CA2028203A1 - Enzyme-containing detergent compositions and their use - Google Patents
Enzyme-containing detergent compositions and their useInfo
- Publication number
- CA2028203A1 CA2028203A1 CA 2028203 CA2028203A CA2028203A1 CA 2028203 A1 CA2028203 A1 CA 2028203A1 CA 2028203 CA2028203 CA 2028203 CA 2028203 A CA2028203 A CA 2028203A CA 2028203 A1 CA2028203 A1 CA 2028203A1
- Authority
- CA
- Canada
- Prior art keywords
- detergent
- detergent composition
- lipase
- composition according
- protease
- 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.)
- Abandoned
Links
- 239000003599 detergent Substances 0.000 title claims abstract description 88
- 239000000203 mixture Substances 0.000 title claims abstract description 85
- 102000004190 Enzymes Human genes 0.000 title claims abstract description 50
- 108090000790 Enzymes Proteins 0.000 title claims abstract description 50
- 108090001060 Lipase Proteins 0.000 claims abstract description 58
- 102000004882 Lipase Human genes 0.000 claims abstract description 57
- 239000004367 Lipase Substances 0.000 claims abstract description 57
- 235000019421 lipase Nutrition 0.000 claims abstract description 57
- 229940088598 enzyme Drugs 0.000 claims abstract description 49
- 108091005804 Peptidases Proteins 0.000 claims abstract description 40
- 239000004365 Protease Substances 0.000 claims abstract description 34
- 102000013142 Amylases Human genes 0.000 claims abstract description 25
- 108010065511 Amylases Proteins 0.000 claims abstract description 25
- 239000004382 Amylase Substances 0.000 claims abstract description 24
- 235000019418 amylase Nutrition 0.000 claims abstract description 24
- 108010059892 Cellulase Proteins 0.000 claims abstract description 18
- 229940106157 cellulase Drugs 0.000 claims abstract description 18
- 239000004094 surface-active agent Substances 0.000 claims abstract description 8
- 239000002736 nonionic surfactant Substances 0.000 claims abstract description 5
- 125000000129 anionic group Chemical group 0.000 claims abstract description 4
- 239000003945 anionic surfactant Substances 0.000 claims abstract description 4
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 claims abstract 6
- 239000007788 liquid Substances 0.000 claims description 14
- 229910019142 PO4 Inorganic materials 0.000 claims description 8
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 claims description 8
- 239000010452 phosphate Substances 0.000 claims description 8
- 239000000843 powder Substances 0.000 claims description 8
- OWEGMIWEEQEYGQ-UHFFFAOYSA-N 100676-05-9 Natural products OC1C(O)C(O)C(CO)OC1OCC1C(O)C(O)C(O)C(OC2C(OC(O)C(O)C2O)CO)O1 OWEGMIWEEQEYGQ-UHFFFAOYSA-N 0.000 claims description 2
- GUBGYTABKSRVRQ-PICCSMPSSA-N Maltose Natural products O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@@H](CO)OC(O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-PICCSMPSSA-N 0.000 claims description 2
- 238000004061 bleaching Methods 0.000 claims 1
- 239000012141 concentrate Substances 0.000 claims 1
- 102000035195 Peptidases Human genes 0.000 description 34
- 235000019419 proteases Nutrition 0.000 description 23
- CDBYLPFSWZWCQE-UHFFFAOYSA-L Sodium Carbonate Chemical compound [Na+].[Na+].[O-]C([O-])=O CDBYLPFSWZWCQE-UHFFFAOYSA-L 0.000 description 12
- PMZURENOXWZQFD-UHFFFAOYSA-L Sodium Sulfate Chemical compound [Na+].[Na+].[O-]S([O-])(=O)=O PMZURENOXWZQFD-UHFFFAOYSA-L 0.000 description 10
- 102000005158 Subtilisins Human genes 0.000 description 9
- 108010056079 Subtilisins Proteins 0.000 description 9
- 239000007844 bleaching agent Substances 0.000 description 9
- 239000012190 activator Substances 0.000 description 8
- 230000007935 neutral effect Effects 0.000 description 8
- 239000010457 zeolite Substances 0.000 description 8
- 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 7
- 229910021536 Zeolite Inorganic materials 0.000 description 7
- HNPSIPDUKPIQMN-UHFFFAOYSA-N dioxosilane;oxo(oxoalumanyloxy)alumane Chemical compound O=[Si]=O.O=[Al]O[Al]=O HNPSIPDUKPIQMN-UHFFFAOYSA-N 0.000 description 7
- 229910052708 sodium Inorganic materials 0.000 description 7
- 239000011734 sodium Substances 0.000 description 7
- DNIAPMSPPWPWGF-UHFFFAOYSA-N Propylene glycol Chemical compound CC(O)CO DNIAPMSPPWPWGF-UHFFFAOYSA-N 0.000 description 6
- 229910017053 inorganic salt Inorganic materials 0.000 description 6
- 108010020132 microbial serine proteinases Proteins 0.000 description 6
- 229920000642 polymer Polymers 0.000 description 6
- 239000002243 precursor Substances 0.000 description 6
- 229910000029 sodium carbonate Inorganic materials 0.000 description 6
- 235000017550 sodium carbonate Nutrition 0.000 description 6
- NTHWMYGWWRZVTN-UHFFFAOYSA-N sodium silicate Chemical group [Na+].[Na+].[O-][Si]([O-])=O NTHWMYGWWRZVTN-UHFFFAOYSA-N 0.000 description 6
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 5
- BGRWYDHXPHLNKA-UHFFFAOYSA-N Tetraacetylethylenediamine Chemical group CC(=O)N(C(C)=O)CCN(C(C)=O)C(C)=O BGRWYDHXPHLNKA-UHFFFAOYSA-N 0.000 description 5
- 239000000654 additive Substances 0.000 description 5
- -1 alkali metal nitrilo-triacetates Chemical class 0.000 description 5
- 239000000463 material Substances 0.000 description 5
- 229910052938 sodium sulfate Inorganic materials 0.000 description 5
- 235000011152 sodium sulphate Nutrition 0.000 description 5
- 238000005406 washing Methods 0.000 description 5
- BTBUEUYNUDRHOZ-UHFFFAOYSA-N Borate Chemical compound [O-]B([O-])[O-] BTBUEUYNUDRHOZ-UHFFFAOYSA-N 0.000 description 4
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical group NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 4
- 239000004115 Sodium Silicate Substances 0.000 description 4
- 239000003513 alkali Substances 0.000 description 4
- KGBXLFKZBHKPEV-UHFFFAOYSA-N boric acid Chemical compound OB(O)O KGBXLFKZBHKPEV-UHFFFAOYSA-N 0.000 description 4
- 239000004327 boric acid Substances 0.000 description 4
- 230000000694 effects Effects 0.000 description 4
- 238000009472 formulation Methods 0.000 description 4
- 229920001983 poloxamer Polymers 0.000 description 4
- 229940024999 proteolytic enzymes for treatment of wounds and ulcers Drugs 0.000 description 4
- 239000000344 soap Substances 0.000 description 4
- 229910052911 sodium silicate Inorganic materials 0.000 description 4
- 235000019832 sodium triphosphate Nutrition 0.000 description 4
- 239000003381 stabilizer Substances 0.000 description 4
- 229910021653 sulphate ion Inorganic materials 0.000 description 4
- 241000193830 Bacillus <bacterium> Species 0.000 description 3
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 3
- IAYPIBMASNFSPL-UHFFFAOYSA-N Ethylene oxide Chemical compound C1CO1 IAYPIBMASNFSPL-UHFFFAOYSA-N 0.000 description 3
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- 229920002125 Sokalan® Polymers 0.000 description 3
- 108090000787 Subtilisin Proteins 0.000 description 3
- 229910052783 alkali metal Inorganic materials 0.000 description 3
- 239000003795 chemical substances by application Substances 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
- 229940079919 digestives enzyme preparation Drugs 0.000 description 3
- 239000004615 ingredient Substances 0.000 description 3
- 108010003855 mesentericopeptidase Proteins 0.000 description 3
- 150000004682 monohydrates Chemical class 0.000 description 3
- 150000004965 peroxy acids Chemical class 0.000 description 3
- 229920005862 polyol Polymers 0.000 description 3
- 150000003077 polyols Chemical class 0.000 description 3
- 238000002360 preparation method Methods 0.000 description 3
- 150000003138 primary alcohols Chemical class 0.000 description 3
- HFQQZARZPUDIFP-UHFFFAOYSA-M sodium;2-dodecylbenzenesulfonate Chemical compound [Na+].CCCCCCCCCCCCC1=CC=CC=C1S([O-])(=O)=O HFQQZARZPUDIFP-UHFFFAOYSA-M 0.000 description 3
- 239000007787 solid Substances 0.000 description 3
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 3
- WBIQQQGBSDOWNP-UHFFFAOYSA-N 2-dodecylbenzenesulfonic acid Chemical compound CCCCCCCCCCCCC1=CC=CC=C1S(O)(=O)=O WBIQQQGBSDOWNP-UHFFFAOYSA-N 0.000 description 2
- 239000004471 Glycine Substances 0.000 description 2
- BPQQTUXANYXVAA-UHFFFAOYSA-N Orthosilicate Chemical compound [O-][Si]([O-])([O-])[O-] BPQQTUXANYXVAA-UHFFFAOYSA-N 0.000 description 2
- NBIIXXVUZAFLBC-UHFFFAOYSA-N Phosphoric acid Chemical compound OP(O)(O)=O NBIIXXVUZAFLBC-UHFFFAOYSA-N 0.000 description 2
- 241000589516 Pseudomonas Species 0.000 description 2
- QAOWNCQODCNURD-UHFFFAOYSA-L Sulfate Chemical compound [O-]S([O-])(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-L 0.000 description 2
- 241000203770 Thermoactinomyces vulgaris Species 0.000 description 2
- 241000223258 Thermomyces lanuginosus Species 0.000 description 2
- NIXOWILDQLNWCW-UHFFFAOYSA-N acrylic acid group Chemical group C(C=C)(=O)O NIXOWILDQLNWCW-UHFFFAOYSA-N 0.000 description 2
- 150000001340 alkali metals Chemical class 0.000 description 2
- 229910021538 borax Inorganic materials 0.000 description 2
- HXTDNAAFCPAMND-UHFFFAOYSA-N boric acid tetrahydrate Chemical compound O.O.O.O.OB(O)O.OB(O)O.OB(O)O.OB(O)O HXTDNAAFCPAMND-UHFFFAOYSA-N 0.000 description 2
- 230000009260 cross reactivity Effects 0.000 description 2
- 235000014113 dietary fatty acids Nutrition 0.000 description 2
- 239000000194 fatty acid Substances 0.000 description 2
- 229930195729 fatty acid Natural products 0.000 description 2
- 150000004665 fatty acids Chemical class 0.000 description 2
- 230000002538 fungal effect Effects 0.000 description 2
- 238000010353 genetic engineering Methods 0.000 description 2
- 239000008187 granular material Substances 0.000 description 2
- 244000005700 microbiome Species 0.000 description 2
- HWGNBUXHKFFFIH-UHFFFAOYSA-I pentasodium;[oxido(phosphonatooxy)phosphoryl] phosphate Chemical compound [Na+].[Na+].[Na+].[Na+].[Na+].[O-]P([O-])(=O)OP([O-])(=O)OP([O-])([O-])=O HWGNBUXHKFFFIH-UHFFFAOYSA-I 0.000 description 2
- 239000002304 perfume Substances 0.000 description 2
- 229910052698 phosphorus Inorganic materials 0.000 description 2
- 229920000058 polyacrylate Polymers 0.000 description 2
- 239000004584 polyacrylic acid Substances 0.000 description 2
- 235000019353 potassium silicate Nutrition 0.000 description 2
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 2
- 150000003839 salts Chemical class 0.000 description 2
- 239000000377 silicon dioxide Substances 0.000 description 2
- 238000002791 soaking Methods 0.000 description 2
- 239000012418 sodium perborate tetrahydrate Substances 0.000 description 2
- 239000004328 sodium tetraborate Substances 0.000 description 2
- 235000010339 sodium tetraborate Nutrition 0.000 description 2
- IBDSNZLUHYKHQP-UHFFFAOYSA-N sodium;3-oxidodioxaborirane;tetrahydrate Chemical compound O.O.O.O.[Na+].[O-]B1OO1 IBDSNZLUHYKHQP-UHFFFAOYSA-N 0.000 description 2
- 239000004753 textile Substances 0.000 description 2
- URAYPUMNDPQOKB-UHFFFAOYSA-N triacetin Chemical compound CC(=O)OCC(OC(C)=O)COC(C)=O URAYPUMNDPQOKB-UHFFFAOYSA-N 0.000 description 2
- OQNZFMZDPKAMHH-UHFFFAOYSA-N 1-methoxyethane-1,1,2-tricarboxylic acid Chemical class COC(C(O)=O)(C(O)=O)CC(O)=O OQNZFMZDPKAMHH-UHFFFAOYSA-N 0.000 description 1
- HZAXFHJVJLSVMW-UHFFFAOYSA-N 2-Aminoethan-1-ol Chemical compound NCCO HZAXFHJVJLSVMW-UHFFFAOYSA-N 0.000 description 1
- JVTIXNMXDLQEJE-UHFFFAOYSA-N 2-decanoyloxypropyl decanoate 2-octanoyloxypropyl octanoate Chemical compound C(CCCCCCC)(=O)OCC(C)OC(CCCCCCC)=O.C(=O)(CCCCCCCCC)OCC(C)OC(=O)CCCCCCCCC JVTIXNMXDLQEJE-UHFFFAOYSA-N 0.000 description 1
- UHPMCKVQTMMPCG-UHFFFAOYSA-N 5,8-dihydroxy-2-methoxy-6-methyl-7-(2-oxopropyl)naphthalene-1,4-dione Chemical compound CC1=C(CC(C)=O)C(O)=C2C(=O)C(OC)=CC(=O)C2=C1O UHPMCKVQTMMPCG-UHFFFAOYSA-N 0.000 description 1
- XSVSPKKXQGNHMD-UHFFFAOYSA-N 5-bromo-3-methyl-1,2-thiazole Chemical compound CC=1C=C(Br)SN=1 XSVSPKKXQGNHMD-UHFFFAOYSA-N 0.000 description 1
- QTBSBXVTEAMEQO-UHFFFAOYSA-M Acetate Chemical compound CC([O-])=O QTBSBXVTEAMEQO-UHFFFAOYSA-M 0.000 description 1
- 229910002012 Aerosil® Inorganic materials 0.000 description 1
- 241000588986 Alcaligenes Species 0.000 description 1
- 241000228212 Aspergillus Species 0.000 description 1
- 244000063299 Bacillus subtilis Species 0.000 description 1
- 235000014469 Bacillus subtilis Nutrition 0.000 description 1
- 241000589513 Burkholderia cepacia Species 0.000 description 1
- 229910021532 Calcite Inorganic materials 0.000 description 1
- CBOCVOKPQGJKKJ-UHFFFAOYSA-L Calcium formate Chemical compound [Ca+2].[O-]C=O.[O-]C=O CBOCVOKPQGJKKJ-UHFFFAOYSA-L 0.000 description 1
- 229920000742 Cotton Polymers 0.000 description 1
- FBPFZTCFMRRESA-FSIIMWSLSA-N D-Glucitol Natural products OC[C@H](O)[C@H](O)[C@@H](O)[C@H](O)CO FBPFZTCFMRRESA-FSIIMWSLSA-N 0.000 description 1
- FBPFZTCFMRRESA-JGWLITMVSA-N D-glucitol Chemical compound OC[C@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-JGWLITMVSA-N 0.000 description 1
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 1
- 108010067770 Endopeptidase K Proteins 0.000 description 1
- 108090000371 Esterases Proteins 0.000 description 1
- PIICEJLVQHRZGT-UHFFFAOYSA-N Ethylenediamine Chemical compound NCCN PIICEJLVQHRZGT-UHFFFAOYSA-N 0.000 description 1
- 241000192125 Firmicutes Species 0.000 description 1
- BDAGIHXWWSANSR-UHFFFAOYSA-M Formate Chemical compound [O-]C=O BDAGIHXWWSANSR-UHFFFAOYSA-M 0.000 description 1
- 241000233866 Fungi Species 0.000 description 1
- 241000223218 Fusarium Species 0.000 description 1
- 241000223198 Humicola Species 0.000 description 1
- 241000203622 Nocardiopsis Species 0.000 description 1
- 102000004316 Oxidoreductases Human genes 0.000 description 1
- 108090000854 Oxidoreductases Proteins 0.000 description 1
- 241001236817 Paecilomyces <Clavicipitaceae> Species 0.000 description 1
- 241000282320 Panthera leo Species 0.000 description 1
- 241001523956 Parengyodontium album Species 0.000 description 1
- ABLZXFCXXLZCGV-UHFFFAOYSA-N Phosphorous acid Chemical compound OP(O)=O ABLZXFCXXLZCGV-UHFFFAOYSA-N 0.000 description 1
- OAICVXFJPJFONN-UHFFFAOYSA-N Phosphorus Chemical compound [P] OAICVXFJPJFONN-UHFFFAOYSA-N 0.000 description 1
- ZLMJMSJWJFRBEC-UHFFFAOYSA-N Potassium Chemical compound [K] ZLMJMSJWJFRBEC-UHFFFAOYSA-N 0.000 description 1
- GOOHAUXETOMSMM-UHFFFAOYSA-N Propylene oxide Chemical compound CC1CO1 GOOHAUXETOMSMM-UHFFFAOYSA-N 0.000 description 1
- 101710194948 Protein phosphatase PhpP Proteins 0.000 description 1
- GBFLZEXEOZUWRN-VKHMYHEASA-N S-carboxymethyl-L-cysteine Chemical compound OC(=O)[C@@H](N)CSCC(O)=O GBFLZEXEOZUWRN-VKHMYHEASA-N 0.000 description 1
- 102000012479 Serine Proteases Human genes 0.000 description 1
- 108010022999 Serine Proteases Proteins 0.000 description 1
- FKNQFGJONOIPTF-UHFFFAOYSA-N Sodium cation Chemical compound [Na+] FKNQFGJONOIPTF-UHFFFAOYSA-N 0.000 description 1
- 101710173714 Subtilisin amylosacchariticus Proteins 0.000 description 1
- 241000223257 Thermomyces Species 0.000 description 1
- DPXJVFZANSGRMM-UHFFFAOYSA-N acetic acid;2,3,4,5,6-pentahydroxyhexanal;sodium Chemical compound [Na].CC(O)=O.OCC(O)C(O)C(O)C(O)C=O DPXJVFZANSGRMM-UHFFFAOYSA-N 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 150000007513 acids Chemical class 0.000 description 1
- 230000000996 additive effect Effects 0.000 description 1
- 229910000288 alkali metal carbonate Inorganic materials 0.000 description 1
- 150000008041 alkali metal carbonates Chemical class 0.000 description 1
- 239000002518 antifoaming agent Substances 0.000 description 1
- JXLHNMVSKXFWAO-UHFFFAOYSA-N azane;7-fluoro-2,1,3-benzoxadiazole-4-sulfonic acid Chemical compound N.OS(=O)(=O)C1=CC=C(F)C2=NON=C12 JXLHNMVSKXFWAO-UHFFFAOYSA-N 0.000 description 1
- 239000001639 calcium acetate Substances 0.000 description 1
- 235000011092 calcium acetate Nutrition 0.000 description 1
- 229960005147 calcium acetate Drugs 0.000 description 1
- 239000004281 calcium formate Substances 0.000 description 1
- 229940044172 calcium formate Drugs 0.000 description 1
- 235000019255 calcium formate Nutrition 0.000 description 1
- 239000001768 carboxy methyl cellulose Substances 0.000 description 1
- 239000012876 carrier material Substances 0.000 description 1
- 150000001860 citric acid derivatives Chemical class 0.000 description 1
- 239000004927 clay Substances 0.000 description 1
- 235000019864 coconut oil Nutrition 0.000 description 1
- 239000003240 coconut oil Substances 0.000 description 1
- 239000002131 composite material Substances 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- JYIMWRSJCRRYNK-UHFFFAOYSA-N dialuminum;disodium;oxygen(2-);silicon(4+);hydrate Chemical group O.[O-2].[O-2].[O-2].[O-2].[O-2].[O-2].[Na+].[Na+].[Al+3].[Al+3].[Si+4] JYIMWRSJCRRYNK-UHFFFAOYSA-N 0.000 description 1
- 150000001991 dicarboxylic acids Chemical class 0.000 description 1
- 235000011180 diphosphates Nutrition 0.000 description 1
- 238000004851 dishwashing Methods 0.000 description 1
- 239000000975 dye Substances 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 239000004744 fabric Substances 0.000 description 1
- 239000006260 foam Substances 0.000 description 1
- 229940044170 formate Drugs 0.000 description 1
- 239000001087 glyceryl triacetate Substances 0.000 description 1
- 235000013773 glyceryl triacetate Nutrition 0.000 description 1
- 125000002887 hydroxy group Chemical group [H]O* 0.000 description 1
- 230000001900 immune effect Effects 0.000 description 1
- 238000010412 laundry washing Methods 0.000 description 1
- 235000019626 lipase activity Nutrition 0.000 description 1
- 230000002366 lipolytic effect Effects 0.000 description 1
- 238000004519 manufacturing process Methods 0.000 description 1
- 238000000034 method Methods 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 239000002245 particle Substances 0.000 description 1
- 235000011007 phosphoric acid Nutrition 0.000 description 1
- 239000011574 phosphorus Substances 0.000 description 1
- 229920000728 polyester Polymers 0.000 description 1
- 229910052700 potassium Inorganic materials 0.000 description 1
- 239000011591 potassium Substances 0.000 description 1
- 108090000623 proteins and genes Proteins 0.000 description 1
- WQGWDDDVZFFDIG-UHFFFAOYSA-N pyrogallol Chemical compound OC1=CC=CC(O)=C1O WQGWDDDVZFFDIG-UHFFFAOYSA-N 0.000 description 1
- 239000003352 sequestering agent Substances 0.000 description 1
- 235000019812 sodium carboxymethyl cellulose Nutrition 0.000 description 1
- 229920001027 sodium carboxymethylcellulose Polymers 0.000 description 1
- KKCBUQHMOMHUOY-UHFFFAOYSA-N sodium oxide Chemical compound [O-2].[Na+].[Na+] KKCBUQHMOMHUOY-UHFFFAOYSA-N 0.000 description 1
- 229910001948 sodium oxide Inorganic materials 0.000 description 1
- 229960001922 sodium perborate Drugs 0.000 description 1
- RBWSWDPRDBEWCR-RKJRWTFHSA-N sodium;(2r)-2-[(2r)-3,4-dihydroxy-5-oxo-2h-furan-2-yl]-2-hydroxyethanolate Chemical group [Na+].[O-]C[C@@H](O)[C@H]1OC(=O)C(O)=C1O RBWSWDPRDBEWCR-RKJRWTFHSA-N 0.000 description 1
- QUCDWLYKDRVKMI-UHFFFAOYSA-M sodium;3,4-dimethylbenzenesulfonate Chemical compound [Na+].CC1=CC=C(S([O-])(=O)=O)C=C1C QUCDWLYKDRVKMI-UHFFFAOYSA-M 0.000 description 1
- YKLJGMBLPUQQOI-UHFFFAOYSA-M sodium;oxidooxy(oxo)borane Chemical compound [Na+].[O-]OB=O YKLJGMBLPUQQOI-UHFFFAOYSA-M 0.000 description 1
- 239000002689 soil Substances 0.000 description 1
- 239000000600 sorbitol Substances 0.000 description 1
- 230000006641 stabilisation Effects 0.000 description 1
- 238000003860 storage Methods 0.000 description 1
- 239000000375 suspending agent Substances 0.000 description 1
- 239000003760 tallow Substances 0.000 description 1
- 150000004685 tetrahydrates Chemical class 0.000 description 1
- 108010031354 thermitase Proteins 0.000 description 1
- 239000002562 thickening agent Substances 0.000 description 1
- 229960002622 triacetin Drugs 0.000 description 1
- 241001446247 uncultured actinomycete Species 0.000 description 1
- 239000004711 α-olefin Substances 0.000 description 1
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
- C11D3/38—Products with no well-defined composition, e.g. natural products
- C11D3/386—Preparations containing enzymes, e.g. protease or amylase
- C11D3/38645—Preparations containing enzymes, e.g. protease or amylase containing cellulase
-
- 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
- C11D17/0004—Non aqueous liquid compositions comprising insoluble particles
-
- 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
- C11D17/0047—Detergents in the form of bars or tablets
- C11D17/0065—Solid detergents containing builders
- C11D17/0069—Laundry bars
-
- 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
- C11D3/38627—Preparations containing enzymes, e.g. protease or amylase containing lipase
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- Life Sciences & Earth Sciences (AREA)
- Engineering & Computer Science (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Oil, Petroleum & Natural Gas (AREA)
- Wood Science & Technology (AREA)
- Organic Chemistry (AREA)
- Detergent Compositions (AREA)
Abstract
Abstract:
A detergent composition contains detergent surfactant, preferably anionic and/or nonionic surfactant, preferably builder, and enzymes including protease and amylase, characterised in that the composition contains a combination of three enzymes comprising protease, amylase and a third enzyme selected from lipase and cellulase.
A detergent composition contains detergent surfactant, preferably anionic and/or nonionic surfactant, preferably builder, and enzymes including protease and amylase, characterised in that the composition contains a combination of three enzymes comprising protease, amylase and a third enzyme selected from lipase and cellulase.
Description
. - 2~2~3 , .
c3339c:
Enzyme-Containing Detergent Compositions and their use This invention relates to detergent compositions, and to their use, and in particular to compositions containing ;~
plural enzymes, and to their use. s Prior Art~
Detergent compositions containing severally protease, ;~
~ lipase, amylase, cellulase, and other enzymes are known, :~: and certain combinations of enzymes in detergents are also : ~ 25 known.
In particular, the use of proteolytic enzymes in both solid and liqu~d detergent compositions is well known;
although these proteolytic enzymes can be of various types ;~ and sources, the proteolytic enzymes commonly used are those produced by Bacillus strains. Although with such ~ proteolytic enzymes satisfactory results as regards `~ performance can be achieved, it is frequently necessary to :include enzyme-stabilizing systems in the case of liquid detergent compositions to provide a satisfactory enzyme ~ 2~2~29~
stability during storage of the enzymatic liquid detergent composition.
We believe that representative examples of relevant prior art concerning proteases are as follows.
Serine proteases from Bacillus subtilis are very widely known and used in detergent compositions. They are available for example under Trade Marks Savinase, o Esperase, Maxatase, Alcalase, etc.
The prior art also includes W0 88/03946 (Novo), which discloses, as detergent additives, combinations of Bacillus proteases with alkaline fungal or actinomycete proteases, e.g. those proteases obtainable from the génera Paecilomyces, Fusarium, and Nocardiopsis. The disclosure extends to the use of the detergent additive as a liquid, with a known enzyme stabiliser such as propylene glycol, ` for addition to a liquid detergent.
USP 3 707 504 (Procter & Gamble) discloses detergents for laundry and dishwashing, comprising protease from Thermoactinomyces vulgaris ATCC 15734, which are formulated as solid or liquid detergent compositions. This document mentions surprising stability of protease from Thermoactinomyces vulgaris in highly-alkaline detergent , systems.
As to lipases, GB 1 372 034 (Unilever) for example discloses lipase from Pseudomonas in specific nonionic-containing detergent compositions for soaking fabrics.
~ .
~ USP 3 950 277 (Procter & Gamble) also describes fabric-- 35 soaking compositions: the described compositions comprise ;; lipase and lipase activators and a number of lipases from ` 2~2~2~3 microorganism and other sources are mentioned: those particularly mentioned as preferred are Amano CE, Amano M-AP, Takeda 1969-4-9, and Meito MY-30 lipases, but no indications are given of the form in which the lipase is s to be prepared or used.
UsP 4 011 169/NL 74 08763 (Procter & Gamble) describes the use of a similar range of enzymes in the preparation of additives for washing agents (detergent compositions).
Examples of known lipase-containing detergent compositions are provided by EP 0 205 208 and 0 206 390 (Unilever), which relate to lipases related to those from Ps.
fluorescens, P gladioli and Chromobacter in detergent compositions.
EP 0 214 761 (Novo) and EP 0 258 068 (Novo), each give detailed description of lipases from certain microorganisms, and also give certain uses in detergent ~ ~
-20 additives and detergent compositions for the enzymes ~ -; described. EP 0 214 761 gives detailed description of lipases derived from organisms of the species Pseudomonas cepacia, and certain uses therefor. EP 0 258 068 gives detailed description of lipases derived ~rom organisms of t~e genus Thermomyces/Humicola, and certain USQS therefor.
,,-~ , .
Also believed to be in use in certain areas is a lipase-~containing granular de,tergent composition containing about 37% detergent actives including 5% nonionic detergent and -~ the remainder substantially anionic detergent, about 16%
~:
zeolite, about 60 LU/g lipase, plus protease and other normal detergent additives.
`~ 35 Further examples of known lipase-containing detergent ~ compositions are provided by JA 63-078000 (1988) (Lion , . . .
.. ~ ,- . ~.
f` 2~2~
, .
- 4 - .
:
Corp/K Mukoyama et al) which discloses properties and uses of a Pseudomonas lipase, including use in a lipase-containing system based on 10-40 % surfactant (e.g. sodium C14-C18 alpha-olefin sulphonate), as well as other conventional detergent ingredients.
Also in the prior art is Research Disclosure 29056 of June 1988 which discloses lipase in connexion with a large number of descriptions of detergent compositions, many of which descriptions also men-tion other enzymes than ~ ;
lipases.
Use of amylase in conjunction with protease is discIosed in for example GB 2 131 826 (Colgate-Palmolive) and specifications cited therein, especially in GB 1 576 946 (Procter & Gamble). Amylase enzyme in detergent compositions is also part of the subject of EP 0 118 933 ; ~ -(Procter & Gamble) and GB 1 247 292 (Novo).
It is known to stabilise enzymes when these are formulated into liquid detergent compositions: representative ~ ~
; examples of prîor art as to enzyme stabilisation in liquid ~ -detergents are as follows.
~;"~
2s JP 47-35192 describes the use of glycerol or sorbitol with borax under certain conditions and proportions, to stabilise enzyme preparations including liquid washing materials. ~ , ! ` . ! ' ' ~ ' ~
DE 27 28 211 (Unilever) describes the use of polyols of 2 to 6 hydroxy groups together with boric acid or borate in ratios less than 1, particularly in unbuilt detergents.
~; ~5 GB 2 079 305 (Unilever) describes the use of polyols together with boric acid and/or borate and polyacrylate .
polymers as stabilising agents, while EP 0 08Q 223 (Unilever) describes the combined use of boric acid or borate and polyol or polyamino compounds with reducing salts, and EP O 126 505 (Unilever) describes the use of boric acid or borate and reducing salts, together with succinic or other dicarboxylic acids. Other prior art deals with the use of stabilisers such as calcium formate/acetate.
The Present Invention:
According to the present invention we have found that detergent compositions containing certain mixtures of S enzymes can give surprisingly good stain-removal effects.
Conmparison with earlier compositions shows that some stains can be removed more effectively, others can be effectively removed with lower total amounts of enzyme than with earlier formulations.
According to the present invention there is provided a detergent composition containing detergent surfactant, preferably anionic and/or nonionic, preferably builder, and a combination of at least two and preferably three 2s enzymes selected from protease, lipase, amylase, and cellulase, preferably in proportions more particularly exemplified below.
In particular, the invention provides for example a ~ detergent composition containing detergent surfactant, preferably anionic and/or nonionic surfactant, preferably builder, and enzymes including protease and amylase, characterised in that the composition contains a combination of three enzymes comprising protease, amylase and a third enzyme selected from lipase and cellulase.
-- 2~2~20~
The ratio between the amount of the amylase and lipase (and/or cellulase) taken together, and the protease is preferably that which is expressed by a ratio in the range 0.3 -540 ( (KNU~KLU*) : KNPU).
KNPU denotes kilo Novo protease units; KNU are kilo Novo units used for measuring amylase activity; KLU are standard kilo units defined by Novo for measuring lipase activity; CEYU are standard units for measuring cellulase o activity. RLU* denotes a composite measure for the purposes herein, in which units of lipase (in KLU) are aggregated with units of cellulase, counted as if l KLU
were constituted by 10 CEVU for this purpose only.
lS Preferably the ratio between the amount of the amylase and lipase (and/or cellulase) taken together, and the protease, is in the range 1-100, e.g. 1-30 ( (KNU+KLU*) : -~
KNPU).
Preferably the relation of amylase to lipase (and/or cellulase) is expressed by a ratio in the range 0.02 - 240 (KNU:KLU*), e.g. a ratio is in the ranqe 0.1-100, e.g. 1-10 (KNU:~CLU*) .
~:~ 25 Several useful embodiments of the invention e.g. as described below contain protease, amylase and lipase.
Cellulase can be added to such mixtures if desired.
The enzymes can usefully be added in the form of granular compositions of enzyme with carrier material.
' ` .:
It is within the scope of the invention to add plural ~-enzyme preparations in the formulation of the detergent compositions, each of which can be in the form of a composition of a respective enzyme with e.g. granular or . ~2~
.
slurrying material, or to add preparations in which the enzymes are present in admixture. At present, for convenience, we usually choose to add plural enzyme preparations each containing an enzyme with carrier s material.
Protease can for example be used in an amount in the range about 0.0002 to about 0.05 Anson units per gram of the detergent composition. Often in practice the quantity of protease added is in the range 0.05-5%, (e.g. 0.2-4%, corresponding in the case of Savinase (TM) to 1-24 KNPU/lOOg).
The protease can be chosen from among a wide range of enzymes, e.g. those available under the Trade Marks Savinase, Esperase, Maxatase, Alcalase, or other subtilisin proteases obtained from Gram-positive bacteria or fungi, e.g. subtilisins from Bacillus strains, namely, subtilisin 168, subtilisin BPN', subtilisin Carlsberg, subtilisin DY, subtilisin amylosacchariticus, and mesentericopeptidase (Kurihara et al., 1972, J.Biol.Chem.
247:5629-5631; Stahl and Ferrari, 1984, J.Bacteriol.
159:811-819, Jacobs et al., 1985, Nucl.Acids Res. 13:8913-8926; Nedkov et al., 1985, Biol.Chem. Hoppe-Seyler 2S 366:421-430, Svendsen et al., 1986, FEBS Lett 196:228-232), and two fungal subtilisins, subtilisin thermitase ~` from Thermoactinymyces vulgaris (Meloun et al., 1985, FEBS
Lett.~ 1983;195-200) and proteinase K from Tritirachium album (Jany and Mayer, 1985, Biol.Chem. Hoppe-Seyler -366:584-492).
Included within the scope of the invention is the use of ~-modified proteases such as those described in EP 0 130 756 ~Genentech), USP 4 760 025 (Genencor), EP 0 214 435 ;~-' ~ ~
c3339c:
Enzyme-Containing Detergent Compositions and their use This invention relates to detergent compositions, and to their use, and in particular to compositions containing ;~
plural enzymes, and to their use. s Prior Art~
Detergent compositions containing severally protease, ;~
~ lipase, amylase, cellulase, and other enzymes are known, :~: and certain combinations of enzymes in detergents are also : ~ 25 known.
In particular, the use of proteolytic enzymes in both solid and liqu~d detergent compositions is well known;
although these proteolytic enzymes can be of various types ;~ and sources, the proteolytic enzymes commonly used are those produced by Bacillus strains. Although with such ~ proteolytic enzymes satisfactory results as regards `~ performance can be achieved, it is frequently necessary to :include enzyme-stabilizing systems in the case of liquid detergent compositions to provide a satisfactory enzyme ~ 2~2~29~
stability during storage of the enzymatic liquid detergent composition.
We believe that representative examples of relevant prior art concerning proteases are as follows.
Serine proteases from Bacillus subtilis are very widely known and used in detergent compositions. They are available for example under Trade Marks Savinase, o Esperase, Maxatase, Alcalase, etc.
The prior art also includes W0 88/03946 (Novo), which discloses, as detergent additives, combinations of Bacillus proteases with alkaline fungal or actinomycete proteases, e.g. those proteases obtainable from the génera Paecilomyces, Fusarium, and Nocardiopsis. The disclosure extends to the use of the detergent additive as a liquid, with a known enzyme stabiliser such as propylene glycol, ` for addition to a liquid detergent.
USP 3 707 504 (Procter & Gamble) discloses detergents for laundry and dishwashing, comprising protease from Thermoactinomyces vulgaris ATCC 15734, which are formulated as solid or liquid detergent compositions. This document mentions surprising stability of protease from Thermoactinomyces vulgaris in highly-alkaline detergent , systems.
As to lipases, GB 1 372 034 (Unilever) for example discloses lipase from Pseudomonas in specific nonionic-containing detergent compositions for soaking fabrics.
~ .
~ USP 3 950 277 (Procter & Gamble) also describes fabric-- 35 soaking compositions: the described compositions comprise ;; lipase and lipase activators and a number of lipases from ` 2~2~2~3 microorganism and other sources are mentioned: those particularly mentioned as preferred are Amano CE, Amano M-AP, Takeda 1969-4-9, and Meito MY-30 lipases, but no indications are given of the form in which the lipase is s to be prepared or used.
UsP 4 011 169/NL 74 08763 (Procter & Gamble) describes the use of a similar range of enzymes in the preparation of additives for washing agents (detergent compositions).
Examples of known lipase-containing detergent compositions are provided by EP 0 205 208 and 0 206 390 (Unilever), which relate to lipases related to those from Ps.
fluorescens, P gladioli and Chromobacter in detergent compositions.
EP 0 214 761 (Novo) and EP 0 258 068 (Novo), each give detailed description of lipases from certain microorganisms, and also give certain uses in detergent ~ ~
-20 additives and detergent compositions for the enzymes ~ -; described. EP 0 214 761 gives detailed description of lipases derived from organisms of the species Pseudomonas cepacia, and certain uses therefor. EP 0 258 068 gives detailed description of lipases derived ~rom organisms of t~e genus Thermomyces/Humicola, and certain USQS therefor.
,,-~ , .
Also believed to be in use in certain areas is a lipase-~containing granular de,tergent composition containing about 37% detergent actives including 5% nonionic detergent and -~ the remainder substantially anionic detergent, about 16%
~:
zeolite, about 60 LU/g lipase, plus protease and other normal detergent additives.
`~ 35 Further examples of known lipase-containing detergent ~ compositions are provided by JA 63-078000 (1988) (Lion , . . .
.. ~ ,- . ~.
f` 2~2~
, .
- 4 - .
:
Corp/K Mukoyama et al) which discloses properties and uses of a Pseudomonas lipase, including use in a lipase-containing system based on 10-40 % surfactant (e.g. sodium C14-C18 alpha-olefin sulphonate), as well as other conventional detergent ingredients.
Also in the prior art is Research Disclosure 29056 of June 1988 which discloses lipase in connexion with a large number of descriptions of detergent compositions, many of which descriptions also men-tion other enzymes than ~ ;
lipases.
Use of amylase in conjunction with protease is discIosed in for example GB 2 131 826 (Colgate-Palmolive) and specifications cited therein, especially in GB 1 576 946 (Procter & Gamble). Amylase enzyme in detergent compositions is also part of the subject of EP 0 118 933 ; ~ -(Procter & Gamble) and GB 1 247 292 (Novo).
It is known to stabilise enzymes when these are formulated into liquid detergent compositions: representative ~ ~
; examples of prîor art as to enzyme stabilisation in liquid ~ -detergents are as follows.
~;"~
2s JP 47-35192 describes the use of glycerol or sorbitol with borax under certain conditions and proportions, to stabilise enzyme preparations including liquid washing materials. ~ , ! ` . ! ' ' ~ ' ~
DE 27 28 211 (Unilever) describes the use of polyols of 2 to 6 hydroxy groups together with boric acid or borate in ratios less than 1, particularly in unbuilt detergents.
~; ~5 GB 2 079 305 (Unilever) describes the use of polyols together with boric acid and/or borate and polyacrylate .
polymers as stabilising agents, while EP 0 08Q 223 (Unilever) describes the combined use of boric acid or borate and polyol or polyamino compounds with reducing salts, and EP O 126 505 (Unilever) describes the use of boric acid or borate and reducing salts, together with succinic or other dicarboxylic acids. Other prior art deals with the use of stabilisers such as calcium formate/acetate.
The Present Invention:
According to the present invention we have found that detergent compositions containing certain mixtures of S enzymes can give surprisingly good stain-removal effects.
Conmparison with earlier compositions shows that some stains can be removed more effectively, others can be effectively removed with lower total amounts of enzyme than with earlier formulations.
According to the present invention there is provided a detergent composition containing detergent surfactant, preferably anionic and/or nonionic, preferably builder, and a combination of at least two and preferably three 2s enzymes selected from protease, lipase, amylase, and cellulase, preferably in proportions more particularly exemplified below.
In particular, the invention provides for example a ~ detergent composition containing detergent surfactant, preferably anionic and/or nonionic surfactant, preferably builder, and enzymes including protease and amylase, characterised in that the composition contains a combination of three enzymes comprising protease, amylase and a third enzyme selected from lipase and cellulase.
-- 2~2~20~
The ratio between the amount of the amylase and lipase (and/or cellulase) taken together, and the protease is preferably that which is expressed by a ratio in the range 0.3 -540 ( (KNU~KLU*) : KNPU).
KNPU denotes kilo Novo protease units; KNU are kilo Novo units used for measuring amylase activity; KLU are standard kilo units defined by Novo for measuring lipase activity; CEYU are standard units for measuring cellulase o activity. RLU* denotes a composite measure for the purposes herein, in which units of lipase (in KLU) are aggregated with units of cellulase, counted as if l KLU
were constituted by 10 CEVU for this purpose only.
lS Preferably the ratio between the amount of the amylase and lipase (and/or cellulase) taken together, and the protease, is in the range 1-100, e.g. 1-30 ( (KNU+KLU*) : -~
KNPU).
Preferably the relation of amylase to lipase (and/or cellulase) is expressed by a ratio in the range 0.02 - 240 (KNU:KLU*), e.g. a ratio is in the ranqe 0.1-100, e.g. 1-10 (KNU:~CLU*) .
~:~ 25 Several useful embodiments of the invention e.g. as described below contain protease, amylase and lipase.
Cellulase can be added to such mixtures if desired.
The enzymes can usefully be added in the form of granular compositions of enzyme with carrier material.
' ` .:
It is within the scope of the invention to add plural ~-enzyme preparations in the formulation of the detergent compositions, each of which can be in the form of a composition of a respective enzyme with e.g. granular or . ~2~
.
slurrying material, or to add preparations in which the enzymes are present in admixture. At present, for convenience, we usually choose to add plural enzyme preparations each containing an enzyme with carrier s material.
Protease can for example be used in an amount in the range about 0.0002 to about 0.05 Anson units per gram of the detergent composition. Often in practice the quantity of protease added is in the range 0.05-5%, (e.g. 0.2-4%, corresponding in the case of Savinase (TM) to 1-24 KNPU/lOOg).
The protease can be chosen from among a wide range of enzymes, e.g. those available under the Trade Marks Savinase, Esperase, Maxatase, Alcalase, or other subtilisin proteases obtained from Gram-positive bacteria or fungi, e.g. subtilisins from Bacillus strains, namely, subtilisin 168, subtilisin BPN', subtilisin Carlsberg, subtilisin DY, subtilisin amylosacchariticus, and mesentericopeptidase (Kurihara et al., 1972, J.Biol.Chem.
247:5629-5631; Stahl and Ferrari, 1984, J.Bacteriol.
159:811-819, Jacobs et al., 1985, Nucl.Acids Res. 13:8913-8926; Nedkov et al., 1985, Biol.Chem. Hoppe-Seyler 2S 366:421-430, Svendsen et al., 1986, FEBS Lett 196:228-232), and two fungal subtilisins, subtilisin thermitase ~` from Thermoactinymyces vulgaris (Meloun et al., 1985, FEBS
Lett.~ 1983;195-200) and proteinase K from Tritirachium album (Jany and Mayer, 1985, Biol.Chem. Hoppe-Seyler -366:584-492).
Included within the scope of the invention is the use of ~-modified proteases such as those described in EP 0 130 756 ~Genentech), USP 4 760 025 (Genencor), EP 0 214 435 ;~-' ~ ~
- 2~2~2~3 - 8 - ;
(Henkel), WO 87/04461 (Amgen), WO 87/05050 (Genex), EP O
303 761 (Genentech), and EP O 260 lOS (Genencor).
Amylase can for example be used in an amount in the range about 1 to about 100 MU (maltose units) per gram of detergent composition, (or 0.014-1.4, e.g. 0.07-0.7, KNU/g (Novo units)), or for example 0.05-5%, (e.g. 0.1-4%, ~
corresponding in the case of Thermamyl (TM) to 6-240 ~-KNU/lOOg). ~
A preferred amylase for use in the invention is Thermamyl (from Novo).
The amount of lipase can be chosen within wide limits, for S example 50 to 30,000 LU/g of granular detergent composition, e.g. often at least 100 LU/g, very usefully at least 500 LU/g, sometimes preferably above 1000, above 2000 LUlg or above 4000 LU/g or more, thus very often within the range 50-4000 LU/g and possibly within the range 200-1000 LU/g.
, .
Often the amount of lipase used is in the range 0.005-5%, ;
(e.g. 0.01-3%, corresponding in the case of Lipolase (TM) to 1-300 KLU/lOOg).
The lipolytic enzyme can be chosen from among a wide range o~ lipases: in particular the lipases described in for example the following patent specifications, EP O 214 761 (Novo), EP O 258 068 (Novo) and especially lipases showing ~ -immunological cross-reactivity with antisera raised against lipase from Thermomyces lanuginosus ATCC 22070, EP
0 205 208 (Unilever) and EP O 206 390 ~Unilever), and ~ - -especially lipases showing immunological cross-reactivity ~; 35 with antisera raised against lipase from Chromobacter ~ viscosum var lipolyticum NRRL B-3673, or against lipase ,~:
: ~ .
--;` 2~2~
from Alcaligenes PL-679, ATCC 31371 and FERM-P 3783, also the lipases described in specifications WO 87/00859 (Gist-Brocades) and EP O 204 284 (Sapporo Breweries). Suitable in particular are for example the following commercially available lipase preparations: Novo Lipolase, Amano lipases CE, P, B, AP, M-AP, AML, and CES, and Meito lipases MY-30, OF, and PL, also esterase MM, Lipozym, SP225, SP285, Saiken lipase, Enzeco lipase, Toyo Jozo lipase and Diosynth lipase (Trade Marks).
Cellulase can for example be used in an amount in the range about 0.3 to about 35 CEVU units per gram (30-3500 CEVU/lOOg) of the detergent composition.
Whenever desired, the enzymes used may be those obtained by genetic engineering on the basis of mutant producer organisms.
Genetic engineering of the enzymes can be achieved by extraction of an appropriate lipase gene, e.g. the gene ~ ;
~; for lipase from Thermomyces lanuginosus or from a mutant t~ereof, and introduction and expression of the qene or derivative thereof in a suitable producer organism such as an Aspergillus. The techniques described in WO 88/02775 2s (Novo), EP O 243 338 (Labofina) and EP O 268 452 ~` (Genencor) may be applied and adapted.
It i8 preferable to choose the enzymes using any one or more of the following ranges and ratios~
For the range of the protease, e.g. about 1 - 24 ~ KNPU/lOOgram detergent composition (e.g. on basis of solid ;~ or liquid composition or of dry components of liquid ` ~ ~5 composition).
,"~ ,, .
.
-` 2~2~2~
For the relation between the amount of the amylase and lipase taken together, and the protease, e.g. a ratio of 0.3 - 540 (KNU + KLU : KNPU).
For the relation of amylase to lipase, e.g. 0.02 - 240 (KNU:KLU).
More-preferred ranges are~
Protease: e.g. 3-6 (XNPU/lOOg);
Ratio of amylase + lipase to protease of 1-100, e.g. 1-30 (KNU+KLU : KNPU);
Ratio of amylase to lipase of 0.1- 100, e.g. 1 - 10 (KNU:KLU).
Where cellulase is present instead of lipase, these ~ -formulae can be applied and adapted reckoning 10 CEVU unit ; as equivalent to 1 KLU.
For several practical embodiments, it has been found convenient to use up to about 1.9% Savinase, (11.4 KNPU/lOOg); up to about 1.8% Thermamyl (108 KNU/lOOg);
and up to about 1.1~ Lipolase (110 KLU/lOOg).
~ 25 .~ Detergent compositions according to the invention may furthermore include the following usual detergent ~-`~ ingredients in th~ usual amounts. They may be built or unbuilt, and may be of the zero-P type (i.e. not containing any phosphorus-containing builders). Thus the ~ `
composition may contain from 1-45%, e.g. 5-30% by weight of one or more organic and/or inorganic builders. Typical examples of such builders include alkali metal ortho, s pyro, and tripolyphosphates, alkali metal carbonates, ` either alone or in admixture with calcite, alkali metal ''` ` ' ~ ' /- 2~2g2~
citrates, alkali metal nitrilo-triacetates, carboxy-methyloxysuccinates, zeolites, polyacetal-carboxylates and so on.
s Furthermore, they may contain e.g. from 1-35% of a bleaching agent or a bleach precursor or a system comprising bleaching agent and/or precursor with activator therefor. Further optional ingredients are lather boosters, foam depressors, anticorrosion agents, soil-o suspending agents, sequestering agents, anti-soil redeposition agents, perfumes, dyes, stabilising agents for the enzymes and so on. The enzymes other than lipase that may be present include pxotease, amylase, oxidase and cellulase.
'~
The compositions may be formulated in any desired way, e.g. as powders, bars, pastes, liquids, including aqueous and nonaqueous liguids (in many cases incorporating enzyme-stabilising materials), according to per-se known formulations thereof with the addition of enzymes in the types and amounts described herein.
:, - The compositions can be used for the washing of textile ~ ~` materials, especially but without limitation cotton and polyester-based textiles and mixtures thereof. Especially suitable are for example washing procesYes carried out at ~-temperatures of about 60-65 deg C or lower, e.g. about 30-35 deg~C or lower.
The invention is further illustrated non-limitatively by . .
the following examples.
' '' ' ;~ Example 1 & 2 ~ ~ 35 ' ~: . ' ' 2~2~2~3 - -In each case a detergent powder composition is formulated as follows:
Zeolite 33%, s Sokalan CP5 3.6%, Nonionic 3E0 3.3%, Nonionic 7E0 8.0%, Sodium linear alkylbenzenesulphonate 7.4~, Fatty acid l.o~, o Sodium sulphate 0.3~, Sodium perborats monohydrate 14.4%, Tetaethylethylenediamine 5.3%, Antifoam 1.5%, Sodium carbonate 7.8%, lS Sodium carboxymethylcellulose 1%, ~
Perfume, fluorescer, minors and water to 100%. ~`
The enzymes mentioned above are added (Example 1) in the :~ quantities ('mixture (a)')~
: Savinase 6T: 0.64% (3.8 KNPU/lOOg);
: Thermamyl 60T: 0.77% (46.2 KNU/lOOg);
Lipolase lOOT: 0.15% (15 KLU/lOOg).
2s The ratio A+L/P is 16.1. The ratio A/L is 2.9.
,~ ' ' The quantities of enzymes added for Example 2 are ('mixture (b)'.)~-, f .
~ savinase 6T: 0.64% (3.8 KNPU/lOOg);
Thermamyl 60T: 0.23% (13.8 KNU/lOOg);
Lipolase lOOT: 0.25% (25 KLU/lOOg). ;
. .
~ ~5 The ratio A+L/P is 6.6. The ratio A/L is 0.55.
' :
2 ~U 2 0 h O ?~
These detergent formulations were found to perform well with a combination of good washing results with economy in total use of enzyme.
Further examples of the invention can be formulated as follows:
Example 3:
o A detergent powder according to an embodiment of the ~ ~`
invention containing phosphate builder is formulated to contain: total active detergent about 16%, ani~nic detergent about 9%, nonionic detergent about 6%, phosphate-containing builder about 20~, acrylic or S equivalent polymer about 3. 5%, perborate or peracid bleach precursor about 6-18%, amino-containing bleach activator about 2%, silicate or other structurant a~out 3.5%, protease enzyme about 8 glycine units/mg, with alkali to ~-;~ adjust to desired pH in use, and neutral inorganic salt, and enzymes. - -~
The anionic detergent is a mixture of sodium dodecylbenzene sulphonate 6% and primary alkyl sulphate ~;~ 3%. The nonionic detergent is an ethoxylate of an approx.
2s C13-C15 primary alcohol with 7 ethoxylate residues per mole. The phosphate builder is sodium tripolyphosphate.
The polymer is polyacrylic acid. The perborate or peracid bleach precursor is so'dium tetraborate tetrahydrate or monohydrate. The activator is tetraacetylethylenediamine.
~; The structurant is sodium silicate. The neutral inorganic salt is sodium sulphate. Plural enzymes are included as described above (e.g. mixture (a) or (b)).
~ ~S ., Example 4:
: :
2~2&~3 A detergent powder according to an embodiment of the invention containing zeolite builder is formulated to contain: total active detergent about 16%, anionic detergent about 9%, nonionic detergent about 6%, zeolite-containing builder about 20~, acrylic or equivalent polymer about 3.5%, perborate or peracid bleach precursor about 6-18%, amino-containing bleach activator about 2%, silicate or other structurant about 3.5%, protease enzyme about 8 glycine units/mg, with alkali to adjust to desired -~
o pH in use, and neutral inorganic salt, and enzymes.
The anionic detergent is a mixture of sodium dodecylbenzene sulphonate 6% and primary alkyl sulphate 3%. The nonionic detergent is an ethoxylate of an approx.
; l5 C13-C15 primary alcohol with 7 ethoxylate residues per mole. The zeolite builder is type A zeolite. The polymer is polyacrylic acid. The perborate bleach precursor is sodiu~ tetraborate tetrahydrate or monohydrate. The -activator is tetraacetyl-ethylenediamine. The structurant 0 is sodium silicate. The neutral inorganic salt is sodium sulphate. Plu~al enzymes are included as described above (e.g. mixture (a) or (b)).
, :
; 2s Example 5:
An aqueous detergent liquid according to an embodiment of the invention is formulated to contain: Dodecylbenzene-sulphonic acid 16%, C12-Cl5 linear alcohol condensed with 7 mol/mol ethylene oxide 7%, monoethanolamine 2%, citric acid 6.5%, sodium xylenesulphonate 6%, sodium hydroxide about 4.1%, protease 0.5%, minors and water to 100%. The pH is adjusted to a value between 9 and 10. Plural ~s enzymes are included as described above (e.g. mixture (a) or (b)).
:
:. .
2~2~2~
Example 6:
-A nonaqueous detergent liquid according to an embodiment of the invention is formulated using 38.5~ C13-C15 linear primary alcohol alkoxylated with 4.9 mol/mol ethylene oxide and 2.7 mol/mol propylene oxide, 5% triacetin, 30%
sodium triphosphate, 4~ soda ash, 15.5% sodium perborate monohydrate containing a minor proportion of oxoborate, 4% ~ ~;
TAED, 0. 25% EDTA of which 0.1% as phosphonic acid, Aerosil o 0.6~, SCMC 1%, and 0.6% protease. The pH is adjusted to a value between 9 and 10, e.g. about 9.8. Plural enzymes are included as described above (e.g. mixture ~a) or (b)).
S Example 7:
A detergent powder according to an embodiment of the ~ invention is formulated in the form of a granulate having - a bulk density of at least 600 g/l, containing about 20%
by weight surfactant of which about 10% is sodium ~-dodecylbenzene sulphonate, and the remainder is a mixture of Synperonic A7 and Synperonic A3 (about 5.5% to 4.5%), and zero neutral inorganic salt (e.g. sodium sulphate), plus phosphate builder about 33%, sodium perborate 2s tetrahydrate about 16%, TAED activator about 4.5%, sodium silicate about 6%, and minors including sodium carbonate about 2%, and moisture content about 10%. Plural enzymes are included as described above (e.g. mixture (a) or!(b))~.
Example 8:
~ .
A detergent powder according to an embodiment of the invention is formulated in the form of a granulate having a bulk density of at least 600 g/l, containing about 20%
"' 202~2ff~
by weight surfactant of which about 9% is sodium dodecylbenzene sulphonate, and the remainder is a mixture :~
of Synperonic A7 and Synperonic A3 (respectively about 5%
& 6%), and zero neutral inorganic salt fff'e.g. sodium .
sulphate), plus zeolite builder about 30%, sodium perborate tetrahydrate about 14%, TAED activator about 3.6~, and minors including sodium carbonate about 9%, Dequest 2047 (TM) about 0.7%, and moisture content about ~ -10%. Plural enzymfes are included as described above (e.g.
o mixture (a) or (b)). ~ , Example 9: :
~:
lS A detergent powder according to an embodiment of the ~ invention is formulated to contain: ;~
: Dodecylbenzenesulphonic acid 6%, C12-C15 linear alcohol condensed with 7 mol/mol ethylene oxide 5%, fatty acid soap 3%, Sokolan CP5 polymer (TM) 3%, zeolite A 22%, :. :
~: 20 sodium carbonate 10%, sodium sulphate 17%, clay particles .
8%, sodium perborate tetrahydrate 13%, tetraacetyl-: ethylenediamine 2%, protease 0.5%, minors and water to ::
100%. The pH is adjusted to a value between 9 and 10.
~i~ Plural enzymes are included as described above (e.g.
2s mixture (a) or (b)).
.
~Example 10: , , f ` f A detergent (soap) bar according to an embodiment of the invention is formulated as follows: soap based on pan-. saponified 82% tallow, 18% coconut oil, neutralised with 0.15% orthophosphoric acid, mixed with protease (about 8 ~:~ 3s GU/mg of the bar composition) and mixed with sodium . formate 2%, borax 2%, propylene glycol 2% and sodium - 2~2~3 - 17 ~
, ~:~' '.''' sulphate 1%, is then plodded on a soap production line.
Plural enzymes are included as described above (e.g.
mixture (a) or (b)).
~ ::
s In further non-limitative Examples of the invention, the indicated quantities of lipase as given in Examples 1-10 (mixtures (a) and (b)) can be replaced by cellulase at the rate of 10 CEVU per KLU activity. - ~;~
~-o In further embodiments of the invention, structured li~uid detergents can for example contain, in addition to plural enzymes as described herein, 2-15% nonionic surfactant, 5-40% total surfactant, comprising nonionic and optionally anionic surfactant, 5-35% phosphate-containing or non-phosphate-containing builder, O.2-0.8% polymeric thickener, e.g. cross-linked acrylic polymer with m.w.
over 10^6, at least 10% sodium silicate, e.g. as neutral waterglass, alkali (e.g. potassium-containing alkali) to adjust to desired pH, preferably in the range 9-10 or 20 upwards, e.g. above pH ll, with a ratio sodium cation:
silicate anion (as free silica) (by weight) less than 0.7:1, and viscosity of 0.3-30 Pa.s (at 20 deg. C and 20 reciprocal secs).
,~, For example such detergents can contain about 5% nonionic surfactant C13-15 alcohol alkoxylated with about 5 EO
groups per mole and with about 2.7 PO groups per mole, 15-23% neutral waterglass,with 3.5 weight ratio between!
silica and sodium oxide, 13-19% KOH, 8-23% STPP, 0-11%
sodium carbonate, 0.5% Carbopol 941 (TM).
.
, The present invention is susceptible of modifications and ~ ~
variations, and the present disclosure extends to the use of all combinations and subcombinations of the features ~ .
2 ~ 9~
mentioned and described herein, optionally in combination with each of the features of the above-cited published patent specifications, each of which is specifically incorporated by reference herein.
'' 10 ~ ' '"
- 20 -` . ~
: ::
;, , , 0 "~
(Henkel), WO 87/04461 (Amgen), WO 87/05050 (Genex), EP O
303 761 (Genentech), and EP O 260 lOS (Genencor).
Amylase can for example be used in an amount in the range about 1 to about 100 MU (maltose units) per gram of detergent composition, (or 0.014-1.4, e.g. 0.07-0.7, KNU/g (Novo units)), or for example 0.05-5%, (e.g. 0.1-4%, ~
corresponding in the case of Thermamyl (TM) to 6-240 ~-KNU/lOOg). ~
A preferred amylase for use in the invention is Thermamyl (from Novo).
The amount of lipase can be chosen within wide limits, for S example 50 to 30,000 LU/g of granular detergent composition, e.g. often at least 100 LU/g, very usefully at least 500 LU/g, sometimes preferably above 1000, above 2000 LUlg or above 4000 LU/g or more, thus very often within the range 50-4000 LU/g and possibly within the range 200-1000 LU/g.
, .
Often the amount of lipase used is in the range 0.005-5%, ;
(e.g. 0.01-3%, corresponding in the case of Lipolase (TM) to 1-300 KLU/lOOg).
The lipolytic enzyme can be chosen from among a wide range o~ lipases: in particular the lipases described in for example the following patent specifications, EP O 214 761 (Novo), EP O 258 068 (Novo) and especially lipases showing ~ -immunological cross-reactivity with antisera raised against lipase from Thermomyces lanuginosus ATCC 22070, EP
0 205 208 (Unilever) and EP O 206 390 ~Unilever), and ~ - -especially lipases showing immunological cross-reactivity ~; 35 with antisera raised against lipase from Chromobacter ~ viscosum var lipolyticum NRRL B-3673, or against lipase ,~:
: ~ .
--;` 2~2~
from Alcaligenes PL-679, ATCC 31371 and FERM-P 3783, also the lipases described in specifications WO 87/00859 (Gist-Brocades) and EP O 204 284 (Sapporo Breweries). Suitable in particular are for example the following commercially available lipase preparations: Novo Lipolase, Amano lipases CE, P, B, AP, M-AP, AML, and CES, and Meito lipases MY-30, OF, and PL, also esterase MM, Lipozym, SP225, SP285, Saiken lipase, Enzeco lipase, Toyo Jozo lipase and Diosynth lipase (Trade Marks).
Cellulase can for example be used in an amount in the range about 0.3 to about 35 CEVU units per gram (30-3500 CEVU/lOOg) of the detergent composition.
Whenever desired, the enzymes used may be those obtained by genetic engineering on the basis of mutant producer organisms.
Genetic engineering of the enzymes can be achieved by extraction of an appropriate lipase gene, e.g. the gene ~ ;
~; for lipase from Thermomyces lanuginosus or from a mutant t~ereof, and introduction and expression of the qene or derivative thereof in a suitable producer organism such as an Aspergillus. The techniques described in WO 88/02775 2s (Novo), EP O 243 338 (Labofina) and EP O 268 452 ~` (Genencor) may be applied and adapted.
It i8 preferable to choose the enzymes using any one or more of the following ranges and ratios~
For the range of the protease, e.g. about 1 - 24 ~ KNPU/lOOgram detergent composition (e.g. on basis of solid ;~ or liquid composition or of dry components of liquid ` ~ ~5 composition).
,"~ ,, .
.
-` 2~2~2~
For the relation between the amount of the amylase and lipase taken together, and the protease, e.g. a ratio of 0.3 - 540 (KNU + KLU : KNPU).
For the relation of amylase to lipase, e.g. 0.02 - 240 (KNU:KLU).
More-preferred ranges are~
Protease: e.g. 3-6 (XNPU/lOOg);
Ratio of amylase + lipase to protease of 1-100, e.g. 1-30 (KNU+KLU : KNPU);
Ratio of amylase to lipase of 0.1- 100, e.g. 1 - 10 (KNU:KLU).
Where cellulase is present instead of lipase, these ~ -formulae can be applied and adapted reckoning 10 CEVU unit ; as equivalent to 1 KLU.
For several practical embodiments, it has been found convenient to use up to about 1.9% Savinase, (11.4 KNPU/lOOg); up to about 1.8% Thermamyl (108 KNU/lOOg);
and up to about 1.1~ Lipolase (110 KLU/lOOg).
~ 25 .~ Detergent compositions according to the invention may furthermore include the following usual detergent ~-`~ ingredients in th~ usual amounts. They may be built or unbuilt, and may be of the zero-P type (i.e. not containing any phosphorus-containing builders). Thus the ~ `
composition may contain from 1-45%, e.g. 5-30% by weight of one or more organic and/or inorganic builders. Typical examples of such builders include alkali metal ortho, s pyro, and tripolyphosphates, alkali metal carbonates, ` either alone or in admixture with calcite, alkali metal ''` ` ' ~ ' /- 2~2g2~
citrates, alkali metal nitrilo-triacetates, carboxy-methyloxysuccinates, zeolites, polyacetal-carboxylates and so on.
s Furthermore, they may contain e.g. from 1-35% of a bleaching agent or a bleach precursor or a system comprising bleaching agent and/or precursor with activator therefor. Further optional ingredients are lather boosters, foam depressors, anticorrosion agents, soil-o suspending agents, sequestering agents, anti-soil redeposition agents, perfumes, dyes, stabilising agents for the enzymes and so on. The enzymes other than lipase that may be present include pxotease, amylase, oxidase and cellulase.
'~
The compositions may be formulated in any desired way, e.g. as powders, bars, pastes, liquids, including aqueous and nonaqueous liguids (in many cases incorporating enzyme-stabilising materials), according to per-se known formulations thereof with the addition of enzymes in the types and amounts described herein.
:, - The compositions can be used for the washing of textile ~ ~` materials, especially but without limitation cotton and polyester-based textiles and mixtures thereof. Especially suitable are for example washing procesYes carried out at ~-temperatures of about 60-65 deg C or lower, e.g. about 30-35 deg~C or lower.
The invention is further illustrated non-limitatively by . .
the following examples.
' '' ' ;~ Example 1 & 2 ~ ~ 35 ' ~: . ' ' 2~2~2~3 - -In each case a detergent powder composition is formulated as follows:
Zeolite 33%, s Sokalan CP5 3.6%, Nonionic 3E0 3.3%, Nonionic 7E0 8.0%, Sodium linear alkylbenzenesulphonate 7.4~, Fatty acid l.o~, o Sodium sulphate 0.3~, Sodium perborats monohydrate 14.4%, Tetaethylethylenediamine 5.3%, Antifoam 1.5%, Sodium carbonate 7.8%, lS Sodium carboxymethylcellulose 1%, ~
Perfume, fluorescer, minors and water to 100%. ~`
The enzymes mentioned above are added (Example 1) in the :~ quantities ('mixture (a)')~
: Savinase 6T: 0.64% (3.8 KNPU/lOOg);
: Thermamyl 60T: 0.77% (46.2 KNU/lOOg);
Lipolase lOOT: 0.15% (15 KLU/lOOg).
2s The ratio A+L/P is 16.1. The ratio A/L is 2.9.
,~ ' ' The quantities of enzymes added for Example 2 are ('mixture (b)'.)~-, f .
~ savinase 6T: 0.64% (3.8 KNPU/lOOg);
Thermamyl 60T: 0.23% (13.8 KNU/lOOg);
Lipolase lOOT: 0.25% (25 KLU/lOOg). ;
. .
~ ~5 The ratio A+L/P is 6.6. The ratio A/L is 0.55.
' :
2 ~U 2 0 h O ?~
These detergent formulations were found to perform well with a combination of good washing results with economy in total use of enzyme.
Further examples of the invention can be formulated as follows:
Example 3:
o A detergent powder according to an embodiment of the ~ ~`
invention containing phosphate builder is formulated to contain: total active detergent about 16%, ani~nic detergent about 9%, nonionic detergent about 6%, phosphate-containing builder about 20~, acrylic or S equivalent polymer about 3. 5%, perborate or peracid bleach precursor about 6-18%, amino-containing bleach activator about 2%, silicate or other structurant a~out 3.5%, protease enzyme about 8 glycine units/mg, with alkali to ~-;~ adjust to desired pH in use, and neutral inorganic salt, and enzymes. - -~
The anionic detergent is a mixture of sodium dodecylbenzene sulphonate 6% and primary alkyl sulphate ~;~ 3%. The nonionic detergent is an ethoxylate of an approx.
2s C13-C15 primary alcohol with 7 ethoxylate residues per mole. The phosphate builder is sodium tripolyphosphate.
The polymer is polyacrylic acid. The perborate or peracid bleach precursor is so'dium tetraborate tetrahydrate or monohydrate. The activator is tetraacetylethylenediamine.
~; The structurant is sodium silicate. The neutral inorganic salt is sodium sulphate. Plural enzymes are included as described above (e.g. mixture (a) or (b)).
~ ~S ., Example 4:
: :
2~2&~3 A detergent powder according to an embodiment of the invention containing zeolite builder is formulated to contain: total active detergent about 16%, anionic detergent about 9%, nonionic detergent about 6%, zeolite-containing builder about 20~, acrylic or equivalent polymer about 3.5%, perborate or peracid bleach precursor about 6-18%, amino-containing bleach activator about 2%, silicate or other structurant about 3.5%, protease enzyme about 8 glycine units/mg, with alkali to adjust to desired -~
o pH in use, and neutral inorganic salt, and enzymes.
The anionic detergent is a mixture of sodium dodecylbenzene sulphonate 6% and primary alkyl sulphate 3%. The nonionic detergent is an ethoxylate of an approx.
; l5 C13-C15 primary alcohol with 7 ethoxylate residues per mole. The zeolite builder is type A zeolite. The polymer is polyacrylic acid. The perborate bleach precursor is sodiu~ tetraborate tetrahydrate or monohydrate. The -activator is tetraacetyl-ethylenediamine. The structurant 0 is sodium silicate. The neutral inorganic salt is sodium sulphate. Plu~al enzymes are included as described above (e.g. mixture (a) or (b)).
, :
; 2s Example 5:
An aqueous detergent liquid according to an embodiment of the invention is formulated to contain: Dodecylbenzene-sulphonic acid 16%, C12-Cl5 linear alcohol condensed with 7 mol/mol ethylene oxide 7%, monoethanolamine 2%, citric acid 6.5%, sodium xylenesulphonate 6%, sodium hydroxide about 4.1%, protease 0.5%, minors and water to 100%. The pH is adjusted to a value between 9 and 10. Plural ~s enzymes are included as described above (e.g. mixture (a) or (b)).
:
:. .
2~2~2~
Example 6:
-A nonaqueous detergent liquid according to an embodiment of the invention is formulated using 38.5~ C13-C15 linear primary alcohol alkoxylated with 4.9 mol/mol ethylene oxide and 2.7 mol/mol propylene oxide, 5% triacetin, 30%
sodium triphosphate, 4~ soda ash, 15.5% sodium perborate monohydrate containing a minor proportion of oxoborate, 4% ~ ~;
TAED, 0. 25% EDTA of which 0.1% as phosphonic acid, Aerosil o 0.6~, SCMC 1%, and 0.6% protease. The pH is adjusted to a value between 9 and 10, e.g. about 9.8. Plural enzymes are included as described above (e.g. mixture ~a) or (b)).
S Example 7:
A detergent powder according to an embodiment of the ~ invention is formulated in the form of a granulate having - a bulk density of at least 600 g/l, containing about 20%
by weight surfactant of which about 10% is sodium ~-dodecylbenzene sulphonate, and the remainder is a mixture of Synperonic A7 and Synperonic A3 (about 5.5% to 4.5%), and zero neutral inorganic salt (e.g. sodium sulphate), plus phosphate builder about 33%, sodium perborate 2s tetrahydrate about 16%, TAED activator about 4.5%, sodium silicate about 6%, and minors including sodium carbonate about 2%, and moisture content about 10%. Plural enzymes are included as described above (e.g. mixture (a) or!(b))~.
Example 8:
~ .
A detergent powder according to an embodiment of the invention is formulated in the form of a granulate having a bulk density of at least 600 g/l, containing about 20%
"' 202~2ff~
by weight surfactant of which about 9% is sodium dodecylbenzene sulphonate, and the remainder is a mixture :~
of Synperonic A7 and Synperonic A3 (respectively about 5%
& 6%), and zero neutral inorganic salt fff'e.g. sodium .
sulphate), plus zeolite builder about 30%, sodium perborate tetrahydrate about 14%, TAED activator about 3.6~, and minors including sodium carbonate about 9%, Dequest 2047 (TM) about 0.7%, and moisture content about ~ -10%. Plural enzymfes are included as described above (e.g.
o mixture (a) or (b)). ~ , Example 9: :
~:
lS A detergent powder according to an embodiment of the ~ invention is formulated to contain: ;~
: Dodecylbenzenesulphonic acid 6%, C12-C15 linear alcohol condensed with 7 mol/mol ethylene oxide 5%, fatty acid soap 3%, Sokolan CP5 polymer (TM) 3%, zeolite A 22%, :. :
~: 20 sodium carbonate 10%, sodium sulphate 17%, clay particles .
8%, sodium perborate tetrahydrate 13%, tetraacetyl-: ethylenediamine 2%, protease 0.5%, minors and water to ::
100%. The pH is adjusted to a value between 9 and 10.
~i~ Plural enzymes are included as described above (e.g.
2s mixture (a) or (b)).
.
~Example 10: , , f ` f A detergent (soap) bar according to an embodiment of the invention is formulated as follows: soap based on pan-. saponified 82% tallow, 18% coconut oil, neutralised with 0.15% orthophosphoric acid, mixed with protease (about 8 ~:~ 3s GU/mg of the bar composition) and mixed with sodium . formate 2%, borax 2%, propylene glycol 2% and sodium - 2~2~3 - 17 ~
, ~:~' '.''' sulphate 1%, is then plodded on a soap production line.
Plural enzymes are included as described above (e.g.
mixture (a) or (b)).
~ ::
s In further non-limitative Examples of the invention, the indicated quantities of lipase as given in Examples 1-10 (mixtures (a) and (b)) can be replaced by cellulase at the rate of 10 CEVU per KLU activity. - ~;~
~-o In further embodiments of the invention, structured li~uid detergents can for example contain, in addition to plural enzymes as described herein, 2-15% nonionic surfactant, 5-40% total surfactant, comprising nonionic and optionally anionic surfactant, 5-35% phosphate-containing or non-phosphate-containing builder, O.2-0.8% polymeric thickener, e.g. cross-linked acrylic polymer with m.w.
over 10^6, at least 10% sodium silicate, e.g. as neutral waterglass, alkali (e.g. potassium-containing alkali) to adjust to desired pH, preferably in the range 9-10 or 20 upwards, e.g. above pH ll, with a ratio sodium cation:
silicate anion (as free silica) (by weight) less than 0.7:1, and viscosity of 0.3-30 Pa.s (at 20 deg. C and 20 reciprocal secs).
,~, For example such detergents can contain about 5% nonionic surfactant C13-15 alcohol alkoxylated with about 5 EO
groups per mole and with about 2.7 PO groups per mole, 15-23% neutral waterglass,with 3.5 weight ratio between!
silica and sodium oxide, 13-19% KOH, 8-23% STPP, 0-11%
sodium carbonate, 0.5% Carbopol 941 (TM).
.
, The present invention is susceptible of modifications and ~ ~
variations, and the present disclosure extends to the use of all combinations and subcombinations of the features ~ .
2 ~ 9~
mentioned and described herein, optionally in combination with each of the features of the above-cited published patent specifications, each of which is specifically incorporated by reference herein.
'' 10 ~ ' '"
- 20 -` . ~
: ::
;, , , 0 "~
Claims (13)
1. A detergent composition containing detergent surfactant, preferably anionic and/or nonionic surfactant, preferably builder, and enzymes including protease and amylase, characterised in that the composition contains a combination of three enzymes comprising protease, amylase and a third enzyme selected from lipase and cellulase.
2. A detergent composition according to claim 1, characterised in that the ratio between the amount of the amylase and lipase (and/or cellulase) taken together, and the protease is expressed by a ratio in the range 0.3 -540 ( (KNU+KLU*) : KNPU).
3. A detergent composition according to claim 2, characterised in that said ratio is in the range 1-100, e.g. 1-30 ( (KNU+KLU*) : KNPU).
4. A detergent composition according to claim 1, characterised in that the relation of amylase to lipase (and/or cellulase) is expressed by a ratio in the range 0.02 - 240 (KNU:KLU*).
5. A detergent composition according to claim 4, characterised in that said ratio is in the range 0.1-100, e.g. l-10 (KNU:KLU*).
6. A detergent composition according to claim 1, characterised in that the protease is present at about 1 - 24 KNPU/100gram detergent composition, e.g. 3-6 (KNPU/100g).
7. A detergent composition according to claim 1, characterised in that the amylase is present in an amount in the range about 1 to about 100 MU (maltose units) per gram of detergent composition, or 0.01-2.5, e.g. 0.1-1, KNU/g (Novo units)), or 0.05-5% by weight, e.g. 0.1-4% by weight.
8. A detergent composition according to claim 1, characterised in that lipase used in the range 0.005-5%, e.g. 0.01-3%.
9. A detergent composition according to claim 1, characterised in that cellulase is present in an amount in the range about 0.3 to about 35 CEVU units per gram of the detergent composition.
10. A detergent composition according to claim 1, wherein the third enzyme is lipase.
11. A detergent composition according to claim 1, in the form of a laundry detergent powder containing a bleaching system and a phosphate-containing or non-phosphate-containing builder.
12. A detergent composition according to claim 1, in the form of a liquid detergent concentrate composition.
13. The detergent composition as claimed in claim 1 and substantially as described herein.
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
GB8923788.7 | 1989-10-23 | ||
GB898923788A GB8923788D0 (en) | 1989-10-23 | 1989-10-23 | Enzymatic detergent compositions and their use |
Publications (1)
Publication Number | Publication Date |
---|---|
CA2028203A1 true CA2028203A1 (en) | 1991-04-24 |
Family
ID=10664993
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
CA 2028203 Abandoned CA2028203A1 (en) | 1989-10-23 | 1990-10-22 | Enzyme-containing detergent compositions and their use |
Country Status (4)
Country | Link |
---|---|
EP (1) | EP0425214A3 (en) |
JP (1) | JPH03185098A (en) |
CA (1) | CA2028203A1 (en) |
GB (1) | GB8923788D0 (en) |
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US5240633A (en) * | 1991-05-31 | 1993-08-31 | Colgate-Palmolive Company | Liquid automatic dishwashing composition containing enzymes |
AU654009B2 (en) * | 1991-05-31 | 1994-10-20 | Colgate-Palmolive Company, The | Phosphate-containing powder automatic dishwashing composition with enzymes |
AU656375B2 (en) * | 1991-05-31 | 1995-02-02 | Colgate-Palmolive Company, The | Powdered automatic dishwashing composition containing enzymes |
DE69204568T2 (en) * | 1991-05-31 | 1996-05-15 | Colgate Palmolive Co | Enzyme-containing non-aqueous liquid dishwasher detergent. |
AU654184B2 (en) * | 1991-05-31 | 1994-10-27 | Colgate-Palmolive Company, The | Improved phosphate-containing powder automatic dishwashing composition with enzymes |
AU655274B2 (en) * | 1991-05-31 | 1994-12-15 | Colgate-Palmolive Company, The | Nonaqueous liquid, phosphate-free, improved automatic dishwashing composition containing enzymes |
DE4312010A1 (en) * | 1993-04-13 | 1994-10-20 | Henkel Kgaa | Enzymatic detergent |
DE4339382A1 (en) * | 1993-11-18 | 1995-05-24 | Henkel Kgaa | Liquid detergents and cleaning agents containing enzyme combinations |
EP0779917A4 (en) * | 1994-09-06 | 1999-03-17 | Johnson & Son Inc S C | A cleaning composition comprising lipase and amylase enzymes |
AU5038396A (en) * | 1996-03-29 | 1997-10-02 | Procter & Gamble Company, The | Low moisture laundry detergent bar with improved enzyme stability |
AU7720796A (en) * | 1996-10-31 | 1998-05-22 | Procter & Gamble Company, The | Process for incorporating enzymes into laundry bars |
WO1998054285A1 (en) * | 1997-05-30 | 1998-12-03 | The Procter & Gamble Company | Laundry bar with improved protease stability |
EP0991746A1 (en) * | 1997-06-27 | 2000-04-12 | The Procter & Gamble Company | Non-aqueous liquid detergent compositions containing enzyme particles having reduced density |
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US8084025B2 (en) | 2008-04-18 | 2011-12-27 | Curemark Llc | Method for the treatment of the symptoms of drug and alcohol addiction |
US9320780B2 (en) | 2008-06-26 | 2016-04-26 | Curemark Llc | Methods and compositions for the treatment of symptoms of Williams Syndrome |
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US10776453B2 (en) | 2008-08-04 | 2020-09-15 | Galenagen, Llc | Systems and methods employing remote data gathering and monitoring for diagnosing, staging, and treatment of Parkinsons disease, movement and neurological disorders, and chronic pain |
US20100092447A1 (en) | 2008-10-03 | 2010-04-15 | Fallon Joan M | Methods and compositions for the treatment of symptoms of prion diseases |
ES2882518T3 (en) | 2009-01-06 | 2021-12-02 | Galenagen Llc | Composition comprising protease, amylase and lipase |
KR20170005191A (en) | 2009-01-06 | 2017-01-11 | 큐어론 엘엘씨 | Compositions and methods for the treatment or the prevention oral infections by e. coli |
US9056050B2 (en) | 2009-04-13 | 2015-06-16 | Curemark Llc | Enzyme delivery systems and methods of preparation and use |
WO2011050135A1 (en) | 2009-10-21 | 2011-04-28 | Curemark Llc | Methods and compositions for the prevention and treatment of influenza |
ES2804223T3 (en) | 2011-04-21 | 2021-02-04 | Curemark Llc | Compounds for the treatment of Neuropsychiatric Disorders |
US10350278B2 (en) | 2012-05-30 | 2019-07-16 | Curemark, Llc | Methods of treating Celiac disease |
US11541009B2 (en) | 2020-09-10 | 2023-01-03 | Curemark, Llc | Methods of prophylaxis of coronavirus infection and treatment of coronaviruses |
Family Cites Families (7)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
DE1940654A1 (en) * | 1969-08-09 | 1971-02-18 | Henkel & Cie Gmbh | Enzymatic detergent |
US3844951A (en) * | 1970-01-14 | 1974-10-29 | Henkel & Cie Gmbh | Detergent compositions containing a textile softener |
DE2021529A1 (en) * | 1970-05-02 | 1971-12-02 | Henkel & Cie Gmbh | Detergent and cleansing agent-containing thiourea dioxide as protein - - dissolving agent |
EP0080748B1 (en) * | 1981-11-13 | 1985-07-10 | Unilever N.V. | Enzymatic liquid cleaning composition |
GB8629538D0 (en) * | 1986-12-10 | 1987-01-21 | Unilever Plc | Enzymatic dishwashing & rinsing composition |
NZ230842A (en) * | 1988-10-21 | 1992-05-26 | Colgate Palmolive Co | Nonionic heavy duty particulate detergent containing protease, amylase and cellulase |
EP0385401A1 (en) * | 1989-02-27 | 1990-09-05 | Occidental Chemical Corporation | Unique Microbial lipases with activity at temperatures and pHs suitable for use in detergents |
-
1989
- 1989-10-23 GB GB898923788A patent/GB8923788D0/en active Pending
-
1990
- 1990-10-22 CA CA 2028203 patent/CA2028203A1/en not_active Abandoned
- 1990-10-22 EP EP19900311540 patent/EP0425214A3/en not_active Withdrawn
- 1990-10-23 JP JP28567690A patent/JPH03185098A/en active Pending
Also Published As
Publication number | Publication date |
---|---|
JPH03185098A (en) | 1991-08-13 |
EP0425214A2 (en) | 1991-05-02 |
GB8923788D0 (en) | 1989-12-13 |
EP0425214A3 (en) | 1992-05-06 |
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