EP3226872A1 - Stabilisateurs enzymatiques - Google Patents
Stabilisateurs enzymatiquesInfo
- Publication number
- EP3226872A1 EP3226872A1 EP15797062.5A EP15797062A EP3226872A1 EP 3226872 A1 EP3226872 A1 EP 3226872A1 EP 15797062 A EP15797062 A EP 15797062A EP 3226872 A1 EP3226872 A1 EP 3226872A1
- Authority
- EP
- European Patent Office
- Prior art keywords
- washing
- protease
- coox
- cleaning agent
- cleaning
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Withdrawn
Links
- 102000004190 Enzymes Human genes 0.000 title claims abstract description 56
- 108090000790 Enzymes Proteins 0.000 title claims abstract description 56
- 239000003381 stabilizer Substances 0.000 title claims abstract description 23
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- 239000003599 detergent Substances 0.000 claims abstract description 39
- 150000001875 compounds Chemical class 0.000 claims abstract description 33
- 238000005406 washing Methods 0.000 claims abstract description 30
- 239000012459 cleaning agent Substances 0.000 claims abstract description 21
- 238000004140 cleaning Methods 0.000 claims abstract description 18
- 238000000034 method Methods 0.000 claims abstract description 15
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 claims abstract 5
- 239000004753 textile Substances 0.000 claims description 11
- 150000003839 salts Chemical class 0.000 claims description 7
- 230000008569 process Effects 0.000 claims description 6
- 239000007787 solid Substances 0.000 claims description 6
- 230000000087 stabilizing effect Effects 0.000 claims description 6
- QGZKDVFQNNGYKY-UHFFFAOYSA-O Ammonium Chemical compound [NH4+] QGZKDVFQNNGYKY-UHFFFAOYSA-O 0.000 claims description 5
- 229910052783 alkali metal Inorganic materials 0.000 claims description 4
- 150000001340 alkali metals Chemical class 0.000 claims description 4
- 201000010099 disease Diseases 0.000 claims description 4
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 claims description 4
- WCQIWZONSZRNOZ-UHFFFAOYSA-N 2-bromo-5,6,7,8-tetrahydro-1,6-naphthyridine Chemical group C1NCCC2=NC(Br)=CC=C21 WCQIWZONSZRNOZ-UHFFFAOYSA-N 0.000 claims description 3
- 206010001935 American trypanosomiasis Diseases 0.000 claims description 3
- 208000024699 Chagas disease Diseases 0.000 claims description 3
- 206010028980 Neoplasm Diseases 0.000 claims description 3
- 241000223109 Trypanosoma cruzi Species 0.000 claims description 3
- 201000011510 cancer Diseases 0.000 claims description 3
- 208000006454 hepatitis Diseases 0.000 claims description 3
- 231100000283 hepatitis Toxicity 0.000 claims description 3
- 208000027866 inflammatory disease Diseases 0.000 claims description 3
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- 208000030852 Parasitic disease Diseases 0.000 claims description 2
- 125000004169 (C1-C6) alkyl group Chemical group 0.000 claims 3
- 229910006127 SO3X Inorganic materials 0.000 claims 3
- 239000000137 peptide hydrolase inhibitor Substances 0.000 abstract description 7
- 229940124158 Protease/peptidase inhibitor Drugs 0.000 abstract description 3
- 150000002894 organic compounds Chemical class 0.000 abstract description 2
- 229940088598 enzyme Drugs 0.000 description 48
- 102000035195 Peptidases Human genes 0.000 description 35
- 239000003795 chemical substances by application Substances 0.000 description 22
- 239000000203 mixture Substances 0.000 description 22
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 12
- 108091005658 Basic proteases Proteins 0.000 description 11
- 230000000694 effects Effects 0.000 description 11
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- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 6
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- 238000004851 dishwashing Methods 0.000 description 5
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- RTZKZFJDLAIYFH-UHFFFAOYSA-N Diethyl ether Chemical compound CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 description 4
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- 239000007844 bleaching agent Substances 0.000 description 3
- KGBXLFKZBHKPEV-UHFFFAOYSA-N boric acid Chemical class OB(O)O KGBXLFKZBHKPEV-UHFFFAOYSA-N 0.000 description 3
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- 238000006243 chemical reaction Methods 0.000 description 3
- KRKNYBCHXYNGOX-UHFFFAOYSA-N citric acid Chemical compound OC(=O)CC(O)(C(O)=O)CC(O)=O KRKNYBCHXYNGOX-UHFFFAOYSA-N 0.000 description 3
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- DNIAPMSPPWPWGF-GSVOUGTGSA-N (R)-(-)-Propylene glycol Chemical compound C[C@@H](O)CO DNIAPMSPPWPWGF-GSVOUGTGSA-N 0.000 description 2
- 241000193422 Bacillus lentus Species 0.000 description 2
- 241000194110 Bacillus sp. (in: Bacteria) Species 0.000 description 2
- 102100032487 Beta-mannosidase Human genes 0.000 description 2
- ZOXJGFHDIHLPTG-UHFFFAOYSA-N Boron Chemical compound [B] ZOXJGFHDIHLPTG-UHFFFAOYSA-N 0.000 description 2
- LYCAIKOWRPUZTN-UHFFFAOYSA-N Ethylene glycol Chemical compound OCCO LYCAIKOWRPUZTN-UHFFFAOYSA-N 0.000 description 2
- 102000004882 Lipase Human genes 0.000 description 2
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- 229910052796 boron Inorganic materials 0.000 description 2
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- 238000010494 dissociation reaction Methods 0.000 description 2
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- 150000002148 esters Chemical class 0.000 description 2
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- 229930195729 fatty acid Natural products 0.000 description 2
- 239000000194 fatty acid Substances 0.000 description 2
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- 239000011521 glass Substances 0.000 description 2
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- 230000003301 hydrolyzing effect Effects 0.000 description 2
- 238000011534 incubation Methods 0.000 description 2
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- 238000010297 mechanical methods and process Methods 0.000 description 2
- 230000005226 mechanical processes and functions Effects 0.000 description 2
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- 235000013772 propylene glycol Nutrition 0.000 description 2
- 230000017854 proteolysis Effects 0.000 description 2
- 230000002797 proteolythic effect Effects 0.000 description 2
- 239000000243 solution Substances 0.000 description 2
- VXWBQOJISHAKKM-UHFFFAOYSA-N (4-formylphenyl)boronic acid Chemical compound OB(O)C1=CC=C(C=O)C=C1 VXWBQOJISHAKKM-UHFFFAOYSA-N 0.000 description 1
- 125000004080 3-carboxypropanoyl group Chemical group O=C([*])C([H])([H])C([H])([H])C(O[H])=O 0.000 description 1
- TYMLOMAKGOJONV-UHFFFAOYSA-N 4-nitroaniline Chemical compound NC1=CC=C([N+]([O-])=O)C=C1 TYMLOMAKGOJONV-UHFFFAOYSA-N 0.000 description 1
- HBAQYPYDRFILMT-UHFFFAOYSA-N 8-[3-(1-cyclopropylpyrazol-4-yl)-1H-pyrazolo[4,3-d]pyrimidin-5-yl]-3-methyl-3,8-diazabicyclo[3.2.1]octan-2-one Chemical class C1(CC1)N1N=CC(=C1)C1=NNC2=C1N=C(N=C2)N1C2C(N(CC1CC2)C)=O HBAQYPYDRFILMT-UHFFFAOYSA-N 0.000 description 1
- 239000004382 Amylase Substances 0.000 description 1
- 241000193830 Bacillus <bacterium> Species 0.000 description 1
- 241000193375 Bacillus alcalophilus Species 0.000 description 1
- 241000193744 Bacillus amyloliquefaciens Species 0.000 description 1
- 241001328119 Bacillus gibsonii Species 0.000 description 1
- 241000194108 Bacillus licheniformis Species 0.000 description 1
- 101710130006 Beta-glucanase Proteins 0.000 description 1
- 108700038091 Beta-glucanases Proteins 0.000 description 1
- BTBUEUYNUDRHOZ-UHFFFAOYSA-N Borate Chemical compound [O-]B([O-])[O-] BTBUEUYNUDRHOZ-UHFFFAOYSA-N 0.000 description 1
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 1
- 108010008885 Cellulose 1,4-beta-Cellobiosidase Proteins 0.000 description 1
- 108010000659 Choline oxidase Proteins 0.000 description 1
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- 102000005744 Glycoside Hydrolases Human genes 0.000 description 1
- DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 1
- GDBQQVLCIARPGH-UHFFFAOYSA-N Leupeptin Natural products CC(C)CC(NC(C)=O)C(=O)NC(CC(C)C)C(=O)NC(C=O)CCCN=C(N)N GDBQQVLCIARPGH-UHFFFAOYSA-N 0.000 description 1
- FYYHWMGAXLPEAU-UHFFFAOYSA-N Magnesium Chemical compound [Mg] FYYHWMGAXLPEAU-UHFFFAOYSA-N 0.000 description 1
- 102000005741 Metalloproteases Human genes 0.000 description 1
- 108010006035 Metalloproteases Proteins 0.000 description 1
- XEJOUMLOLRMBOS-UHFFFAOYSA-N N1=CN=CC=C1.NCCCCCC(=O)O Chemical compound N1=CN=CC=C1.NCCCCCC(=O)O XEJOUMLOLRMBOS-UHFFFAOYSA-N 0.000 description 1
- 108010038807 Oligopeptides Proteins 0.000 description 1
- 102000015636 Oligopeptides Human genes 0.000 description 1
- 108010064983 Ovomucin Proteins 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- ZLMJMSJWJFRBEC-UHFFFAOYSA-N Potassium Chemical compound [K] ZLMJMSJWJFRBEC-UHFFFAOYSA-N 0.000 description 1
- 102100038946 Proprotein convertase subtilisin/kexin type 6 Human genes 0.000 description 1
- 229920002472 Starch Polymers 0.000 description 1
- 108700037663 Subtilisin-like proteases Proteins 0.000 description 1
- KDYFGRWQOYBRFD-UHFFFAOYSA-N Succinic acid Natural products OC(=O)CCC(O)=O KDYFGRWQOYBRFD-UHFFFAOYSA-N 0.000 description 1
- QAOWNCQODCNURD-UHFFFAOYSA-L Sulfate Chemical compound [O-]S([O-])(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-L 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 239000012190 activator Substances 0.000 description 1
- 239000004480 active ingredient Substances 0.000 description 1
- 239000013543 active substance Substances 0.000 description 1
- 125000003172 aldehyde group Chemical group 0.000 description 1
- 150000001299 aldehydes Chemical class 0.000 description 1
- 150000007933 aliphatic carboxylic acids Chemical class 0.000 description 1
- 239000003513 alkali Substances 0.000 description 1
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- 102000004139 alpha-Amylases Human genes 0.000 description 1
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- 150000001413 amino acids Chemical class 0.000 description 1
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- 239000003963 antioxidant agent Substances 0.000 description 1
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- 125000003118 aryl group Chemical group 0.000 description 1
- 230000004888 barrier function Effects 0.000 description 1
- LZCZIHQBSCVGRD-UHFFFAOYSA-N benzenecarboximidamide;hydron;chloride Chemical compound [Cl-].NC(=[NH2+])C1=CC=CC=C1 LZCZIHQBSCVGRD-UHFFFAOYSA-N 0.000 description 1
- 229910021538 borax Inorganic materials 0.000 description 1
- 235000010338 boric acid Nutrition 0.000 description 1
- 125000005619 boric acid group Chemical class 0.000 description 1
- 125000005620 boronic acid group Chemical class 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
- 229910052791 calcium Inorganic materials 0.000 description 1
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- PZWNKBUDRGSEOU-UHFFFAOYSA-D decasodium;n-[2-[bis(phosphonatomethyl)amino]ethyl]-n,n',n'-tris(phosphonatomethyl)ethane-1,2-diamine Chemical compound [Na+].[Na+].[Na+].[Na+].[Na+].[Na+].[Na+].[Na+].[Na+].[Na+].[O-]P(=O)([O-])CN(CP([O-])([O-])=O)CCN(CP([O-])(=O)[O-])CCN(CP([O-])([O-])=O)CP([O-])([O-])=O PZWNKBUDRGSEOU-UHFFFAOYSA-D 0.000 description 1
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- 125000002485 formyl group Chemical group [H]C(*)=O 0.000 description 1
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- FUZZWVXGSFPDMH-UHFFFAOYSA-N hexanoic acid Chemical group CCCCCC(O)=O FUZZWVXGSFPDMH-UHFFFAOYSA-N 0.000 description 1
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- GDBQQVLCIARPGH-ULQDDVLXSA-N leupeptin Chemical compound CC(C)C[C@H](NC(C)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@H](C=O)CCCN=C(N)N GDBQQVLCIARPGH-ULQDDVLXSA-N 0.000 description 1
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Classifications
-
- 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
- C11D3/20—Organic compounds containing oxygen
- C11D3/2075—Carboxylic acids-salts thereof
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K31/00—Medicinal preparations containing organic active ingredients
- A61K31/33—Heterocyclic compounds
- A61K31/395—Heterocyclic compounds having nitrogen as a ring hetero atom, e.g. guanethidine or rifamycins
- A61K31/53—Heterocyclic compounds having nitrogen as a ring hetero atom, e.g. guanethidine or rifamycins having six-membered rings with three nitrogens as the only ring hetero atoms, e.g. chlorazanil, melamine
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K31/00—Medicinal preparations containing organic active ingredients
- A61K31/185—Acids; Anhydrides, halides or salts thereof, e.g. sulfur acids, imidic, hydrazonic or hydroximic acids
- A61K31/19—Carboxylic acids, e.g. valproic acid
- A61K31/195—Carboxylic acids, e.g. valproic acid having an amino group
- A61K31/197—Carboxylic acids, e.g. valproic acid having an amino group the amino and the carboxyl groups being attached to the same acyclic carbon chain, e.g. gamma-aminobutyric acid [GABA], beta-alanine, epsilon-aminocaproic acid or pantothenic acid
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P11/00—Drugs for disorders of the respiratory system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P29/00—Non-central analgesic, antipyretic or antiinflammatory agents, e.g. antirheumatic agents; Non-steroidal antiinflammatory drugs [NSAID]
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/12—Antivirals
- A61P31/14—Antivirals for RNA viruses
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/12—Antivirals
- A61P31/14—Antivirals for RNA viruses
- A61P31/18—Antivirals for RNA viruses for HIV
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P33/00—Antiparasitic agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P33/00—Antiparasitic agents
- A61P33/02—Antiprotozoals, e.g. for leishmaniasis, trichomoniasis, toxoplasmosis
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P33/00—Antiparasitic agents
- A61P33/02—Antiprotozoals, e.g. for leishmaniasis, trichomoniasis, toxoplasmosis
- A61P33/06—Antimalarials
-
- 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
- C11D17/00—Detergent materials or soaps characterised by their shape or physical properties
- C11D17/08—Liquid soap, e.g. for dispensers; capsuled
-
- 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
- C11D3/26—Organic compounds containing nitrogen
- C11D3/28—Heterocyclic compounds containing nitrogen in the ring
-
- 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
- C11D3/26—Organic compounds containing nitrogen
- C11D3/33—Amino carboxylic acids
-
- 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
- C11D3/34—Organic compounds containing sulfur
- C11D3/349—Organic compounds containing sulfur additionally containing nitrogen atoms, e.g. nitro, nitroso, amino, imino, nitrilo, nitrile groups containing compounds or their derivatives or thio urea
-
- 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
- C11D3/38663—Stabilised liquid enzyme compositions
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K8/00—Cosmetics or similar toiletry preparations
- A61K8/18—Cosmetics or similar toiletry preparations characterised by the composition
-
- D—TEXTILES; PAPER
- D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
- D06L—DRY-CLEANING, WASHING OR BLEACHING FIBRES, FILAMENTS, THREADS, YARNS, FABRICS, FEATHERS OR MADE-UP FIBROUS GOODS; BLEACHING LEATHER OR FURS
- D06L1/00—Dry-cleaning or washing fibres, filaments, threads, yarns, fabrics, feathers or made-up fibrous goods
- D06L1/02—Dry-cleaning or washing fibres, filaments, threads, yarns, fabrics, feathers or made-up fibrous goods using organic solvents
- D06L1/04—Dry-cleaning or washing fibres, filaments, threads, yarns, fabrics, feathers or made-up fibrous goods using organic solvents combined with specific additives
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
- Y02A—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE
- Y02A50/00—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE in human health protection, e.g. against extreme weather
- Y02A50/30—Against vector-borne diseases, e.g. mosquito-borne, fly-borne, tick-borne or waterborne diseases whose impact is exacerbated by climate change
Definitions
- the present invention relates to detergents and cleaners containing at least one enzyme and at least one organic compound which acts as a protease inhibitor and is thus a suitable enzyme stabilizer, and the use of these compounds as enzyme stabilizer in enzyme-containing detergents and cleaners.
- enzymes in detergents and cleaners have been established in the art for decades. They serve to extend the range of services of the funds concerned according to their specific activities. These include in particular hydrolytic enzymes such as proteases, amylases, lipases and cellulases. The first three hydrolyze proteins, starches and fats and thus contribute directly to soil removal. Cellulases are used in particular because of their tissue effect.
- hydrolytic enzymes such as proteases, amylases, lipases and cellulases.
- the first three hydrolyze proteins, starches and fats and thus contribute directly to soil removal.
- Cellulases are used in particular because of their tissue effect.
- Another group of washing and cleaning agent enzymes are oxidative enzymes, in particular oxidases, which may be present in the
- Interaction with other components preferably serves to bleach stains or to produce the bleaching agents in situ.
- further enzymes are constantly being made available for use in detergents and cleaners in order to be able to optimally address particular soiling, such as pectinases, ⁇ -glucanases, mannanases or other hemicellulases (glycosidases) Hydrolysis in particular of special vegetable polymers.
- One goal in the development of detergent formulations is to stabilize the enzymes contained, especially during storage. This is understood as protection against various unfavorable influences, such as denaturation or decay by physical influences or oxidation.
- One focus of these developments is the protection of the contained proteins and / or enzymes against proteolytic cleavage. This can be done by the construction of physical barriers, such as by encapsulation of the enzymes in special enzyme granules or by packaging the means in two- or multi-chamber systems. The other often trodden path is chemical
- Polyols in particular glycerol and 1,2-propylene glycol, benzamidine hydrochloride, borax, boric acids, boronic acids or their salts or esters are established as reversible protease inhibitors in the prior art.
- These include, in particular, derivatives with aromatic groups, for example ortho, meta or para-substituted phenylboronic acids, in particular 4-formylphenylboronic acid, or the salts or esters of the compounds mentioned.
- a particularly good protection results when boric acid derivatives are used together with polyols, since these can then form a complex stabilizing the enzyme.
- peptide aldehydes that is, oligopeptides with reduced C-terminus, especially those of 2 to 50 monomers are described for this purpose.
- peptidic reversible protease inhibitors include ovomucoid and leupeptin.
- specific, reversible peptide inhibitors and fusion proteins from proteases and specific peptide inhibitors are used for this purpose.
- amino alcohols such as mono-, di-, triethanol- and -propanolamine and mixtures thereof, aliphatic carboxylic acids up to C12, such as succinic acid, other dicarboxylic acids or salts of said acids.
- End-capped fatty acid amide alkoxylates are established for this purpose.
- Certain organic acids used as builders are capable, as disclosed in WO 97/18287, of stabilizing an enzyme in addition to their builder function.
- protease classes are established, for example metalloproteases. Take under the detergent and detergent proteases Proteases of the subtilisin type (subtilases, subtilopeptidases, EC 3.4.21.62), however, due to their favorable enzymatic properties such as stability or pH optimum a prominent position. They are attributed to the serine proteases due to the catalytically active amino acids. They act as nonspecific endopeptidases, that is, they hydrolyze any acid amide linkages that are internal to peptides or proteins. Their pH optimum is usually in the clearly alkaline range.
- subtilisins Subtilisin-like Proteases
- R. Siezen pages 75-95 in "Subtilisin enzymes", edited by R. Bott and C. Betzel, New York, 1996.
- Subtilases become natural formed by microorganisms; Of these, in particular, the subtilisins formed and secreted by Bacillus species are to be mentioned as the most important group within the subtilases.
- polyols such as glycerol and 1, 2-propylene glycol have proved to be unfavorable due to their high necessary use concentrations, because the other active ingredients of the respective agents can thus be contained only in proportionally smaller proportions.
- boric acid derivatives occupy an outstanding position among the serine protease inhibitors, which are effective at comparatively low concentrations.
- the boric acid derivatives have a significant disadvantage: many of them, such as borate, form undesirable by-products with some other detergent ingredients, so that they are no longer available in the agents concerned for the desired cleaning purpose, or even remain as an impurity on the laundry.
- the object of the present invention was therefore to identify boron-free compounds that act as protease inhibitors and for use as enzyme stabilizers in detergents and
- Detergents are suitable. Here, the use in total liquid, gel or pasty detergents and cleaning agents of particular interest, and including in particular those containing water.
- washing or cleaning agents which comprise at least one protease and at least one enzyme stabilizer, the at least one enzyme stabilizer being selected from compounds of the general structural formula (I)
- R 21, R 22 and R 23 independently of one another denote C 1-6 -alkyl substituted by COOX, OH, SO 3 X, NH 2 , CHO or SH, especially (CH 2 ) o-COOX, (CH 2 ) o -OH, (CH 2 ) o- S0 3 X, (CH 2 ) o -NH 2 , (CH 2 ) o -CHO or (CH 2 ) o -SH, where o is an integer from 0 to 6; and
- X is H, an alkali metal or ammonium.
- the invention also includes stereoisomers, in particular enantiomers and diastereomers, tautomers and salts of those described above
- R21-R23 are identical in various embodiments and are in particular (CH2) o-COOX, more preferably caproic acid groups of formula (CH2) 5-COOX.
- X is H, an alkali or alkaline earth metal, especially sodium, potassium, calcium, magnesium or ammonium.
- Preferred according to the invention are the free acids or the sodium salts.
- An exemplary compound of formula (I) includes, but is not limited to, 2,4,6-tri (6-aminocaproic acid) -1,3,3-triazine.
- a detergent or cleaning agent according to the invention are all means that are suitable for washing or cleaning of particular textiles and / or solid surfaces.
- Other suitable ingredients are described in detail below.
- a protease is to be understood as meaning all enzymes which are capable of hydrolyzing acid amide linkages of proteins.
- the proteases are also described in detail below.
- invention-relevant compound in the substrate binding pocket of the protease incorporated and non-covalently bonded there.
- the active site of the protease is replaced by the blocked by this enzyme non-hydrolysable compound and is not available for hydrolysis of other added proteins.
- This is a reversible bond, ie a balance between association and dissociation.
- the equilibrium coefficient of this reaction is called the inhibition constant or K.
- Detergents have usable proteases.
- the inhibitors thus bind reversibly, i. they do not interfere with solid and not too loose transient interactions with the enzyme.
- the majority of the protease relevant to the invention is thus present during storage in the form of a protease-inhibitor complex.
- the protease and optionally other proteins contained, in particular other enzymes are protected in this way against proteolysis by this enzyme (stabilized against proteolysis) and are thus fully efficient even after storage.
- the second advantage of the invention relevant connections over the prior art is that they have as elements only C, H, N and O and in particular are free of boron. Thus, they do not form the undesirable boron-derived by-products with other detergent or cleaning ingredients.
- the compounds mentioned probably act as reversible inhibitors because, similar to the substrate of the proteases, they are structurally adapted to the conditions of the binding pocket. This applies in particular to serine proteases, as illustrated by the examples of the present application with the positive effect of those described experimentally there
- washing or cleaning agent for washing and / or cleaning textiles and / or hard surfaces; such as
- the enzyme i. the protease in an amount of 0.05-5% by weight, preferably 0.05-2% by weight, and the enzyme stabilizer in an amount of 0.05-15% by weight, preferably 0.05- 5 wt .-%, based on the total weight of the washing or cleaning agent contained in this.
- the enzyme and the enzyme stabilizer may be pre-formulated in an enzyme composition, wherein the enzyme is present in the enzyme composition in an amount of 0.05-15% by weight, preferably 0.05-5% by weight and the enzyme stabilizer in one Amount of 0.05-35 wt .-%, preferably 0.05-10 wt .-% based on the total weight in the enzyme composition.
- This enzyme composition which is also a constituent of the present invention, can then be used in detergents or cleaners according to the invention in amounts which lead to the above-mentioned final concentrations in the washing or cleaning agent.
- an agent according to the invention may contain at least one further stabilizer, in particular a polyol, such as glycerol or 1,2-ethylene glycol, and / or an antioxidant.
- a further stabilizer in particular a polyol, such as glycerol or 1,2-ethylene glycol, and / or an antioxidant.
- the protease stabilized or reversibly inhibited according to the invention is preferably a serine protease, in particular a subtilase, more preferably a subtilisin.
- the subtilisin may be a wild-type enzyme or a subtilisin variant, wherein the wild-type enzyme or the starting enzyme of the variant is preferably selected from one of the following:
- alkaline protease from Bacillus lentus, preferably from Bacillus lentus (DSM 5483),
- alkaline protease from Bacillus sp. (DSM 14390) or an at least 98.5% identical alkaline protease, and
- alkaline protease from Bacillus sp. (DSM 14392) or an at least 98.1% identical alkaline protease.
- compositions according to the invention may contain, in addition to the protease, one or more further enzymes, in particular from the following group: one or more further proteases, amylases,
- Hemicellulases Hemicellulases, cellulases, lipases and oxidoreductases.
- the amylase (s) is preferably an ⁇ -amylase.
- the hemicellulase is preferably a ⁇ -glucanase, a pectinase, a pullulanase and / or a mannanase.
- the cellulase is preferably a cellulase mixture or a one-component cellulase, preferably or predominantly an endoglucanase and / or a cellobiohydrolase.
- the oxidoreductase is preferably an oxidase, in particular a choline oxidase, or a perhydrolase.
- compositions described herein include all conceivable types of detergents or cleaners, both concentrates and neat agents, for use on a commercial scale, in the washing machine or in hand washing or cleaning. These include detergents for textiles, carpets, or natural fibers for which the
- Label detergent is used. These include, for example, dishwashing detergents for dishwashers or manual dishwashing detergents or cleaners for hard surfaces such as metal, glass, porcelain, ceramics, tiles, stone, painted surfaces, plastics, wood or leather, for which the term detergent is used, ie in addition to manual and machine Dishwashing agents, for example, scouring agents, glass cleaners, toilet scenters, etc.
- the washing and cleaning agents in the invention also include washing aids which are added to the actual detergent in the manual or machine textile laundry to achieve a further effect. Furthermore count to washing and
- Textilvor- and post-treatment agent ie those means with which the garment is brought into contact before the actual laundry, for example, to dissolve stubborn dirt, and also such agents, the laundry downstream in one of the actual textile laundry further desirable Give properties such as a comfortable grip, crease resistance or low static charge.
- the fabric softeners are calculated.
- Embodiments of the present invention include all solid, powdered, liquid, gelatinous or pasty administration forms of agents described herein, which if appropriate can also consist of several phases and can be present in compressed or uncompressed form.
- the agent can be present as a free-flowing powder, in particular with a bulk density of 300 g / l to 1200 g / l, in particular 500 g / l to 900 g / l or 600 g / l to 850 g / l.
- the solid dosage forms of the composition also include extrudates, granules, tablets or pouches.
- the agent can also be liquid, gelatinous or pasty, for example in the form of a non-aqueous liquid washing or dishwashing detergent or a non-aqueous paste or in the form of an aqueous liquid washing or dishwashing detergent or a water-containing paste.
- the agent may be present as a one-component system. Such funds consist of one phase.
- an agent can also consist of several phases. Such an agent is therefore divided into several components.
- the detergents or cleaners described herein which may be in the form of powdered solids, in densified particulate form, as homogeneous solutions or suspensions, may further additionally contain all known ingredients customary in such compositions, preferably at least one further ingredient being present in the composition.
- agents described may contain surfactants, builders, bleaches or bleach activators. Furthermore, they can water-miscible organic solvents, sequestering agents, electrolytes, pH regulators and / or other auxiliaries such as optical brighteners, grayness inhibitors, foam regulators and dyes and perfumes and
- Patent Application WO2009 / 121725 beginning on page 5, penultimate paragraph, and ending on page 13 after the second paragraph. This disclosure is incorporated herein by reference and the disclosure is incorporated herein by reference.
- a further subject of the invention is a method for the cleaning of textiles or hard surfaces, which is characterized in that in at least one method step a means described herein is used.
- Processes for the purification of textiles are generally distinguished by the fact that various cleaning-active substances are applied to the fabric in several process steps
- the material to be cleaned is applied and washed off after the action time, or the material to be cleaned is treated in any other way with a detergent or a solution or dilution of this agent.
- the same applies to processes for cleaning all other materials than textiles, especially hard surfaces. All conceivable washing or cleaning methods can be enriched in at least one of the method steps to the application of a washing or cleaning agent described herein and then provide
- Another subject of the invention is the use of an agent described herein for cleaning or washing textiles or for cleaning hard surfaces.
- protease-containing detergents and cleaners in the presence of candidate compounds for use as enzyme stabilizers was investigated.
- candidate compounds in the presence of 1, 2-propanediol were each formulated at 1% (w / w) in a detergent or cleaner formulation (see Table 2).
- the protease (1% PUR) was added to the formulation and the formulation stored at 30 ° C for 8 weeks.
- AAPFpNA Bachem L-1400
- the release of pNA causes an increase in absorbance at 410 nm, the time course of which is a measure of the enzymatic activity.
- the measurement was carried out at a temperature of 25 ° C, at pH 8.6 and a wavelength of 410 nm.
- the measuring time was 5 min at a measuring interval of 20 to 60 seconds.
- the initial values for the proteolytic activity of the agent in question are compared with the values determined after storage.
- the stabilizing effect of each tested compound is therefore measured as a relative percentage increase in protease residual activity.
- the pH of the formulation was adjusted to 8.4 by the NaOH.
- the formulation clear and colorless.
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- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
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- Chemical Kinetics & Catalysis (AREA)
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- Veterinary Medicine (AREA)
- Medicinal Chemistry (AREA)
- Public Health (AREA)
- General Health & Medical Sciences (AREA)
- Animal Behavior & Ethology (AREA)
- Pharmacology & Pharmacy (AREA)
- Engineering & Computer Science (AREA)
- Wood Science & Technology (AREA)
- Oil, Petroleum & Natural Gas (AREA)
- General Chemical & Material Sciences (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Tropical Medicine & Parasitology (AREA)
- Epidemiology (AREA)
- Virology (AREA)
- Molecular Biology (AREA)
- Communicable Diseases (AREA)
- Oncology (AREA)
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Abstract
La présente invention concerne des agents de lavage et de nettoyage contenant au moins une protéase et au moins un composé organique de la formule (I), qui agit comme inhibiteur de protéase et est donc un stabilisateur enzymatique approprié, et l'utilisation de ces composés comme stabilisateur enzymatique dans des agents de lavage et de nettoyage contenant des protéases. L'invention concerne également les procédés de lavage et de nettoyage correspondants et l'utilisation des agents décrits ici.
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
DE102014224746.2A DE102014224746A1 (de) | 2014-12-03 | 2014-12-03 | Enzymstabilisatoren |
PCT/EP2015/076747 WO2016087182A1 (fr) | 2014-12-03 | 2015-11-17 | Stabilisateurs enzymatiques |
Publications (1)
Publication Number | Publication Date |
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EP3226872A1 true EP3226872A1 (fr) | 2017-10-11 |
Family
ID=54557401
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
EP15797062.5A Withdrawn EP3226872A1 (fr) | 2014-12-03 | 2015-11-17 | Stabilisateurs enzymatiques |
Country Status (4)
Country | Link |
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US (1) | US20170349860A1 (fr) |
EP (1) | EP3226872A1 (fr) |
DE (1) | DE102014224746A1 (fr) |
WO (1) | WO2016087182A1 (fr) |
Family Cites Families (6)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JPH02219571A (ja) * | 1989-02-20 | 1990-09-03 | Kanebo Ltd | 修飾プロテアーゼ及びその製造法 |
US5741767A (en) | 1995-11-16 | 1998-04-21 | Lever Brothers Company, Division Of Conopco, Inc. | Peracid based dishwashing detergent composition |
US7597766B2 (en) * | 2007-08-03 | 2009-10-06 | American Sterilizer Company | Biodegradable detergent concentrate for medical instruments and equipment |
DE102007041754A1 (de) * | 2007-09-04 | 2009-03-05 | Henkel Ag & Co. Kgaa | Polycyclische Verbindungen als Enzymstabilisatoren |
US8293174B2 (en) * | 2007-10-17 | 2012-10-23 | American Sterilizer Company | Prion deactivating composition and methods of using same |
DE102008017103A1 (de) | 2008-04-02 | 2009-10-08 | Henkel Ag & Co. Kgaa | Wasch- und Reinigungsmittel enthaltend Proteasen aus Xanthomonas |
-
2014
- 2014-12-03 DE DE102014224746.2A patent/DE102014224746A1/de not_active Withdrawn
-
2015
- 2015-11-17 WO PCT/EP2015/076747 patent/WO2016087182A1/fr active Application Filing
- 2015-11-17 US US15/532,505 patent/US20170349860A1/en not_active Abandoned
- 2015-11-17 EP EP15797062.5A patent/EP3226872A1/fr not_active Withdrawn
Non-Patent Citations (2)
Title |
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None * |
See also references of WO2016087182A1 * |
Also Published As
Publication number | Publication date |
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DE102014224746A1 (de) | 2016-06-09 |
US20170349860A1 (en) | 2017-12-07 |
WO2016087182A1 (fr) | 2016-06-09 |
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