₂-C ₁₈Alkyl or hydroxyalkyl, A is oxyethyl group or propoxy-unit, m is greater than 0, generally between about 0.5 to about 6, more preferably between 0.5 to about 3, and M is H or a positively charged ion, and described positively charged ion can be for example metallic cation (for example sodium, potassium, lithium, calcium, magnesium etc.), ammonium or replace ammonium cation.Alkyl ethoxylated sulfate and alkyl propoxylated sulphates are to consider in this.The object lesson that replaces ammonium cation comprises first ammonium, dimethylammonium, TMA (TriMethylAmine) positively charged ion and quaternary ammonium cation such as tetramethylammonium and lupetidine positively charged ion and comes from the positively charged ion etc. of alkylamine such as ethamine, diethylamine, triethylamine, its mixture.The example of this tensio-active agent has C ₁₂-C ₁₈Alkyl polyethoxylated (1.0) vitriol (C ₁₂-C ₁₈E (1.0) M), C ₁₂-C ₁₈Alkyl polyethoxylated (2.25) vitriol (C ₁₂-C ₁₈E (2.25) M), C ₁₂-C ₁₈Alkyl polyethoxylated (3.0) vitriol (C ₁₂-C ₁₈E (3.0) M) and C ₁₂-C ₁₈Alkyl polyethoxylated (4.0) vitriol (C ₁₂-C ₁₈E (4.0) M), M is selected from sodium and potassium easily in the formula.

Cats product

Be applicable to that the cationic detergent tensio-active agent in the cleaning compositions of the present invention is those cats products with a long chain hydrocarbon groups.The example of this cats product comprises that ammonium surfactant such as alkyltrimethylammonium halogenide and those have the tensio-active agent of following formula:

[R ²(OR ³) _y] [R ⁴(OR ³) _y] ₂R ⁵N ⁺X ^-R in the formula ²For its alkyl chain has about 8 alkyl or alkyl benzyls to about 18 carbon atoms, each R ³Be selected from-CH ₂CH ₂-,-CH ₂CH (CH ₃)-,-CH ₂CH (CH ₂OH)-,-CH ₂CH ₂CH ₂-and its mixture; Each R ⁴Be selected from C ₁-C ₄Alkyl, C ₁-C ₄Hydroxyalkyl, two R ⁴Group is in conjunction with the benzyl rings structure that forms ,-CH ₂CHOH-CHOHCOR ⁶CHOHCH ₂OH, wherein R ⁶Be lower than about 1000 hexose or hexose polymkeric substance and hydrogen (when y is not 0) for molecular weight; R ⁵With R ⁴Identical or an alkyl chain, wherein R ²Add R ⁵The sum of carbon atom be no more than about 18; Each y is 0 to about 10, and the y value and be 0 to about 15; X is any compatible negatively charged ion.

Be applicable to that quaternary ammonium surfactant of the present invention has formula (I):

R in the formula I formula ₁Be a short chain (C ₆-C ₁₀) the alkyl amido alkyl of alkyl or formula (II):

Formula IIy is 2 to 4, preferred 3; R wherein ₂Be H or C ₁-C ₃Alkyl, x are 0 to 4, and be preferred 0 to 2, most preferably 0; R ₃, R ₄And R ₅Can be identical or different and can be a short chain (C ₁-C ₃) alkoxylated alkyl of alkyl or formula III; X-is a counter ion, is preferably haloid acid root for example spirit of salt root or methylsulfate

Formula III R ₆Be C ₁-C ₄And z is 1 or 2.

Preferred quaternary ammonium surfactant be those suc as formula defined tensio-active agent among the I, in the formula:

R ₁Be C ₈, C ₁₀Or its mixture, x=0,

R ₃, R ₄=CH ₃And R ₅=CH ₂CH ₂OH.

Highly preferred cats product is the water-soluble quaternary ammonium compound that can be used in the present composition, and it has following formula:

R ¹R ²R ³R ⁴N ⁺X ^-(i) R in the formula ¹Be C ₈-C ₁₆Alkyl; R ², R ³And R ⁴Each is C independently ₁-C ₄Alkyl, C ₁-C ₄Hydroxyalkyl, benzyl and-(C ₂H ₄₀) _xH, wherein x has 2 to 5 value, and X is a negatively charged ion.R ², R ³And R ⁴In be no more than one and should be benzyl.

Be preferably used as R ¹The chain length of alkyl be C ₁₂-C ₁₅, particularly wherein said alkyl be come from cocounut oil fat or palm kernel fat chain length mixture or increase synthetic or pure synthetic the obtaining of OXO by alkene.Preferred R ², R ³And R ⁴Group be methyl and hydroxyethyl, and negatively charged ion X can be selected from haloid acid root, methylsulfate, acetate moiety and phosphate anion.

The example that is applicable to the quaternary ammonium compound of the formula (i) in this has:

Cocoyl trimethyl ammonium chloride or brometo de amonio;

Cocoyl methyl dihydroxy ethyl ammonium chloride or brometo de amonio;

The decyl triethyl ammonium chloride;

Decyl dimethyl hydroxyethyl ammonium chloride or brometo de amonio;

C _12-15Dimethyl hydroxyethyl ammonium chloride or brometo de amonio;

Cocoyl dimethyl hydroxyethyl ammonium chloride or brometo de amonio;

Myristyl trimethyl ammonium Methylsulfate;

Lauryl dimethyl benzyl ammonium chloride or brometo de amonio;

Lauryl dimethyl (vinyloxy group) 4 ammonium chlorides or brometo de amonio;

Cholinesterase (compound of formula (i), wherein R ¹Be CH ₂-CH ₂-O-CO-C _12-14Alkyl and R ², R ³, R ⁴Be methyl);

Dialkylimidazolium quinoline [compound of formula (i)].

Other cats product that can be used in this also is described in the United States Patent (USP) 4228044 and European patent application EP 000224 of the Cambre that authorized on October 14th, 1980.

Typical cationic fabric softening component comprises the softening actives of water-soluble quaternary ammonium fabric or its corresponding amine precursor, and the most frequently used is two-long alkyl chain ammonium chloride or Methylsulfate.

Wherein the preferred cation tenderizer comprises following material:

1) ditallow dimethyl ammonium chloride (DTDMAC);

2) dihydro tallow alkyl dimethyl ammonium chloride;

3) dihydro tallow Dimethyl Ammonium Methylsulfate;

4) VARISOFT TA100;

5) two oil base alkyl dimethyl ammonium chlorides;

6) two palmityl hydroxyethyl ammonio methacrylates;

7) stearyl benzyl dimethyl ammonium chloride;

8) tallow trimethyl ammonium chloride;

9) h-tallow base trimethyl ammonium chloride;

10) C _12-14Alkyl hydroxyethyl dimethyl ammonium chloride;

11) C _12-18Alkyl dihydroxy ethyl ammonio methacrylate;

12) two (stearoyl keto ethyl) alkyl dimethyl ammonium chlorides (DSOEDMAC);

13) two (tallow oxygen ethyl) alkyl dimethyl ammonium chloride;

14) ditallow tetrahydroglyoxaline Methylsulfate;

15) 1-(2-tallow amido ethyl)-2-tallow tetrahydroglyoxaline Methylsulfate.

Biodegradable quaternary ammonium compound occurs as the two-long alkyl chain ammonium chloride of tradition use and the surrogate of Methylsulfate.This quaternary ammonium compound comprises by functional group such as carboxyl chain alkyl (alkenyl) at interval.Described material is disclosed among numerous publications such as EP-A-0040562 and the EP-A-0239910 with the fabric softening compositions that comprises it.

Quaternary ammonium compound in this and amine precursor have following formula (I) or (II):

Or Wherein Q be selected from-O-C (O)-,-C (O)-O-,-O-C (O)-O-,-NR ⁴-C (O)-,-C (O)-NR ⁴-; R ¹Be (CH ₂) _n-Q-T ²Or T ³R ²Be (CH ₂) _m-Q-T ⁴Or T ⁵Or R ³R ³Be C ₁-C ₄Alkyl or C ₁-C ₄Hydroxyalkyl or H; R ⁴Be H or C ₁-C ₄Alkyl or C ₁-C ₄Hydroxyalkyl; T ¹, T ², T ³, T ⁴, T ⁵Be C independently ₁₁-C ₂₂Alkyl or alkenyl; N and m are 1 to 4 integer; With X-be the compatible negatively charged ion of a tenderizer.The compatible anionic non-limiting example of tenderizer comprises spirit of salt root or methylsulfate.

Described alkyl or alkenyl chain T ¹, T ², T ³, T ⁴, T ⁵Must comprise at least 11 carbon atoms, preferred at least 16 carbon atoms.Described chain can be a straight or branched.Tallow is the convenience of chain alkyl and alkenyl material and cheap source.Especially preferred T wherein ¹, T ², T ³, T ⁴, T ⁵Representative is generally from the mixture of the long-chain material of tallow.

The specific examples that is applicable to the quaternary ammonium compound in the aqueous fabric softening compositio in this comprises:

1) N, two (tallow-oxygen-the ethyl)-N of N-, N-alkyl dimethyl ammonium chloride;

2) N, two (tallow-oxygen-the ethyl)-N-methyl of N-, N-(2-hydroxyethyl) ammonium methyl sulphate;

3) N, two (2-tallow-oxygen-2-the oxoethyl)-N of N-, N-alkyl dimethyl ammonium chloride;

4) N, two (2-tallow-oxygen-ethyl carbonyl-oxygen-ethyl)-N of N-, N-alkyl dimethyl ammonium chloride;

5) N-(2-tallow-oxygen-2-ethyl)-N-(2-tallow-oxygen-2-oxoethyl)-N, the N-alkyl dimethyl ammonium chloride;

6) N, N, N-three (tallow-oxygen-ethyl)-N-ammonio methacrylate;

7) N-(2-tallow-oxygen-2-oxoethyl)-N-(tallow-N, N-alkyl dimethyl ammonium chloride); With

8) 1,2-ditallow-oxygen-3-three methylamino-chloropropanes; Mixture with any above-mentioned substance.

When this cats product existed, cleaning compositions of the present invention generally comprised about 25%, the preferred cats product of about 1-about 8% (weight) of about 0.2-.

SYNTHETIC OPTICAL WHITNER

Find uncannily that now the cleaning compositions of the present invention that also comprises SYNTHETIC OPTICAL WHITNER, particularly bleach activator bleach system provides the removal of enhanced food stain, dirty thing cleaning and whiteness to keep.Be not wishing to be bound by theory, believe that the less color development particle that is produced by the enzymic hydrolysis of combination enzyme is easier in bleaching activity bleach system erosion, all the more so at low temperatures.

These SYNTHETIC OPTICAL WHITNER comprise that hydrogen peroxide, PB1, PB4 and granularity are the percarbonate of 400-800 micron.These bleaching components can comprise one or more oxygen bleaching agents and also can comprise one or more bleach activators according to selected SYNTHETIC OPTICAL WHITNER.

These bleaching components can comprise one or more oxygen bleaching agents, and also can comprise one or more bleach activators according to selected SYNTHETIC OPTICAL WHITNER.When having the oxygen bleaching compound, it generally exists with the level of about 1-about 25%.

Used bleaching components can be any SYNTHETIC OPTICAL WHITNER that can be used for cleaning compositions in this, comprises that oxygen bleaching agent and other are the SYNTHETIC OPTICAL WHITNER that those skilled in the art were familiar with.Be applicable to that SYNTHETIC OPTICAL WHITNER of the present invention can be activation or non-activated SYNTHETIC OPTICAL WHITNER.

Available one class oxygen bleaching agent comprises percarboxylic acids SYNTHETIC OPTICAL WHITNER and its salt.The suitable example of this class SYNTHETIC OPTICAL WHITNER comprises the magnesium salts of Magnesium monoperoxyphthalate hexahydrate, metachloroperbenzoic acid, 4-amino in the ninth of the ten Heavenly Stems-4-oxo Perbutyric Acid and diperoxy dodecanedioic acid.This SYNTHETIC OPTICAL WHITNER is disclosed in United States Patent (USP) 4483781, U.S. Patent application 740446, european patent application 0133354 and the United States Patent (USP) 4412934.Highly preferred SYNTHETIC OPTICAL WHITNER comprises that also 6-amino in the ninth of the ten Heavenly Stems-6-oxo that is described in the United States Patent (USP) 4634551 crosses oxy hexanoic acid.

Another kind of available SYNTHETIC OPTICAL WHITNER comprises the halogen SYNTHETIC OPTICAL WHITNER.For example the example of hypohalite SYNTHETIC OPTICAL WHITNER comprises sodium salt and sylvite and the N-chlorine and the N-bromine alkane sulfonamide of TCCA (Trichloroisocyanuric acid) and dichloroisocyanuric acid.This material-as add with the level of finished product 0.5-10% (weight), preferred 1-5% (weight).

The hydrogen peroxide releasing agent can with bleach activator such as tetra acetyl ethylene diamine (TAED), nonanoly acyloxy benzene sulfonate (NOBS; be described in United States Patent (USP) 4412934), 3; 5-trimethyl acetyl oxygen base benzene sulfonate (ISONOBS; be described in EP 120591) or the sulfophenylate (NACA-OBS of penta-acetyl glucose (PAG) or N-nonanoyl-6-aminocaprolc acid; be described in WO94/28106) use together, but these bleach activator peroxidation hydrogenolysis and form the peracid of the active albic material that produces the bleaching effect that improves.The activator that is suitable for for example be disclosed in ining addition in the European Patent Application No. 91870207.7 of pending trial simultaneously acylated citrate esters and as being disclosed in Procter ﹠amp; The asymmetric acyclic imide bleach promoting agent of the following formula in the U.S. Patent application series No. 60/022786 (submission on July 30th, 1996) and No. 60/028122 (submission on October 15th, 1996) of Gamble while pending trial:

R wherein ₁Be C ₇-C ₁₃Linearity or branch's catenate, saturated or unsaturated alkyl; R ₂Be C ₁-C ₈Linearity or the saturated or unsaturated alkyl of branch's catenate; R ₃Be C ₁-C ₄Linearity or the saturated or unsaturated alkyl of branch's catenate.

Be used for according to detergent composition of the present invention the available SYNTHETIC OPTICAL WHITNER, comprise peroxy acid and contain bleach activator and the bleach system of peroxy bleaching compound is described among our copending application USSN 08/136626, PCT/US95/07823, WO95/27772, WO95/27773, WO95/27774 and the WO95/27775.

Hydrogen peroxide also can exist by add the enzyme system (being a kind of enzyme and a kind of substrate) that can produce hydrogen peroxide during washing beginning or washing and/or in the rinse cycle.This kind of enzyme system is described in the european patent application of submitting on October 9th, 1,991 91202655.6.

The containing metal catalyzer that is used for bleaching composition comprises cobalt-containing catalyst such as acetate five amine cobalt (III) salt and contains Mn catalyst such as being described in EPA 549271; EPA 549272; EPA458397; US 5246621; EPA 458398; This class catalyzer among US 5194416 and the US 5114611.The bleaching composition that comprise peralcohol, contains manganese bleaching catalyst and sequestrant is described in the female application 94870206.3 of patent.

SYNTHETIC OPTICAL WHITNER beyond the oxygen bleaching agent also is familiar with by those skilled in the art and is can be used in this.The significant especially non-oxygen bleaching agent of one class comprises that the SYNTHETIC OPTICAL WHITNER of photoactivation is such as Sulfonated zinc phthalocyanine and/or aluminium.These materials can be deposited in washing process on the dirt-carrying body.Behind photoirradiation, such as by clothes being hung under the daylight when dry, thereby Sulfonated zinc phthalocyanine is activated and the dirt-carrying body is bleached in the presence of oxygen.Preferred zinc phthalocyanine and photoactivation bleaching method are described in the United States Patent (USP) 4033718.In general, detergent composition will comprise the sulfonated zinc phthalocyanine of about 1.25% (weight) of about 0.025-.

Adjuvant system

Cleaning compositions of the present invention will preferably include auxiliary agent, more preferably comprise inorganic assistant agent, most preferably comprise zeolite A, lamina sodium silicate and/or tripoly phosphate sodium STPP.Now find uncannily to comprise that also the cleaning compositions of the present invention of auxiliary agent provides the enhanced cleaning performance.Be not wishing to be bound by theory, believe that calcium is deposited on the top and the restriction enzyme hydrolysis according to this of hydro-colloid natural gum.So, expectation used additives is removed calcium of carrying secretly and the effect that helps the enzyme of combination of the present invention.

Conventional adjuvant system all is applicable in this, and the material, metal ion sequestering agent that comprise silico-aluminate material, silicate, polycarboxylate, alkyl or alkenyl succinic and fatty acid material such as edetate, diethylenetriamine pentamethylene acetate are such as amino poly phosphonate, particularly ethylenediamine tetramethylene phosphonic acid and diethylenetriamine pentamethylenophosphonic acid(DTPP).Phosphate builder also can be used in this.

The auxiliary agent that is suitable for can be an inorganic ion exchange material, and normally inorganic hydrated aluminosilicate material more specifically is that the hydration synthetic zeolite is such as hydrated zeolite A, X, B, HS or MAP.

The another kind of inorganic assistant agent material that is suitable for is for example SKS-6 (Hoechst) of layered silicate.SKS-6 is a kind of water glass (Na that comprises ₂Si ₂O ₅) crystalline layered silicate.

The polycarboxylate that comprises a carboxyl that is suitable for comprises lactic acid, oxyacetic acid and its ether derivant that is disclosed in belgian patent 831368,821369 and 821370.The polycarboxylate that contains two carboxyls comprises the water-soluble salt of succsinic acid, propanedioic acid, (ethylenedioxy) oxalic acid, toxilic acid, diglycollic acid, tartrate, tartronic acid and fumaric acid, and comprise German prospectus (Offenlegenschrift) 2446686 and 2446687 and U.S. Patent number 3935257 described at ether carboxylate and at the sulfinyl carboxylate salt described in the belgian patent numbers 840623.The polycarboxylate that contains three carboxyls specifically comprises newborn acyloxy succinate described in the carboxy methoxy-succinic acid salt described in water-soluble citrate, aconitrates and citraconate and succinate derivative such as the British Patent No. 1379241, the Netherlands patent applications 7205873 and the 2-oxa--1 of oxygen polycarboxylate material described in British Patent No. 1387447,1,3-tricarballylic acid salt.

The polycarboxylate that contains four carboxyls comprises disclosed oxygen disuccinate, 1,1,2 in the British Patent No. 1261829,2-ethane tetracarboxylic acid hydrochlorate, 1,1,3,3-propane tetracarboxylic acid salt and 1,1,2,3-propane tetracarboxylic acid salt.Contain the substituent polycarboxylate of sulfo group comprise be disclosed in British Patent No. 1398421 and 1398422 and U.S. Patent number 3936448 in the sulfo-succinic acid salt derivative and the sulfonated pyrolysis Citrate trianion described in the British Patent No. 1082179, be disclosed in the British Patent No. 1439000 and contain the substituent polycarboxylate of phosphone.

Alicyclic ring and heterocycle polycarboxylate comprise pentamethylene-suitable, suitable, suitable-tetracarboxylic acid hydrochlorate, cyclopentadienide anion pentacarboxylic acid salt, 2,3,4,5-tetrahydrofuran (THF)-suitable, suitable, suitable-tetracarboxylic acid hydrochlorate, 2,5-tetrahydrofuran (THF)-suitable-dicarboxylate, 2,2,5,5-tetrahydrofuran (THF)-tetracarboxylic acid hydrochlorate, 1,2,3,4,5, the carboxymethyl derivant of 6-hexane-hexacarboxylic acid salt and polyvalent alcohol such as sorbyl alcohol, mannitol and Xylitol.The aromatics polycarboxylate comprises mellitic acid, 1,2,4, disclosed phthalic acid derivatives in 5-pyromellitic acid and the British Patent No. 1425343.

In the superincumbent polycarboxylate, preferably per molecule contains the hydroxycarboxylate of 3 carboxyls, particularly Citrate trianion at the most.

Be preferred for the mixture that adjuvant system in the composition of the present invention comprises water-insoluble silico-aluminate auxiliary agent such as zeolite A or layered silicate (SKS-6) and water-soluble carboxylate sequestrant such as citric acid.Other preferred adjuvant system comprises the mixture of water-insoluble silico-aluminate auxiliary agent such as zeolite A and water-soluble carboxylate sequestrant such as citric acid.The adjuvant system that is preferred in the liquid detergent composition of the present invention is soap and polycarboxylate.

Other promoter material that can be configured for the adjuvant system part of particulate composition comprises inorganic materials such as alkaline carbonate, supercarbonate, silicate and organic substance such as organic phosphonate, amino polyolefine phosphonate and aminopolycarboxylic salt.Other water-soluble organic salt that is suitable for has homopolymerization or co-polymeric acids or its salt, and wherein said poly carboxylic acid comprises at least two by being no more than the carboxyl that two carbon atoms are separated mutually.Such polymkeric substance is disclosed among the GB-A-1596756.It is the multipolymer of 2000 to 5000 polyacrylate and itself and maleic anhydride that the example of this salt has molecular weight, and this multipolymer has 20000 to 70000 molecular weight, particularly about 40000 molecular weight.

Washing auxiliary detergent salt normally with account for composition 5-80%, preferred 10-70%, most preferably the amount of 30-60% (weight) is included in wherein.

Other surfactant system

Cleaning compositions of the present invention also can comprise positively charged ion, both sexes, zwitter-ion and semi-polarity tensio-active agent, and nonionic and/or anion surfactant beyond noted earlier.

Amphoterics also is applicable to cleaning compositions of the present invention.These tensio-active agents can be loosely referred to as the aliphatic derivatives of secondary amine or tertiary amine, or the aliphatic derivatives of heterocyclic secondary and tertiary amine (wherein said aliphatic group can be straight or branched).One of described aliphatic substituting group comprises at least about 8 carbon atoms, generally about 8 arrives about 18 carbon atoms, and at least one comprises negatively charged ion water solubilization group for example carboxyl, sulfonate radical, sulfate radical.For the example of amphoterics, can be referring to 19 hurdles, 18 to 35 row of the people's such as Laughlin that authorized on December 30th, 1975 U.S. Patent number 3929678.

When this amphoterics existed, cleaning compositions of the present invention generally comprised 0.2 to about 15%, the preferred this amphoterics of about 10% (weight) of about 1-.

Zwitterionics also is applicable to cleaning compositions.These tensio-active agents can be loosely referred to as the derivative of derivative, heterocyclic secondary and tertiary amine of secondary amine and tertiary amine or the derivative of quaternary ammonium, quaternary phosphine or uncle's sulfonium compound.For the example of zwitterionics, can be referring to 19 hurdles, 38 row of the people's such as Laughlin that authorized on December 30th, 1975 U.S. Patent number 3929678 to 22 hurdles, 48 row.

When this zwitterionics existed, cleaning compositions of the present invention generally comprised 0.2 to about 15%, the preferred this zwitterionics of about 10% (weight) of about 1-.

Semi-polar nonionic surfactants is a kind of non-ionic surface active agent of Special Category, it comprise the water-soluble amine oxide (described amine oxide comprise one contain about 10 be selected to the moieties of about 18 carbon atoms and two contain about 1 part to alkyl and the hydroxyalkyl of about 3 carbon atoms), the water-soluble phosphine oxide (described phosphine oxide comprise one contain about 10 be selected to the moieties of about 18 carbon atoms and two contain about 1 part to alkyl and the hydroxyalkyl of about 3 carbon atoms) and water-soluble sulfoxide (described sulfoxide comprise one contain about 10 be selected to the moieties of about 18 carbon atoms and one contain about 1 to the 3 approximately alkyl of a carbon atom and the part of hydroxyalkyl).

Semi-polarity nonionic detergent tensio-active agent comprises the amine oxide tensio-active agent with following formula:

R in the formula ³Be alkyl, hydroxyalkyl or alkyl phenyl or its mixture, it contains about 8 to about 22 carbon atoms; R ⁴For containing about 2 alkylidene group or hydroxy alkylidene or its mixtures to about 3 carbon atoms; X is 0 to about 3; Each R ⁵For containing about 1 to the alkyl or the hydroxyalkyl of about 3 carbon atoms or contain about 1 polyoxyethylene groups to about 3 oxyethylene groups group.Described R ⁵Group can for example interconnect by Sauerstoffatom or nitrogen-atoms and form ring structure.

These amine oxide tensio-active agents specifically comprise C ₁₀-C ₁₈Alkyl dimethyl amine oxide and C ₈-C ₁₂Alkoxyethyl dihydroxyl amine oxides.

When this semi-polar nonionic surfactants existed, cleaning compositions of the present invention generally comprised about 15%, the preferred this semi-polar nonionic surfactants of about 10% (weight) of about 1-of 0.2-.

Cleaning compositions of the present invention also can comprise the cosurfactant that is selected from primary amine or tertiary amine.

Be applicable to that the primary amine in this comprises according to formula R ¹NH ₂Amine, R in the formula ¹Be C ₆-C ₁₂, preferred C ₆-C ₁₀Alkyl chain or R ⁴X (CH ₂) _n, X is-O-,-C (O) NH-or-NH-, R ⁴Be a C ₆-C ₁₂Alkyl chain, n are 1 to 5 and are preferably 3.R ¹Alkyl chain can be straight or branched and can by last to 12, preferably be less than 5 oxyethylene groups and separate.

Preferably the amine according to following formula is positive alkylamine.The amine that is suitable in this can be selected from 1-hexylamine, 1-octylame, 1-decyl amine and lauryl amine.Other preferred primary amine comprises C ₈-C ₁₀Oxygen propylamine, octyloxy propylamine, 2-ethyl hexyl oxy propylamine, the amino propylamine of lauroyl and amido propylamine.

Be applicable to that the tertiary amine in this comprises having formula R ₁R ₂R ₃The tertiary amine of N, R in the formula ₁And R ₂Be C ₁-C ₈Alkyl chain or

R ₃Be C ₆-C ₁₂, preferred C ₆-C ₁₀Alkyl chain or R ₃Be R ₄X (CH ₂) _n, wherein X be-O-,-C (O) NH-or-NH-, R ₄Be C ₄-C ₁₂, n is 1 to 5, preferred 2 to 3.R ₅Be H or C ₁-C ₂Alkyl, and x is 1 to 6.R ₃And R ₄Can be linearity or branch; R ₃Alkyl chain can by last to 12, preferably be less than 5 oxyethylene groups and separate.

Preferred tertiary amine is formula R ₁R ₂R ₃N, wherein R ₁Be C ₆-C ₁₂Alkyl chain, R ₂And R ₃Be C ₁-C ₃Alkyl or R in the formula ₅Be H or CH ₃And x is 1 to 2 tertiary amine.

The preferred amidoamines that also has following formula:

R in the formula ₁Be C ₆-C ₁₂Alkyl; N is 2 to 4, and preferred n is 3; R ₂And R ₃Be C ₁-C ₄

Most preferred amine of the present invention comprises 1-octylame, 1-hexylamine, 1-decyl amine, 1-n-Laurylamine, C ₈-C ₁₀Oxygen base propylamine, N-cocoyl-1,3-diaminopropanes, cocoyl alkyl dimethylamine, lauryl dimethylamine, two (hydroxyethyl) amine of lauryl, two (hydroxyethyl) amine of cocoyl, 2 moles of propoxides of lauryl amine, 2 moles of propoxides of octylame, the amino propyl group dimethylamine of lauroyl, C ₈-C ₁₀Amido propyl group dimethylamine and C ₁₀Amido propyl group dimethylamine.

The amine that most preferably is used for composition of the present invention is 1-hexylamine, 1-octylame, 1-decyl amine, 1-n-Laurylamine.What need especially is the amino propylamine of oleyl amine, lauroyl and the cocounut oil amido propylamine of dodecyl dimethylamine and double hydroxyethyl cocounut oil alkylamine and 7 times of ethoxylations.

Conventional washing enzyme

Except enzyme of the present invention, described cleaning compositions also comprises the enzyme enzyme that one or more provide clean-up performance, fabric nursing and/or sanitation benefits.

Described enzyme comprises the enzyme that is selected from hemicellulase, peroxidase, proteolytic enzyme, glucoamylase, zytase, lipase, phospholipase, esterase, keratanase, M-Zyme (keratanase), reductase enzyme, oxydase, phenol oxidase, lipoxidase, lignoenzyme, Starch debranching enzyme, tannase, pentosanase, malanases, beta-glucanase, Unidasa, chondroitinase, laccase or its mixture.

A kind of preferred combination is to have the conventional enzyme that uses as proteolytic enzyme, amylase, lipase, keratanase and/or the cellulase cleaning compositions together with the mixture of one or more plant cell-wall degrading enzymes.

Peroxidase is together with oxygen source for example percarbonate, perborate, persulphate, hydrogen peroxide etc. and use as the phenol substrate that bleaching strengthens molecule.They are used for " solution bleaching ", prevent promptly in the washing process that the dyestuff removed from the dirt-carrying body or pigment transfers on other dirt-carrying body the washing soln.Peroxidase is familiar with by those skilled in the art and is comprised for example horseradish peroxidase, lignoenzyme and halo peroxidase such as chloro and bromoperoxidase.The detergent composition that contains peroxidase is disclosed in European patent application EP of for example submitting in PCT International Application No. WO 89/099813, WO89/09813 and on November 6th, 1,991 91202882.6 and the EP 96870013.8 that submitted on February 20th, 1996.The laccase in addition that is suitable for.

Synergistic agent generally accounts for the 0.1-5% (weight) of total composition.The thiodiphenylamine that preferred synergistic agent is replacement and phenoxazine lysivane propionic acid (PPT), 10-ethyl thiodiphenylamine-4-carboxylic acid (EPC), 10-phenoxazine propionic acid (POP) and 10-first base phenoxazine (being described in WO94/12621) and the cloves hydrochlorate (syringate) (the alkyl cloves hydrochlorate that C3-C5 replaces) and the phenol that replace.SPC-D or Sodium peroxoborate are preferred hydrogen peroxide cources.

Described peroxidase normally is incorporated in the described detergent composition with the level that accounts for the pure enzyme of described detergent composition 0.0001-2%.

Other enzyme that preferably can be included in the detergent composition of the present invention comprises lipase.The lipase that is applicable to the washing composition purposes comprises the lipase that disclosed Pseudomonas stutzeri (Pseudomonas stutzeri) ATCC 19.154 produces in the microorganism of Rhodopseudomonas such as the English Patent 1372034.The lipase that is suitable for comprises the lipase that demonstrates with the antibody positive immunological cross-reaction of the lipase that is produced by microorganism Pseudomonas fluorescens (Pseudomonasfluoresent) IAM 1057.This lipase can be bought (hereinafter being called " Amano-P ") with the trade(brand)name of lipase P " Amano " from the AmanoPharmaceutical Co.Ltd. of Japanese Nagoya.Other commercial lipases that is suitable for comprises Amano-CES, come from thickness look bacillus (Chromobacter viscosum) as the lipase from the mutation liolyticumNRRLB 3673 of the thickness look bacillus of the Toyo Jozo Co. of Japanese Tagata; From the U.S.Biochemical Corp. of the U.S. and the thickness look bacillus lipase and the lipase that comes from gladiolus pseudomonas (Pseudomonasgladioli) of the Disoynth Co of Holland.The lipase of particularly suitable be have been found that when using together with composition of the present invention very effective as M1 Lipase ^And Lipomax ^(Gist-Brocades) and Lipolase ^With Lipolase Ultra ^(Novo) lipase.What be suitable for also has EP258068, WO92/05249 and WO94/03578, the WO95/35381 of WO 95/22615 and Unilever and the lipolytic enzyme described in the WO96/00292 at Novo Nordisk.

The lipase that can think a kind of particular variety in addition that is suitable for does not promptly need the keratanase [EC 3.1.1.50] of the lipase of interface activation.The situation that keratanase is joined in the detergent composition is described in for example WO-A-88/09367 (Genencor), WO90/09446 (Plant GeneticSystem) and WO 9,4/1 4963 and WO94/1 4964 (Unilever).

Described lipase and/or keratanase normally are incorporated in the described detergent composition with the level of the pure enzyme of 0.0001-2% that accounts for described detergent composition weight.

Useful proteases has the Validase TSP Concentrate II (Validase TSP Concentrate II BPN and BPN ') that obtains from the concrete bacterial strain of subtilis and Bacillus licheniformis.A kind of useful proteases is to obtain and have maximum active and by Novo Industries A/S (hereinafter being called " the Novo ") exploitation of Denmark and with ESPERASE in whole 8 to 12 pH scope from the bacterial strain of bacillus ^The proteolytic enzyme sold of trade(brand)name.The preparation of this kind of enzyme and its similar enzyme is described among the GB1243784 of Novo.Other useful proteases comprises the ALCALASE from Novo ^, DURAZYM ^And SAVINASE ^And from the MAXATASE of Gist-Brocades ^, MAXACAL ^, PROPERASE ^And MAXAPEM ^(Maxacal of protein engineering).Proteolytic ferment also comprises modified bacterial serine proteolytic enzyme, described in the european patent application series number of submitting on April 28th, 1,987 87 303761.8 (particularly 17,24 and 98 pages) and be called this proteinoid enzyme of " proteolytic enzyme B " hereinto and be called the modified bacterial serine proteolytic ferment of " protease A " hereinto and at this proteinoid enzyme described in the european patent application 199404 of Venegas on the 29th October in 1986.Useful proteases is the proteolytic enzyme that is called " proteolytic enzyme C " in this, it is a kind of variant that comes from the alkaline serine protease of genus bacillus, and wherein Methionin has replaced at 27 that arginine, tyrosine have replaced Xie Ansuan at 104, Serine has changed l-asparagine in 123 positions and L-Ala has replaced Threonine at 274.Proteolytic enzyme C is described among the disclosed EP 90915958.4 on May 16th, suitable with WO91/06637 1.The variant of genetic modification, particularly proteolytic enzyme C is also included within wherein.

The preferred proteolytic enzyme of a kind of being called " proteolytic enzyme D " is to have the carbonylic hydrolase variant that does not have the aminoacid sequence found in natural, as WO95/10591 with described in applying for of the mother with " Bleaching Compositions Comprising Protease Enzymes " by name that the people such as C.Ghosh of U.S. Patent Application Serial 08/322677 submitted on October 13rd, 1994, it is according to the numbering of bacillus amyloliquefaciens spores of bacillus subtilin proteolytic enzyme, by be equivalent to a kind of different amino-acid substitution+the described carbonylic hydrolase of 76 positions in the position, preferably also together be equivalent to be selected from+99, + 101, + 103, + 104, + 107, + 123, + 27, + 105, + 109, + 126, + 128, + 135, + 156, + 166, + 195, + 197, + 204, + 206, + 210, + 216, + 217, + 218, + 222, + 260, + 265 and/or+numerous amino-acid residues at one or more amino acid residue positions place of 274 derive from the precursor carbonylic hydrolase.The enzyme that is suitable for is described in the carbonylic hydrolase variant of the proteolytic enzyme among the WO95/10591 in addition, it has by displacement and is equivalent in pre-enzyme+a plurality of amino-acid residues of metathetical on 210 and the metathetical aminoacid sequence of one or more following residues :+33, + 62, + 67, + 76, + 100, + 101, + 103, + 104, + 107, + 128, + 129, + 130, + 132, + 135, + 156, + 158, + 164, + 166, + 167, + 170, + 209, + 215, + 217, + 218 and+222, wherein Bian Ma position and naturally occurring from bacillus amyloliquefaciens Validase TSP Concentrate II quite or suitable with the amino-acid residue of imitating in other carbonylic hydrolase or Validase TSP Concentrate II such as bacillus lentus Validase TSP Concentrate II (U.S. Patent Application Serial 60/048550 of pending trial in the application on June 4th, 1997) moderate.

Be applicable to that proteolytic enzyme of the present invention also comprises the proteolytic enzyme that is described among patent application EP 251446 and the WO91/06637, is described in the proteolytic enzyme BLAP among the WO 91/02792 ^With its variant that is described among the WO 95/23221.

Also referring to high pH proteolytic enzyme from the bacillus bacterial classification NCIMB 40338 among the WO 93/18140A that is described in Novo.The enzyme detergent that comprises proteolytic enzyme, one or more other enzymes and reversible protease inhibitors is described among the WO92/03529A of Novo.When needing, having the proteolytic enzyme that has reduced absorption and increased hydrolysis can be as Procter ﹠amp; Obtain like that described in the WO 95/07791 of Gamble.A kind of proteolytic enzyme of trypsin-like of the reorganization that is used for being suitable for this washing composition is described among the WO 94/25583 of Novo.Other useful proteases is described among the EP516200 of Unilever.

Described proteolytic ferment is with 0.0001-2%, the preferred 0.001-0.2% of the weight that accounts for described composition, more preferably the level of the pure enzyme of 0.005-0.1% is incorporated in the detergent composition of the present invention.

Above-mentioned enzyme can be from any suitable source such as plant, animal, bacterium, fungi and yeast.Described source can further be mesopilous organisms or have a liking for extremely biological (psychrophilic organism, psychrophilic bacteria, thermophile, have a liking for press biological, have a liking for alkali biology, acidophils, have a liking for halogen biology etc.).Can use purified or these enzymes of purified form not.Now, in order to make the optimizing effect in cleaning compositions of the present invention, the enzyme of modifying agriotype through protein/genetic engineering technique is conventional practice.For example, thus can design the compatibleness that described variant improves the composition commonly used of described enzyme and this composition.Perhaps described variant can be designed so that best pH, bleaching or sequestrant stability, the catalytic activity etc. of described enzyme variants are fit to concrete cleaning purposes.

Specifically, concerning bleach stability, attention should be placed on the amino acid to oxidation-sensitive, concerning the tensio-active agent compatibleness, attention should be placed on the surface charge.The iso-electric point of this kind of enzyme can change by the replacement of some charge residues, and for example the raising of iso-electric point can help to improve the compatibleness with anion surfactant.The stability of described enzyme can be further by the generation of for example other salt bridge with strengthen the calcium binding site and increase to improve sequestrant stability.Because most of cellulases have independent in conjunction with territory (CBD), special attention should be placed on the cellulase.The character of this kind of enzyme can change by the modification in these territories.

Described enzyme normally is incorporated in the described detergent composition with the level of the pure enzyme of 0.0001-2% that accounts for described detergent composition weight.Described enzyme can be used as independently single composition (containing a kind of spherolite, particle of enzyme, the liquid of stabilization etc.) or adds as the mixture (for example cogranulates) of two or more enzymes.

Other detergent ingredients that is suitable for that can add is the oxydasis scavenging agent that is described in the european patent application 92870018.6 of pending trial when submitting on January 31st, 1992.The example of this kind of enzyme oxidation scavengers has ethoxylation four ethylidene polyamine.

Enzyme material and its method in the synthetic detergent composition of mixing also is described in people's such as the WO8908694A of the WO9307263 A of GenencorInternational and WO9307260 A, Novo and McCarty the United States Patent (USP) 3553139 on 5 days January in 1971.Enzyme also is disclosed among US 4101457 on July 18th, 1978, people such as Place and in March, 1985 US4507219 26 days, Hughes.Can be used for the enzyme material of liquid detergent preparation and its mixing in this preparation is described among the US4261868 on April 14th, 1981, people such as Hora.The enzyme that is used for washing composition can be by various consistent.The stable technology of enzyme open and be illustrated in people's such as Gedge on the 17th August in 1971 US3600319, in October, 1986 EP199405 29 days, Venegas and EP 200586 in.The enzyme stabilising system also is described in for example in US3519570.A kind of bacterial classification AC13 of the useful genus bacillus of proteolytic enzyme, zytase and cellulase that provides is described among the WO9401532A of Novo.

Protect look and fabric nursing benefit

Also can comprise the technology of protecting the look benefit is provided.The example of these technologies is useful on the metal catalyst that color keeps.This metal catalyst is described in the european patent application 92870181.2 of while pending trial.Laking agent, be used for crease-resistant and improve absorptive polyolefin dispersion, be used to protect that look is handled and the spices and the amino-functional polymkeric substance of the affine processing of spices are other examples that protects look/fabric nursing technology, and be described in the patent application 96870140.9 of pending trial when submitting on November 7th, 1996.

Fabric softener also can be incorporated into according in the cleaning compositions of the present invention.These tenderizers can be that inorganic type also can be organic type.The example of inorganic tenderizer has the terre verte that is disclosed in GB-A-1400898 and the United States Patent (USP) 5019292.The organic fabric tenderizer comprises the water-insoluble tertiary amine that is disclosed among GB-A1514276 and the EP-B0011340 and is disclosed in the mixture of itself and single C12-C14 quaternary ammonium salt among EP-B-0026527 and the EP-B-0026528 and is disclosed in two-long-chain acid amides among the EP-B-0242919.The useful organic composition of the fabric-softening system that other is useful comprises as being disclosed in the high molecular weight peo material in EP-A-0299575 and 0313146.

The level of terre verte normally is 2-20%, more preferably 5-15% (weight), and this material adds as the form with the component of other composition dry mixed of preparation.Organic fabric tenderizer such as water-insoluble tertiary amine or two long-chain acid amides materials mix with the level of 0.5-5% (weight), normal 1-3% (weight), and high molecular weight peo material and water-soluble cationic material are with the level adding of 0.1-2%, normal 0.15-1.5% (weight).These materials join the spraying drying part of composition usually, although sometimes they are added as the particulate matter of dry mixed or be sprayed on other solid ingredient of composition them more convenient as melt liquid.

Sequestrant

Cleaning compositions of the present invention also can be chosen wantonly and comprise one or more iron and/or manganese sequestrant.This sequestrant can be selected from aromatic chelating agent and its mixture of aminocarboxylate, amino phosphonates do, multifunctional replacement, and all are all as hereinafter definition.Be not wishing to be bound by theory, the benefit of believing these materials partly is because it is by forming the extraordinary ability of removing iron and manganese from washings that the soluble chelating thing causes.

The aminocarboxylate that can be used as optional sequestrant comprises edetate, N-hydroxyethyl-ethylenediamine triacetate, nitrilotriacetic acid(NTA) salt, ethylenediamine tetrapropionic acid(EDTP) salt, triethylenetetraaminehexaacetic acid salt, diethylentriamine pentacetate and ethanol Diglycocol, its basic metal, ammonium and substituted ammonium salt and its mixture.

Allow when being present in the detergent composition that when low-level at least total phosphorus amino phosphonates do also is suitable for as the sequestrant in the composition of the present invention, and comprise ethylenediamine tetraacetic (methylene phosphonic acid salt) as DEQUEST.Preferred these amino phosphonates do do not comprise alkyl or the alkenyl more than about 6 carbon atoms.

The aromatic chelating agent of multifunctional replacement also can be used in the composition of the present invention.United States Patent (USP) 3812044 referring to the people such as Connor that authorized on May 21st, 1974.Such compound of preferred acid be the dihydroxyl disulfobenzene such as 1,2-dihydroxyl-3,5-disulfobenzene.

A kind of biodegradable sequestrant that is preferred in this be ethylenediamine disuccinate (" EDDS "), particularly on November 3rd, 1987 Hartman and Perkins United States Patent (USP) 4704233 described in [S, S] isomer.

Composition in this also can comprise water-soluble methylglycine oxalic acid (MGDA) salt (or acid) conduct can be with the sequestrant or the washing assistant of uses such as for example insoluble auxiliary agent such as zeolite, layered silicate.

If use, these sequestrants generally account for about 15% (weight) of about 0.1-of detergent composition of the present invention.More preferably, if use, described sequestrant accounts for about 3.0% (weight) of about 0.1-of this composition.

Suds suppressor

Another kind of optional ingredients is a suds suppressor, for example siloxanes and silica-mixture of siloxanes.Siloxanes can generally be represented by alkylation polysiloxane material, and silica normally uses with form in small, broken bits, for example silica aerosol and xerogel and various types of hydrophobic silex.These materials can mix with the particulate matter form, and that wherein said suds suppressor advantageously is incorporated into releasedly is water-soluble or water dispersible, basically in the impermeable carrier of non-surface active washing composition.Perhaps described suds suppressor solubilized or be scattered in the liquid vehicle and can use by being sprayed on one or more other components.

A kind of preferred silicone foam control agent is disclosed in people's such as Bartollota the United States Patent (USP) 3933672.Other useful especially suds suppressor is the self-emulsifying silicone suds suppressor that is described among the disclosed German patent application DTOS 2646126 on April 28th, 1977.An example of this compound is can be available from the DC-544 of Dow Coming, and it is a kind of siloxanes-divalent alcohol copolymers.Particularly preferred Foam Control is the suds suppressor system that comprises the mixture of silicone oil and 2-alkyl chain triacontanol.The 2-alkyl chain triacontanol that is suitable for is the 2-butyl-octanol that can buy with the trade(brand)name of Isofol 12R.

This suds suppressor system is described among the european patent application N92870174.7 of pending trial when submitting on November 10th, 1992.

Particularly preferred silicone foam control agent is described in the European Patent Application No. 92201649.8 of while pending trial.Described composition can comprise together with pyrolysis method atresia silica such as Aerosil ^Siloxanes/silica mixture.

Above-mentioned suds suppressor normally uses with the 0.001-2% (weight) that accounts for composition, the level of preferred 0.01-1% (weight).

Other

Can use other component that is used for cleaning compositions, such as soil-suspending agent, stain remover, white dyes, friction agent, sterilant, tarnish inhibitor, tinting material and/or seal or non-encapsulated perfume.

Particularly suitable encapsulating substance is the water-soluble capsule that comprises such as at the matrix of polysaccharide described in the GB1464616 and polyol.Other water-soluble encapsulating substance that is suitable for comprises the dextrin of the not gelation starch acid esters of the replacement di-carboxylic acid that comes from described in US3455838.These acid esters dextrin are preferably from preparing such as waxy corn, wax Chinese sorghum, sago, tapioca (flour) and yam starch.The example of the described encapsulating substance that is suitable for comprises the N-Lok that is produced by National Starch.Described N-Lok encapsulating substance comprises the W-Gum and the glucose of modification.Described starch passes through to add the group of simple function replacement such as the octenyl succinic acid anhydride modification.

Be applicable to that anti redeposition agent and soil-suspending agent among the present invention comprise derivatived cellulose such as methylcellulose gum, carboxymethyl cellulose and Natvosol and homopolymerization or copolymerization poly carboxylic acid or its salt.Such polymkeric substance comprises aforementioned multipolymer for the polyacrylate of auxiliary agent and copolymer of maleic anhydride and acrylic acid and maleic anhydride and ethene, methylvinylether or methacrylic acid, and described maleic anhydride accounts at least 20% (mole) of this multipolymer.These materials are 0.5-10% (weight), more preferably 0.75-8% (weight), the most preferably level use of 1-6% (weight) to account for composition normally.

Preferred white dyes is the white dyes with anionic nature, and its example is 4,4 '-two (2-diethanolamino-4-anilino-s-triazine-6-base is amino) stilbene-2,2 '-disulfonic acid disodium; 4,4 '-two (2-morpholino-4-anilino-s-triazine-6-base amino stilbene-2,2 '-disulfonic acid disodiums; 4,4 '-two (2,4-hexichol amido-s-triazine-6-base is amino) stilbene-2,2 '-disulfonic acid disodium; 4 ', 4 " stilbene-2-sulfonic acid one sodium-two (2,4-hexichol amido-s-triazine-6-base is amino); 4,4 '-two (2-anilino-4-(N-methyl-N-2-hydroxyethylamino)-S-triazine-6-base is amino) stilbene-2,2 '-disulfonic acid disodium; 4,4 '-two (4-phenyl-2,1,3-triazole-2-yl)-stilbenes-2,2 '-disulfonic acid disodium; 4,4 '-two (2-anilino-4-(1-methyl-2-hydroxyethylamino)-s-triazine-6-base is amino) stilbene-2,2 '-disulfonic acid disodium; 2 ( base-4 "-(naphtho--1 ', 2 ': 4,5-)-1,2,3-triazoles-2 "-sodium sulfonate and 4,4 '-two (2-sulfo group styryl) biphenyl.Highly preferred white dyes is the concrete white dyes that is disclosed among the EP 753567.

Other available polymeric material is polyoxyethylene glycol, particularly molecular weight 1000 to 10000, more specifically is 2000 to 8000, most preferably from about 4000 polyoxyethylene glycol.They can be with 0.20-5%, the more preferably level use of 0.25-2.5% (weight).Whiteness keeps for improving for these polymkeric substance and aforesaid homopolymerization or copolymerization polycarboxylate, fabric ash-deposition and be extremely valuable to earth, clean-up performance protein-based and oxidable dirt in the presence of transition metal impurity.

The stain remover that can be used in the present composition is conventional terephthalic acid and various ethylene glycol of arranging and/or unitary multipolymer of propylene glycol or terpolymer.The example of this polymkeric substance be disclosed in common transfer U.S. Patent number 4116885 and 4711730 and European disclosed number of patent application 0272033 in.A kind of particularly preferred polymkeric substance according to EP-A-0272033 has following formula:

(CH ₃(PEG) ₄₃) _0.75(POH) _0.25[(T-PO) _2.8(T-PEG) _0.4] T (POH) _0.25((PEG) ₄₃CH ₃) _0.75PEG is-(OC in the formula ₂H ₄) O-, PO is (OC ₃H ₆O) and T be (pcOC ₆H ₄CO).

The very useful modified poly ester that also has as the random copolymers of dimethyl terephthalate (DMT), sulfoisophthalic acid dimethyl ester, ethylene glycol and 1,2 propylene glycol, its end group mainly comprises sulfosalicylic acid salt, next comprises the monoesters of ethylene glycol and/or propylene glycol.Target is to obtain two ends all by the end capped polymkeric substance of sulfosalicylic acid salt group, and " mainly " is meant that here most of described multipolymers are by sulfosalicylic acid salt group end-blocking in patent specification.But some multipolymers are by end-blocking fully, so its end group may comprise ethylene glycol and/or the third 1, the monoesters of 2 glycol, therefore " secondly " comprise this material.

Selected polyester comprises about 46% (weight) dimethyl terephthalate (DMT), about 16% (weight) propane 1 in this, 2-glycol, about 10% (weight) ethylene glycol, about 13% (weight) sulfosalicylic acid dimethyl ester and about 15% (weight) sulfoisophthalic acid and have about 3000 molecular weight.Described polyester and its preparation method are described in detail among the EPA311342.

Those skilled in the art know the enzyme that comprises in the quick passivation detergent composition of free chlorine in tap water.Therefore, in prescription, use chlorine scavenger such as perborate, ammonium sulfate, S-WAT or polyethylene imine based so that the wash stability of the whole enzyme for detergent of improvement is provided with the level more than about 0.1% (weight) that accounts for total composition.The composition that comprises chlorine scavenger is described in the european patent application of submitting on January 31st, 1,992 92870018.6.

The alkoxylate polycarboxylate is such as the degreasing performance that can be used for hereinto from those of polyacrylic ester preparation providing other.This substance description reaches hereinafter in the page 4 of WO91/08281 that all incorporates this paper by reference into and PCT90/01815.Chemically, these materials comprise the polyacrylic ester of an oxyethyl group side chain of per 7 to 8 acrylic ester unit.Described side chain is formula-(CH ₂CH ₂O) _m(CH ₂) _nCH ₃, m is 2 to 3 in the formula, and n is 6 to 12.Described side chain is connected to polyacrylic ester " skeleton " by ester and goes up so that " comb " polymer type structure to be provided.Described molecular weight can be different, but generally in about 2000 to about 50000 scope.This alkoxylate polycarboxylate can account for about 10% (weight) of about 0.05-of composition in this.

Dispersion agent

Cleaning compositions of the present invention also can comprise dispersion agent.The water-soluble organic salt that is fit to is homopolymerization or co-polymeric acids or its salt, and wherein said poly carboxylic acid comprises at least two by being no more than two carbon atom carboxyls spaced apart from each other.Such polymkeric substance is disclosed among the GB-A-1596756.It is the multipolymer of 2000 to 5000 polyacrylate and itself and maleic anhydride that the example of this salt has molecular weight, and this multipolymer has 1000 to 100000 molecular weight.

Particularly can join in the cleaning compositions of the present invention with the level of the 0.5-20% (weight) of composition such as the multipolymer of the acrylate of the 480N of molecular weight about 4000 and methacrylate.

Composition of the present invention can comprise and preferably has as hereinafter definedly being not more than 8, preferably being not more than 7, most preferably being not more than the calcium soap peptizing agent compound of 6 dispersion of calcium soap (LSDP).Described calcium soap peptizing agent compound preferably exists with the level of 0-20% (weight).

The digital measurement that the calcium soap peptizing agent is renderd a service is by using as providing at the dispersion of calcium soap (LSDP) that the lime soap dispersing agent test method described in the article of 88 to 90 pages of nineteen fifty J.Am.Oil.Chem.Soc. the 27th volumes records at H.C.Borghetty and C.A.Bergman.This calcium soap distributed test method is extensive use of for those skilled in the art, and appears in for example following survey article: W.N.Linfield is at the article of Surfactant science Series the 7th volume page 3; W.N.Linfield is at the article of 159 to 163 pages of nineteen ninety Tenside surf.det. the 27th volumes; Roll up 71 to 73 pages article with M.K.Nagarajan, W.F.Masler at Cosmetics andToiletries the 104th in 1989.Described LSDP is at 30 milliliters of 333ppmCaCO ₃(Ca: Mg=3: 2) disperse in the water of equivalent hardness to deposit the required dispersion agent and the weight percent ratio of sodium oleate by the calcium soap that 0.025 gram sodium oleate forms.

Tensio-active agent with good calcium soap peptizing power comprises some amine oxide, trimethyl-glycine, sultaine, alkyl ethoxy sulfate and ethoxylated alcohol.

The example that can be no more than 8 tensio-active agent by the LSDP that the present invention uses comprises C ₁₆-C ₁₈The dimethylamine oxide compound; Average degree of ethoxylation is 1 to 5 C ₁₂-C ₁₈Alkyl ethoxy sulfate, particularly ethoxylation degree are the C of 3 (LSDP=4) ₁₂-C ₁₅Alkyl ethoxy sulfate surfactant; Be the C of 12 (LSDP=6) or 30 with the average degree of ethoxylation that the trade(brand)name of Lutensol A012 and Lutensol A030 is sold respectively by BASF GmbH ₁₄-C ₁₅Ethoxylated alcohol.

Be applicable to that the polymerization calcium soap peptizing agent in this is described in the article of 71 to 73 pages of Cosmetics and Toiletries in 1989 the 104th volumes by M.K.Nagarajan and W.F.Masler.

The amino caproyl of hydrophobic bleach agent such as 4-[N-capryloyl-6-] benzene sulfonate, the amino caproyl of 4-[N-nonanoyl-6-] benzene sulfonate, the amino caproyl of 4-[N-decanoyl-6-] benzene sulfonate and its mixture and nonanoly acyloxy benzene sulfonate also can be used as calcium soap peptizing agent compound with the hydrophilic/hydrophobic bleaching preparations.

Dye transfer suppresses

Cleaning compositions of the present invention also can comprise and is used for being suppressed at dissolving that the fabric washing operation that includes yarn dyed fabric runs into and suspension dyestuff are transferred to another kind of fabric from a kind of fabric compound.

The polymeric dye transfer inhibitor

Also comprise 0.001-10%, preferred 0.01-2%, the more preferably polymeric dye transfer inhibitor of 0.05-1% (weight) according to cleaning compositions of the present invention.Dyestuff is transferred to from colored fabric on other fabric that is washed in order to suppress to wash, and usually described polymeric dye transfer inhibitor is incorporated in the cleaning compositions.These polymkeric substance have before dyestuff adheres to other fabric that is washed the ability that cooperates or be adsorbed with the fugitive dye that yarn dyed fabric washes out.

The polymeric dye transfer inhibitor of particularly suitable is multipolymer, polyvinylpyrrolidonepolymers polymers, Ju Yi Xi oxazolidinone and polyvinyl imidazol or its mixture of polyamine N-oxide pllymers, N-vinyl pyrrolidone and N-vinyl imidazole.

The adding of this polymkeric substance has also strengthened the usefulness according to enzyme of the present invention.

A) polyamine N-oxide pllymers

The polyamine N-oxide pllymers that is suitable for comprises the unit of following structural:

P is a polymerizable unit in the formula, can connect above it R-N-O group or wherein the R-N-O group constituted the combination of a part or two kinds of situations of polymerizable unit.A is NC.

-N-; X is 0 or 1; R is aliphatic series, aliphatic, the aromatics of ethoxylation, heterocycle or alicyclic group or its combination, can connect it on the nitrogen of N-O group or wherein the nitrogen of N-O group be the part of these groups.

Described N-O group can be represented by following general formula: Wherein R1, R2 and R3 are aliphatic group, aromatics, heterocycle or alicyclic group or its combination, x or/and y or/and z is 0 or 1, and wherein can connect the nitrogen of N-O group or wherein the nitrogen of N-O group constitute the part of these groups.

Described N-O group can be the part of polymerizable unit (P) or can be connected on the polymeric skeleton or both combinations.

The polyamine N-oxide that the wherein N-O group that is suitable for constitutes the part of polymerizable unit comprises that R is selected from the polyamine N-oxide of aliphatic series, aromatics, alicyclic ring or heterocyclic group.

The described polyamine N-oxide of one class comprises the wherein polyamine N-oxide of the nitrogen formation R group part of N-O group.Preferred polyamine N-oxide compound is that wherein R is the polyamine N-oxide of heterocyclic group such as pyridine, pyrroles, imidazoles, tetramethyleneimine, piperidines, quinoline, acridine and its derivative.

Another kind of described polyamine N-oxide comprises that the nitrogen of N-O group wherein is connected to the polyamine N-oxide on the R group.

Other polyamine N-oxide that is suitable for is connected to polyamine oxide compound on the polymerizable unit for N-O group wherein.

The polyamine N-oxide of preferred type for have in general formula (I) and the formula R be aromatics, heterocycle or alicyclic group and wherein N-O functional group's nitrogen be the polyamine N-oxide of the part of described R base.

The example of these types has wherein, and R is the polyamine oxide compound of heterogeneous ring compound such as pyridine, pyrroles, imidazoles and its derivative.

R is the polyamine oxide compound of aromatics, heterocycle or alicyclic group (wherein N-O functional group's nitrogen is connected on the described R group) to the polyamine N-oxide of another preferred type in general formula (I) and the formula in order to have.

The example of the polyamine oxide compound of these types has wherein, and the R group is the polyamine oxide compound of aromatic group such as phenyl.

As long as formed amine oxide polymkeric substance is water-soluble and has the dye transfer rejection that any polymer backbone all can use.The example of the polymer backbone that is suitable for has polyethylene, polyolefine, polyester, polyethers, polymeric amide, polyimide, polyacrylic ester and its mixture.

Amine n-oxide polymkeric substance of the present invention generally has 10: 1 to 1: 1000000 the amine and the ratio of amine n-oxide.But the amount of the oxidation amido that exists in the polyamine oxide polymer can change by suitable copolymerization or the N-oxidation by appropriateness.The ratio of preferred amines and amine n-oxide is 2: 3 to 1: 1000000.More preferably 1: 4 to 1: 1000000, most preferably from 1: 7 to 1: 1000000.Polymkeric substance of the present invention is actual to be comprised random or segmented copolymer, and wherein a kind of monomer type is an amine n-oxide, and another kind of monomer type can be that amine n-oxide can not be yet.The amine oxide unit of described polyamine N-oxide has＜and 10, preferred＜7, pKa more preferably＜6.

Can obtain the almost polyamine oxide compound of any extent of polymerization.The polymeric degree is unimportant, as long as this material has required water-soluble and dye suspension ability.

In general, its average molecular weight range is 500 to 1000000; Preferred 1000 to 50000; More preferably 2000 to 30000.Most preferably 3000 to 20000.

B) multipolymer of N-vinyl pyrrolidone and N-vinyl imidazole

Be used for N-vinyl imidazole of the present invention and N-vinylpyrrolidone copolymers and have 5000 to 1000000, preferred 5000 to 200000 molecular-weight average.

Be used for comprising the polymkeric substance that is selected from N-vinyl imidazole and N-vinylpyrrolidone copolymer that described polymkeric substance has 5000 to 50000, more preferably 8000 to 30000,10000 to 20000 molecular-weight average most preferably according to the highly preferred polymkeric substance of detergent composition of the present invention.

Described average molecular weight range such as Barth H.G. and Mays J.W. pass through light scattering determining described in ChemicalAnalysis the 113rd volume " Modem Methods of Polymer Characterization ".

Highly preferred N-vinyl imidazole and N-vinylpyrrolidone copolymers have 5000 to 50000, more preferably 8000 to 30000,10000 to 20000 molecular-weight average most preferably.

N-vinyl imidazole and N-vinylpyrrolidone copolymers with described mean molecule measure feature provide excellent dye metastasis inhibition performance, simultaneously can negative impact with the clean-up performance of the detergent composition of its preparation.

N-vinyl imidazole of the present invention and N-vinylpyrrolidone copolymer have 1 to 0.2, more preferably 0.8 to 0.3, most preferably 0.6 to 0.4 the N-vinyl imidazole and the molar ratio of N-vinyl pyrrolidone.

C) Polyvinylpyrolidone (PVP)

Detergent composition of the present invention also can use has about 2500 to about 400000, preferred about 5000 to about 200000, more preferably from about 5000 Polyvinylpyrolidone (PVP)s (" PVP ") to about molecular-weight average of 50000, most preferably from about 5000 to about 15000.The Polyvinylpyrolidone (PVP) that is suitable for is can be from New York, the Polyvinylpyrolidone (PVP) that the ISP Corporation in NY and Canadian Montreal buys with the trade(brand)name of PVP K-15 (10000 viscosity molecular weight), PVP K-30 (40000 molecular-weight average), PVP K-60 (160000 molecular-weight average) and PVP K-90 (360000 molecular-weight average).What other was suitable for can comprise Sokalan HP 165 and Sokalan HP12 available from the Polyvinylpyrolidone (PVP) of BASFCooperation; The Polyvinylpyrolidone (PVP) of being familiar with for the detergent applications technician (referring to for example EP-A-262897 and EP-A-256696).

D) Ju Yi Xi oxazolidinone

Detergent composition of the present invention also can use Ju Yi Xi oxazolidinone as the polymeric dye transfer inhibitor.Described Ju Yi Xi oxazolidinone has about 2500 and arrives about 400000, preferred about 5000 to about 200000, more preferably from about 5000 to about molecular-weight average of 50000, most preferably from about 5000 to about 15000.

E) polyvinyl imidazol:

Detergent composition of the present invention also can use polyvinyl imidazol as the polymeric dye transfer inhibitor.Described polyvinyl imidazol has about 2500 and arrives about 400000, preferred about 5000 to about 200000, more preferably from about 5000 to about molecular-weight average of 50000, most preferably from about 5000 to about 15000.

F) crosslinked polymkeric substance:

Cross-linked polymer is that its skeleton is interconnected to polymkeric substance to a certain degree; These connections can be that chemical property also can be a physical properties, may have the active group in skeleton or the branch; Cross-linked polymer has been described in 22 of Journal of Polymer Science and has rolled up 1035 to 1039 pages.In one embodiment, cross-linked polymer is prepared to three-dimensional rigid structure, its can be in the hole that three-dimensional structure forms the double team dyestuff.In another embodiment, described cross-linked polymer is by swelling double team dyestuff.This cross-linked polymer is described in the patent application 94870213.9 of while pending trial.

Washing methods

Composition of the present invention can adopt any washing or cleaning method basically, comprises pickling process, method for pretreating and has the rinse step method of (can add independent rinse aid composition).

Method described in this comprises fabric, tableware or any crust is contacted with cleaning soln in common and following illustrational mode.

Method of the present invention is carried out in cleaning course easily.Described cleaning method is preferably under 5-95 ℃, particularly carry out between 10-60 ℃.The pH of treatment soln is preferably 7 to 12.

A kind of preferred tableware machine washing method comprises with wherein dissolving or having disperseed the tableware machine cleaning composition of significant quantity or the water liquid of rinse composition to handle band dirt product.The significant quantity of tableware machine cleaning composition is meant that 8 to 60 gram products are dissolved or dispersed in 3 to 10 liters the wash volumes.According to tableware hand washing method, contact with the dish washing detergent of dirty tableware with the significant quantity of general 0.5 to 20 gram (25 bowl dish of every processing).Preferred tableware hand washing method comprises that the strong solution with described detergent composition is applied to bowl dish surface or the bowl dish is immersed in the large volume dilute solution of described detergent composition.

The following examples are used to illustrate composition of the present invention, but and do not mean that restriction or limit scope of the present invention.

Unless add explanation in addition, in described detergent composition, enzyme level is represented as the weight ratio that pure enzyme accounts for total composition, and detergent ingredients is represented with the weight ratio that accounts for total composition.The component title of abridging in this has following meaning:

LAS: linear C _11-13Sodium alkyl benzene sulfonate;

TAS: tallow sodium alkyl sulfate;

CxyAS:C _1x-C _1ySodium alkyl sulfate;

CxySAS:C _1x-C _1ySecondary (2,3) sodium alkyl sulfate;

CxyEz: with the C of average z mole oxygen ethene condensation _1x-C _1yBe mainly linear primary alconol;

CxyEzS: with the C of average z mole oxygen ethene condensation _1x-C _1ySodium alkyl sulfate;

QAS:R ₂N ⁺(CH ₃) ₂(C ₂H ₄OH), its R ₂Be C ₁₂-C ₁₄

QAS1:R ₂N ⁺(CH ₃) ₂(C ₂H ₄OH), its R ₂Be C ₈-C ₁₁

APA:C _8-10Amido propyl group dimethylamine;

Soap: the linear alkyl carboxylic acid sodium that comes from the mixture of 80/20 tallow and fatty acid distribution of coconut oil;

Nonionic: the C of the ethoxylation degree of tool average 3.8 and average 4.5 propoxylation degree ₁₃-C ₁₅The blended ethoxylated/propoxylated fatty alcohol;

Neodol 45-13: by the C of Shell Chemical Co. sale ₁₄-C ₁₅The linear primary alcohol ethoxylate;

STS: toluenesulfonic acid sodium salt;

CFAA:C ₁₂-C ₁₄Alkyl N-methyl glucose amide;

TFAA:C ₁₆-C ₁₈Alkyl N-methyl glucose amide;

TPKFA:C ₁₂-C ₁₄The full cut lipid acid of topping;

Silicate: amorphous sodium silicate (SiO ₂: Na ₂The O ratio is 1.6 to 3.2);

Silicate (Metasilicate): water glass (SiO ₂: Na ₂The O ratio is 1.0);

Zeolite A: primary particle diameter is 0.1 to 10 micron formula Na ₁₂(AlO ₂SiO ₂) ₁₂.27H ₂The hydrated sodium aluminosilicate of O (weight is represented by anhydrous situation).

Na-SKS-6: formula δ-Na ₂Si ₂O ₅Crystalline layered silicate;

Citrate trianion: the activity of size distribution between 425 to 850 microns is 86.4% citrate trisodium dihydrate;

Citric acid: Citric Acid, usp, Anhydrous Powder;

Borate: Sodium Tetraborate;

Carbonate: the anhydrous sodium carbonate of particle diameter between 200 to 900 microns;

Supercarbonate: the anhydrous sodium bicarbonate of size distribution between 400 to 1200 microns;

Vitriol: anhydrous sodium sulphate;

Sal epsom: anhydrous magnesium sulfate;

STPP: tripoly phosphate sodium STPP;

TSPP: tetrasodium pyrophosphate;

MA/AA: molecular-weight average is 4: 1 acrylate/maleate random copolymers of about 70000 to 80000;

MA/AA1: molecular-weight average is 6: 4 acrylate/maleate random copolymers of about 10000;

AA: molecular-weight average is about 4500 polyacrylic acid sodium polymer;

PA30: the polyacrylic acid of molecular-weight average between 4500 to 8000;

480N: 7: the 3 acrylate/methacrylate random copolymers of molecular-weight average about 3500;

Polygel/Carbopol: high molecular weight crosslinked polyacrylic ester;

PB1: rational formula NaBO ₂.H ₂O ₂The anhydride of sodium perborate monohydrate;

PB4: rational formula NaBO ₂.3H ₂O.H ₂O ₂Four hydrated sodium perborates;

Percarbonate: rational formula 2Na ₂CO ₃.3H ₂O ₂Anhydrous SPC-D;

NaDCC: dichloroisocyanuric acid sodium;

TAED: tetra acetyl ethylene diamine;

NOBS: the nonanoly acyloxy benzene sulfonate of sodium-salt form;

The amino caproyl of NACA-OBS:(6-nonanoyl) oxygen benzene sulfonate;

DTPA: diethylene triaminepentaacetic acid(DTPA);

HEDP:1,1-hydroxyl ethane di 2 ethylhexyl phosphonic acid;

DETPMP: five (methylene radical) phosphonic acids diethyl triamine salt of introducing to the market with the trade(brand)name of Dequest2060 by Monsanto;

EDDS: the quadrol-N of sodium-salt form, N '-disuccinic acid, (S, S) isomer;

MnTACN:1,4,7-trimethylammonium-1,4,7-7-triazacyclononane manganese;

Photoactivation SYNTHETIC OPTICAL WHITNER: be encapsulated in the sulfonated zinc phthalocyanine in the dextrin soluble polymer;

Photoactivation SYNTHETIC OPTICAL WHITNER 1: be encapsulated in the sulfonated phthalocyanine aluminium in the dextrin soluble polymer;

PAAC: acetate five amine cobalt (III) salt;

Paraffin: by the paraffin oil of Wintershall with the trade(brand)name sale of Winog 70;

NaBz: Sodium Benzoate;

Xyloglucanase enzymes: described in U.S. Patent application series SN60/045826 number of pending trial when submitting on May 5th, 1997 and WO94/14953 to the special endoglucanase that is called EGII of xyloglucan.

Mannase: come from Bacillus agaradherens, the mannase of NCIMB 40482;

Proteolytic enzyme: proteolytic ferment of selling with the trade(brand)name of Savinase, Alcalase and Durazym by Novo Nordisk A/S and the proteolytic ferment of selling with Maxacal, Maxapem by Gist-Brocades and be described in patent WO91/06637 and/or WO95/10591 and/or EP251446 in proteolytic enzyme;

Amylase: be described in WO94/18314, WO96/05295 by Genercor with PurafactOx Am ^The starch lyase sold of trade(brand)name; Can be available from the Termamyl of Novo Nordisk A/S ^, Fungamyl ^And Duramyl ^With the amylase described in the WO95/26397;

Lipase: the lipolytic enzyme that lipolytic enzyme that Novo Nordisk A/S sells with the trade(brand)name of Lipolase, Lipolase Ultra and Gist-Brocades sell with the trade(brand)name of Lipomax;

Polygalacturonase: the pectin degrading enzyme that described in the Agr.Biol.Chem.285-293 page or leaf in 1972 36 (2), produces by bacillus P-4-N;

Cellulase: the cellulolytic enzyme that Novo Nordisk A/S sells with the trade(brand)name of Carezyme, Celluzyme and/or Endolase;

CMC: Xylo-Mucine;

PVP: molecular-weight average is 60000 polyethylene polymer;

PVNO: molecular-weight average is polyvinylpyridine-N-oxide compound of 50000;

PVPVI: molecular-weight average is 20000 vinyl imidazole and vinylpyrrolidone copolymers;

Brightener 1:4,4 '-two (2-sulfo group styryl) biphenyl disodium;

Brightener 2:4,4 '-two (4-anilino-6-morpholino (morpholino)-1,3,5-triazines-2-yl) stilbene-2,2 '-disulfonic acid disodium;

Silicone antifoam agent: with the polydimethylsiloxane Foam Control of siloxanes-oxyalkylene copolymers as dispersion agent, the ratio of described Foam Control and described dispersion agent is 10: 1 to 100: 1;

Suds suppressor: 12% siloxanes/silica, 18% stearyl alcohol, 70% particle form starch;

Opalizer: by the water base single styrene latex mixture of BASF Aktiengesellschaft with the trade(brand)name sale of Lytron 621;

SRP1: the end capped polyester of negatively charged ion;

SRP2: the short block polymer of diethoxyization poly-(terephthalic acid 1,2-propylene glycol ester);

QEA: two ((C ₂H ₅O) (C ₂H ₄O) _n(CH ₃)-N ⁺-C ₆H ₁₂-N ⁺-(CH ₃) two ((C ₂H ₅O)-(C ₂H ₄O)) _n, wherein n is 20 to 30;

PEI: molecular-weight average is 1800 and the polymine of the average degree of ethoxylation of 7 ethylene oxy residues of each nitrogen;

SCS: cumene sodium sulfonate;

HMWPEO: high molecular polyoxyethylene;

PEGx: molecular weight is the polyoxyethylene glycol of x;

PEO: molecular-weight average is 5000 polyoxyethylene;

TEPAE: tetren ethoxylate.

BTA: benzotriazole

Silica dental abrasive material: the precipitated silica that is accredited as Zeodent 119 that provides by J.M.Huber;

Carboxy vinyl polymer: the Carbopol that provides by B.F.Goodrich Chemical Company;

Carrageenin: the lota carrageenin that provides by Hercules Chemical Company;

PH: under 20 ℃, measure with 1% distilled water solution.

Embodiment 1

Prepare following high-density cleaning compositions according to the present invention:

	??I	??II	??III	??IV	??V	??VI
	??I	??II	??III	??IV	??V	??VI	??LAS	??8.0	??8.0	??8.0	??2.0	??6.0	??6.0
??TAS	??-	??0.5	??-	??0.5	??1.0	??0.1	??LAS	??8.0	??8.0	??8.0	??2.0	??6.0	??6.0
??TAS	??-	??0.5	??-	??0.5	??1.0	??0.1	??C46(S)AS	??2.0	??2.5	??-	??-	??-	??-
??C25AS	??-	??-	??-	??7.0	??4.5	??5.5	??C46(S)AS	??2.0	??2.5	??-	??-	??-	??-
??C25AS	??-	??-	??-	??7.0	??4.5	??5.5	??C68AS	??2.0	??5.0	??7.0	??-	??-	??-
??C25E5	??-	??-	??3.4	??10.0	??4.6	??4.6	??C68AS	??2.0	??5.0	??7.0	??-	??-	??-
??C25E5	??-	??-	??3.4	??10.0	??4.6	??4.6	??C25E7	??3.4	??3.4	??1.0	??-	??-	??-
??C25E3S	??-	??-	??-	??2.0	??5.0	??4.5	??C25E7	??3.4	??3.4	??1.0	??-	??-	??-
??C25E3S	??-	??-	??-	??2.0	??5.0	??4.5	??QAS	??-	??0.8	??-	??-	??-	??-
??QAS1	??-	??-	??-	??0.8	??0.5	??1.0	??QAS	??-	??0.8	??-	??-	??-	??-
??QAS1	??-	??-	??-	??0.8	??0.5	??1.0	Zeolite A	??18.1	??18.0	??14.1	??18.1	??20.0	??18.1
Citric acid	??-	??-	??-	??2.5	??-	??2.5	Zeolite A	??18.1	??18.0	??14.1	??18.1	??20.0	??18.1
Citric acid	??-	??-	??-	??2.5	??-	??2.5	Carbonate	??13.0	??13.0	??27.0	??10.0	??10.0	??13.0
???Na-SKS-6	??-	??-	??-	??10.0	??-	??10.0	Carbonate	??13.0	??13.0	??27.0	??10.0	??10.0	??13.0
???Na-SKS-6	??-	??-	??-	??10.0	??-	??10.0	Silicate	??1.4	??1.4	??3.0	??0.3	??0.5	??0.3
Citrate trianion	??-	??1.0	??-	??3.0	??-	??-	Silicate	??1.4	??1.4	??3.0	??0.3	??0.5	??0.3
Citrate trianion	??-	??1.0	??-	??3.0	??-	??-	Vitriol	??26.1	??26.1	??26.1	??6.0	??-	??-
Sal epsom	??0.3	??-	??-	??0.2	??-	??0.2	Vitriol	??26.1	??26.1	??26.1	??6.0	??-	??-
Sal epsom	??0.3	??-	??-	??0.2	??-	??0.2	??MA/AA	??0.3	??0.3	??0.3	??4.0	??1.0	??1.0
??CMC	??0.2	??0.2	??0.2	??0.2	??0.4	??0.4	??MA/AA	??0.3	??0.3	??0.3	??4.0	??1.0	??1.0
??CMC	??0.2	??0.2	??0.2	??0.2	??0.4	??0.4	??PB4	??9.0	??9.0	??5.0	??-	??-	??-
Percarbonate	??-	??-	??-	??-	??18.0	??18.0	??PB4	??9.0	??9.0	??5.0	??-	??-	??-
Percarbonate	??-	??-	??-	??-	??18.0	??18.0	??TAED	??1.5	??0.4	??1.5	??-	??3.9	??4.2

NACA-OBS	-	2.0	1.0	-	-	-
NACA-OBS	-	2.0	1.0	-	-	-	DETPMP	0.25	0.25	0.25	0.25	-	-
SRP1	-	-	-	0.2	-	0.2	DETPMP	0.25	0.25	0.25	0.25	-	-
SRP1	-	-	-	0.2	-	0.2	EDDS	-	0.25	0.4	-	0.5	0.5
CFAA	-	1.0	-	2.0	-	-	EDDS	-	0.25	0.4	-	0.5	0.5
CFAA	-	1.0	-	2.0	-	-	HEDP	0.3	0.3	0.3	0.3	0.4	0.4
QEA	-	-	-	0.2	-	0.5	HEDP	0.3	0.3	0.3	0.3	0.4	0.4
QEA	-	-	-	0.2	-	0.5	Mannase	0.005	0.002	0.001	0.001	0.002	0.001
Polygalacturonase	-	-	-	-	0.001	0.005	Mannase	0.005	0.002	0.001	0.001	0.002	0.001
Polygalacturonase	-	-	-	-	0.001	0.005	Xyloglucanase enzymes	0.001	0.005	-	-	-	-
Proteolytic enzyme	0.009	0.009	0.01	0.04	0.05	0.03	Xyloglucanase enzymes	0.001	0.005	-	-	-	-
Proteolytic enzyme	0.009	0.009	0.01	0.04	0.05	0.03	Amylase	0.002	0.002	0.002	0.006	0.008	0.008
Cellulase	0.0007	-	-	0.0007	0.0007	-	Amylase	0.002	0.002	0.002	0.006	0.008	0.008
Cellulase	0.0007	-	-	0.0007	0.0007	-	Lipase	0.006	-	-	0.01	0.01	0.01
Photoactivation SYNTHETIC OPTICAL WHITNER (ppm)	15	15	15	-	20	20	Lipase	0.006	-	-	0.01	0.01	0.01
Photoactivation SYNTHETIC OPTICAL WHITNER (ppm)	15	15	15	-	20	20	PVNO/PVPVI	-	-	-	0.1	-	-
Brightener 1	0.09	0.09	0.09	-	0.09	0.09	PVNO/PVPVI	-	-	-	0.1	-	-
Brightener 1	0.09	0.09	0.09	-	0.09	0.09	Spices	0.3	0.3	0.3	0.4	0.4	0.4
Silicone antifoam agent	0.5	0.5	0.5	-	0.3	0.3	Spices	0.3	0.3	0.3	0.4	0.4	0.4
Silicone antifoam agent	0.5	0.5	0.5	-	0.3	0.3	Density, g/l	850	850	850	850	850	850
Miscellaneous and minor component	To 100%						Density, g/l	850	850	850	850	850	850

Embodiment 2

Granular laundry detergent composition below specifically under European washing machine wash conditions, using according to the present invention preparation:

	??I	??II	??III	??IV	??V	??VI
	??I	??II	??III	??IV	??V	??VI	??LAS	??5.5	??7.5	??5.0	??5.0	??6.0	??7.0
??TAS	??1.25	??1.9	??-	??0.8	??0.4	??0.3	??LAS	??5.5	??7.5	??5.0	??5.0	??6.0	??7.0
??TAS	??1.25	??1.9	??-	??0.8	??0.4	??0.3	??C24AS/C25AS	??-	??2.2	??5.0	??5.0	??5.0	??2.2
??C25E3S	??-	??0.8	??1.0	??1.5	??3.0	??1.0	??C24AS/C25AS	??-	??2.2	??5.0	??5.0	??5.0	??2.2
??C25E3S	??-	??0.8	??1.0	??1.5	??3.0	??1.0	??C45E7	??3.25	??-	??-	??-	??-	??3.0
??TFAA	??-	??-	??2.0	??-	??-	??-	??C45E7	??3.25	??-	??-	??-	??-	??3.0
??TFAA	??-	??-	??2.0	??-	??-	??-	??C25E5	??-	??5.5	??-	??-	??-	??-
??QAS	??0.8	??-	??-	??-	??-	??-	??C25E5	??-	??5.5	??-	??-	??-	??-
??QAS	??0.8	??-	??-	??-	??-	??-	??QAS1	??-	??0.7	??1.0	??0.5	??1.0	??0.7
??STPP	??19.7	??-	??-	??-	??-	??-	??QAS1	??-	??0.7	??1.0	??0.5	??1.0	??0.7
??STPP	??19.7	??-	??-	??-	??-	??-	Zeolite A	??-	??19.5	??25.0	??19.5	??20.0	??17.0
NaSKS-6/ citric acid (79: 21)	??-	??10.6	??-	??10.6	??-	??-	Zeolite A	??-	??19.5	??25.0	??19.5	??20.0	??17.0
NaSKS-6/ citric acid (79: 21)	??-	??10.6	??-	??10.6	??-	??-	??Na-SKS-6	??-	??-	??9.0	??-	??10.0	??10.0
Carbonate	??6.1	??21.4	??9.0	??10.0	??10.0	??18.0	??Na-SKS-6	??-	??-	??9.0	??-	??10.0	??10.0
Carbonate	??6.1	??21.4	??9.0	??10.0	??10.0	??18.0	Supercarbonate	??-	??2.0	??7.0	??5.0	??-	??2.0
Silicate	??6.8	??-	??-	??0.3	??0.5	??-	Supercarbonate	??-	??2.0	??7.0	??5.0	??-	??2.0
Silicate	??6.8	??-	??-	??0.3	??0.5	??-	Citrate trianion	??-	??-	??4.0	??4.0	??-	??-
Vitriol	??39.8	??-	??-	??5.0	??-	??12.0	Citrate trianion	??-	??-	??4.0	??4.0	??-	??-
Vitriol	??39.8	??-	??-	??5.0	??-	??12.0	Sal epsom	??-	??-	??0.1	??0.2	??0.2	??-
??MA/AA	??0.5	??1.6	??3.0	??4.0	??1.0	??1.0	Sal epsom	??-	??-	??0.1	??0.2	??0.2	??-
??MA/AA	??0.5	??1.6	??3.0	??4.0	??1.0	??1.0	??CMC	??0.2	??0.4	??1.0	??1.0	??0.4	??0.4
??PB4	??5.0	??12.7	??-	??-	??-	??-	??CMC	??0.2	??0.4	??1.0	??1.0	??0.4	??0.4
??PB4	??5.0	??12.7	??-	??-	??-	??-	Percarbonate	??-	??-	??-	??-	??18.0	??15.0
?TAED	??0.5	??3.1	??-	??-	??5.0	??-	Percarbonate	??-	??-	??-	??-	??18.0	??15.0
?TAED	??0.5	??3.1	??-	??-	??5.0	??-	?NACA-OBS	??1.0	??3.5	??-	??-	??-	??2.5

DETPMP	0.25	0.2	0.3	0.4	-	0.2
DETPMP	0.25	0.2	0.3	0.4	-	0.2	HEDP	-	0.3	-	0.3	0.3	0.3
QEA	-	-	1.0	1.0	1.0	-	HEDP	-	0.3	-	0.3	0.3	0.3
QEA	-	-	1.0	1.0	1.0	-	Mannase	0.005	0.002	0.008	0.005	0.002	0.001
Proteolytic enzyme	0.009	0.03	0.03	0.05	0.05	0.02	Mannase	0.005	0.002	0.008	0.005	0.002	0.001
Proteolytic enzyme	0.009	0.03	0.03	0.05	0.05	0.02	Lipase	0.003	0.003	0.006	0.006	0.006	0.004
Cellulase	0.0006	0.0006	0.0005	-	-	0.0007	Lipase	0.003	0.003	0.006	0.006	0.006	0.004
Cellulase	0.0006	0.0006	0.0005	-	-	0.0007	Amylase	0.002	0.002	0.006	0.006	0.01	0.003
PVNO/PVPVI	-	-	0.2	0.2	-	-	Amylase	0.002	0.002	0.006	0.006	0.01	0.003
PVNO/PVPVI	-	-	0.2	0.2	-	-	PVP	0.9	1.3	-	-	-	0.9
SRP1	-	-	0.2	0.2	0.2	-	PVP	0.9	1.3	-	-	-	0.9
SRP1	-	-	0.2	0.2	0.2	-	Photoactivation SYNTHETIC OPTICAL WHITNER (ppm)	15	27	-	-	20	20
Photoactivation SYNTHETIC OPTICAL WHITNER 1 (ppm)	15	-	-	-	-	-	Photoactivation SYNTHETIC OPTICAL WHITNER (ppm)	15	27	-	-	20	20
Photoactivation SYNTHETIC OPTICAL WHITNER 1 (ppm)	15	-	-	-	-	-	Brightener 1	0.08	0.2	-	-	0.09	0.15
Brightener 2	-	0.04	-	-	-	-	Brightener 1	0.08	0.2	-	-	0.09	0.15
Brightener 2	-	0.04	-	-	-	-	Spices	0.3	0.5	0.4	0.3	0.4	0.3
Silicone antifoam agent	0.5	2.4	0.3	0.5	0.3	2.0	Spices	0.3	0.5	0.4	0.3	0.4	0.3
Silicone antifoam agent	0.5	2.4	0.3	0.5	0.3	2.0	Density, g/l	750	750	750	750	750	750
Miscellaneous and minor component	To 100%						Density, g/l	750	750	750	750	750	750

Embodiment 3

Detergent composition below specifically under European washing machine wash conditions, using according to the present invention preparation:

	??I		??II	??III	??IV
	??I		??II	??III	??IV	The blowing powder
??LAS	??6.0		??5.0	??11.0	??6.0	The blowing powder
??LAS	??6.0		??5.0	??11.0	??6.0	??TAS	??2.0		??-	??-	??2.0
Zeolite A	??24.0		??-	??-	??20.0	??TAS	??2.0		??-	??-	??2.0
Zeolite A	??24.0		??-	??-	??20.0	??STPP	??-		??27.0	??24.0
Vitriol	??4.0		??6.0	??13.0	??-	??STPP	??-		??27.0	??24.0
Vitriol	??4.0		??6.0	??13.0	??-	??MA/AA	??1.0		??4.0	??6.0	??2.0
Silicate	??1.0		??7.0	??3.0	??3.0	??MA/AA	??1.0		??4.0	??6.0	??2.0
Silicate	??1.0		??7.0	??3.0	??3.0	??CMC	??1.0		??1.0	??0.5	??0.6
Brightener 1	??0.2		??0.2	??0.2	??0.2	??CMC	??1.0		??1.0	??0.5	??0.6
Brightener 1	??0.2		??0.2	??0.2	??0.2	Silicone antifoam agent	??1.0		??1.0	??1.0	??0.3
??DETPMP	??0.4		??0.4	??0.2	??0.4	Silicone antifoam agent	??1.0		??1.0	??1.0	??0.3
??DETPMP	??0.4		??0.4	??0.2	??0.4	Spraying
Brightener	??0.02		??-	??-	??0.02	Spraying
Brightener	??0.02		??-	??-	??0.02	??C45E7	??-		??-	??-	??5.0
??C45E2	??2.5		??2.5	??2.0	??-	??C45E7	??-		??-	??-	??5.0
??C45E2	??2.5		??2.5	??2.0	??-	??C45E3	??2.6		??2.5	??2.0	??-
Spices	??0.5		??0.3	??0.5	??0.2	??C45E3	??2.6		??2.5	??2.0	??-
Spices	??0.5		??0.3	??0.5	??0.2	Silicone antifoam agent	??0.3		??0.3	??0.3	??-
Dried additive						Silicone antifoam agent	??0.3		??0.3	??0.3	??-
Dried additive						??QEA		??-	??-	??-	??1.0
??EDDS		??0.3	??-	??-	??-	??QEA		??-	??-	??-	??1.0
??EDDS		??0.3	??-	??-	??-	Vitriol		??2.0	??3.0	??5.0	??10.0
Carbonate		??6.0	??13.0	??15.0	??14.0	Vitriol		??2.0	??3.0	??5.0	??10.0
Carbonate		??6.0	??13.0	??15.0	??14.0	Citric acid		??2.5	??-	??-	??2.0

QAS1	0.5	-	-	0.5
QAS1	0.5	-	-	0.5	Na-SKS-6	10.0	-	-	-
Percarbonate	18.5	-	-	-	Na-SKS-6	10.0	-	-	-
Percarbonate	18.5	-	-	-	PB4	-	18.0	10.0	21.5
TAED	2.0	2.0	-	2.0	PB4	-	18.0	10.0	21.5
TAED	2.0	2.0	-	2.0	NACA-OBS	3.0	2.0	4.0	-
Mannase	0.005	0.002	0.0008	0.001	NACA-OBS	3.0	2.0	4.0	-
Mannase	0.005	0.002	0.0008	0.001	Cellulase	0.005	-	0.005	-
Xyloglucanase enzymes	0.001	0.003	-	-	Cellulase	0.005	-	0.005	-
Xyloglucanase enzymes	0.001	0.003	-	-	Proteolytic enzyme	0.03	0.03	0.03	0.03
Lipase	0.008	0.008	0.008	0.004	Proteolytic enzyme	0.03	0.03	0.03	0.03
Lipase	0.008	0.008	0.008	0.004	Amylase	0.003	0.003	0.003	0.006
Brightener	0.05	-	-	0.05	Amylase	0.003	0.003	0.003	0.006
Brightener	0.05	-	-	0.05	Miscellaneous and minor component	To 100%

Embodiment 4

Prepare following granular detergent composition according to the present invention:

	??I	??II	??III	??IV	??V	??VI
	??I	??II	??III	??IV	??V	??VI	The blowing powder
??LAS	??23.0	??8.0	??7.0	??9.0	??7.0	??7.0	The blowing powder
??LAS	??23.0	??8.0	??7.0	??9.0	??7.0	??7.0	??TAS	??-	??-	??-	??-	??1.0	??-
??C45AS	??6.0	??6.0	??5.0	??8.0	??-	??-	??TAS	??-	??-	??-	??-	??1.0	??-
??C45AS	??6.0	??6.0	??5.0	??8.0	??-	??-	??C45AE3	??-	??1.0	??1.0	??1.0	??-	??-
??C45E35	??-	??-	??-	??-	??2.0	??4.0	??C45AE3	??-	??1.0	??1.0	??1.0	??-	??-
??C45E35	??-	??-	??-	??-	??2.0	??4.0	Zeolite A	??10.0	??18.0	??14.0	??12.0	??10.0	??10.0
??MA/AA	??-	??0.5	??-	??-	??-	??2.0	Zeolite A	??10.0	??18.0	??14.0	??12.0	??10.0	??10.0
??MA/AA	??-	??0.5	??-	??-	??-	??2.0	??MA/AA1	??7.0	??-	??-	???-	??-	??-
??AA	??-	??3.0	??3.0	??2.0	??3.0	??3.0	??MA/AA1	??7.0	??-	??-	???-	??-	??-
??AA	??-	??3.0	??3.0	??2.0	??3.0	??3.0	Vitriol	??5.0	??6.3	??14.3	??11.0	??15.0	??19.3

Silicate	10.0		1.0	1.0	1.0	1.0		1.0
Silicate	10.0		1.0	1.0	1.0	1.0		1.0	Carbonate	15.0		20.0	10.0	20.7	8.0		6.0
PEG4000	0.4		1.5	1.5	1.0	1.0		1.0	Carbonate	15.0		20.0	10.0	20.7	8.0		6.0
PEG4000	0.4		1.5	1.5	1.0	1.0		1.0	DTPA	-		0.9	0.5	-	-		0.5
Brightener 2	0.3		0.2	0.3	-	0.1		0.3	DTPA	-		0.9	0.5	-	-		0.5
Brightener 2	0.3		0.2	0.3	-	0.1		0.3	Spraying
C45E7	-		2.0	-	-	2.0		2.0	Spraying
C45E7	-		2.0	-	-	2.0		2.0	C25E9	3.0		-	-	-	-		-
C23E9	-		-	1.5	2.0	-		2.0	C25E9	3.0		-	-	-	-		-
C23E9	-		-	1.5	2.0	-		2.0	Spices	0.3		0.3	0.3	2.0	0.3		0.3
Agglomerate									Spices	0.3		0.3	0.3	2.0	0.3		0.3
Agglomerate									C45AS	-		5.0	5.0	2.0	-		5.0
LAS	-		2.0	2.0	-	-		2.0	C45AS	-		5.0	5.0	2.0	-		5.0
LAS	-		2.0	2.0	-	-		2.0	Zeolite A	-		7.5	7.5	8.0	-		7.5
Carbonate	-		4.0	4.0	5.0	-		4.0	Zeolite A	-		7.5	7.5	8.0	-		7.5
Carbonate	-		4.0	4.0	5.0	-		4.0	PEG4000	-		0.5	0.5	-	-		0.5
Miscellaneous (water etc.)	-		2.0	2.0	2.0	-		2.0	PEG4000	-		0.5	0.5	-	-		0.5
Miscellaneous (water etc.)	-		2.0	2.0	2.0	-		2.0	Dried additive
QAS		-	-	-	-		1.0	-	Dried additive
QAS		-	-	-	-		1.0	-	Citric acid		-	-	-	-		2.0	-
PB4		-	-	-	-		12.0	1.0	Citric acid		-	-	-	-		2.0	-
PB4		-	-	-	-		12.0	1.0	PB1		4.0	1.0	3.0	2.0		-	-
Percarbonate		-	-	-	-		2.0	10.0	PB1		4.0	1.0	3.0	2.0		-	-
Percarbonate		-	-	-	-		2.0	10.0	Carbonate		-	5.3	1.8	-		4.0	4.0
NOBS		4.0	-	6.0	-		-	0.6	Carbonate		-	5.3	1.8	-		4.0	4.0
NOBS		4.0	-	6.0	-		-	0.6	Methylcellulose gum		0.2	-	-	-		-	-
Na-SKS-6		8.0	-	-	-		-	-	Methylcellulose gum		0.2	-	-	-		-	-
Na-SKS-6		8.0	-	-	-		-	-	STS		-	-	2.0	-		1.0	-
Cumene sulfonic acid		-	1.0	-	-		-	2.0	STS		-	-	2.0	-		1.0	-

Mannase	0.005	0.002	0.001	0.008	0.001	0.001
Mannase	0.005	0.002	0.001	0.008	0.001	0.001	Polygalacturonase	-	-	-	-	0.001	0.01
Proteolytic enzyme	0.02	0.02	0.02	0.01	0.02	0.02	Polygalacturonase	-	-	-	-	0.001	0.01
Proteolytic enzyme	0.02	0.02	0.02	0.01	0.02	0.02	Lipase	0.004	-	0.004	-	0.004	0.008
Amylase	0.003	-	0.002	-	0.003	-	Lipase	0.004	-	0.004	-	0.004	0.008
Amylase	0.003	-	0.002	-	0.003	-	Cellulase	0.0005	0.0008	0.0005	0.0005	0.0005	0.0008
PVPVI	-	-	-	-	0.5	0.1	Cellulase	0.0005	0.0008	0.0005	0.0005	0.0005	0.0008
PVPVI	-	-	-	-	0.5	0.1	PVP	-	-	-	-	0.5	-
PVNO	-	-	0.5	0.3	-	-	PVP	-	-	-	-	0.5	-
PVNO	-	-	0.5	0.3	-	-	QEA	-	-	-	-	1.0	-
SRP1	0.2	0.5	0.3	-	0.2	-	QEA	-	-	-	-	1.0	-
SRP1	0.2	0.5	0.3	-	0.2	-	Silicone antifoam agent	0.2	0.4	0.2	0.4	0.1	-
Sal epsom	-	-	0.2	-	0.2	-	Silicone antifoam agent	0.2	0.4	0.2	0.4	0.1	-
Sal epsom	-	-	0.2	-	0.2	-	Miscellaneous and minor component	To 100%

Embodiment 5

According to the present invention preparation specifically be used for washing colored clothes below contain the detergent composition of zero SYNTHETIC OPTICAL WHITNER:

	??I	??II	??III
	??I	??II	??III	The blowing powder
Zeolite A	??15.0	??15.0	-	The blowing powder
Zeolite A	??15.0	??15.0	-	Vitriol	??-	??5.0	-
??LAS	??3.0	??3.0	-	Vitriol	??-	??5.0	-
??LAS	??3.0	??3.0	-	??DETPMP	??0.4	??0.5	-
??CMC	??0.4	??0.4	-	??DETPMP	??0.4	??0.5	-
??CMC	??0.4	??0.4	-	?MA/AA	??4.0	??4.0	-
Agglomerate				?MA/AA	??4.0	??4.0	-

C45AS	-	-	11.0
C45AS	-	-	11.0	LAS	6.0	5.0	-
TAS	3.0	2.0	-	LAS	6.0	5.0	-
TAS	3.0	2.0	-	Silicate	4.0	4.0	-
Zeolite A	10.0	15.0	13.0	Silicate	4.0	4.0	-
Zeolite A	10.0	15.0	13.0	CMC	-	-	0.5
MA/AA	-	-	2.0	CMC	-	-	0.5
MA/AA	-	-	2.0	Carbonate	9.0	7.0	7.0
Spraying				Carbonate	9.0	7.0	7.0
Spraying				Spices	0.3	0.3	0.5
C45E7	4.0	4.0	4.0	Spices	0.3	0.3	0.5
C45E7	4.0	4.0	4.0	C25E3	2.0	2.0	2.0
Dried additive				C25E3	2.0	2.0	2.0
Dried additive				MA/AA	-	-	3.0
Na-SKS-6	-	-	12.0	MA/AA	-	-	3.0
Na-SKS-6	-	-	12.0	Citric acid	10.0	-	8.0
Supercarbonate	7.0	3.0	5.0	Citric acid	10.0	-	8.0
Supercarbonate	7.0	3.0	5.0	Carbonate	8.0	5.0	7.0
PVPVI/PVNO	0.5	0.5	0.5	Carbonate	8.0	5.0	7.0
PVPVI/PVNO	0.5	0.5	0.5	Mannase	0.0008	0.0005	0.01
Proteolytic enzyme	0.03	0.02	0.05	Mannase	0.0008	0.0005	0.01
Proteolytic enzyme	0.03	0.02	0.05	Lipase	0.008	0.008	0.008
Amylase	0.01	0.01	0.01	Lipase	0.008	0.008	0.008
Amylase	0.01	0.01	0.01	Cellulase	0.001	0.001	0.001
Silicone antifoam agent	5.0	5.0	5.0	Cellulase	0.001	0.001	0.001
Silicone antifoam agent	5.0	5.0	5.0	Vitriol	-	9.0	-
Density (g/l)	700	700	700	Vitriol	-	9.0	-
Density (g/l)	700	700	700	Miscellaneous and minor component	To 100%

Embodiment 6

Prepare following detergent composition according to the present invention:

	??I	??II	??III	??IV
	??I	??II	??III	??IV	Base particle
Zeolite A	??30.0	??22.0	??24.0	??10.0	Base particle
Zeolite A	??30.0	??22.0	??24.0	??10.0	Vitriol	??10.0	??5.0	??10.0	??7.0
??MA/AA	??3.0	??-	??-	??-	Vitriol	??10.0	??5.0	??10.0	??7.0
??MA/AA	??3.0	??-	??-	??-	??AA	??-	??1.6	??2.0	??-
??MA/AA1	??-	??12.0	??-	??6.0	??AA	??-	??1.6	??2.0	??-
??MA/AA1	??-	??12.0	??-	??6.0	??LAS	??14.0	??10.0	??9.0	??20.0
??C45AS	??8.0	??7.0	??9.0	??7.0	??LAS	??14.0	??10.0	??9.0	??20.0
??C45AS	??8.0	??7.0	??9.0	??7.0	??C45AES	??-	??1.0	??1.0	??-
Silicate	??-	??1.0	??0.5	??10.0	??C45AES	??-	??1.0	??1.0	??-
Silicate	??-	??1.0	??0.5	??10.0	Soap	??-	??2.0	??-	??-
Brightener 1	??0.2	??0.2	??0.2	??0.2	Soap	??-	??2.0	??-	??-
Brightener 1	??0.2	??0.2	??0.2	??0.2	Carbonate	??6.0	??9.0	??10.0	??10.0
??PEG?4000	??-	??1.0	??1.5	??-	Carbonate	??6.0	??9.0	??10.0	??10.0
??PEG?4000	??-	??1.0	??1.5	??-	??DTPA	??-	??0.4	??-	??-
Spraying					??DTPA	??-	??0.4	??-	??-
Spraying					??C25E9	??-	??-	??-	??5.0
??C45E7	??1.0	??1.0	??-	??0	??C25E9	??-	??-	??-	??5.0
??C45E7	??1.0	??1.0	??-	??0	??C23E9	??-	??1.0	??2.5	??-
Spices	??0.2	??0.3	??0.3	??-	??C23E9	??-	??1.0	??2.5	??-
Spices	??0.2	??0.3	??0.3	??-	Dried additive
Carbonate	??5.0	??10.0	??18.0	??8.0	Dried additive
Carbonate	??5.0	??10.0	??18.0	??8.0	??PVPVI/PVNO	??0.5	??-	??0.3	??-
Mannase	??0.005	??0.002	??0.0008	??0.001	??PVPVI/PVNO	??0.5	??-	??0.3	??-
Mannase	??0.005	??0.002	??0.0008	??0.001	Proteolytic enzyme	??0.03	??0.03	??0.03	??0.02
Lipase	??0.008	??-	??-	??0.008	Proteolytic enzyme	??0.03	??0.03	??0.03	??0.02

Amylase	0.002	-	-	0.002
Amylase	0.002	-	-	0.002	Cellulase	0.0002	0.0005	0.0005	0.0002
NOBS	-	4.0	-	4.5	Cellulase	0.0002	0.0005	0.0005	0.0002
NOBS	-	4.0	-	4.5	PB1	1.0	5.0	1.5	6.0
Vitriol	4.0	5.0	-	5.0	PB1	1.0	5.0	1.5	6.0
Vitriol	4.0	5.0	-	5.0	SRP1	-	0.4	-	-
Suds suppressor	-	0.5	0.5	-	SRP1	-	0.4	-	-
Suds suppressor	-	0.5	0.5	-	Miscellaneous and minor component	To 100%

Embodiment 7

	??I	??II	??III
	??I	??II	??III	The blowing powder
Zeolite A	??20.0	??-	??15.0	The blowing powder
Zeolite A	??20.0	??-	??15.0	??STPP	??-	??20.0	??-
Vitriol	??-	??-	??5.0	??STPP	??-	??20.0	??-
Vitriol	??-	??-	??5.0	Carbonate	??-	??-	??5.0
??TAS	??-	??-	??1.0	Carbonate	??-	??-	??5.0
??TAS	??-	??-	??1.0	??LAS	??6.0	??6.0	??6.0
??C68AS	??2.0	??2.0	??-	??LAS	??6.0	??6.0	??6.0
??C68AS	??2.0	??2.0	??-	Silicate	??3.0	??8.0	??-
??MA/AA	??4.0	??2.0	??2.0	Silicate	??3.0	??8.0	??-
??MA/AA	??4.0	??2.0	??2.0	??CMC	??0.6	??0.6	??0.2
Brightener 1	??0.2	??0.2	??0.1	??CMC	??0.6	??0.6	??0.2
Brightener 1	??0.2	??0.2	??0.1	??DETPMP	??0.4	??0.4	??0.1
??STS	??-	??-	??1.0	??DETPMP	??0.4	??0.4	??0.1
??STS	??-	??-	??1.0	Spraying
??C45E7	??5.0	??5.0	??4.0	Spraying
??C45E7	??5.0	??5.0	??4.0	Silicone antifoam agent	??0.3	??0.3	??0.1

Spices	0.2	0.2	0.3
Spices	0.2	0.2	0.3	Dried additive
QEA	-	-	1.0	Dried additive
QEA	-	-	1.0	Carbonate	14.0	9.0	10.0
PB1	1.5	2.0	-	Carbonate	14.0	9.0	10.0
PB1	1.5	2.0	-	PB4	18.5	13.0	13.0
TAED	2.0	2.0	2.0	PB4	18.5	13.0	13.0
TAED	2.0	2.0	2.0	QAS	-	-	1.0
The photoactivation SYNTHETIC OPTICAL WHITNER	15ppm	15ppm	15ppm	QAS	-	-	1.0
The photoactivation SYNTHETIC OPTICAL WHITNER	15ppm	15ppm	15ppm	Na-SKS-6	-	-	3.0
Mannosans	0.005	0.002	0.0008	Na-SKS-6	-	-	3.0
Mannosans	0.005	0.002	0.0008	Polygalacturonase	-	0.008	-
Xyloglucanase enzymes	0.008	0.008	0.008	Polygalacturonase	-	0.008	-
Xyloglucanase enzymes	0.008	0.008	0.008	Proteolytic enzyme	0.003	0.003	0.007
Lipase	0.004	0.004	0.004	Proteolytic enzyme	0.003	0.003	0.007
Lipase	0.004	0.004	0.004	Amylase	0.006	0.006	0.003
Cellulase	0.0002	0.0002	0.0005	Amylase	0.006	0.006	0.003
Cellulase	0.0002	0.0002	0.0005	Vitriol	10.0	20.0	5.0
Density (g/l)	700	700	700	Vitriol	10.0	20.0	5.0
Density (g/l)	700	700	700	Miscellaneous and minor component	To 100%

Embodiment 8

Prepare following detergent composition according to the present invention:

	??I	??II	??III
	??I	??II	??III	The blowing powder
Zeolite A	??15.0	??15.0	??15.0	The blowing powder
Zeolite A	??15.0	??15.0	??15.0	Vitriol	??-	??5.0	??-
??LAS	??3.0	??3.0	??3.0	Vitriol	??-	??5.0	??-
??LAS	??3.0	??3.0	??3.0	??QAS	??-	??1.5	??1.5

DETPMP	0.4	0.2	0.4
DETPMP	0.4	0.2	0.4	EDDS	-	0.4	0.2
CMC	0.4	0.4	0.4	EDDS	-	0.4	0.2
CMC	0.4	0.4	0.4	MA/AA	4.0	2.0	2.0
Agglomerate				MA/AA	4.0	2.0	2.0
Agglomerate				LAS	5.0	5.0	5.0
TAS	2.0	2.0	1.0	LAS	5.0	5.0	5.0
TAS	2.0	2.0	1.0	Silicate	3.0	3.0	4.0
Zeolite A	8.0	8.0	8.0	Silicate	3.0	3.0	4.0
Zeolite A	8.0	8.0	8.0	Carbonate	8.0	8.0	4.0
Spraying				Carbonate	8.0	8.0	4.0
Spraying				Spices	0.3	0.3	0.3
C45E7	2.0	2.0	2.0	Spices	0.3	0.3	0.3
C45E7	2.0	2.0	2.0	C25E3	2.0	-	-
Dried additive				C25E3	2.0	-	-
Dried additive				Citrate trianion	5.0	-	2.0
Supercarbonate	-	3.0	-	Citrate trianion	5.0	-	2.0
Supercarbonate	-	3.0	-	Carbonate	8.0	15.0	10.0
TAED	6.0	2.0	5.0	Carbonate	8.0	15.0	10.0
TAED	6.0	2.0	5.0	PB1	14.0	7.0	10.0
PEO	-	-	0.2	PB1	14.0	7.0	10.0
PEO	-	-	0.2	Wilkinite	-	-	10.0
Mannase	0.005	0.002	0.0008	Wilkinite	-	-	10.0
Mannase	0.005	0.002	0.0008	Polygalacturonase	-	0.003	-
Xyloglucanase enzymes	-	-	0.005	Polygalacturonase	-	0.003	-
Xyloglucanase enzymes	-	-	0.005	Proteolytic enzyme	0.03	0.03	0.03
Lipase	0.008	0.008	0.008	Proteolytic enzyme	0.03	0.03	0.03
Lipase	0.008	0.008	0.008	Cellulase	0.001	0.001	0.001
Amylase	0.01	0.01	0.01	Cellulase	0.001	0.001	0.001

Silicone antifoam agent	5.0	5.0	5.0
Silicone antifoam agent	5.0	5.0	5.0	Vitriol	-	3.0	-
Density (g/l)	850	850	850	Vitriol	-	3.0	-
Density (g/l)	850	850	850	Miscellaneous and minor component	To 100%

Embodiment 9

Prepare following detergent composition according to the present invention:

	??I	??II	??III	??IV
	??I	??II	??III	??IV	??LAS	??18.0	??14.0	??24.0	??20.0
??QAS	??0.7	??1.0	??-	??0.7	??LAS	??18.0	??14.0	??24.0	??20.0
??QAS	??0.7	??1.0	??-	??0.7	??TFAA	??-	??1.0	??-	??-
??C23E56.5	??-	??-	??1.0	??-	??TFAA	??-	??1.0	??-	??-
??C23E56.5	??-	??-	??1.0	??-	??C45E7	??-	??1.0	??-	??-
??C45E3S	??1.0	??2.5	??1.0	??-	??C45E7	??-	??1.0	??-	??-
??C45E3S	??1.0	??2.5	??1.0	??-	??STPP	??32.0	??18.0	??30.0	??22.0
Silicate	??9.0	??5.0	??9.0	??8.0	??STPP	??32.0	??18.0	??30.0	??22.0
Silicate	??9.0	??5.0	??9.0	??8.0	Carbonate	??11.0	??7.7	??10.0	??5.0
Supercarbonate	??-	??7.5	??-	??-	Carbonate	??11.0	??7.7	??10.0	??5.0
Supercarbonate	??-	??7.5	??-	??-	??PB1	??3.0	??1.0	??-	??-
??PB4	??-	??1.0	??-	??-	??PB1	??3.0	??1.0	??-	??-
??PB4	??-	??1.0	??-	??-	??NOBS	??2.0	??1.0	??-	??-
??DETPMP	??-	??1.0	??-	??-	??NOBS	??2.0	??1.0	??-	??-
??DETPMP	??-	??1.0	??-	??-	??DTPA	??0.5	??-	??0.2	??0.3
??SRP1	??0.3	??0.2	??-	??0.1	??DTPA	??0.5	??-	??0.2	??0.3
??SRP1	??0.3	??0.2	??-	??0.1	??MA/AA	??1.0	??1.5	??2.0	??0.5
??CMC	??0.8	??0.4	??0.4	??0.2	??MA/AA	??1.0	??1.5	??2.0	??0.5
??CMC	??0.8	??0.4	??0.4	??0.2	??PEI	??-	??-	??0.4	??-
Vitriol	??20.0	??10.0	??20.0	??30.0	??PEI	??-	??-	??0.4	??-
Vitriol	??20.0	??10.0	??20.0	??30.0	Sal epsom	??0.2	??-	??0.4	??0.9

Mannase	0.005	0.002	0.005	0.001
Mannase	0.005	0.002	0.005	0.001	Polygalacturonase	-	0.001	-	0.001
Proteolytic enzyme	0.03	0.03	0.02	0.02	Polygalacturonase	-	0.001	-	0.001
Proteolytic enzyme	0.03	0.03	0.02	0.02	Amylase	0.008	0.007	-	0.004
Cellulase	0.0003	-	0.0003	0.0001	Amylase	0.008	0.007	-	0.004
Cellulase	0.0003	-	0.0003	0.0001	The photoactivation SYNTHETIC OPTICAL WHITNER	30ppm	20ppm	-	10ppm
Spices	0.3	0.3	0.1	0.2	The photoactivation SYNTHETIC OPTICAL WHITNER	30ppm	20ppm	-	10ppm
Spices	0.3	0.3	0.1	0.2	Brightener 1/2	0.05	0.02	0.08	0.1
Miscellaneous and minor component	To 100%				Brightener 1/2	0.05	0.02	0.08	0.1

Embodiment 10

Prepare following liquid detergent preparation (its level is in weight part, and enzyme is in pure enzyme) according to the present invention:

	??I	??II	??III	??IV	??V
	??I	??II	??III	??IV	??V	??LAS	??11.5	??8.8	??-	??3.9	??-
??C25E2.5S	??-	??3.0	??18.0	??-	??16.0	??LAS	??11.5	??8.8	??-	??3.9	??-
??C25E2.5S	??-	??3.0	??18.0	??-	??16.0	??C45E2.25S	??11.5	??3.0	??-	??15.7	??-
??C23E9	??-	??2.7	??1.8	??2.0	??1.0	??C45E2.25S	??11.5	??3.0	??-	??15.7	??-
??C23E9	??-	??2.7	??1.8	??2.0	??1.0	??C23E7	??3.2	??-	??-	??-	??-
??CFAA	??-	??-	??5.2	??-	??3.1	??C23E7	??3.2	??-	??-	??-	??-
??CFAA	??-	??-	??5.2	??-	??3.1	??TPKFA	??1.6	??-	??2.0	??0.5	??2.0
Citric acid (50%)	??6.5	??1.2	??2.5	??4.4	??2.5	??TPKFA	??1.6	??-	??2.0	??0.5	??2.0
Citric acid (50%)	??6.5	??1.2	??2.5	??4.4	??2.5	Calcium formiate	??0.1	??0.06	??0.1	??-	??-
Sodium formiate	??0.5	??0.06	??0.1	??0.05	??0.05	Calcium formiate	??0.1	??0.06	??0.1	??-	??-
Sodium formiate	??0.5	??0.06	??0.1	??0.05	??0.05	??SCS	??4.0	??1.0	??3.0	??1.2	??-
Borate	??0.6	??-	??3.0	??2.0	??2.9	??SCS	??4.0	??1.0	??3.0	??1.2	??-
Borate	??0.6	??-	??3.0	??2.0	??2.9	Sodium hydroxide	??5.8	??2.0	??3.5	??3.7	??2.7
Ethanol	??1.75	??1.0	??3.6	??4.2	??2.9	Sodium hydroxide	??5.8	??2.0	??3.5	??3.7	??2.7
Ethanol	??1.75	??1.0	??3.6	??4.2	??2.9	1, the 2-propylene glycol	??3.3	??2.0	??8.0	??7.9	??5.3

Monoethanolamine	3.0	1.5	1.3	2.5	0.8
Monoethanolamine	3.0	1.5	1.3	2.5	0.8	TEPAE	1.6	-	1.3	1.2	1.2
Mannase	0.005	0.001	0.002	0.0005	0.0002	TEPAE	1.6	-	1.3	1.2	1.2
Mannase	0.005	0.001	0.002	0.0005	0.0002	Polygalacturonase	0.003	0.003	-	-	-
Xyloglucanase enzymes	0.008	0.01	-	0.008	0.005	Polygalacturonase	0.003	0.003	-	-	-
Xyloglucanase enzymes	0.008	0.01	-	0.008	0.005	Proteolytic enzyme	0.03	0.01	0.03	0.02	0.02
Lipase	-	-	0.002	-	-	Proteolytic enzyme	0.03	0.01	0.03	0.02	0.02
Lipase	-	-	0.002	-	-	Amylase	-	-	-	0.002	-
Cellulase	-	-	0.0002	0.0005	0.0001	Amylase	-	-	-	0.002	-
Cellulase	-	-	0.0002	0.0005	0.0001	SRP1	0.2	-	0.1	-	-
DTPA	-	-	0.3	-	-	SRP1	0.2	-	0.1	-	-
DTPA	-	-	0.3	-	-	PVNO	-	-	0.3	-	0.2
Brightener 1	0.2	0.07	0.1	-	-	PVNO	-	-	0.3	-	0.2
Brightener 1	0.2	0.07	0.1	-	-	Silicone antifoam agent	0.04	0.02	0.1	0.1	0.1
Miscellaneous and water						Silicone antifoam agent	0.04	0.02	0.1	0.1	0.1

Embodiment 11

	??I	??II	??III	??IV
	??I	??II	??III	??IV	??LAS	??10.0	??13.0	??9.0	??-
??C25AS	??4.0	??1.0	??2.0	??10.0	??LAS	??10.0	??13.0	??9.0	??-
??C25AS	??4.0	??1.0	??2.0	??10.0	??C25E3S	??1.0	??-	??-	??3.0
??C25E7	??6.0	??8.0	??13.0	??2.5	??C25E3S	??1.0	??-	??-	??3.0
??C25E7	??6.0	??8.0	??13.0	??2.5	??TFAA	??-	??-	??-	??4.5
??APA	??-	??1.4	??-	??-	??TFAA	??-	??-	??-	??4.5
??APA	??-	??1.4	??-	??-	??TPKFA	??2.0	??-	??13.0	??7.0
Citric acid	??2.0	??3.0	??1.0	??1.5	??TPKFA	??2.0	??-	??13.0	??7.0
Citric acid	??2.0	??3.0	??1.0	??1.5	Dodecenyl succinic/14	??12.0	??10.0	???-	??-

Carbene base succsinic acid
Carbene base succsinic acid					Vegetable seed lipid acid	4.0	2.2	1.0	-
Ethanol	4.0	4.0	7.0	2.0	Vegetable seed lipid acid	4.0	2.2	1.0	-
Ethanol	4.0	4.0	7.0	2.0	1, the 2-propylene glycol	4.0	4.0	2.0	7.0
Monoethanolamine	-	-	-	5.0	1, the 2-propylene glycol	4.0	4.0	2.0	7.0
Monoethanolamine	-	-	-	5.0	Trolamine	-	-	8.0	-
TEPAE	0.5	-	0.5	0.2	Trolamine	-	-	8.0	-
TEPAE	0.5	-	0.5	0.2	DETPMP	1.0	1.0	0.5	1.0
Mannase	0.0002	0.0005	0.005	0.0005	DETPMP	1.0	1.0	0.5	1.0
Mannase	0.0002	0.0005	0.005	0.0005	Polygalacturonase	-	0.009	-	-
Xyloglucanase enzymes	-	-	0.01	-	Polygalacturonase	-	0.009	-	-
Xyloglucanase enzymes	-	-	0.01	-	Proteolytic enzyme	0.02	0.02	0.01	0.008
Lipase	-	0.002	-	0.002	Proteolytic enzyme	0.02	0.02	0.01	0.008
Lipase	-	0.002	-	0.002	Amylase	0.004	0.004	0.01	0.008
Cellulase	-	-	-	0.002	Amylase	0.004	0.004	0.01	0.008
Cellulase	-	-	-	0.002	SRP2	0.3	-	0.3	0.1
Boric acid	0.1	0.2	1.0	2.0	SRP2	0.3	-	0.3	0.1
Boric acid	0.1	0.2	1.0	2.0	Calcium chloride	-	0.02	-	0.01
Brightener 1	-	0.4	-	-	Calcium chloride	-	0.02	-	0.01
Brightener 1	-	0.4	-	-	Suds suppressor	0.1	0.3	-	0.1
Opalizer	0.5	0.4	-	0.3	Suds suppressor	0.1	0.3	-	0.1
Opalizer	0.5	0.4	-	0.3	Add NaOH to pH	8.0	8.0	7.6	7.7
Miscellaneous and water					Add NaOH to pH	8.0	8.0	7.6	7.7

Embodiment 12

Prepare following liquid detergent composition (its level is in weight part, and enzyme is in pure enzyme) according to the present invention:

	??I	??II	??III	??IV
	??I	??II	??III	??IV	??LAS	??25.0	??-	??-	??-
??C25AS	??-	??13.0	??18.0	??15.0	??LAS	??25.0	??-	??-	??-
??C25AS	??-	??13.0	??18.0	??15.0	??C25E3S	??-	??2.0	??2.0	??4.0
??C25E7	??-	??-	??4.0	??4.0	??C25E3S	??-	??2.0	??2.0	??4.0
??C25E7	??-	??-	??4.0	??4.0	??TFAA	??-	??6.0	??8.0	??8.0
??APA	??3.0	??1.0	??2.0	??-	??TFAA	??-	??6.0	??8.0	??8.0
??APA	??3.0	??1.0	??2.0	??-	??TPKFA	??-	??15.0	??11.0	??11.0
Citric acid	??1.0	??1.0	??1.0	??1.0	??TPKFA	??-	??15.0	??11.0	??11.0
Citric acid	??1.0	??1.0	??1.0	??1.0	Dodecenyl succinic/tetradecene base succsinic acid	??15.0
Vegetable seed lipid acid	??1.0	??-	??3.5	???-	Dodecenyl succinic/tetradecene base succsinic acid	??15.0
Vegetable seed lipid acid	??1.0	??-	??3.5	???-	Ethanol	??7.0	??2.0	??3.0	??2.0
1, the 2-propylene glycol	??6.0	??8.0	??10.0	??13.0	Ethanol	??7.0	??2.0	??3.0	??2.0
1, the 2-propylene glycol	??6.0	??8.0	??10.0	??13.0	Monoethanolamine	??-	??-	??9.0	??9.0
??TEPAE	??-	??-	??0.4	??0.3	Monoethanolamine	??-	??-	??9.0	??9.0
??TEPAE	??-	??-	??0.4	??0.3	??DETPMP	??2.0	??1.2	??1.0	??-
Mannase	??0.0001	??0.0002	??0.005	??0.0005	??DETPMP	??2.0	??1.2	??1.0	??-
Mannase	??0.0001	??0.0002	??0.005	??0.0005	Polygalacturonase	??-	??0.008	??-	??-
Xyloglucanase enzymes	??0.005	???-	??-	??-	Polygalacturonase	??-	??0.008	??-	??-
Xyloglucanase enzymes	??0.005	???-	??-	??-	Proteolytic enzyme	??0.08	??0.02	??0.01	??0.02
Lipase	??-	??-	??0.003	??0.003	Proteolytic enzyme	??0.08	??0.02	??0.01	??0.02
Lipase	??-	??-	??0.003	??0.003	Amylase	??0.004	??0.01	??0.01	??0.01
Cellulase	??-	??-	??0.004	??0.003	Amylase	??0.004	??0.01	??0.01	??0.01
Cellulase	??-	??-	??0.004	??0.003	??SRP2	??-	??-	??0.2	??0.1
Boric acid	??1.0	??1.5	??2.5	??2.5	??SRP2	??-	??-	??0.2	??0.1

Wilkinite	4.0	4.0	-	-
Wilkinite	4.0	4.0	-	-	Brightener 1	0.1	0.2	0.3	-
Suds suppressor	0.4	-	-	-	Brightener 1	0.1	0.2	0.3	-
Suds suppressor	0.4	-	-	-	Opalizer	0.8	0.7	-	-
Add NaOH to pH	8.0	7.5	8.0	8.2	Opalizer	0.8	0.7	-	-
Add NaOH to pH	8.0	7.5	8.0	8.2	Miscellaneous and water

Embodiment 13

	??I	??II
	??I	??II	??LAS	??27.6	??18.9
??C45AS	??13.8	??5.9	??LAS	??27.6	??18.9
??C45AS	??13.8	??5.9	??C13E8	??3.0	??3.1
Oleic acid	??3.4	??2.5	??C13E8	??3.0	??3.1
Oleic acid	??3.4	??2.5	Citric acid	??5.4	??5.4
Sodium hydroxide	??0.4	??3.6	Citric acid	??5.4	??5.4
Sodium hydroxide	??0.4	??3.6	Calcium formiate	??0.2	??0.1
Sodium formiate	??-	??0.5	Calcium formiate	??0.2	??0.1
Sodium formiate	??-	??0.5	Ethanol	??7.0	??-
Monoethanolamine	??16.5	??8.0	Ethanol	??7.0	??-
Monoethanolamine	??16.5	??8.0	1, the 2-propylene glycol	??5.9	??5.5
Xylene monosulfonic acid	??-	??2.4	1, the 2-propylene glycol	??5.9	??5.5
Xylene monosulfonic acid	??-	??2.4	??TEPAE	??1.5	??0.8
Proteolytic enzyme	??0.05	??0.02	??TEPAE	??1.5	??0.8
Proteolytic enzyme	??0.05	??0.02	Mannase	??0.005	??0.0002
Xyloglucanase enzymes	??0.005	??-	Mannase	??0.005	??0.0002
Xyloglucanase enzymes	??0.005	??-	Amylase	??0.002	??0.002

PEG	-	0.7
PEG	-	0.7	Brightener 2	0.4	0.1
Spices	0.5	0.3	Brightener 2	0.4	0.1
Spices	0.5	0.3	Water and minor component

Embodiment 14

Prepare following gel detergent compositions according to the present invention:

	??I	??II	??III	??IV
	??I	??II	??III	??IV	??C12-15E2.5S	??21	??20.2	??22.7	??13.6
??C12LAS	??-	??-	??-	??9.1	??C12-15E2.5S	??21	??20.2	??22.7	??13.6
??C12LAS	??-	??-	??-	??9.1	The C12-14 glucamide	??4.0	??2.5	??-	??-
??C12-14EO7	??4.5	??-	??-	??-	The C12-14 glucamide	??4.0	??2.5	??-	??-
??C12-14EO7	??4.5	??-	??-	??-	??C12-14O9	??-	??0.6	??0.6	??0.6
C8-10 amido propylamine	??1.3	??-	??-	??-	??C12-14O9	??-	??0.6	??0.6	??0.6
C8-10 amido propylamine	??1.3	??-	??-	??-	C10 amido propylamine	??-	??1.3	??1.3	??1.3
Citric acid	??1.0	??5.0	??1.0	??1.0	C10 amido propylamine	??-	??1.3	??1.3	??1.3
Citric acid	??1.0	??5.0	??1.0	??1.0	C12/14 lipid acid	??-	??10.0	??10.0	??10.0
Palm kernel fatty acid	??8.0	??-	??-	??-	C12/14 lipid acid	??-	??10.0	??10.0	??10.0
Palm kernel fatty acid	??8.0	??-	??-	??-	Vegetable seed lipid acid	??8.0	??-	??-	??-
Mannase	??0.0001	??0.0002	??0.005	??0.0005	Vegetable seed lipid acid	??8.0	??-	??-	??-
Mannase	??0.0001	??0.0002	??0.005	??0.0005	Xyloglucanase enzymes	??-	??0.008	??-	??0.001
Proteolytic enzyme	??0.02	??0.03	??0.03	??0.03	Xyloglucanase enzymes	??-	??0.008	??-	??0.001
Proteolytic enzyme	??0.02	??0.03	??0.03	??0.03	Lipase	??0.001	??0.002	??0.003	??0.002
Amylase	??0.003	??0.002	??0.002	??0.002	Lipase	??0.001	??0.002	??0.003	??0.002
Amylase	??0.003	??0.002	??0.002	??0.002	Cellulase	??0.0007	??0.0001	??0.0001	??0.0001
Whitening agent 1	??0.15	??0.15	??0.15	??0.15	Cellulase	??0.0007	??0.0001	??0.0001	??0.0001
Whitening agent 1	??0.15	??0.15	??0.15	??0.15	Polymer A	??0.7	??0.6	??0.6	??0.6
Polymer B	??-	??1.2	??1.2	??1.2	Polymer A	??0.7	??0.6	??0.6	??0.6

Polyamine-polymeric amide	2.0	1.0	1.0	-
Polyamine-polymeric amide	2.0	1.0	1.0	-	The polyethoxylated polyamine	-	2.0	-	-
Stain remover	-	0.1	0.1	0.1	The polyethoxylated polyamine	-	2.0	-	-
Stain remover	-	0.1	0.1	0.1	Ethanol	0.7	0.5	0.5	0.5
1, the 2-propylene glycol	4.0	4.0	4.0	4.0	Ethanol	0.7	0.5	0.5	0.5
1, the 2-propylene glycol	4.0	4.0	4.0	4.0	Monoethanolamine	0.7	0.5	0.5	0.5
NaOH	2.8	7.0	7.0	7.0	Monoethanolamine	0.7	0.5	0.5	0.5
NaOH	2.8	7.0	7.0	7.0	Boric acid	2.0	-	-	-
Borax	-	2.5	2.5	2.5	Boric acid	2.0	-	-	-
Borax	-	2.5	2.5	2.5	Suds suppressor	-	0.1	0.1	0.1
Polydimethylsiloxane	0.2	-	-	-	Suds suppressor	-	0.1	0.1	0.1
Polydimethylsiloxane	0.2	-	-	-	Spices	0.5	0.75	0.75	0.75
Dyestuff	-	0.04	0.04	0.04	Spices	0.5	0.75	0.75	0.75
Dyestuff	-	0.04	0.04	0.04	Miscellaneous and water	To 100%

Embodiment 15

	??I	??II	??III	??IV
	??I	??II	??III	??IV	??C12-15E2.5S	??18.2	??22.6	??27.6	??22.6
??C12-15EO9	??0.6	??0.6	??0.6	??0.6	??C12-15E2.5S	??18.2	??22.6	??27.6	??22.6
??C12-15EO9	??0.6	??0.6	??0.6	??0.6	C10 amido propylamine	??1.3	??1.3	??1.3	??1.3
Citric acid	??1.0	??1.0	??1.0	??1.0	C10 amido propylamine	??1.3	??1.3	??1.3	??1.3
Citric acid	??1.0	??1.0	??1.0	??1.0	C12/14 lipid acid	??10.0	??10.0	??7.5	??10.0
??Quat	??1.0	??5.0	??-	??-	C12/14 lipid acid	??10.0	??10.0	??7.5	??10.0
??Quat	??1.0	??5.0	??-	??-	Mannase	??0.005	??0.001	??0.002	??0.0005
Polygalacturonase	??-	??0.005	???-	??0.002	Mannase	??0.005	??0.001	??0.002	??0.0005
Polygalacturonase	??-	??0.005	???-	??0.002	Proteolytic enzyme	??0.03	??0.01	??0.03	??0.03
Lipase	??0.002	??0.002	??0.002	??0.002	Proteolytic enzyme	??0.03	??0.01	??0.03	??0.03

Amylase	0.003	0.002	0.001	0.002
Amylase	0.003	0.002	0.001	0.002	Cellulase	0.0001	0.0004	0.0001	0.0001
Whitening agent 1	0.15	0.15	0.15	0.15	Cellulase	0.0001	0.0004	0.0001	0.0001
Whitening agent 1	0.15	0.15	0.15	0.15	Polymer A	0.6	0.3	0.6	0.6
Polymer B	1.2	0.6	1.2	1.2	Polymer A	0.6	0.3	0.6	0.6
Polymer B	1.2	0.6	1.2	1.2	Stain remover	0.1	0.1	0.1	0.1
Ethanol	0.5	0.5	0.5	0.5	Stain remover	0.1	0.1	0.1	0.1
Ethanol	0.5	0.5	0.5	0.5	1, the 2-propylene glycol	4.0	4.0	4.0	4.0
Monoethanolamine	0.5	0.5	0.5	0.5	1, the 2-propylene glycol	4.0	4.0	4.0	4.0
Monoethanolamine	0.5	0.5	0.5	0.5	NaOH	7.0	7.0	7.0	7.0
Boric acid	-	-	-	-	NaOH	7.0	7.0	7.0	7.0
Boric acid	-	-	-	-	Borax	2.5	2.5	2.5	-
Suds suppressor	0.1	0.1	0.1	0.1	Borax	2.5	2.5	2.5	-
Suds suppressor	0.1	0.1	0.1	0.1	Spices	0.75	0.75	0.75	0.75
Dyestuff	0.04	0.04	0.04	0.04	Spices	0.75	0.75	0.75	0.75
Dyestuff	0.04	0.04	0.04	0.04	Miscellaneous and water	To 100%

Embodiment 16

The following particle fabric detergent composition of " softening by washing " is provided according to the present invention's preparation:

	??I	??II
	??I	??II	?C45EAS	??-	??10.0
??LAS	??7.6	??-	?C45EAS	??-	??10.0
??LAS	??7.6	??-	??C68AS	??1.3	??-
??C45E7	??4.0	??-	??C68AS	??1.3	??-
??C45E7	??4.0	??-	??C25E3	??-	??5.0
Cocounut oil alkyl dimethyl hydroxyethyl ammonium chloride	??1.4	??1.0	??C25E3	??-	??5.0
Cocounut oil alkyl dimethyl hydroxyethyl ammonium chloride	??1.4	??1.0	Citrate trianion	??5.0	??3.0

Na-SKS-6	-	11.0
Na-SKS-6	-	11.0	Zeolite A	15.0	15.0
MA/AA	4.0	4.0	Zeolite A	15.0	15.0
MA/AA	4.0	4.0	DETPMP	0.4	0.4
PB1	15.0	-	DETPMP	0.4	0.4
PB1	15.0	-	Percarbonate	-	15.0
TAED	5.0	5.0	Percarbonate	-	15.0
TAED	5.0	5.0	Terre verte	10.0	10.0
HMWPEO	-	0.1	Terre verte	10.0	10.0
HMWPEO	-	0.1	Mannase	0.01	0.001
Polygalacturonase	0.01	-	Mannase	0.01	0.001
Polygalacturonase	0.01	-	Xyloglucanase enzymes	-	0.01
Proteolytic enzyme	0.02	0.01	Xyloglucanase enzymes	-	0.01
Proteolytic enzyme	0.02	0.01	Lipase	0.02	0.01
Amylase	0.03	0.005	Lipase	0.02	0.01
Amylase	0.03	0.005	Cellulase	0.001	-
Silicate	3.0	5.0	Cellulase	0.001	-
Silicate	3.0	5.0	Carbonate	10.0	10.0
Suds suppressor	1.0	4.0	Carbonate	10.0	10.0
Suds suppressor	1.0	4.0	CMC	0.2	0.1
Miscellaneous and water	To 100%		CMC	0.2	0.1

Embodiment 17

Prepare following laundry with detergent bar composition (its level by weight, enzyme is represented with pure enzyme) according to the present invention:

	??I	??II	??III	??VI	??V	??III	??VI	??V
	??I	??II	??III	??VI	??V	??III	??VI	??V	??LAS	??-	??-	??19.0	??15.0	??21.0	??6.75	??8.8	??-
??C28AS	??30.0	??13.5	??-	??-	??-	??15.75	??11.2	??22.5	??LAS	??-	??-	??19.0	??15.0	??21.0	??6.75	??8.8	??-
??C28AS	??30.0	??13.5	??-	??-	??-	??15.75	??11.2	??22.5	Sodium laurate	??2.5	??9.0	??-	??-	??-	??-	??-	??-
Zeolite A	??2.0	??1.25	??-	??-	??-	??1.25	??1.25	??1.25	Sodium laurate	??2.5	??9.0	??-	??-	??-	??-	??-	??-
Zeolite A	??2.0	??1.25	??-	??-	??-	??1.25	??1.25	??1.25	Carbonate	??20.0	??3.0	??13.0	??8.0	??10.0	??15.0	??15.0	??10.0
Lime carbonate	??27.5	??39.0	??35.0	??-	??-	??40.0	??-	??40.0	Carbonate	??20.0	??3.0	??13.0	??8.0	??10.0	??15.0	??15.0	??10.0
Lime carbonate	??27.5	??39.0	??35.0	??-	??-	??40.0	??-	??40.0	Vitriol	??5.0	??5.0	??3.0	??5.0	??3.0	??-	??-	??5.0
??TSPP	??5.0	??-	??-	??-	??-	??5.0	??2.5	??-	Vitriol	??5.0	??5.0	??3.0	??5.0	??3.0	??-	??-	??5.0
??TSPP	??5.0	??-	??-	??-	??-	??5.0	??2.5	??-	??STPP	??5.0	??15.0	??10.0	??-	??-	??7.0	??8.0	??10.0
Wilkinite	??-	??10.0	??-	??-	??5.0	??-	??-	??-	??STPP	??5.0	??15.0	??10.0	??-	??-	??7.0	??8.0	??10.0
Wilkinite	??-	??10.0	??-	??-	??5.0	??-	??-	??-	??DETPMP	??-	??0.7	??0.6	??-	??0.6	??0.7	??0.7	??0.7
??CMC	??-	??1.0	??1.0	??1.0	??1.0	??-	??-	??1.0	??DETPMP	??-	??0.7	??0.6	??-	??0.6	??0.7	??0.7	??0.7
??CMC	??-	??1.0	??1.0	??1.0	??1.0	??-	??-	??1.0	Talcum powder	??-	??-	??10.0	??15.0	??10.0	??-	??-	??-
Silicate	??-	??-	??4.0	??5.0	??3.0	??-	??-	??-	Talcum powder	??-	??-	??10.0	??15.0	??10.0	??-	??-	??-
Silicate	??-	??-	??4.0	??5.0	??3.0	??-	??-	??-	??PVNO	??0.02	??0.03	??-	??0.01	??-	??0.02	??-	??-
??MA/AA	??0.4	??1.0	??-	??-	??0.2	??0.4	??0.5	??0.4	??PVNO	??0.02	??0.03	??-	??0.01	??-	??0.02	??-	??-
??MA/AA	??0.4	??1.0	??-	??-	??0.2	??0.4	??0.5	??0.4	??SRP1	??0.3	??0.3	??0.3	??0.3	??0.3	??0.3	??0.3	??0.3
Mannase	??0.001	??0.001	??0.002	??0.001	??0.002	??0.004	??0.001	??0.0005	??SRP1	??0.3	??0.3	??0.3	??0.3	??0.3	??0.3	??0.3	??0.3
Mannase	??0.001	??0.001	??0.002	??0.001	??0.002	??0.004	??0.001	??0.0005	Polygalacturonase	??-	??0.008	??-	??-	??0.005	??-	??0.002	??-
Xyloglucanase enzymes	??-	??-	??0.005	??-	??-	??0.003	??0.003	??-	Polygalacturonase	??-	??0.008	??-	??-	??0.005	??-	??0.002	??-
Xyloglucanase enzymes	??-	??-	??0.005	??-	??-	??0.003	??0.003	??-	Amylase	??0.01	??-	??0.01	??0.002	??-	??-	??0.002	??-
Proteolytic enzyme	??-	??0.004	??-	??0.003	??0.003	??-	??-	??0.003	Amylase	??0.01	??-	??0.01	??0.002	??-	??-	??0.002	??-
Proteolytic enzyme	??-	??0.004	??-	??0.003	??0.003	??-	??-	??0.003	Lipase	??-	??0.002	??-	??0.002	??-	??-	??-	??-

Cellulase	-	0.0003	-	-	0.0003	0.0002	-	0.003
Cellulase	-	0.0003	-	-	0.0003	0.0002	-	0.003	PEO	-	0.2	-	0.2	0.3	-	-	0.3
Spices	1.0	0.5	0.3	0.2	0.4	-	-	0.4	PEO	-	0.2	-	0.2	0.3	-	-	0.3
Spices	1.0	0.5	0.3	0.2	0.4	-	-	0.4	Sal epsom	-	-	3.0	3.0	3.0	-	-	-
Brightener	0.15	0.1	0.15	-	-	-	-	0.1	Sal epsom	-	-	3.0	3.0	3.0	-	-	-
Brightener	0.15	0.1	0.15	-	-	-	-	0.1	Photoactivation SYNTHETIC OPTICAL WHITNER (ppm)	-	15.0	15.0	15.0	15.0	-	-	15.0

Embodiment 18

Prepare following laundry additive composition according to the present invention:

	??I	??II	??III
	??I	??II	??III	??LAS	??-	??5.0	??5.0
??STPP	??30.0	??-	??20.0	??LAS	??-	??5.0	??5.0
??STPP	??30.0	??-	??20.0	Zeolite A	??-	??35.0	??20.0
??PB1	??20.0	??15.0	??-	Zeolite A	??-	??35.0	??20.0
??PB1	??20.0	??15.0	??-	??TAED	??10.0	??8.0	??-
Mannase	??0.005	??0.0002	??0.001	??TAED	??10.0	??8.0	??-
Mannase	??0.005	??0.0002	??0.001	Polygalacturonase	??0.003	??-	??0.002
Xyloglucanase enzymes	??-	??0.005	??0.002	Polygalacturonase	??0.003	??-	??0.002
Xyloglucanase enzymes	??-	??0.005	??0.002	Proteolytic enzyme	??-	??0.3	??0.3
Amylase	??-	??0.06	??0.06	Proteolytic enzyme	??-	??0.3	??0.3
Amylase	??-	??0.06	??0.06	Minor component, water and miscellaneous	To 100%

Embodiment 19

Prepare following extrusion type high-density (0.96Kg/l) dish washing detergent compositions according to the present invention:

	??I	??II	??III	??IV	??V	??VI	??VII	??VII
	??I	??II	??III	??IV	??V	??VI	??VII	??VII	??STPP	??-	??-	??54.3	??51.4	??51.4	??-	??-	??50.9
Citrate trianion	??35.0	??17.0	??-	??-	??-	??46.1	??40.2	??-	??STPP	??-	??-	??54.3	??51.4	??51.4	??-	??-	??50.9
Citrate trianion	??35.0	??17.0	??-	??-	??-	??46.1	??40.2	??-	Carbonate	??-	??17.5	??14.0	??14.0	??14.0	??-	??8.0	??32.1
Supercarbonate	??-	??-	??-	??-	??-	??25.4	??-	??-	Carbonate	??-	??17.5	??14.0	??14.0	??14.0	??-	??8.0	??32.1
Supercarbonate	??-	??-	??-	??-	??-	??25.4	??-	??-	Silicate	??32.0	??14.8	??14.8	??10.0	??10.0	??1.0	??25.0	??3.1
Silicate (metasilicate)	??-	??2.5	??-	??9.0	??9.0	??-	??-	??-	Silicate	??32.0	??14.8	??14.8	??10.0	??10.0	??1.0	??25.0	??3.1
Silicate (metasilicate)	??-	??2.5	??-	??9.0	??9.0	??-	??-	??-	??PB1	??1.9	??9.7	??7.8	??7.8	??7.8	??-	??-	??-
??PB4	??8.6	??-	??-	??-	??-	??-	??-	??-	??PB1	??1.9	??9.7	??7.8	??7.8	??7.8	??-	??-	??-
??PB4	??8.6	??-	??-	??-	??-	??-	??-	??-	Percarbonate	??-	??-	??-	??-	??-	??6.7	??11.8	??4.8
Nonionic	??1.5	??2.0	??1.5	??1.7	??1.5	??2.6	??1.9	??5.3	Percarbonate	??-	??-	??-	??-	??-	??6.7	??11.8	??4.8
Nonionic	??1.5	??2.0	??1.5	??1.7	??1.5	??2.6	??1.9	??5.3	??TAED	??5.2	??2.4	??-	??-	??-	??-	??2.2	??1.4
??HEDP	??-	??1.0	??-	??-	??-	??-	??-	??-	??TAED	??5.2	??2.4	??-	??-	??-	??-	??2.2	??1.4
??HEDP	??-	??1.0	??-	??-	??-	??-	??-	??-	??DETPMP	??-	??0.6	??-	??-	??-	??-	??-	??-
??MnTACN	??-	??-	??-	??-	??-	??-	??0.008	??-	??DETPMP	??-	??0.6	??-	??-	??-	??-	??-	??-
??MnTACN	??-	??-	??-	??-	??-	??-	??0.008	??-	??PAAC	??-	??-	??0.008	??0.01	??0.007	??-	??-	??-
??BzP	??-	??-	??-	??-	??1.4	??-	??-	??-	??PAAC	??-	??-	??0.008	??0.01	??0.007	??-	??-	??-
??BzP	??-	??-	??-	??-	??1.4	??-	??-	??-	Paraffin	??0.5	??0.5	??0.5	??0.5	???0.5	??0.6	??-	??-
Mannase	??0.001	??0.002	??0.002	??0.005	??0.02	??0.001	??0.01	??0.01	Paraffin	??0.5	??0.5	??0.5	??0.5	???0.5	??0.6	??-	??-
Mannase	??0.001	??0.002	??0.002	??0.005	??0.02	??0.001	??0.01	??0.01	Proteolytic enzyme	??0.072	??0.072	??0.029	??0.053	??0.046	??0.026	??0.059	??0.06
Amylase	??0.012	??0.012	??0.006	??0.012	??0.013	??0.009	??0.017	??0.03	Proteolytic enzyme	??0.072	??0.072	??0.029	??0.053	??0.046	??0.026	??0.059	??0.06
Amylase	??0.012	??0.012	??0.006	??0.012	??0.013	??0.009	??0.017	??0.03	Lipase	??-	??0.001	??-	??0.005	??-	??-	??-	??-
??BTA	??0.3	??0.3	??0.3	??0.3	??0.3	??-	??0.3	??0.3	Lipase	??-	??0.001	??-	??0.005	??-	??-	??-	??-
??BTA	??0.3	??0.3	??0.3	??0.3	??0.3	??-	??0.3	??0.3	??MA/AA	??-	??-	??-	??-	??-	??-	??4.2	??-
??480N	??3.3	??6.0	??-	??-	??-	??-	??-	??0.9	??MA/AA	??-	??-	??-	??-	??-	??-	??4.2	??-
??480N	??3.3	??6.0	??-	??-	??-	??-	??-	??0.9	Spices	??0.2	??0.2	??0.2	??0.2	??0.2	??0.2	??0.1	??0.1
Vitriol	??7.0	??20.0	??5.0	??2.2	??0.8	??12.0	??4.6	??-	Spices	??0.2	??0.2	??0.2	??0.2	??0.2	??0.2	??0.1	??0.1
Vitriol	??7.0	??20.0	??5.0	??2.2	??0.8	??12.0	??4.6	??-	??pH	??10.8	??11.0	??10.8	??11.3	??11.3	??9.6	??10.8	??10.9
Miscellaneous and water	To 100%								??pH	??10.8	??11.0	??10.8	??11.3	??11.3	??9.6	??10.8	??10.9

Embodiment 20

Prepare the particle dish washing compositions that following tap density is 1.02Kg/l according to the present invention:

	??I	??II	??III	??IV	??V	??VI	??VII	??VII
	??I	??II	??III	??IV	??V	??VI	??VII	??VII	??STPP	??30.0	??30.0	??33.0	??34.2	??29.6	??31.1	??26.6	??17.6
Carbonate	??30.5	??30.5	??31.0	??30.0	??23.0	??39.4	??4.2	??45.0	??STPP	??30.0	??30.0	??33.0	??34.2	??29.6	??31.1	??26.6	??17.6
Carbonate	??30.5	??30.5	??31.0	??30.0	??23.0	??39.4	??4.2	??45.0	Silicate	??7.4	??7.4	??7.5	??7.2	??13.3	??3.4	??43.7	??12.4
Silicate (metasilicate)	??-	??-	??4.5	??5.1	??-	??-	??-	??-	Silicate	??7.4	??7.4	??7.5	??7.2	??13.3	??3.4	??43.7	??12.4
Silicate (metasilicate)	??-	??-	??4.5	??5.1	??-	??-	??-	??-	Percarbonate	??-	??-	??-	??-	??-	??4.0	??-	??-
??PB1	??4.4	??4.2	??4.5	??4.5	??-	??-	??-	??-	Percarbonate	??-	??-	??-	??-	??-	??4.0	??-	??-
??PB1	??4.4	??4.2	??4.5	??4.5	??-	??-	??-	??-	??NADCC	??-	??-	??-	??-	??2.0	??-	??1.6	??1.0
Nonionic	??1.2	??1.0	??0.7	??0.8	??1.9	??0.7	??0.6	??0.3	??NADCC	??-	??-	??-	??-	??2.0	??-	??1.6	??1.0
Nonionic	??1.2	??1.0	??0.7	??0.8	??1.9	??0.7	??0.6	??0.3	??TAED	??1.0	??-	??-	??-	??-	??0.8	??-	??-
??PACC	??-	??0.004	??0.004	??0.004	??-	???-	??-	??-	??TAED	??1.0	??-	??-	??-	??-	??0.8	??-	??-
??PACC	??-	??0.004	??0.004	??0.004	??-	???-	??-	??-	??BzP	??-	??-	??-	??1.4	??-	???-	??-	??-
Paraffin	??0.25	??0.25	??0.25	??0.25	??-	???-	??-	??-	??BzP	??-	??-	??-	??1.4	??-	???-	??-	??-
Paraffin	??0.25	??0.25	??0.25	??0.25	??-	???-	??-	??-	Mannase	??0.01	??0.002	??0.01	??0.002	??0.02	??0.001	??0.005	??0.005
Proteolytic enzyme	??0.036	??0.015	??0.03	??0.028	??-	??0.03	??-	??-	Mannase	??0.01	??0.002	??0.01	??0.002	??0.02	??0.001	??0.005	??0.005
Proteolytic enzyme	??0.036	??0.015	??0.03	??0.028	??-	??0.03	??-	??-	Amylase	??0.003	??0.003	??0.01	??0.006	??0.006	??0.01	??0.006	??0.006
Lipase	??0.005	??-	??0.001	??-	??-	??-	??-	??-	Amylase	??0.003	??0.003	??0.01	??0.006	??0.006	??0.01	??0.006	??0.006
Lipase	??0.005	??-	??0.001	??-	??-	??-	??-	??-	??BTA	??0.15	??0.15	??0.15	??0.15	??-	??-	??-	??-
Spices	??0.2	??0.2	??0.2	??0.2	??0.1	??0.2	??0.2	??-	??BTA	??0.15	??0.15	??0.15	??0.15	??-	??-	??-	??-
Spices	??0.2	??0.2	??0.2	??0.2	??0.1	??0.2	??0.2	??-	Vitriol	??23.4	??25.0	??22.0	??18.5	??30.1	??19.3	??23.1	??23.6
??pH	??10.8	??10.8	??11.3	??11.3	??10.7	??11.5	??12.7	??10.9	Vitriol	??23.4	??25.0	??22.0	??18.5	??30.1	??19.3	??23.1	??23.6
??pH	??10.8	??10.8	??11.3	??11.3	??10.7	??11.5	??12.7	??10.9	Miscellaneous and water	To 100%

Embodiment 21

Compacting by 12 rotary press of use standard machine washing particle dish washing compositions under the pressure of 13,000 Ns/square centimeter prepares following tablet detergent composition according to the present invention:

	??I	??II	??III	??IV	??V	??VI
	??I	??II	??III	??IV	??V	??VI	??STPP	??-	??48.8	??49.2	??38.0	??-	??46.8
Citrate trianion	??26.4	??-	??-	??-	??31.1	??-	??STPP	??-	??48.8	??49.2	??38.0	??-	??46.8
Citrate trianion	??26.4	??-	??-	??-	??31.1	??-	Carbonate	??-	??5.0	??14.0	??15.4	??14.4	??23.0
Silicate	??26.4	??14.8	??15.0	??12.6	??17.7	??2.4	Carbonate	??-	??5.0	??14.0	??15.4	??14.4	??23.0
Silicate	??26.4	??14.8	??15.0	??12.6	??17.7	??2.4	Mannase	??0.001	??0.002	??0.002	??0.001	??0.005	??0.02
Proteolytic enzyme	??0.058	??0.072	??0.041	??0.033	??0.052	??0.013	Mannase	??0.001	??0.002	??0.002	??0.001	??0.005	??0.02
Proteolytic enzyme	??0.058	??0.072	??0.041	??0.033	??0.052	??0.013	Amylase	??0.01	??0.03	??0.012	??0.007	??0.016	??0.002
Lipase	??0.005	??-	??-	??-	??-	??-	Amylase	??0.01	??0.03	??0.012	??0.007	??0.016	??0.002
Lipase	??0.005	??-	??-	??-	??-	??-	??PB1	??1.6	??7.7	??12.2	??10.6	??15.7	??-
??PB4	??6.9	??-	???-	???-	???-	??14.4	??PB1	??1.6	??7.7	??12.2	??10.6	??15.7	??-
??PB4	??6.9	??-	???-	???-	???-	??14.4	Nonionic	??1.5	??2.0	??1.5	??1.65	??0.8	??6.3
??PAAC	??-	??-	??0.02	??0.009	??-	??-	Nonionic	??1.5	??2.0	??1.5	??1.65	??0.8	??6.3
??PAAC	??-	??-	??0.02	??0.009	??-	??-	??MnTACN	??-	??-	??-	??-	??0.007	??-
??TAED	??4.3	??2.5	??-	??-	??1.3	??1.8	??MnTACN	??-	??-	??-	??-	??0.007	??-
??TAED	??4.3	??2.5	??-	??-	??1.3	??1.8	??HEDP	??0.7	??-	??-	??0.7	??-	??0.4
??DETPMP	??0.65	??-	???-	??-	??-	??-	??HEDP	??0.7	??-	??-	??0.7	??-	??0.4
??DETPMP	??0.65	??-	???-	??-	??-	??-	Paraffin	??0.4	??0.5	??0.5	??0.55	??-	??-
??BTA	??0.2	??0.3	??0.3	??0.3	??-	??-	Paraffin	??0.4	??0.5	??0.5	??0.55	??-	??-
??BTA	??0.2	??0.3	??0.3	??0.3	??-	??-	??PA30	??3.2	??-	??-	??-	??-	??-
??MA/AA	??-	??-	??-	??-	??4.5	??0.55	??PA30	??3.2	??-	??-	??-	??-	??-
??MA/AA	??-	??-	??-	??-	??4.5	??0.55	Spices	??-	??-	??0.05	??0.05	??0.2	??0.2
Vitriol	??24.0	??13.0	??2.3	??-	??10.7	??3.4	Spices	??-	??-	??0.05	??0.05	??0.2	??0.2
Vitriol	??24.0	??13.0	??2.3	??-	??10.7	??3.4	Tablet weight	??25g	??25g	??20g	??30g	??18g	??20g

PH	??10.6	??10.6	??10.7	??10.7	???10.9	???11.2
PH	??10.6	??10.6	??10.7	??10.7	???10.9	???11.2	Miscellaneous and water	To 100%

Embodiment 22

The liquid dishwashing detergent compositions for preparing density 1.40Kg/L according to the present invention:

	??I	??II	??III	??IV
	??I	??II	??III	??IV	??STPP	??17.5	??17.5	??17.2	??16.0
Carbonate	??2.0	??-	??2.4	??-	??STPP	??17.5	??17.5	??17.2	??16.0
Carbonate	??2.0	??-	??2.4	??-	Silicate	??5.3	??6.1	??14.6	??15.7
??NaOCl	??1.15	??1.15	??1.15	??1.25	Silicate	??5.3	??6.1	??14.6	??15.7
??NaOCl	??1.15	??1.15	??1.15	??1.25	??Polygen/Caropol	??1.1	??1.0	??1.1	??1.25
Nonionic	??-	??-	??0.1	??-	??Polygen/Caropol	??1.1	??1.0	??1.1	??1.25
Nonionic	??-	??-	??0.1	??-	??NaBz	??0.75	??0.75	??-	??-
Mannase	??0.001	??0.002	??0.002	??0.002	??NaBz	??0.75	??0.75	??-	??-
Mannase	??0.001	??0.002	??0.002	??0.002	Amylase	??0.005	??0.005	??0.005	??0.005
??NaOH	??-	??1.9	??-	??3.5	Amylase	??0.005	??0.005	??0.005	??0.005
??NaOH	??-	??1.9	??-	??3.5	??KOH	??2.8	??3.5	??3.0	??-
??pH	??11.0	??11.7	??10.9	??11.0	??KOH	??2.8	??3.5	??3.0	??-
??pH	??11.0	??11.7	??10.9	??11.0	Vitriol, miscellaneous and water	To 100%

Embodiment 23

Prepare following liquid dishwashing detergent compositions according to the present invention:

	??I	??II	??III	??IV	??V
	??I	??II	??III	??IV	??V	??C17ES	??28.5	??27.4	??19.2	??34.1	??34.1
Amine oxide	??2.6	??5.0	??2.0	??3.0	??3.0	??C17ES	??28.5	??27.4	??19.2	??34.1	??34.1
Amine oxide	??2.6	??5.0	??2.0	??3.0	??3.0	Trimethyl-glycine	??0.9	??-	??-	??2.0	??2.0
Xylenesulfonate	??2.0	??4.0	??-	??2.0	??-	Trimethyl-glycine	??0.9	??-	??-	??2.0	??2.0
Xylenesulfonate	??2.0	??4.0	??-	??2.0	??-	??Neodol?C11E9	??-	??-	??5.0	??-	??-
Polyhydroxy fatty acid amide	??-	??-	??-	??6.5	??6.5	??Neodol?C11E9	??-	??-	??5.0	??-	??-

Diethylidene pentaacetic acid sodium (40%)	-	-	0.03	-	-
Diethylidene pentaacetic acid sodium (40%)	-	-	0.03	-	-	TAED	-	-	-	0.06	0.06
Sucrose	-	-	-	1.5	1.5	TAED	-	-	-	0.06	0.06
Sucrose	-	-	-	1.5	1.5	Ethanol	4.0	5.5	5.5	9.1	9.1
Alkyl diphenyl base oxygen stilbene-4,4'-bis-(1-azo-3, 4-dihydroxy-benzene)-2,2'-disulfonate	-	-	-	-	2.3	Ethanol	4.0	5.5	5.5	9.1	9.1
	-	-	-	-	2.3	Calcium formiate	-	-	-	0.5	1.1
Ammonium citrate	0.06	0.1	-	-	-	Calcium formiate	-	-	-	0.5	1.1
Ammonium citrate	0.06	0.1	-	-	-	Sodium-chlor	-	1.0	-	-	-
Magnesium chloride	3.3	-	0.7	-	-	Sodium-chlor	-	1.0	-	-	-
Magnesium chloride	3.3	-	0.7	-	-	Calcium chloride	-	-	0.4	-	-
Sodium sulfate	-	-	0.06	-	-	Calcium chloride	-	-	0.4	-	-
Sodium sulfate	-	-	0.06	-	-	Sal epsom	0.08	-	-	-	-
Magnesium hydroxide	-	-	-	2.2	2.2	Sal epsom	0.08	-	-	-	-
Magnesium hydroxide	-	-	-	2.2	2.2	Sodium hydroxide	-	-	-	1.1	1.1
Hydrogen peroxide	200 ppm	0.16	0.006	-	-	Sodium hydroxide	-	-	-	1.1	1.1
Hydrogen peroxide	200 ppm	0.16	0.006	-	-	Mannase	0.001	0.02	0.005	0.001	0.02
Amylase	0.005	0.003	0.01	0.005	0.005	Mannase	0.001	0.02	0.005	0.001	0.02
Amylase	0.005	0.003	0.01	0.005	0.005	Proteolytic enzyme	0.017	0.005	0.0035	0.003	0.002
Spices	0.18	0.09	0.09	0.2	0.2	Proteolytic enzyme	0.017	0.005	0.0035	0.003	0.002
Spices	0.18	0.09	0.09	0.2	0.2	Water and minor component	To 100%

Embodiment 24

Prepare following liquid hard-surface cleaning compositions according to the present invention:

	??I	??II	??III	??IV	??V
	??I	??II	??III	??IV	??V	Mannase	??0.001	??0.002	??0.001	??0.002	??0.02
Amylase	??0.01	??0.002	??0.005	??0.002	??0.002	Mannase	??0.001	??0.002	??0.001	??0.002	??0.02
Amylase	??0.01	??0.002	??0.005	??0.002	??0.002	Proteolytic enzyme	??0.05	??0.01	??0.02	??-	??-
Hydrogen peroxide	??-	??-	??-	??6.0	??6.8	Proteolytic enzyme	??0.05	??0.01	??0.02	??-	??-
Hydrogen peroxide	??-	??-	??-	??6.0	??6.8	Acetyl triethyl Citrate trianion	??-	??-	??-	??2.5	??-
??DTPA	??-	??-	??-	??0.2	??-	Acetyl triethyl Citrate trianion	??-	??-	??-	??2.5	??-
??DTPA	??-	??-	??-	??0.2	??-	The fourth hydroxytoluene	??-	??-	??-	??0.05	??-
??EDTA ^*	??0.05	??0.05	??0.05	??-	??-	The fourth hydroxytoluene	??-	??-	??-	??0.05	??-
??EDTA ^*	??0.05	??0.05	??0.05	??-	??-	Citric acid/citrate	??2.9	??2.9	??2.9	??1.0	??-
??LAS	??0.5	??0.5	??0.5	??-	??-	Citric acid/citrate	??2.9	??2.9	??2.9	??1.0	??-
??LAS	??0.5	??0.5	??0.5	??-	??-	??C12AS	??0.5	??0.5	??0.5	??-	??-
??C10AS	??-	??-	??-	??-	??1.7	??C12AS	??0.5	??0.5	??0.5	??-	??-
??C10AS	??-	??-	??-	??-	??1.7	??C12(E)S	??0.5	??0.5	??0.5	??-	??-
The C12.13E6.5 nonionic	??7.0	??7.0	??7.0	??-	??-	??C12(E)S	??0.5	??0.5	??0.5	??-	??-
The C12.13E6.5 nonionic	??7.0	??7.0	??7.0	??-	??-	??Neodol?23-6.5	??-	??-	??-	??12.0	??-
??Dobanol?23-3	??-	??-	??-	??-	??1.5	??Neodol?23-6.5	??-	??-	??-	??12.0	??-
??Dobanol?23-3	??-	??-	??-	??-	??1.5	??Dobanol?91-10	??-	??-	??-	??-	??1.6
??C25AE1.8S	??-	??-	??-	??6.0	??-	??Dobanol?91-10	??-	??-	??-	??-	??1.6
??C25AE1.8S	??-	??-	??-	??6.0	??-	Sodium alkanesulfonate	??-	??-	??-	??6.0	??-
Spices	??1.0	??1.0	??1.0	??0.5	??0.2	Sodium alkanesulfonate	??-	??-	??-	??6.0	??-
Spices	??1.0	??1.0	??1.0	??0.5	??0.2	Propylene glycol	??-	??-	??-	??1.5	??-
The ethoxylation tetren	??-	??-	??-	??1.0	??-	Propylene glycol	??-	??-	??-	??1.5	??-
The ethoxylation tetren	??-	??-	??-	??1.0	??-	2-butyl octanol	??-	??-	??-	??-	??0.5

The hexyl Trivalin SF ^**	1.0	1.0	1.0	-	-
The hexyl Trivalin SF ^**	1.0	1.0	1.0	-	-	SCS	1.3	1.3	1.3	-	-
PH regulator arrives	7-12	7-12	7-12	4	-	SCS	1.3	1.3	1.3	-	-
PH regulator arrives	7-12	7-12	7-12	4	-	Miscellaneous and water	To 100%

^*Ethylenediamine-N,N'-diacetic acid(EDDA) four sodium ^*The Diethylene Glycol monohexyl ether

Embodiment 25

Be used for cleaning of hard surfaces and remove the sprays that household implements goes mouldy according to the present invention's preparation:

Mannase	0.005
Mannase	0.005	Amylase	0.01
Proteolytic enzyme	0.01	Amylase	0.01
Proteolytic enzyme	0.01	Sodium octyl sulfate	2.0
Sodium lauryl sulphate	4.0	Sodium octyl sulfate	2.0
Sodium lauryl sulphate	4.0	Sodium hydroxide	0.8
Silicate	0.04	Sodium hydroxide	0.8
Silicate	0.04	Diethylene glycol monobutyl ether ^*	4.0
Spices	0.35	Diethylene glycol monobutyl ether ^*	4.0
Spices	0.35	Water/micro substance	To 100%

^*The Diethylene Glycol single-butyl ether

Embodiment 26

Prepare following individual layer effervesce tooth cleaning tablet according to the present invention:

	??I	??II
	??I	??II	Mannase	??0.0001	??0.0002
Amylase	??0.0005	??0.0005	Mannase	??0.0001	??0.0002
Amylase	??0.0005	??0.0005	Proteolytic enzyme	??0.05	??2.0
Sodium bicarbonate	??39.0	??39.0	Proteolytic enzyme	??0.05	??2.0
Sodium bicarbonate	??39.0	??39.0	Oxysuccinic acid	??14.0	??14.0
Thionamic acid	??3.0	??3.0	Oxysuccinic acid	??14.0	??14.0
Thionamic acid	??3.0	??3.0	??TAED	??2.0	??2.0
Dyestuff/flavouring agent	??2.0	??2.0	??TAED	??2.0	??2.0
Dyestuff/flavouring agent	??2.0	??2.0	??PB1	??16.0	??16.0
??EDTA	??3.0	??3.0	??PB1	??16.0	??16.0
??EDTA	??3.0	??3.0	??PEG?10000	??6.0	??6.0
One Potassium Persulphate	??13.0	??13.0	??PEG?10000	??6.0	??6.0
One Potassium Persulphate	??13.0	??13.0	??LAS	??1.0	??1.0
Heat is given birth to silicon-dioxide	??1.0	??1.0	??LAS	??1.0	??1.0
Heat is given birth to silicon-dioxide	??1.0	??1.0	Miscellaneous and water	To 100%

Embodiment 27

Prepare following Dentrifice composition according to the present invention:

	??I	??II	??III	??IV
	??I	??II	??III	??IV	Sorbyl alcohol (70% aqueous solution)	??35.0	??35.0	??35.0	??35.0
??PEG-6	??1.0	??1.0	??1.0	??1.0	Sorbyl alcohol (70% aqueous solution)	??35.0	??35.0	??35.0	??35.0
??PEG-6	??1.0	??1.0	??1.0	??1.0	The silica dentifrice abrasives	??20.0	??20.0	??20.0	??20.0
Sodium Fluoride	??0.2	??0.2	??0.2	??0.2	The silica dentifrice abrasives	??20.0	??20.0	??20.0	??20.0
Sodium Fluoride	??0.2	??0.2	??0.2	??0.2	Titanium dioxide	??0.5	??0.5	??0.5	??0.5
Soluble saccharin	??0.3	??0.3	??0.3	??0.3	Titanium dioxide	??0.5	??0.5	??0.5	??0.5
Soluble saccharin	??0.3	??0.3	??0.3	??0.3	Mannase	??0.0001	??0.0001	??0.0001	??0.0001
Amylase	??0.0005	??0.005	??0.002	??0.0001	Mannase	??0.0001	??0.0001	??0.0001	??0.0001
Amylase	??0.0005	??0.005	??0.002	??0.0001	Proteolytic enzyme	??0.05	??0.1	??0.9	??2.0
Sodium alkyl sulfate (27.9% aqueous solution)	??4.0	??4.0	??4.0	??4.0	Proteolytic enzyme	??0.05	??0.1	??0.9	??2.0
Sodium alkyl sulfate (27.9% aqueous solution)	??4.0	??4.0	??4.0	??4.0	Flavouring agent	??1.0	??1.0	??1.0	??1.0
Carboxy vinyl polymer	??0.3	??0.3	??0.3	??0.3	Flavouring agent	??1.0	??1.0	??1.0	??1.0
Carboxy vinyl polymer	??0.3	??0.3	??0.3	??0.3	Carrageenin	??0.8	??0.8	??0.8	??0.8
Miscellaneous and water	To 100%				Carrageenin	??0.8	??0.8	??0.8	??0.8

Embodiment 28

Prepare following mouth wash shua according to the present invention:

	??I	??II	??III	??IV
	??I	??II	??III	??IV	??SDA?40?Alcohol	??8.0	??8.0	??8.0	??8.0
Flavouring agent	??0.08	??0.08	??0.08	??0.08	??SDA?40?Alcohol	??8.0	??8.0	??8.0	??8.0
Flavouring agent	??0.08	??0.08	??0.08	??0.08	Emulsifying agent	??0.08	??0.08	??0.08	??0.08
Sodium Fluoride	??0.05	??0.05	??0.05	??0.05	Emulsifying agent	??0.08	??0.08	??0.08	??0.08
Sodium Fluoride	??0.05	??0.05	??0.05	??0.05	Glycerine	??10.0	??10.0	??10.0	??10.0
Sweeting agent	??0.02	??0.02	??0.02	??0.02	Glycerine	??10.0	??10.0	??10.0	??10.0
Sweeting agent	??0.02	??0.02	??0.02	??0.02	Mannase	??0.0005	??0.0005	??0.0005	??0.0005
Amylase	??0.0005	??0.0005	??0.0005	??0.0005	Mannase	??0.0005	??0.0005	??0.0005	??0.0005
Amylase	??0.0005	??0.0005	??0.0005	??0.0005	Proteolytic enzyme	??0.01	??0.09	??0.2	??2.0
Phenylformic acid	??0.05	??0.05	??0.05	??0.05	Proteolytic enzyme	??0.01	??0.09	??0.2	??2.0
Phenylformic acid	??0.05	??0.05	??0.05	??0.05	Sodium hydroxide	??0.2	??0.2	??0.2	??0.2
Dyestuff	??0.04	??0.04	??0.04	??0.04	Sodium hydroxide	??0.2	??0.2	??0.2	??0.2
Dyestuff	??0.04	??0.04	??0.04	??0.04	Miscellaneous and water	To 100%

Embodiment 29

Prepare following soapy liquid personal cleansing composition according to the present invention:

	??I	??II
	??I	??II	Mannase	??0.001	??0.001
Amylase	??0.0004	??0.0004	Mannase	??0.001	??0.001
Amylase	??0.0004	??0.0004	Proteolytic enzyme	??0.10	??-
Soap (K or Na)	??15.0	??-	Proteolytic enzyme	??0.10	??-
Soap (K or Na)	??15.0	??-	30% lauroleate	??-	??-
30% myristate	??-	??-	30% lauroleate	??-	??-
30% myristate	??-	??-	25% palmitate	??-	??-
15% stearate	??-	??-	25% palmitate	??-	??-

Lipid acid (above-mentioned ratio)	4.5	-
Lipid acid (above-mentioned ratio)	4.5	-	Sodium lauryl sarcosinate	6.0	-
Zetesol NL	0.7	12.0	Sodium lauryl sarcosinate	6.0	-
Zetesol NL	0.7	12.0	Cocounut oil acyl aminopropyl trimethyl-glycine	1.3	3.0
Glycerine	15.0	-	Cocounut oil acyl aminopropyl trimethyl-glycine	1.3	3.0
Glycerine	15.0	-	Propylene glycol	9.0	-
Unister E 275 (EDTA)	1.5	0.4	Propylene glycol	9.0	-
Unister E 275 (EDTA)	1.5	0.4	Coconut oleoyl amine MEA	-	0.2
Spices	-	0.6	Coconut oleoyl amine MEA	-	0.2
Spices	-	0.6	^*Polyquaterium-7	-	0.1
The DMDM glycolylurea	-	0.14	^*Polyquaterium-7	-	0.1
The DMDM glycolylurea	-	0.14	Sodium Benzoate	-	0.25
EDTA four sodium dihydrates	-	0.1	Sodium Benzoate	-	0.25
EDTA four sodium dihydrates	-	0.1	Citric acid	-	0.1
Propylparaben	0.10	-	Citric acid	-	0.1
Propylparaben	0.10	-	Methyl p-hydroxybenzoate	0.20	-
Calcium sulfate	3.0	-	Methyl p-hydroxybenzoate	0.20	-
Calcium sulfate	3.0	-	Acetate	3.0	-
Water and micro substance	To 100%		Acetate	3.0	-
Water and micro substance	To 100%		KOH/NaOH (pH regulator)

^*The multipolymer of dimethyl dialkyl ammonium chloride and acrylamide

Embodiment 30

Prepare following personal cleansing bar bar composition according to the present invention:

Cocoyl ethylenehydrinsulfonic acid sodium 47.20

Ceterayl sodium sulfate 9.14

Paraffin 9.05

Soda soap (preparation on the spot) 3.67

Ethylenehydrinsulfonic acid sodium 5.51

Sodium-chlor 0.45

Titanium dioxide 0.4

EDTA trisodium 0.1

Sodium etidronate 0.1

Spices 1.20

Vitriol 0.87

Mannase 0.0001

Amylase 0.0002

Proteinase-10 .10

Miscellaneous and micro substance to 100%

Embodiment 31

Prepare the spices shampoo composite according to the present invention:

	??I	??II	??III	??IV	??V	??VI
	??I	??II	??III	??IV	??V	??VI	Lauryl ether-3-ammonium sulfate	??16.0	??18.0	??10.0	??16.0	??14.0	??18.0
Texapon Special	??5.0	??6.0	??3.0	??3.0	??4.0	??6.0	Lauryl ether-3-ammonium sulfate	??16.0	??18.0	??10.0	??16.0	??14.0	??18.0
Texapon Special	??5.0	??6.0	??3.0	??3.0	??4.0	??6.0	Sodium lauryl sarcosinate	??-	??-	??2.0	??-	??-	??-
Coconut oleoyl amine MEA	??1.0	??-	??-	??1.0	??0.6	??-	Sodium lauryl sarcosinate	??-	??-	??2.0	??-	??-	??-
Coconut oleoyl amine MEA	??1.0	??-	??-	??1.0	??0.6	??-	??Dimethicone ??40/60	??0.8	??1.0	??0.4	??3.0	??2.0	??1.0
??Polyquatenium- ??10	??-	??-	??0.01	??-	??0.2	??-	??Dimethicone ??40/60	??0.8	??1.0	??0.4	??3.0	??2.0	??1.0
??Polyquatenium- ??10	??-	??-	??0.01	??-	??0.2	??-	Cetyl alcohol	??0.5	??0.4	??-	??0.4	??0.4	??0.1
Stearyl alcohol	??-	??0.2	??-	??0.5	??0.1	??0.2	Cetyl alcohol	??0.5	??0.4	??-	??0.4	??0.4	??0.1
Stearyl alcohol	??-	??0.2	??-	??0.5	??0.1	??0.2	The panthenyl ethyl ether	??0.2	??-	??-	??0.2	??0.2	??0.2
Panthenol 10%	??-	??0.03	??-	??0.03	??-	??-	The panthenyl ethyl ether	??0.2	??-	??-	??0.2	??0.2	??0.2
Panthenol 10%	??-	??0.03	??-	??0.03	??-	??-	Tallow	??-	??-	??-	??-	??-	??0.5
Mineral oil	??-	??-	??-	??-	??0.5	??-	Tallow	??-	??-	??-	??-	??-	??0.5
Mineral oil	??-	??-	??-	??-	??0.5	??-	EDTA four sodium	??0.09	??0.09	??0.07	??0.09	??0.09	??0.09

The DMDM glycolylurea	0.14	0.14	0.14	0.12	0.14	0.14
The DMDM glycolylurea	0.14	0.14	0.14	0.12	0.14	0.14	Sodium Benzoate	0.25	0.25	-	0.25	0.25	0.25
Citrate trianion	1.0	-	-	1.0	1.0	-	Sodium Benzoate	0.25	0.25	-	0.25	0.25	0.25
Citrate trianion	1.0	-	-	1.0	1.0	-	Citric acid	0.1	-	0.3	0.1	-	-
Sodium hydroxide	-	-	0.3	-	-	-	Citric acid	0.1	-	0.3	0.1	-	-
Sodium hydroxide	-	-	0.3	-	-	-	Sodium phosphate	-	0.6	-	-	-	0.6
Di-Sodium Phosphate	-	0.2	-	-	-	0.2	Sodium phosphate	-	0.6	-	-	-	0.6
Di-Sodium Phosphate	-	0.2	-	-	-	0.2	Sodium-chlor	1.5	1.5	3.0	1.5	2.0	1.5
PEG-12	-	-	0.15	-	-	0.4	Sodium-chlor	1.5	1.5	3.0	1.5	2.0	1.5
PEG-12	-	-	0.15	-	-	0.4	Ammonium xylene sulfonate	0.4	0.4	-	0.4	0.4	0.4
Unister E 275	1.0	3.0	1.5	2.0	3.0	0.5	Ammonium xylene sulfonate	0.4	0.4	-	0.4	0.4	0.4
Unister E 275	1.0	3.0	1.5	2.0	3.0	0.5	The 2-mercaptopyridine zinc oxide	-	-	1.0	-	-	-
Amylase	0.001	0.001	0.001	0.001	0.001	0.001	The 2-mercaptopyridine zinc oxide	-	-	1.0	-	-	-
Amylase	0.001	0.001	0.001	0.001	0.001	0.001	Mannase	0.001	0.001	0.001	0.001	0.001	0.001
Spices	0.2	0.6	0.6	0.2	0.4	0.6	Mannase	0.001	0.001	0.001	0.001	0.001	0.001
Spices	0.2	0.6	0.6	0.2	0.4	0.6	Miscellaneous and water	To 100%

Sequence table

(1) physical data

(i) applicant:

(A) addressee: The Procter ﹠amp; Gamble Company

(B) street: One Procter ﹠amp; Gamble Plaza

(C) city: Cincinnati

(D) state: Ohio

(E) country: the U.S.

(F) postcode: 45202

(ii) denomination of invention: enzymatic cleaning compositions

(iii) sequence number: 6

(iv) computer-reader form:

(A) medium type: floppy disk

(B) computer: IBM PC compatible

(C) operating system: PC-DOS/MS-DOS

(D) software: PatentIn Release#1.0, version 1.25 (EPO)

(2) information of SEQ ID NO:1

(i) sequence signature

(A) length: 1407 base pairs

(B) type: nucleic acid

(C) chain: strand

(D) topology: linearity

(ii) molecule type: DNA genome

(iii) originate

(iv) feature:

(A) title/keyword: CDS

(B) position: 1-1482

( v ) ：SEQ ID NO：1ATGAAAAAAAAGTTATCACAGATTTATCATTTAATTATTTGCACACTTATAATAAGTGTGGGAATAATGGGGATTACAACGTCCCCATCAGCAGCAAGTACAGGCTTTTATGTTGATGGCAATACGTTATATGACGCAAATGGGCAGCCATTTGTCATGAGAGGTATTAACCATGGACATGCTTGGTATAAAGACACCGCTTCAACAGCTATTCCTGCCATTGCAGAGCAAGGCGCCAACACGATTCGTATTGTTTTATCAGATGGCGGTCAATGGGAAAAAGACGACATTGACACCATTCGTGAAGTCATTGAGCTTGCGGAGCAAAATAAAATGGTGGCTGTCGTTGAAGTTCATGATGCCACGGGTCGCGATTCGCGCAGTGATTTAAATCGAGCCGTTGATTATTGGATAGAAATGAAAGATGCGCTTATCGGTAAAGAAGATACGGTTATTATTAACATTGCAAACGAGTGGTATGGGAGTTGGGATGGCTCAGCTTGGGCCGATGGCTATATTGATGTCATTCCGAAGCTTCGCGATGCCGGCTTAACACACACCTTAATGGTTGATGCAGCAGGATGGGGGCAATATCCGCAATCTATTCATGATTACGGACAAGATGTGTTTAATGCAGATCCGTTAAAAAATACGATGTTCTCCATCCATATGTATGAGTATGCTGGTGGTGATGCTAACACTGTTAGATCAAATATTGATAGAGTCATAGATCAAGACCTTGCTCTCGTAATAGGTGAATTCGGTCATAGACATACTGATGGTGATGTTGATGAAGATACAATCCTTAGTTATTCTGAAGAAACTGGCACAGGGTGGCTCGCTTGGTCTTGGAAAGGCAACAGTACCGAATGGGACTATTTAGACCTTTCAGAAGACTGGGCTGGTCAACATTTAACTGATTGGGGGAATAGAATTGTCCACGGGGCCGATGGCTTACAGGAAACCTCCAAACCATCCACCGTATTTACAGATGATAACGGTGGTCACCCTGAACCGCCAACTGCTACTACCTTGTATGACTTTGAAGGAAGCACACAAGGGTGGCATGGAAGCAACGTGACCGGTGGCCCTTGGTCCGTAACAGAATGGGGTGCTTCAGGTAACTACTCTTTAAAAGCCGATGTAAATTTAACCTCAAATTCTTCACATGAACTGTATAGTGAACAAAGTCGTAATCTACACGGATACTCTCAGCTCAACGCAACCGTTCGCCATGCCAATTGGGGAAATCCCGGTAATGGCATGAATGCAAGACTTTACGTGAAAACGGGCTCTGATTATACATGGCATAGCGGTCCTTTTACACGTATCAATAGCTCCAACTCAGGAACAACGTTATCTTTTGATTTAAACAACATCGAAAATAGTCATCATGTTAGGGAAATAGGCGTGCAATTTTCAGCGGCAGATAATAGCAGTGGTCAAACTGCTCTATACGTTGATAACGTTACTTTAAGATAG

(3) information of SEQ ID NO:2

(i) sequence signature

(A) length: 493 amino acid

(B) type: amino acid

(C) topology: linearity

(ii) molecule type: protein

(iii) sequence description: SEQ ID NO:2MKKKLSQIYHLIICTLIISVGIMGITTSPSAASTGFYVDGNTLYDANGQPFV MRGINHGHAWYKDTASTAIPAIAEQGANTIRIVLSDGGQWEKDDIDTIREVIELAE QNKMVAWEVHDATGRDSRSDLNRAVDYWIEMKDALIGKEDTVIINIANEWYGSWDG SAWADGYIDVIPKLRDAGLTHTLMVDAAGWGQYPQSIHDYGQDVFNADPLKNTMFS IHMYEYAGGDANTVRSNIDRVIDQDLALVIGEFGHRHTDGDVDEDTILSYSEETGT GWLAWSWKGNSTEWDYLDLSEDWAGQHLTDWGNRIVHGADGLQETSKPSTVFTDDN GGHPEPPTATTLYDFEGSTQGWHGSNVTGGPWSVTEWGASGNYSLKADVNLTSNSS HELYSEQSRNLHGYSQLNATVRHANWGNPGNGMNARLYVKTGSDYTWHSGPFTRIN SSNSGTTLSFDLNNIENSHHVREIGVQFSAADNSSGQTALYVDNVTLR

(4) information of SEQ ID NO:3

(i) sequence signature

(A) length: 1407 base pairs

(B) type: nucleic acid

(C) chain: strand

(D) topology: linearity

(ii) molecule type: DNA genome

( iii ) ：SEQ ID NO：3ATGAAAAAAAAGTTATCACAGATTTATCATTTAATTATTTGCACACTTATAATAAGTGTGGGAATAATGGGGATTACAACGTCCCCATCAGCAGCAAGTACAGGCTTTTATGTTGATGGCAATACGTTATATGACGCAAATGGGCAGCCATTTGTCATGAGAGGTATTAACCATGGACATGCTTGGTATAAAGACACCGCTTCAACAGCTATTCCTGCCATTGCAGAGCAAGGCGCCAACACGATTCGTATTGTTTTATCAGATGGCGGTCAATGGGAAAAAGACGACATTGACACCATTCGTGAAGTCATTGAGCTTGCGGAGCAAAATAAAATGGTGGCTGTCGTTGAAGTTCATGATGCCACGGGTCGCGATTCGCGCAGTGATTTAAATCGAGCCGTTGATTATTGGATAGAAATGAAAGATGCGCTTATCGGTAAAGAAGATACGGTTATTATTAACATTGCAAACGAGTGGTATGGGAGTTGGGATGGCTCAGCTTGGGCCGATGGCTATATTGATGTCATTCCGAAGCTTCGCGATGCCGGCTTAACACACACCTTAATGGTTGATGCAGCAGGATGGGGGCAATATCCGCAATCTATTCATGATTACGGACAAGATGTGTTTAATGCAGATCCGTTAAAAAATACGATGTTCTCCATCCATATGTATGAGTATGCTGGTGGTGATGCTAACACTGTTAGATCAAATATTGATAGAGTCATAGATCAAGACCTTGCTCTCGTAATAGGTGAATTCGGTCATAGACATACTGATGGTGATGTTGATGAAGATACAATCCTTAGTTATTCTGAAGAAACTGGCACAGGGTGGCTCGCTTGGTCTTGGAAAGGCAACAGTACCGAATGGGACTATTTAGACCTTTCAGAAGACTGGGCTGGTCAACATTTAACTGATTGGGGGAATAGAATTGTCCACGGGGCCGATGGCTTACAGGAAACCTCCAAACCATCCACCGTATTTACAGATGATAACGGTGGTCACCCTGAACCGCCAACTGCTACTACCTTGTATGACTTTGAAGGAAGCACACAAGGGTGGCATGGAAGCAACGTGACCGGTGGCCCTTGGTCCGTAACAGAATGGGGTGCTTCAGGTAACTACTCTTTAAAAGCCGATGTAAATTTAACCTCAAATTCTTCACATGAACTGTATAGTGAACAAAGTCGTAATCTACACGGATACTCTCAGCTCAACGCAACCGTTCGCCATGCCAATTGGGGAAATCCCGGTAATGGCATGAATGCAAGACTTTACGTGAAAACGGGCTCTGATTATACATGGCATAGCGGTCCTTTACACGTATCAATAGCTCCAACTCAGGAACAACGTTATCTTTTGATTTAAACAACATCGAAAATATCATCATGTTAGGGAAATAG

(5) information of SEQ ID NO:4

(i) sequence signature

(A) length: 468 amino acid

(B) type: amino acid

(C) topology: linearity

(ii) molecule type: protein

(iii) sequence description: SEQ ID NO:4MKKKLSQIYHLIICTLIISVGIMGITTSPSAASTGFYVDGNTLYDANGQPFV MRGINHGHAWYKDTASTAIPAIAEQGANTIRIVLSDGGQWEKDDIDTIREVIELAE QNKMVAVVEVHDATGRDSRSDLNRAVDYWIEMKDALIGKEDTVIINIANEWYGSWD GSAWADGYIDVIPKLRDAGLTHTLMVDAAGWGQYPQSIHDYGQDVFNADPLKNTMF SIHMYEYAGGDANTVRSNIDRVIDQDLALVIGEFGHRHTDGDVDEDTILSYSEETG TGWLAWSWKGNSTEWDYLDLSEDWAGQHLTDWGNRIVHGADGLQETSKPSTVFTDD NGGHPEPPTATTLYDFEGSTQGWHGSNVTGGPWSVTEWGASGNYSLKADVNLTSNS SHELYSEQSRNLHGYSQLNATVRHANWGNPGNGMNARLYVKTGSDYTWHSGPFTRI NSSNSGTTLSFDLNNIENIIMLGK

(6) information of SEQ ID NO:5

(i) sequence signature

(A) length: 1029 base pairs

(B) type: nucleic acid

(C) chain: strand

(D) topology: linearity

(ii) molecule type: DNA genome

( iii ) ：SEQIDNO：55′ AAT TGG CGC ATA CTG TGT CGC CTG TGA ATC CTA ATG CCC AGCAGA CAA CAA AAA CAG TGA TGA ACT GGC TTG CGC ACC TGC CGA ACCGAA CGG AAA ACA GAG TCC TTT CCG GAG CGT TCG GAG GTT ACA GCCATG ACA CAT TTT CTA TGG CTG AGG CTG ATA GAA TCC GAA GCG CCACCG GGC AAT CGC CTG CTA TTT ATG GCT GCG ATT ATG CCA GAG GATGGC TTG AAA CAG CAA ATA TTG AAG ATT CAA TAG ATG TAA GCT GCAACG GCG ATT TAA TGT CGT ATT GGA AAA ATG GCG GAA TTC CGC AAATCA GTT TGC ACC TGG CGA ACC CTG CTT TTC AGT CAG GGC ATT TTAAAA CAC CGA TTA CAA ATG ATC AGT ATA AAA ACA TAT TAG ATT CAGCAA CAG CGG AAG GGA AGC GGC TAA ATG CCA TGC TCA GCA AAA TTGCTG ACG GAC TTC AAG AGT TGG AGA ACC AAG GTG TGC CTG TTC TGTTCA GGC CGC TGC ATG AAA TGA ACG GCG AAT GGT TTT GGT GGG GACTCA CAT CAT ATA ACC AAA AGG ATA ATG AAA GAA TCT CTC TAT ATAAAC AGC TCT ACA AGA AAA TCT ATC ATT ATA TGA CCG ACA CAA GAGGAC TTG ATC ATT TGA TTT GGG TTT ACT CTC CCG ACG CCA ACC GAGATT TTA AAA CTG ATT TTT ACC CGG GCG CGT CTT ACG TGG ATA TTGTCG GAT TAG ATG CGT ATT TTC AAG ATG CCT ACT CGA TCA ATG GATACG ATC AGC TAA CAG CGC TTA ATA AAC CAT TTG CTT TTA CAG AAGTCG GCC CGC AAA CAG CAA ACG GCA GCT TCG ATT ACA GCC TGT TCATCA ATG CAA TAA AAC AAA AAT ATC CTA AAA CCA TTT ACT TTC TGGCAT GGA ATG ATG AAT GGA GCG CAG CAG TAA ACA AGG GTG CTT CAGCTT TAT ATC ATG ACA GCT GGA CAC TCA ACA AGG GAG AAA TAT GGAATG GTG ATT CTT TAA CGC CAA TCG TTG AGT GAA TCC GGG ATC 3′

(7) information of SEQ ID NO:6

(i) sequence signature

(A) length: 363 amino acid

(B) type: amino acid

(C) topology: linearity

(ii) molecule type: protein

(iii) sequence description: SEQ ID NO:6ydhT 1LFKKHTISLLIIFLLASAVLAKPIEAHTVSPVNPNAQQTTKTVMNWLAHL 50ydhT 51PNRTENRVLSGAFGGYSHDTFSMAEADRIRSATGQSPAIYGCDYARGWLE 100ydhT 101TANIEDSIDVSCNGDLMSYWKNGGIPQISLHLANPAFQSGHFKTPITNDQ 150ydhT 151YKNILDSATAEGKRLNAMLSKIADGLQELENQGVPVLFRPLHEMNGEWFW 200ydhT 201WGLTSYNQKDNERISLYKQLYKKIYHYMTDTRGLDHLIWVYSPDANRDFK 250ydhT 251TDFYPGASYVDIVGLDAYFQDAYSINGYDQLTALNKPFAFTEVGPQTANG 300ydhT 301SFDYSLFINAIKQKYPKTIYFLAWNDEWSAAVNKGASALYHDSWTLNKGE 350ydhT 351IWNGDSLTPIVE^*.363

Claims

1. one kind comprises a kind of detergent ingredients, a kind of mannase and a kind of cleaning compositions that is selected from cellulase, amylase, pectin degrading enzyme, xyloglucanase enzymes and/or its mixture.

2. according to the cleaning compositions of claim 1, wherein said mannase is with the 0.0001-2% (weight) that accounts for total composition, preferred 0.0005-0.5% (weight), the more preferably level existence of the pure enzyme of 0.001-0.02% (weight).

3. according to the cleaning compositions of claim 1 to 2, wherein said cellulase, pectin degrading enzyme, xyloglucanase enzymes are with the 0.0001-2% (weight) that accounts for total composition, preferred 0.0005-0.5% (weight), the more preferably level existence of the pure enzyme of 0.001-0.1% (weight).

4. according to the cleaning compositions of claim 1 to 3, wherein said carbohydrase is a kind of amylase (the preferably amylase of selling with the trade(brand)name of Termamyl, Duramyl, Maxamyl), show alpha-amylase variants and/or its mixture of the thermostability with increase described in SEQID No.2 among the WO96/23873.

5. according to the cleaning compositions of claim 4, wherein said amylase is with the 0.0001-2% (weight) that accounts for total composition, preferred 0.00018-0.06% (weight), the more preferably level existence of the pure enzyme of 0.00024-0.048% (weight).

6. according to the cleaning compositions of claim 1 to 5, wherein said carbohydrase is a kind of cellulase, preferably comes from the 43kD cellulase of Humicola insolens DSM 1800.

7. according to each cleaning compositions of aforementioned claim, also comprise a kind of tensio-active agent that is selected from nonionogenic tenside, anion surfactant, cats product and/or its mixture.

8. according to each cleaning compositions of aforementioned claim, also comprise a kind of SYNTHETIC OPTICAL WHITNER.

9. according to each cleaning compositions of aforementioned claim, also comprise a kind of auxiliary agent, the auxiliary agent of preferred zeolite A, layered silicate, tripoly phosphate sodium STPP and/or its mixture.

10. mannase and the carbohydrase that is selected from cellulase, amylase, pectin degrading enzyme, xyloglucanase enzymes and/or its mixture are in the purposes that is used for the cleaning compositions that clean fabric and/or textile stains remove.

11. mannase and be selected from the purposes of the carbohydrase of cellulase, amylase, pectin degrading enzyme, xyloglucanase enzymes and/or its mixture at the cleaning compositions that is used for cleaning of hard surfaces such as floor, wall, bathroom tile etc.

12. mannase and the carbohydrase that is selected from cellulase, amylase, pectin degrading enzyme, xyloglucanase enzymes and/or its mixture are being used for hand-washing and the purposes of the cleaning compositions of the tableware of machine-washing.

13. mannase and the carbohydrase that is selected from cellulase, amylase, pectin degrading enzyme, xyloglucanase enzymes and/or its mixture are in the purposes that is used for the cleaning compositions aspect oral cavity, tooth, contact lens and the personal cleanliness.