WO1998030669A1 - Protease- und amylasehaltiges waschmittel - Google Patents
Protease- und amylasehaltiges waschmittel Download PDFInfo
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- WO1998030669A1 WO1998030669A1 PCT/EP1997/007171 EP9707171W WO9830669A1 WO 1998030669 A1 WO1998030669 A1 WO 1998030669A1 EP 9707171 W EP9707171 W EP 9707171W WO 9830669 A1 WO9830669 A1 WO 9830669A1
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- Prior art keywords
- weight
- protease
- amylase
- amino acid
- mutant
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- ZOKXTWBITQBERF-UHFFFAOYSA-N Molybdenum Chemical compound [Mo] ZOKXTWBITQBERF-UHFFFAOYSA-N 0.000 description 1
- 229910000503 Na-aluminosilicate Inorganic materials 0.000 description 1
- KVYWNGXWIPNBMD-UHFFFAOYSA-N O1CC=CC1.C(CO)O Chemical compound O1CC=CC1.C(CO)O KVYWNGXWIPNBMD-UHFFFAOYSA-N 0.000 description 1
- BPQQTUXANYXVAA-UHFFFAOYSA-N Orthosilicate Chemical compound [O-][Si]([O-])([O-])[O-] BPQQTUXANYXVAA-UHFFFAOYSA-N 0.000 description 1
- 102000004316 Oxidoreductases Human genes 0.000 description 1
- 108090000854 Oxidoreductases Proteins 0.000 description 1
- 108700020962 Peroxidase Proteins 0.000 description 1
- 102000003992 Peroxidases Human genes 0.000 description 1
- ABLZXFCXXLZCGV-UHFFFAOYSA-N Phosphorous acid Chemical class OP(O)=O ABLZXFCXXLZCGV-UHFFFAOYSA-N 0.000 description 1
- LGRFSURHDFAFJT-UHFFFAOYSA-N Phthalic anhydride Natural products C1=CC=C2C(=O)OC(=O)C2=C1 LGRFSURHDFAFJT-UHFFFAOYSA-N 0.000 description 1
- 229920000805 Polyaspartic acid Polymers 0.000 description 1
- 229920000388 Polyphosphate Polymers 0.000 description 1
- 241000589630 Pseudomonas pseudoalcaligenes Species 0.000 description 1
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
- CDBYLPFSWZWCQE-UHFFFAOYSA-L Sodium Carbonate Chemical compound [Na+].[Na+].[O-]C([O-])=O CDBYLPFSWZWCQE-UHFFFAOYSA-L 0.000 description 1
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 1
- 241000187392 Streptomyces griseus Species 0.000 description 1
- KDYFGRWQOYBRFD-UHFFFAOYSA-N Succinic acid Natural products OC(=O)CCC(O)=O KDYFGRWQOYBRFD-UHFFFAOYSA-N 0.000 description 1
- FEWJPZIEWOKRBE-UHFFFAOYSA-N Tartaric acid Natural products [H+].[H+].[O-]C(=O)C(O)C(O)C([O-])=O FEWJPZIEWOKRBE-UHFFFAOYSA-N 0.000 description 1
- 241000223258 Thermomyces lanuginosus Species 0.000 description 1
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 1
- 239000004473 Threonine Substances 0.000 description 1
- RTAQQCXQSZGOHL-UHFFFAOYSA-N Titanium Chemical compound [Ti] RTAQQCXQSZGOHL-UHFFFAOYSA-N 0.000 description 1
- XTXRWKRVRITETP-UHFFFAOYSA-N Vinyl acetate Chemical compound CC(=O)OC=C XTXRWKRVRITETP-UHFFFAOYSA-N 0.000 description 1
- QYKIQEUNHZKYBP-UHFFFAOYSA-N Vinyl ether Chemical class C=COC=C QYKIQEUNHZKYBP-UHFFFAOYSA-N 0.000 description 1
- UAOKXEHOENRFMP-ZJIFWQFVSA-N [(2r,3r,4s,5r)-2,3,4,5-tetraacetyloxy-6-oxohexyl] acetate Chemical compound CC(=O)OC[C@@H](OC(C)=O)[C@@H](OC(C)=O)[C@H](OC(C)=O)[C@@H](OC(C)=O)C=O UAOKXEHOENRFMP-ZJIFWQFVSA-N 0.000 description 1
- 150000001253 acrylic acids Chemical class 0.000 description 1
- 239000013543 active substance Substances 0.000 description 1
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- 229960003767 alanine Drugs 0.000 description 1
- 235000004279 alanine Nutrition 0.000 description 1
- 125000001931 aliphatic group Chemical group 0.000 description 1
- 229910001854 alkali hydroxide Inorganic materials 0.000 description 1
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- 125000005011 alkyl ether group Chemical group 0.000 description 1
- 125000005263 alkylenediamine group Polymers 0.000 description 1
- BJEPYKJPYRNKOW-UHFFFAOYSA-N alpha-hydroxysuccinic acid Natural products OC(=O)C(O)CC(O)=O BJEPYKJPYRNKOW-UHFFFAOYSA-N 0.000 description 1
- JFCQEDHGNNZCLN-UHFFFAOYSA-N anhydrous glutaric acid Natural products OC(=O)CCCC(O)=O JFCQEDHGNNZCLN-UHFFFAOYSA-N 0.000 description 1
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- 125000004429 atom Chemical group 0.000 description 1
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- 239000007853 buffer solution Substances 0.000 description 1
- KDYFGRWQOYBRFD-NUQCWPJISA-N butanedioic acid Chemical compound O[14C](=O)CC[14C](O)=O KDYFGRWQOYBRFD-NUQCWPJISA-N 0.000 description 1
- JHIWVOJDXOSYLW-UHFFFAOYSA-N butyl 2,2-difluorocyclopropane-1-carboxylate Chemical compound CCCCOC(=O)C1CC1(F)F JHIWVOJDXOSYLW-UHFFFAOYSA-N 0.000 description 1
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- 150000001244 carboxylic acid anhydrides Chemical class 0.000 description 1
- 239000008112 carboxymethyl-cellulose Substances 0.000 description 1
- 239000000969 carrier Substances 0.000 description 1
- 239000005018 casein Substances 0.000 description 1
- BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical compound NCCCCC(C(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(CC(C)C)N=C(O)C(CCC(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(C(C)O)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(COP(O)(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(N)CC1=CC=CC=C1 BECPQYXYKAMYBN-UHFFFAOYSA-N 0.000 description 1
- 235000021240 caseins Nutrition 0.000 description 1
- 230000003197 catalytic effect Effects 0.000 description 1
- 150000001768 cations Chemical class 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 235000011967 chocolate pudding Nutrition 0.000 description 1
- 238000004140 cleaning Methods 0.000 description 1
- 239000011248 coating agent Substances 0.000 description 1
- 238000000576 coating method Methods 0.000 description 1
- 238000001816 cooling Methods 0.000 description 1
- 108010005400 cutinase Proteins 0.000 description 1
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 1
- 238000004851 dishwashing Methods 0.000 description 1
- 239000000975 dye Substances 0.000 description 1
- 239000003792 electrolyte Substances 0.000 description 1
- 230000000058 esterolytic effect Effects 0.000 description 1
- 150000002148 esters Chemical class 0.000 description 1
- 150000002170 ethers Chemical class 0.000 description 1
- 125000004494 ethyl ester group Chemical group 0.000 description 1
- 239000013613 expression plasmid Substances 0.000 description 1
- 238000001125 extrusion Methods 0.000 description 1
- 150000002191 fatty alcohols Chemical class 0.000 description 1
- 238000000855 fermentation Methods 0.000 description 1
- 230000004151 fermentation Effects 0.000 description 1
- 239000003205 fragrance Substances 0.000 description 1
- 235000012209 glucono delta-lactone Nutrition 0.000 description 1
- 229960003681 gluconolactone Drugs 0.000 description 1
- 229960002449 glycine Drugs 0.000 description 1
- 125000001046 glycoluril group Chemical group [H]C12N(*)C(=O)N(*)C1([H])N(*)C(=O)N2* 0.000 description 1
- 238000005469 granulation Methods 0.000 description 1
- 230000003179 granulation Effects 0.000 description 1
- 108010002430 hemicellulase Proteins 0.000 description 1
- 229920001519 homopolymer Polymers 0.000 description 1
- 230000007062 hydrolysis Effects 0.000 description 1
- 238000006460 hydrolysis reaction Methods 0.000 description 1
- 230000003301 hydrolyzing effect Effects 0.000 description 1
- 150000002440 hydroxy compounds Chemical class 0.000 description 1
- 230000001771 impaired effect Effects 0.000 description 1
- 230000002779 inactivation Effects 0.000 description 1
- 229910052500 inorganic mineral Inorganic materials 0.000 description 1
- 150000002500 ions Chemical class 0.000 description 1
- 229960000310 isoleucine Drugs 0.000 description 1
- 235000014705 isoleucine Nutrition 0.000 description 1
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 1
- 150000003951 lactams Chemical class 0.000 description 1
- 239000004310 lactic acid Substances 0.000 description 1
- 235000014655 lactic acid Nutrition 0.000 description 1
- 239000003446 ligand Substances 0.000 description 1
- 235000019421 lipase Nutrition 0.000 description 1
- 159000000003 magnesium salts Chemical class 0.000 description 1
- 229910052943 magnesium sulfate Inorganic materials 0.000 description 1
- 235000019341 magnesium sulphate Nutrition 0.000 description 1
- VZCYOOQTPOCHFL-UPHRSURJSA-N maleic acid Chemical compound OC(=O)\C=C/C(O)=O VZCYOOQTPOCHFL-UPHRSURJSA-N 0.000 description 1
- 239000011976 maleic acid Substances 0.000 description 1
- 150000002689 maleic acids Chemical class 0.000 description 1
- 239000001630 malic acid Substances 0.000 description 1
- 235000011090 malic acid Nutrition 0.000 description 1
- 150000002696 manganese Chemical class 0.000 description 1
- 239000000594 mannitol Substances 0.000 description 1
- 235000010355 mannitol Nutrition 0.000 description 1
- 238000004519 manufacturing process Methods 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 125000005395 methacrylic acid group Chemical class 0.000 description 1
- 125000001360 methionine group Chemical group N[C@@H](CCSC)C(=O)* 0.000 description 1
- XJRBAMWJDBPFIM-UHFFFAOYSA-N methyl vinyl ether Chemical class COC=C XJRBAMWJDBPFIM-UHFFFAOYSA-N 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- 235000013336 milk Nutrition 0.000 description 1
- 239000008267 milk Substances 0.000 description 1
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- 239000011707 mineral Substances 0.000 description 1
- 235000010755 mineral Nutrition 0.000 description 1
- 238000000302 molecular modelling Methods 0.000 description 1
- 150000005673 monoalkenes Chemical class 0.000 description 1
- 150000002762 monocarboxylic acid derivatives Chemical class 0.000 description 1
- 150000004682 monohydrates Chemical class 0.000 description 1
- 238000002703 mutagenesis Methods 0.000 description 1
- 231100000350 mutagenesis Toxicity 0.000 description 1
- 230000035772 mutation Effects 0.000 description 1
- MGFYIUFZLHCRTH-UHFFFAOYSA-N nitrilotriacetic acid Chemical compound OC(=O)CN(CC(O)=O)CC(O)=O MGFYIUFZLHCRTH-UHFFFAOYSA-N 0.000 description 1
- QJGQUHMNIGDVPM-UHFFFAOYSA-N nitrogen group Chemical group [N] QJGQUHMNIGDVPM-UHFFFAOYSA-N 0.000 description 1
- JRZJOMJEPLMPRA-UHFFFAOYSA-N olefin Natural products CCCCCCCC=C JRZJOMJEPLMPRA-UHFFFAOYSA-N 0.000 description 1
- 150000007524 organic acids Chemical class 0.000 description 1
- 235000005985 organic acids Nutrition 0.000 description 1
- 150000004967 organic peroxy acids Chemical class 0.000 description 1
- 239000007800 oxidant agent Substances 0.000 description 1
- PATMLLNMTPIUSY-UHFFFAOYSA-N phenoxysulfonyl 7-methyloctanoate Chemical compound CC(C)CCCCCC(=O)OS(=O)(=O)OC1=CC=CC=C1 PATMLLNMTPIUSY-UHFFFAOYSA-N 0.000 description 1
- 229910052615 phyllosilicate Inorganic materials 0.000 description 1
- 108010064470 polyaspartate Proteins 0.000 description 1
- 229920005646 polycarboxylate Polymers 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 239000001205 polyphosphate Substances 0.000 description 1
- 235000011176 polyphosphates Nutrition 0.000 description 1
- 229920001296 polysiloxane Polymers 0.000 description 1
- 239000001267 polyvinylpyrrolidone Substances 0.000 description 1
- 229920000036 polyvinylpyrrolidone Polymers 0.000 description 1
- 235000013855 polyvinylpyrrolidone Nutrition 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 230000002028 premature Effects 0.000 description 1
- UIIIBRHUICCMAI-UHFFFAOYSA-N prop-2-ene-1-sulfonic acid Chemical compound OS(=O)(=O)CC=C UIIIBRHUICCMAI-UHFFFAOYSA-N 0.000 description 1
- 229940024999 proteolytic enzymes for treatment of wounds and ulcers Drugs 0.000 description 1
- 239000011541 reaction mixture Substances 0.000 description 1
- 239000004576 sand Substances 0.000 description 1
- 229920006395 saturated elastomer Polymers 0.000 description 1
- 150000004671 saturated fatty acids Chemical class 0.000 description 1
- 235000003441 saturated fatty acids Nutrition 0.000 description 1
- 239000003352 sequestering agent Substances 0.000 description 1
- 229960001153 serine Drugs 0.000 description 1
- 235000004400 serine Nutrition 0.000 description 1
- 239000001632 sodium acetate Substances 0.000 description 1
- 235000017281 sodium acetate Nutrition 0.000 description 1
- 235000012217 sodium aluminium silicate Nutrition 0.000 description 1
- NTHWMYGWWRZVTN-UHFFFAOYSA-N sodium silicate Chemical compound [Na+].[Na+].[O-][Si]([O-])=O NTHWMYGWWRZVTN-UHFFFAOYSA-N 0.000 description 1
- 229910052911 sodium silicate Inorganic materials 0.000 description 1
- 239000000600 sorbitol Substances 0.000 description 1
- 238000001694 spray drying Methods 0.000 description 1
- 238000010561 standard procedure Methods 0.000 description 1
- 150000005846 sugar alcohols Polymers 0.000 description 1
- 230000019635 sulfation Effects 0.000 description 1
- 238000005670 sulfation reaction Methods 0.000 description 1
- BDHFUVZGWQCTTF-UHFFFAOYSA-M sulfonate Chemical compound [O-]S(=O)=O BDHFUVZGWQCTTF-UHFFFAOYSA-M 0.000 description 1
- 238000006277 sulfonation reaction Methods 0.000 description 1
- 125000001273 sulfonato group Chemical group [O-]S(*)(=O)=O 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 230000009885 systemic effect Effects 0.000 description 1
- 239000011975 tartaric acid Substances 0.000 description 1
- 235000002906 tartaric acid Nutrition 0.000 description 1
- 229920001897 terpolymer Polymers 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 229960002898 threonine Drugs 0.000 description 1
- VZCYOOQTPOCHFL-UHFFFAOYSA-N trans-butenedioic acid Natural products OC(=O)C=CC(O)=O VZCYOOQTPOCHFL-UHFFFAOYSA-N 0.000 description 1
- 150000003623 transition metal compounds Chemical class 0.000 description 1
- 150000003918 triazines Chemical class 0.000 description 1
- YNJBWRMUSHSURL-UHFFFAOYSA-N trichloroacetic acid Chemical compound OC(=O)C(Cl)(Cl)Cl YNJBWRMUSHSURL-UHFFFAOYSA-N 0.000 description 1
- 150000004670 unsaturated fatty acids Chemical class 0.000 description 1
- 235000021122 unsaturated fatty acids Nutrition 0.000 description 1
- GPPXJZIENCGNKB-UHFFFAOYSA-N vanadium Chemical compound [V]#[V] GPPXJZIENCGNKB-UHFFFAOYSA-N 0.000 description 1
- 229920001567 vinyl ester resin Polymers 0.000 description 1
- 125000000391 vinyl group Chemical group [H]C([*])=C([H])[H] 0.000 description 1
- 210000002268 wool Anatomy 0.000 description 1
- 238000012982 x-ray structure analysis Methods 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
- C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
- C12N9/2405—Glucanases
- C12N9/2408—Glucanases acting on alpha -1,4-glucosidic bonds
- C12N9/2411—Amylases
- C12N9/2414—Alpha-amylase (3.2.1.1.)
- C12N9/2417—Alpha-amylase (3.2.1.1.) from microbiological source
-
- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
- C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
- C11D3/16—Organic compounds
- C11D3/38—Products with no well-defined composition, e.g. natural products
- C11D3/386—Preparations containing enzymes, e.g. protease or amylase
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
- C12N9/52—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from bacteria or Archaea
- C12N9/54—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from bacteria or Archaea bacteria being Bacillus
Definitions
- the present invention relates to enzyme-containing detergents which, in addition to the usual constituents, contain a certain protease and a certain amylase.
- Enzymes are used extensively in washing, auxiliary washing and cleaning agents.
- proteases from the subtilisin family are used. These are extracellular proteins with a molecular weight in the range from approximately 20,000 to 45,000.
- Subtilisins are relatively unspecific enzymes which, in addition to the hydrolytic effect on peptide bonds, also have esterolytic properties (M. Bahn, RD Schmidt, Biotec j_, 119, 1987).
- Many representatives of the subtilisins are precisely characterized physically and chemically. Their spatial structure is often known in detail through X-ray structure analysis. This provides the prerequisites for molecular modeling and so-called protein engineering in the form of targeted mutagenesis (Kraut, Ann. Rev. Biochem.
- proteases have been widely described; in June 1991, 219 protein variants of the subtilisins obtained by protein engineering were already known (A. Recktenwald et al., J.Biotechnol. 28, 1-23, 1993). Most of these variants were created to improve the stability of the proteases.
- a protease from the subtilisin family that is stable and active under strongly alkaline conditions can be produced in Bacillus lentus (DSM 5483) as described in international patent application WO 91/02792.
- This Bacillus lentus alkaline protease (BLAP) can be produced by fermentation of Bacillus licheniformis which has been transformed with an expression plasmid which carries the gene for BLAP under the control of the Bacillus licheniformis ATCC 53926 promoter.
- the composition as well as the spatial structure of BLAP is known (DW Godette et al. J. Mol. Biol. 228, 580-595, 1992).
- protease is characterized by the sequence of 269 amino acids described in the cited literature, a calculated molecular weight of 26,823 daltons and a theoretical isoelectric point of 9.7. Variants of this Bacillus lentus DSM 5483 protease accessible by mutation are described in US Pat. No. 5,340,735. Among these are protease enzymes, which in particular with multiple washing treatment of Textiles made of proteinogenic fibers, for example textile fabrics made of natural silk or wool, lead to particularly low substance damage or destruction of the fiber dressings without loss of cleaning performance.
- Amylases have the task of facilitating the removal of starchy soiling by the catalytic hydrolysis of the starch polysaccharide and have also been used for a long time in dishwashing detergents, but also in detergents. It has been observed that the performance of amylases, which correspond to the enzymes found in nature, is relatively severely impaired by bleaching agents usually contained in such agents. In addition to increasing their performance, the genetic modification of amylases essentially aims to increase the stability against attack by oxidants.
- the invention therefore relates to a protease- and amylase-containing textile detergent which, in addition to the usual ingredients compatible with such enzymes, is a mutant protease in which, at position 211 (BLAP count), the amino acid leucine present at this point in the wild-type protease is replaced by aspartic acid or glutamic acid and an amylase mutant in which at least one methionine, tryptophan, cysteine or tyrosine present in the wild-type amylase is removed or through another amino acid is exchanged, which in particular is not cysteine or methionine.
- the agent preferably has a proteolytic activity in the range from about 100 PE / g to about 7500 PE / g, in particular 500 PE / g to 5000 PE / g.
- the protease activity is determined according to the standardized method described below, as described in Tenside 7 (1970), 125: A solution containing 12 g / 1 casein and 30 mM sodium tripolyphosphate in water of 15 ° dH hardness (containing 0.058% by weight CaCl 2 2 H 2 O, 0.028% by weight MgCl 2 6 H 2 O and 0.042% by weight NaHCO 3 ) is heated to 70 ° C., the pH is adjusted to 8 by adding 0.1 N NaOH, 5 set at 50 ° C.
- the absorption of this solution at 290 nm is determined with the aid of an absorption spectrometer, the absorption zero value being obtained by measuring a centrifuged solution which is prepared by mixing 600 ml of the above-mentioned TCA solution with 600 ml of the above-mentioned substrate solution and then adding the enzyme solution determine is.
- the proteolytic activity of a protease solution which causes an absorption of 0.500 OD under the specified measurement conditions, is defined as 10 PE (protease units) per ml.
- the agent preferably has an amylolytic activity of 50 NU / g to 1000 NU / g, in particular 75 NU / g to 750 NU / g ("Novo units" per gram according to the Novo standard method, 1 kilo Novo unit is the amount of enzyme that breaks down 5.26 g of starch at pH 5.6 and 37 ° C., based on that from P. Bernfeld in SP Colowick and ND Kaplan, Methods in Enzymology, Volume 1, 1955, page 149 described method).
- proteases which can be used according to the invention include genetically modified proteases of the abovementioned BLAP type, in which, in position 21 1 (BLAP count), the amino acid leucine (L in the customary one-letter code) present in the wild-type protease at this point against aspartic acid (D) or glutamic acid (E) is exchanged (L211D or L211E). These can be produced as described in international patent application WO 95/23221.
- other changes to the original Bacillus lentus protease such as at least one of the amino acid exchanges S3T, V4I, R99G, R99A, R99S, A188P, V193M and / or V199I, may have been made.
- Particularly preferred is the variant listed as F49 in the international patent application mentioned, in which the amino acid exchanges
- amylases which can be used according to the invention include, in particular, genetically modified amylases which, by replacing the methionine in position 197 with another amino acid, in particular leucine, threonine, alanine, glycine, serine, isoleucine, asparagine or aspartic acid, are derived from the ⁇ - found in Bacillus licheniformis Derive amylase (wild-type amylase). Analogous to the nomenclature described above for proteases, these amylases are designated as M197L, M197T, M197A, M197G, M197S, Ml 971, M197N and M197D.
- Wild-type amylases from other microorganisms such as Bacillus amyloliquefaciens or Bacillus stearothermophilus, whose amino acid sequence homology to Bacillus licheniformis amylase is known from international patent application WO 94/18314, can be used according to the invention.
- Commercial genetically modified amylases in the sense of the invention are, for example, Duramyl® from Novo Nordisk and Purafect® OxAm from Genencor International.
- the combination of genetically modified protease and genetically modified amylase which is essential to the invention, can be achieved by incorporating the two separate or, in a known manner, separately assembled enzymes or by means of protease and amylase made up together in a granulate, as for example from international patent applications WO 96/00772 or WO 96 / Known 00773 can be used in detergents according to the invention.
- the detergents according to the invention which can be present in particular as powdery solids, in post-compacted particle form, as homogeneous solutions or suspensions, can in principle contain all known ingredients which are customary in such compositions.
- the agents according to the invention can in particular builder substances, surface-active surfactants, bleaching agents based on organic and / or inorganic peroxygen compounds, bleach activators, water-miscible organic solvents, additional enzymes, sequestering agents, electrolytes, pH regulators and further auxiliaries, such as optical brighteners, graying inhibitors, color transfer inhibitors, foam regulators, Contain dyes and fragrances.
- the agents according to the invention can contain surfactants, anionic surfactants, nonionic surfactants and mixtures thereof being particularly suitable.
- Suitable nonionic surfactants are, in particular, alkyl glycosides and ethoxylation and / or propoxylation products of alkyl glycosides or linear or branched alcohols each having 12 to 18 carbon atoms in the alkyl part and 3 to 20, preferably 4 to 10, alkyl ether groups.
- corresponding ethoxylation and / or propoxylation products of N-alkylamines, vicinal diols, fatty acid esters and fatty acid amides are the in terms of the alkyl part correspond to the long-chain alcohol derivatives mentioned, and of alkylphenols having 5 to 12 carbon atoms in the alkyl radical.
- Suitable anionic surfactants are, in particular, soaps and those which contain sulfate or sulfonate groups with preferably alkali ions as cations.
- Usable soaps are preferably the alkali salts of saturated or unsaturated fatty acids with 12 to 18 carbon atoms. Such fatty acids can also be used in a form that is not completely neutralized.
- the surfactants of the sulfate type which can be used include the salts of the sulfuric acid half-esters of fatty alcohols having 12 to 18 carbon atoms and the sulfation products of the nonionic surfactants mentioned with a low degree of ethoxylation.
- the surfactants of the sulfonate type that can be used include linear alkylbenzenesulfonates with 9 to 14 carbon atoms in the alkyl part, alkanesulfonates with 12 to 18 carbon atoms, and olefin sulfonates with 12 to 18 carbon atoms, which are used in the reaction of corresponding monoolefins with sulfur trioxide arise, as well as alpha-sulfofatty acid esters, which arise in the sulfonation of fatty acid methyl or ethyl esters.
- Surfactants are present in the detergents according to the invention in proportions of preferably 5% by weight to 50% by weight, in particular 8% by weight to 30% by weight.
- An agent according to the invention preferably contains at least one water-soluble and / or water-insoluble, organic and / or inorganic builder.
- the water-soluble organic builder substances include polycarboxylic acids, in particular citric acid and sugar acids, monomeric and polymeric aminopolycarboxylic acids, in particular methylglycinediacetic acid, nitrilotriacetic acid and ethylenediaminetetraacetic acid, and also polyaspartic acid, polyphosphonic acids, in particular aminotris (methylene-phosphinophenonic acid), ethylenediamine (1) ethylenediamine (1) 1 -diphosphonic acid, polymeric hydroxy compounds such as dextrin and polymeric (poly) carboxylic acids, in particular the polycarboxylates of international patent application WO 93/16110 or international patent application WO 92/18542 or European patent EP 0232 202, which are accessible by oxidation of polysaccharides or dextrins.
- the relative molecular weight of the homopolymers of unsaturated carboxylic acids is generally between 5,000 and 200,000, that of the copolymers between 2,000 and 200,000, preferably 50,000 to 120,000, in each case based on free acid.
- a particularly preferred acrylic acid-maleic acid copolymer has a relative molecular weight of 50,000 to 100,000.
- Suitable, albeit less preferred, compounds of this class are copolymers of acrylic acid or methacrylic acid with vinyl ethers, such as vinyl methyl ethers, vinyl esters, ethylene, propylene and styrene, in which the proportion of acid is at least 50% by weight.
- vinyl ethers such as vinyl methyl ethers, vinyl esters, ethylene, propylene and styrene
- Terpolymers can also be used as water-soluble organic builder substances which contain two unsaturated acids and / or their salts as monomers and vinyl alcohol and / or an esterified vinyl alcohol or a carbohydrate as the third monomer.
- the first acidic monomer or its salt is derived from a monoethylenically unsaturated C 3 -C 8 carboxylic acid and preferably from a C 3 -C monocarboxylic acid, in particular from (meth) acrylic acid.
- the second acidic monomer or its salt can be a derivative of a C -C 8 dicarboxylic acid, maleic acid being particularly preferred, and / or a derivative of an allylsulfonic acid which is substituted in the 2-position by an alkyl or aryl radical.
- Polymers of this type can be produced in particular by processes which are described in German patent specification DE 42 21 381 and German patent application DE 43 00 772 and generally have a relative molecular weight of between 1,000 and 200,000.
- copolymers are those which are described in German patent applications DE 43 03 320 and DE 44 17 734 and which preferably contain acrolein and acrylic acid / acrylic acid salts or vinyl acetate as monomers.
- the organic builder substances can be used, in particular for the production of liquid agents, in the form of aqueous solutions, preferably in the form of 30 to 50 percent by weight aqueous solutions. All of the acids mentioned are generally used in the form of their water-soluble salts, in particular their alkali metal salts.
- Such organic builder substances can, if desired, be present in amounts of up to 40% by weight, in particular up to 25% by weight and preferably from 1% by weight to 8% by weight. Amounts close to the above upper limit are preferably in paste-like or liquid, in particular water-containing agents according to the invention.
- Alkali silicates and polyphosphates are particularly suitable as water-soluble inorganic builder materials.
- crystalline or amorphous alkali alumosilicates are used as water-insoluble, water-dispersible inorganic builder materials, in amounts of up to 50% by weight, preferably not more than 40% by weight, and in liquid compositions in particular from 1% by weight to 5% by weight. used.
- the detergent grade crystalline sodium aluminosilicates, particularly zeolite A, P and optionally X are preferred. Amounts close to the upper limit mentioned are preferably used in solid, particulate compositions.
- Suitable aluminosilicates in particular have no particles with a grain size above 30 ⁇ m and preferably consist of at least 80% by weight of particles with a size below 10 ⁇ m.
- Their calcium binding capacity which can be determined according to the information in German patent DE 24 12 837, is generally in the range from 100 to 200 mg CaO per gram.
- Suitable substitutes or partial substitutes for the aluminosilicate mentioned are crystalline alkali silicates, which can be present alone or in a mixture with amorphous silicates.
- the alkali silicates which can be used as builders in the agents according to the invention preferably have a molar ratio of alkali oxide to SiO 2 below 0.95, in particular from 1: 1.1 to 1:12, and can be amorphous or crystalline.
- Preferred alkali silicates are the sodium silicates, in particular the amorphous sodium silicates, with a molar ratio Na O: SiO 2 of 1: 2 to 1: 2.8.
- crystalline silicates which may be present alone or in a mixture with amorphous silicates
- crystalline sheet silicates of the general formula Na 2 Si x O 2x + ⁇ y HO are preferably used, in which x, the so-called modulus, is a number from 1.9 to 4 and y is a number from 0 to 20 and preferred values for x are 2, 3 or 4.
- Crystalline layered silicates which fall under this general formula are described, for example, in European patent application EP 0 164 514.
- Preferred crystalline layered silicates are those in which x in the general formula mentioned assumes the values .2 or 3.
- ⁇ - and ⁇ -sodium disilicate Na 2 Si 2 O 5 y H 2 0
- ⁇ -sodium disilicate being obtainable, for example, by the method described in international patent application WO 91/08171.
- ⁇ -sodium silicates with a modulus between 1.9 and 3.2 can be produced according to Japanese patent applications JP 04/238 809 or JP 04/260 610.
- Practically anhydrous crystalline alkali silicates of the above general formula, in which x denotes a number from 1.9 to 2.1, can also be prepared from amorphous alkali silicates, as described in European patent applications EP 0 548 599, EP 0 502 325 and EP 0452 428 , can be used in agents according to the invention.
- a crystalline layered sodium silicate with a modulus of 2 to 3 is used, as can be produced from sand and soda by the process of European patent application EP 0 436 835.
- Crystalline sodium silicates with a modulus in the range from 1.9 to 3.5 are used in a further preferred embodiment of agents according to the invention.
- alkali aluminum silicate, in particular zeolite is also present as an additional builder substance
- the weight ratio aluminum silicate to silicate, in each case based on anhydrous active substances is preferably 1:10 to 10: 1.
- the weight ratio of amorphous alkali silicate to crystalline alkali silicate is preferably 1: 2 to 2: 1 and in particular 1: 1 to 2: 1.
- Builder substances are contained in the detergents according to the invention preferably in amounts of up to 60% by weight, in particular from 5% by weight to 40% by weight.
- Suitable peroxygen compounds are in particular organic peracids or peracidic salts of organic acids, such as phthalimidopercaproic acid, perbenzoic acid or salts of diperdodecanedioic acid, hydrogen peroxide and inorganic salts which give off hydrogen peroxide under the washing conditions, such as perborate, percarbonate and / or persilicate.
- organic acids such as phthalimidopercaproic acid, perbenzoic acid or salts of diperdodecanedioic acid, hydrogen peroxide and inorganic salts which give off hydrogen peroxide under the washing conditions, such as perborate, percarbonate and / or persilicate.
- solid peroxygen compounds can be used in the form of powders or granules, which can also be coated in a manner known in principle.
- Alkali percarbonate, alkali perborate monohydrate or hydrogen peroxide is particularly preferred Form of aqueous solutions containing 3 wt .-% to 10 wt .-% hydrogen peroxide used.
- a detergent according to the invention contains peroxygen compounds, these are present in amounts of preferably up to 50% by weight, in particular from 5% by weight to 30% by weight.
- bleach stabilizers such as, for example, phosphonates, borates or metaborates and metasilicates, and magnesium salts such as magnesium sulfate may be useful.
- Bleach activators which can be used are compounds which, under perhydrolysis conditions, give aliphatic peroxocarboxylic acids having preferably 1 to 10 C atoms, in particular 2 to 4 C atoms, and / or optionally substituted perbenzoic acid. Suitable substances are those which carry O- and / or N-acyl groups of the number of carbon atoms mentioned and / or optionally substituted benzoyl groups.
- polyacylated alkylenediamines especially tetraacetylethylenediamine (TAED), acylated triazine derivatives, especially 1,5-diacetyl-2,4-dioxohexahydro-1,3,5-triazine (DADHT), acylated glycolurils, especially tetraacetylglycoluril (TAGU), N- Acylimides, in particular N-nonanoylsuccinimide (NOSI), acylated phenolsulfonates, in particular n-nonanoyl- or isononanoyloxybenzenesulfonate (n- or iso-NOBS), carboxylic acid anhydrides, in particular phthalic anhydride, acylated polyhydric alcohols, in particular triacetyloxy, 2,5-acetiacetyl, ethylene glycol 2,5-dihydrofuran and the enol esters known from
- hydrophilically substituted acylacetals known from German patent application DE 196 16 769 and the acyl lactams described in German patent application DE 196 16 770 and international patent application WO 95/14075 are also preferably used.
- the known from the German patent application DE 4443 177 combinations of conventional bleach activators can be used. Bleach activators of this type are present in the customary quantitative range, preferably in amounts of 1% by weight to 10% by weight, in particular 2% by weight to 8% by weight, based on the total agent.
- the sulfonimines known from European patents EP 0446 982 and EP 0 453 003 and or bleach-enhancing transition metal salts or transition metal complexes can also be present as so-called bleaching catalysts.
- the transition metal compounds in question include, in particular, the manganese, iron, cobalt, ruthenium or molybdenum salen complexes known from German patent application DE 195 29 905 and their N-analog compounds known from German patent application DE 196 20 267, which consist of the German patent application DE 195 36 082 known manganese, iron, cobalt, ruthenium or molybdenum carbonyl complexes, the manganese, iron, cobalt, ruthenium, molybdenum, titanium described in German patent application DE 196 05 688 -, Vanadium and copper complexes with nitrogen-containing tripod ligands, the cobalt, iron, copper and ruthenium amine complexes known from German patent application DE 196 20 41 1, the manganese described in German patent application DE 44 16 438 , Copper and cobalt complexes, the cobalt complexes described in European patent application EP 0 272 030, the manganese com.
- Bleach-enhancing transition metal complexes in particular with the central atoms Mn, Fe, Co, Cu, Mo, V, Ti and / or Ru, are used in conventional amounts, preferably in one Amount up to 1% by weight, in particular from 0.0025% by weight to 0.25% by weight and particularly preferably from 0.01% by weight to 0.1% by weight, in each case based on the total Means used.
- Enzymes which can be used in the compositions in addition to the protease / amylase combination which is essential to the invention are those from the class of the lipases, cutinases, PuUulanases, hemicellulases, cellulases, oxidases and peroxidases and mixtures thereof. If necessary, proteases and / or amylases other than those of the invention may also be present in addition to these.
- Enzymes obtained from fungi or bacteria such as Bacillus subtilis, Bacillus licheniformis, Streptomyces griseus, Humicola lanuginosa, Humicola insolens, Pseudomonas pseudoalcaligenes or Pseudomonas cepacia are particularly suitable.
- the enzymes which are essential to the invention and, if appropriate, additionally used can, as described, for example, in international patent applications WO 92/1 1347 or WO 94/23005, be adsorbed on carriers and / or be embedded in coating substances in order to protect them against premature inactivation. They are contained in the detergents according to the invention preferably in amounts of up to 5% by weight, in particular from 0.2% by weight to 2% by weight.
- the organic solvents which can be used in the agents according to the invention, in particular if they are in liquid or pasty form, in addition to water include alcohols with 1 to 4 carbon atoms, in particular methanol, ethanol, isopropanol and tert-butanol, diols with 2 to 4 carbon atoms -Atoms, especially ethylene glycol and propylene glycol, as well as their mixtures and the ethers derivable from the compound classes mentioned.
- Such water-miscible solvents are preferably present in the detergents according to the invention in amounts not exceeding 30% by weight, in particular from 6% by weight to 20% by weight.
- the agents according to the invention can contain systemic and environmentally compatible acids, in particular citric acid, acetic acid, tartaric acid, malic acid, lactic acid, glycolic acid, succinic acid, glutaric acid and or adipic acid also mineral acids, especially sulfuric acid, or bases, especially ammonium or alkali hydroxides.
- systemic and environmentally compatible acids in particular citric acid, acetic acid, tartaric acid, malic acid, lactic acid, glycolic acid, succinic acid, glutaric acid and or adipic acid also mineral acids, especially sulfuric acid, or bases, especially ammonium or alkali hydroxides.
- pH regulators are preferably not contained in the agents according to the invention in excess of 20% by weight, in particular from 1.2% by weight to 17% by weight.
- the agents can contain further constituents customary in washing and cleaning agents.
- These optional components include, in particular, enzyme stabilizers, additional graying inhibitors such as carboxymethyl cellulose, color transfer inhibitors, for example polyvinylpyrrolidone or polyvinylpyridine-N-oxide, foam inhibitors, for example organopolysiloxanes and / or paraffins, and optical brighteners, for example stilbene disulfonic acid derivatives.
- the preparation of solid agents according to the invention presents no difficulties and can be carried out in a known manner, for example by spray drying or granulation, the enzymes and any further thermally sensitive ingredients, such as bleaching agents, optionally being added separately later.
- agents according to the invention with increased bulk density in particular in the range from 650 g / 1 to 950 g / 1, a process known from European patent EP 486 592 and having an extrusion step is preferred.
- Liquid or pasty washing or cleaning agents according to the invention in the form of solutions containing customary solvents are generally produced by simply mixing the ingredients, which can be added in bulk or as a solution to an automatic mixer.
- Table 1 below shows the washing results (in dE initial value minus dE after washing, measuring device Minolta® CR 310) for a detergent V2 which contains 0.6% by weight amylase granules (Termamyl® 60T) and 1.2% not according to the invention .-% of a protease granules (activity 200,000 PE / g) with the genetically modified protease F 49 according to WO 95/23221, for one Detergent VI, which was otherwise of the same composition, but contained BLAP in amounts of protein activity equal to BLAP instead of F 49, a detergent V3 which was otherwise composed of VI and which, instead of Termamyl®, contained the same amount of protein activity as the genetically modified amylase Duramyl®, an otherwise detergent V4 which was composed of VI instead of Termamyl®, the amount of the genetically modified Amylase Purafect® OxAm containing the same protein activity and for detergents Ml or M2 according to the invention, which were otherwise composed
- Soiling A oatmeal / cocoa
- B chocolate pudding
- C milk / cocoa
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Abstract
Description
Claims
Priority Applications (2)
Application Number | Priority Date | Filing Date | Title |
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JP53050298A JP2001507748A (ja) | 1997-01-08 | 1997-12-19 | プロテアーゼおよびアミラーゼ含有清浄剤 |
EP97954439A EP0964911A1 (de) | 1997-01-08 | 1997-12-19 | Protease- und amylasehaltiges waschmittel |
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
DE1997100327 DE19700327A1 (de) | 1997-01-08 | 1997-01-08 | Protease- und amylasehaltiges Waschmittel |
DE19700327.3 | 1997-01-08 |
Publications (1)
Publication Number | Publication Date |
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WO1998030669A1 true WO1998030669A1 (de) | 1998-07-16 |
Family
ID=7816930
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
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PCT/EP1997/007171 WO1998030669A1 (de) | 1997-01-08 | 1997-12-19 | Protease- und amylasehaltiges waschmittel |
Country Status (4)
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EP (1) | EP0964911A1 (de) |
JP (1) | JP2001507748A (de) |
DE (1) | DE19700327A1 (de) |
WO (1) | WO1998030669A1 (de) |
Cited By (7)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US7262042B2 (en) | 2001-12-20 | 2007-08-28 | Henkel Kommanditgesellschaft Auf Aktien (Henkel Kgaa) | Alkaline protease from Bacillus gibsonii (DSM 14393) and washing and cleaning products comprising said alkaline protease |
US7320887B2 (en) | 2001-10-31 | 2008-01-22 | Henkel Kommanditgesellschaft Auf Aktien | Alkaline protease variants |
US7449187B2 (en) | 2001-12-20 | 2008-11-11 | Henkel Kommanditgesellschaft Auf Aktien (Henkel Kgaa) | Alkaline protease from Bacillus gibsonii (DSM 14391) and washing and cleaning products comprising said alkaline protease |
US7569226B2 (en) | 2001-12-22 | 2009-08-04 | Henkel Kommanditgesellschaft Auf Aktien (Henkel Kgaa) | Alkaline protease from Bacillus sp. (DSM 14392) and washing and cleaning products comprising said alkaline protease |
WO2010115028A3 (en) * | 2009-04-01 | 2010-12-16 | Danisco Us Inc. | Cleaning system comprising an alpha-amylase and a protease |
JP2015507033A (ja) * | 2011-12-15 | 2015-03-05 | ヘンケル・アクチェンゲゼルシャフト・ウント・コムパニー・コマンディットゲゼルシャフト・アウフ・アクチェンHenkel AG & Co.KGaA | プロテアーゼおよびアミラーゼを含有する貯蔵安定性液状洗剤または洗浄剤 |
EP3044302B1 (de) | 2013-09-12 | 2017-10-25 | Henkel AG & Co. KGaA | Festes textilwaschmittel mit verbesserter proteaseleistung |
Families Citing this family (4)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
DE19824705A1 (de) * | 1998-06-03 | 1999-12-09 | Henkel Kgaa | Amylase und Protease enthaltende Wasch- und Reinigungsmittel |
DE10007608A1 (de) * | 2000-02-18 | 2001-08-30 | Henkel Kgaa | Protease und Percarbonat enthaltende Wasch- und Reinigungsmittel |
DE102011118021A1 (de) * | 2011-10-28 | 2013-05-02 | Henkel Ag & Co. Kgaa | Leistungsverbesserte und temperaturstabile Proteasevarianten |
DE102012201522A1 (de) * | 2012-02-02 | 2013-08-08 | Basf Se | Lagerstabiles flüssiges Geschirrspülmittel enthaltend Protease und Amylase |
Citations (4)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO1991002792A1 (en) * | 1989-08-25 | 1991-03-07 | Henkel Research Corporation | Alkaline proteolytic enzyme and method of production |
DE4041752A1 (de) * | 1990-12-24 | 1992-06-25 | Henkel Kgaa | Enzymzubereitung fuer wasch- und reinigungsmittel |
WO1994018314A1 (en) * | 1993-02-11 | 1994-08-18 | Genencor International, Inc. | Oxidatively stable alpha-amylase |
WO1996000772A1 (de) * | 1994-06-28 | 1996-01-11 | Henkel Kommanditgesellschaft Auf Aktien | Mehrenzymgranulat sowie dessen herstellung |
-
1997
- 1997-01-08 DE DE1997100327 patent/DE19700327A1/de not_active Withdrawn
- 1997-12-19 WO PCT/EP1997/007171 patent/WO1998030669A1/de not_active Application Discontinuation
- 1997-12-19 EP EP97954439A patent/EP0964911A1/de not_active Ceased
- 1997-12-19 JP JP53050298A patent/JP2001507748A/ja active Pending
Patent Citations (4)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO1991002792A1 (en) * | 1989-08-25 | 1991-03-07 | Henkel Research Corporation | Alkaline proteolytic enzyme and method of production |
DE4041752A1 (de) * | 1990-12-24 | 1992-06-25 | Henkel Kgaa | Enzymzubereitung fuer wasch- und reinigungsmittel |
WO1994018314A1 (en) * | 1993-02-11 | 1994-08-18 | Genencor International, Inc. | Oxidatively stable alpha-amylase |
WO1996000772A1 (de) * | 1994-06-28 | 1996-01-11 | Henkel Kommanditgesellschaft Auf Aktien | Mehrenzymgranulat sowie dessen herstellung |
Cited By (8)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US7320887B2 (en) | 2001-10-31 | 2008-01-22 | Henkel Kommanditgesellschaft Auf Aktien | Alkaline protease variants |
US7262042B2 (en) | 2001-12-20 | 2007-08-28 | Henkel Kommanditgesellschaft Auf Aktien (Henkel Kgaa) | Alkaline protease from Bacillus gibsonii (DSM 14393) and washing and cleaning products comprising said alkaline protease |
US7449187B2 (en) | 2001-12-20 | 2008-11-11 | Henkel Kommanditgesellschaft Auf Aktien (Henkel Kgaa) | Alkaline protease from Bacillus gibsonii (DSM 14391) and washing and cleaning products comprising said alkaline protease |
US7569226B2 (en) | 2001-12-22 | 2009-08-04 | Henkel Kommanditgesellschaft Auf Aktien (Henkel Kgaa) | Alkaline protease from Bacillus sp. (DSM 14392) and washing and cleaning products comprising said alkaline protease |
WO2010115028A3 (en) * | 2009-04-01 | 2010-12-16 | Danisco Us Inc. | Cleaning system comprising an alpha-amylase and a protease |
US8852912B2 (en) | 2009-04-01 | 2014-10-07 | Danisco Us Inc. | Compositions and methods comprising alpha-amylase variants with altered properties |
JP2015507033A (ja) * | 2011-12-15 | 2015-03-05 | ヘンケル・アクチェンゲゼルシャフト・ウント・コムパニー・コマンディットゲゼルシャフト・アウフ・アクチェンHenkel AG & Co.KGaA | プロテアーゼおよびアミラーゼを含有する貯蔵安定性液状洗剤または洗浄剤 |
EP3044302B1 (de) | 2013-09-12 | 2017-10-25 | Henkel AG & Co. KGaA | Festes textilwaschmittel mit verbesserter proteaseleistung |
Also Published As
Publication number | Publication date |
---|---|
EP0964911A1 (de) | 1999-12-22 |
DE19700327A1 (de) | 1998-07-09 |
JP2001507748A (ja) | 2001-06-12 |
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