AU3163195A - Enzymatic bleach booster compositions - Google Patents
Enzymatic bleach booster compositionsInfo
- Publication number
- AU3163195A AU3163195A AU31631/95A AU3163195A AU3163195A AU 3163195 A AU3163195 A AU 3163195A AU 31631/95 A AU31631/95 A AU 31631/95A AU 3163195 A AU3163195 A AU 3163195A AU 3163195 A AU3163195 A AU 3163195A
- Authority
- AU
- Australia
- Prior art keywords
- bleach
- enzymatic
- bleaching
- washing
- composition
- 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.)
- Granted
Links
- 239000007844 bleaching agent Substances 0.000 title claims description 111
- 239000000203 mixture Substances 0.000 title claims description 94
- 230000002255 enzymatic effect Effects 0.000 title claims description 55
- 102000004190 Enzymes Human genes 0.000 claims description 51
- 108090000790 Enzymes Proteins 0.000 claims description 51
- 229940088598 enzyme Drugs 0.000 claims description 51
- 238000004061 bleaching Methods 0.000 claims description 45
- 238000004140 cleaning Methods 0.000 claims description 30
- 238000005406 washing Methods 0.000 claims description 30
- 230000001012 protector Effects 0.000 claims description 19
- 238000000034 method Methods 0.000 claims description 16
- 239000012190 activator Substances 0.000 claims description 14
- 239000000758 substrate Substances 0.000 claims description 13
- 108091005804 Peptidases Proteins 0.000 claims description 12
- 239000004365 Protease Substances 0.000 claims description 11
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 claims description 10
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N EtOH Substances CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 claims description 9
- VGYYSIDKAKXZEE-UHFFFAOYSA-L hydroxylammonium sulfate Chemical group O[NH3+].O[NH3+].[O-]S([O-])(=O)=O VGYYSIDKAKXZEE-UHFFFAOYSA-L 0.000 claims description 9
- 239000004366 Glucose oxidase Substances 0.000 claims description 8
- 108010015776 Glucose oxidase Proteins 0.000 claims description 8
- 229940116332 glucose oxidase Drugs 0.000 claims description 8
- 235000019420 glucose oxidase Nutrition 0.000 claims description 8
- 230000008569 process Effects 0.000 claims description 8
- 102000004316 Oxidoreductases Human genes 0.000 claims description 7
- 108090000854 Oxidoreductases Proteins 0.000 claims description 7
- 239000004094 surface-active agent Substances 0.000 claims description 7
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 claims description 6
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 claims description 6
- 239000008103 glucose Substances 0.000 claims description 6
- 150000001875 compounds Chemical class 0.000 claims description 5
- PYMYPHUHKUWMLA-LMVFSUKVSA-N Ribose Natural products OC[C@@H](O)[C@@H](O)[C@@H](O)C=O PYMYPHUHKUWMLA-LMVFSUKVSA-N 0.000 claims description 4
- HMFHBZSHGGEWLO-UHFFFAOYSA-N alpha-D-Furanose-Ribose Natural products OCC1OC(O)C(O)C1O HMFHBZSHGGEWLO-UHFFFAOYSA-N 0.000 claims description 4
- 229940123748 Catalase inhibitor Drugs 0.000 claims description 3
- 125000002791 glucosyl group Chemical group C1([C@H](O)[C@@H](O)[C@H](O)[C@H](O1)CO)* 0.000 claims description 3
- 108010025188 Alcohol oxidase Proteins 0.000 claims description 2
- HMFHBZSHGGEWLO-SOOFDHNKSA-N D-ribofuranose Chemical compound OC[C@H]1OC(O)[C@H](O)[C@@H]1O HMFHBZSHGGEWLO-SOOFDHNKSA-N 0.000 claims description 2
- BGRWYDHXPHLNKA-UHFFFAOYSA-N Tetraacetylethylenediamine Chemical group CC(=O)N(C(C)=O)CCN(C(C)=O)C(C)=O BGRWYDHXPHLNKA-UHFFFAOYSA-N 0.000 claims 1
- 239000000126 substance Substances 0.000 description 32
- 239000003599 detergent Substances 0.000 description 26
- FRPJTGXMTIIFIT-UHFFFAOYSA-N tetraacetylethylenediamine Chemical compound CC(=O)C(N)(C(C)=O)C(N)(C(C)=O)C(C)=O FRPJTGXMTIIFIT-UHFFFAOYSA-N 0.000 description 22
- 238000012360 testing method Methods 0.000 description 18
- 230000000694 effects Effects 0.000 description 12
- 239000004744 fabric Substances 0.000 description 12
- 239000002689 soil Substances 0.000 description 12
- 238000004519 manufacturing process Methods 0.000 description 11
- 239000004753 textile Substances 0.000 description 10
- 238000004453 electron probe microanalysis Methods 0.000 description 8
- UFZOPKFMKMAWLU-UHFFFAOYSA-N ethoxy(methyl)phosphinic acid Chemical compound CCOP(C)(O)=O UFZOPKFMKMAWLU-UHFFFAOYSA-N 0.000 description 8
- 239000004615 ingredient Substances 0.000 description 8
- 229920000742 Cotton Polymers 0.000 description 7
- 102000016938 Catalase Human genes 0.000 description 6
- 108010053835 Catalase Proteins 0.000 description 6
- 230000007613 environmental effect Effects 0.000 description 6
- 239000003381 stabilizer Substances 0.000 description 6
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 6
- 230000008901 benefit Effects 0.000 description 5
- 238000009472 formulation Methods 0.000 description 5
- 244000005700 microbiome Species 0.000 description 5
- MHAJPDPJQMAIIY-UHFFFAOYSA-N Hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 description 4
- 238000000855 fermentation Methods 0.000 description 4
- 230000004151 fermentation Effects 0.000 description 4
- 235000015097 nutrients Nutrition 0.000 description 4
- 235000020095 red wine Nutrition 0.000 description 4
- MWNQXXOSWHCCOZ-UHFFFAOYSA-L sodium;oxido carbonate Chemical compound [Na+].[O-]OC([O-])=O MWNQXXOSWHCCOZ-UHFFFAOYSA-L 0.000 description 4
- ZAMOUSCENKQFHK-UHFFFAOYSA-N Chlorine atom Chemical compound [Cl] ZAMOUSCENKQFHK-UHFFFAOYSA-N 0.000 description 3
- 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 3
- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 3
- 239000008280 blood Substances 0.000 description 3
- 210000004369 blood Anatomy 0.000 description 3
- 230000015556 catabolic process Effects 0.000 description 3
- 238000006243 chemical reaction Methods 0.000 description 3
- 239000000460 chlorine Substances 0.000 description 3
- 229910052801 chlorine Inorganic materials 0.000 description 3
- 238000006731 degradation reaction Methods 0.000 description 3
- 229960001484 edetic acid Drugs 0.000 description 3
- 239000007788 liquid Substances 0.000 description 3
- 150000004965 peroxy acids Chemical class 0.000 description 3
- 150000003839 salts Chemical class 0.000 description 3
- 239000012418 sodium perborate tetrahydrate Substances 0.000 description 3
- IBDSNZLUHYKHQP-UHFFFAOYSA-N sodium;3-oxidodioxaborirane;tetrahydrate Chemical compound O.O.O.O.[Na+].[O-]B1OO1 IBDSNZLUHYKHQP-UHFFFAOYSA-N 0.000 description 3
- 239000004382 Amylase Substances 0.000 description 2
- 102000013142 Amylases Human genes 0.000 description 2
- 108010065511 Amylases Proteins 0.000 description 2
- ZOXJGFHDIHLPTG-UHFFFAOYSA-N Boron Chemical compound [B] ZOXJGFHDIHLPTG-UHFFFAOYSA-N 0.000 description 2
- 244000025254 Cannabis sativa Species 0.000 description 2
- HEDRZPFGACZZDS-UHFFFAOYSA-N Chloroform Chemical compound ClC(Cl)Cl HEDRZPFGACZZDS-UHFFFAOYSA-N 0.000 description 2
- 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 2
- 239000006057 Non-nutritive feed additive Substances 0.000 description 2
- 102000035195 Peptidases Human genes 0.000 description 2
- 244000269722 Thea sinensis Species 0.000 description 2
- 235000019418 amylase Nutrition 0.000 description 2
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 2
- 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 2
- 230000009286 beneficial effect Effects 0.000 description 2
- 230000015572 biosynthetic process Effects 0.000 description 2
- 229910052796 boron Inorganic materials 0.000 description 2
- 230000006378 damage Effects 0.000 description 2
- 238000004090 dissolution Methods 0.000 description 2
- 235000013399 edible fruits Nutrition 0.000 description 2
- 239000008187 granular material Substances 0.000 description 2
- 235000019589 hardness Nutrition 0.000 description 2
- WQYVRQLZKVEZGA-UHFFFAOYSA-N hypochlorite Chemical compound Cl[O-] WQYVRQLZKVEZGA-UHFFFAOYSA-N 0.000 description 2
- 238000011065 in-situ storage Methods 0.000 description 2
- -1 manganese diols Chemical class 0.000 description 2
- 238000005259 measurement Methods 0.000 description 2
- 230000007246 mechanism Effects 0.000 description 2
- 229910021645 metal ion Inorganic materials 0.000 description 2
- 230000003287 optical effect Effects 0.000 description 2
- 230000003647 oxidation Effects 0.000 description 2
- 238000007254 oxidation reaction Methods 0.000 description 2
- 239000001301 oxygen Substances 0.000 description 2
- 229910052760 oxygen Inorganic materials 0.000 description 2
- 229940068196 placebo Drugs 0.000 description 2
- 239000000902 placebo Substances 0.000 description 2
- 231100000572 poisoning Toxicity 0.000 description 2
- 230000000607 poisoning effect Effects 0.000 description 2
- 239000011734 sodium Substances 0.000 description 2
- 229910052708 sodium Inorganic materials 0.000 description 2
- 238000003756 stirring Methods 0.000 description 2
- 235000000346 sugar Nutrition 0.000 description 2
- 150000008163 sugars Chemical class 0.000 description 2
- 235000013616 tea Nutrition 0.000 description 2
- XSVSPKKXQGNHMD-UHFFFAOYSA-N 5-bromo-3-methyl-1,2-thiazole Chemical group CC=1C=C(Br)SN=1 XSVSPKKXQGNHMD-UHFFFAOYSA-N 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 108010059892 Cellulase Proteins 0.000 description 1
- 241000196324 Embryophyta Species 0.000 description 1
- 241000233866 Fungi Species 0.000 description 1
- 102000004157 Hydrolases Human genes 0.000 description 1
- 108090000604 Hydrolases Proteins 0.000 description 1
- 239000004367 Lipase Substances 0.000 description 1
- 102000004882 Lipase Human genes 0.000 description 1
- 108090001060 Lipase Proteins 0.000 description 1
- 102000004317 Lyases Human genes 0.000 description 1
- 108090000856 Lyases Proteins 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- BPQQTUXANYXVAA-UHFFFAOYSA-N Orthosilicate Chemical compound [O-][Si]([O-])([O-])[O-] BPQQTUXANYXVAA-UHFFFAOYSA-N 0.000 description 1
- 108700020962 Peroxidase Proteins 0.000 description 1
- 102000003992 Peroxidases Human genes 0.000 description 1
- 241000589516 Pseudomonas Species 0.000 description 1
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 1
- BQCADISMDOOEFD-UHFFFAOYSA-N Silver Chemical compound [Ag] BQCADISMDOOEFD-UHFFFAOYSA-N 0.000 description 1
- CDBYLPFSWZWCQE-UHFFFAOYSA-L Sodium Carbonate Chemical compound [Na+].[Na+].[O-]C([O-])=O CDBYLPFSWZWCQE-UHFFFAOYSA-L 0.000 description 1
- 239000005708 Sodium hypochlorite Substances 0.000 description 1
- 241000187747 Streptomyces Species 0.000 description 1
- 244000299461 Theobroma cacao Species 0.000 description 1
- 235000009470 Theobroma cacao Nutrition 0.000 description 1
- 229910021536 Zeolite Inorganic materials 0.000 description 1
- UAOKXEHOENRFMP-ZJIFWQFVSA-N [(2r,3r,4s,5r)-2,3,4,5-tetraacetyloxy-6-oxohexyl] acetate Chemical compound CC(=O)OC[C@@H](OC(C)=O)[C@@H](OC(C)=O)[C@H](OC(C)=O)[C@@H](OC(C)=O)C=O UAOKXEHOENRFMP-ZJIFWQFVSA-N 0.000 description 1
- CKUAXEQHGKSLHN-UHFFFAOYSA-N [C].[N] Chemical compound [C].[N] CKUAXEQHGKSLHN-UHFFFAOYSA-N 0.000 description 1
- XJJWWOUJWDTXJC-UHFFFAOYSA-N [Mn].N1C(C=C2N=C(C=C3NC(=C4)C=C3)C=C2)=CC=C1C=C1C=CC4=N1 Chemical class [Mn].N1C(C=C2N=C(C=C3NC(=C4)C=C3)C=C2)=CC=C1C=C1C=CC4=N1 XJJWWOUJWDTXJC-UHFFFAOYSA-N 0.000 description 1
- 238000010521 absorption reaction Methods 0.000 description 1
- 238000009825 accumulation Methods 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 230000004913 activation Effects 0.000 description 1
- 239000000654 additive Substances 0.000 description 1
- 230000002411 adverse Effects 0.000 description 1
- 150000001298 alcohols Chemical class 0.000 description 1
- 239000003513 alkali Substances 0.000 description 1
- 239000003708 ampul Substances 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 239000004410 anthocyanin Substances 0.000 description 1
- 235000010208 anthocyanin Nutrition 0.000 description 1
- 229930002877 anthocyanin Natural products 0.000 description 1
- 150000004636 anthocyanins Chemical class 0.000 description 1
- 238000013459 approach Methods 0.000 description 1
- 244000052616 bacterial pathogen Species 0.000 description 1
- 239000003054 catalyst Substances 0.000 description 1
- 229940106157 cellulase Drugs 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 235000019805 chlorophyllin Nutrition 0.000 description 1
- 239000001752 chlorophylls and chlorophyllins Substances 0.000 description 1
- 235000016213 coffee Nutrition 0.000 description 1
- 235000013353 coffee beverage Nutrition 0.000 description 1
- 238000002485 combustion reaction Methods 0.000 description 1
- 238000001816 cooling Methods 0.000 description 1
- HWDGVJUIHRPKFR-UHFFFAOYSA-I copper;trisodium;18-(2-carboxylatoethyl)-20-(carboxylatomethyl)-12-ethenyl-7-ethyl-3,8,13,17-tetramethyl-17,18-dihydroporphyrin-21,23-diide-2-carboxylate Chemical class [Na+].[Na+].[Na+].[Cu+2].N1=C(C(CC([O-])=O)=C2C(C(C)C(C=C3C(=C(C=C)C(=C4)[N-]3)C)=N2)CCC([O-])=O)C(=C([O-])[O-])C(C)=C1C=C1C(CC)=C(C)C4=N1 HWDGVJUIHRPKFR-UHFFFAOYSA-I 0.000 description 1
- 239000013078 crystal Substances 0.000 description 1
- 230000001419 dependent effect Effects 0.000 description 1
- 125000000597 dioxinyl group Chemical group 0.000 description 1
- HNPSIPDUKPIQMN-UHFFFAOYSA-N dioxosilane;oxo(oxoalumanyloxy)alumane Chemical compound O=[Si]=O.O=[Al]O[Al]=O HNPSIPDUKPIQMN-UHFFFAOYSA-N 0.000 description 1
- 238000009826 distribution Methods 0.000 description 1
- 239000003651 drinking water Substances 0.000 description 1
- 235000020188 drinking water Nutrition 0.000 description 1
- 239000000428 dust Substances 0.000 description 1
- 230000007247 enzymatic mechanism Effects 0.000 description 1
- 238000011156 evaluation Methods 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 235000013305 food Nutrition 0.000 description 1
- 239000011521 glass Substances 0.000 description 1
- 230000036541 health Effects 0.000 description 1
- 238000011081 inoculation Methods 0.000 description 1
- 229910052500 inorganic mineral Inorganic materials 0.000 description 1
- 238000009434 installation Methods 0.000 description 1
- 238000011031 large-scale manufacturing process Methods 0.000 description 1
- 238000010412 laundry washing Methods 0.000 description 1
- 235000019421 lipase Nutrition 0.000 description 1
- 229920002521 macromolecule Polymers 0.000 description 1
- 239000002075 main ingredient Substances 0.000 description 1
- 229910052748 manganese Inorganic materials 0.000 description 1
- 239000011572 manganese Substances 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 239000011159 matrix material Substances 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- 239000011707 mineral Substances 0.000 description 1
- 238000002156 mixing Methods 0.000 description 1
- 239000005445 natural material Substances 0.000 description 1
- 235000006286 nutrient intake Nutrition 0.000 description 1
- 239000003960 organic solvent Substances 0.000 description 1
- 238000004806 packaging method and process Methods 0.000 description 1
- 229920005862 polyol Polymers 0.000 description 1
- 150000003077 polyols Chemical class 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 102000004169 proteins and genes Human genes 0.000 description 1
- 108090000623 proteins and genes Proteins 0.000 description 1
- 229940024999 proteolytic enzymes for treatment of wounds and ulcers Drugs 0.000 description 1
- 238000005086 pumping Methods 0.000 description 1
- 239000002994 raw material Substances 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 239000010865 sewage Substances 0.000 description 1
- 229910052709 silver Inorganic materials 0.000 description 1
- 239000004332 silver Substances 0.000 description 1
- 239000002002 slurry Substances 0.000 description 1
- SUKJFIGYRHOWBL-UHFFFAOYSA-N sodium hypochlorite Chemical compound [Na+].Cl[O-] SUKJFIGYRHOWBL-UHFFFAOYSA-N 0.000 description 1
- 229960001922 sodium perborate Drugs 0.000 description 1
- 229940045872 sodium percarbonate Drugs 0.000 description 1
- YKLJGMBLPUQQOI-UHFFFAOYSA-M sodium;oxidooxy(oxo)borane Chemical compound [Na+].[O-]OB=O YKLJGMBLPUQQOI-UHFFFAOYSA-M 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 230000007480 spreading Effects 0.000 description 1
- 238000003892 spreading Methods 0.000 description 1
- 238000003860 storage Methods 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 239000001648 tannin Substances 0.000 description 1
- 229920001864 tannin Polymers 0.000 description 1
- 235000018553 tannin Nutrition 0.000 description 1
- 150000004685 tetrahydrates Chemical class 0.000 description 1
- 239000010457 zeolite 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
- C11D3/38654—Preparations containing enzymes, e.g. protease or amylase containing oxidase or reductase
-
- 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
- C11D3/39—Organic or inorganic per-compounds
- C11D3/3902—Organic or inorganic per-compounds combined with specific additives
-
- 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
- D06L4/00—Bleaching fibres, filaments, threads, yarns, fabrics, feathers or made-up fibrous goods; Bleaching leather or furs
- D06L4/10—Bleaching fibres, filaments, threads, yarns, fabrics, feathers or made-up fibrous goods; Bleaching leather or furs using agents which develop oxygen
- D06L4/12—Bleaching fibres, filaments, threads, yarns, fabrics, feathers or made-up fibrous goods; Bleaching leather or furs using agents which develop oxygen combined with specific additives
Landscapes
- Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Oil, Petroleum & Natural Gas (AREA)
- Wood Science & Technology (AREA)
- Organic Chemistry (AREA)
- Inorganic Chemistry (AREA)
- Textile Engineering (AREA)
- Detergent Compositions (AREA)
- Immobilizing And Processing Of Enzymes And Microorganisms (AREA)
Description
ENZYMATIC BLEACH BOOSTER COMPOSITIONS
Field of the invention
The present invention relates to bleaching of textiles.
Background of the invention
In previous ages, most stubborn stains, e.g. fruit, red wine, coffee and tea, which could not be washed out from textiles, were oxidatively "removed" via grass bleaching i.e. spreading the washed fabrics on the lawn and exposing it for a longer time to bright sunlight. In the early 1900's this time consuming method was replaced by washing with a mixture of soda, silicate and perborate, thus allowing for one-step washing and bleaching. Over the years these prototype mixtures have evolved in rather complex formulations that may contain as many as 15 - 20 different ingredients which all have their specific tasks in textile cleaning. Volume-wise the most important ingredients are surfactants, builders and bleaches. The total world production of synthetic surfactants in 1992 amounted ± 4 million tons, for builders this was + 4 million tons, and for bleaches this amounted to + 2 million tons per annum. From these figures it is obvious that the natural resources needed to produce these volumes are really outrageous, and that, from an environmental burden point of view, these components are quite suspicious. Focussing on the biodegradability of bleaches the issues may be summarised as follows:
The two mostly used bleaches in detergents are chlorine bleach (sodium hypochlorite) and perborate (sodium perborate mono/tetra hydrate) . Notably chlorine bleach is the most dangerous chemical that is being used in house- holds. Use of chlorine may cause the synthesis of very poisoning organo-chloro compounds, such as trihalomethans (chloroform) and dioxines, which in general are also very hard to degrade. Also the use of perborate is growingly troublesome, because of the very large quantities that are currently being used, there is considerable accumulation (in the drinking water) of mineral boron, which cannot be degraded in the environment and cannot be removed from the water by sewage treatment installations. Boron is low poisoning for aquatic animals, but quite problematic for aquatic plants.
An extra negative for the use of perborate is that its bleaching activity at low temperatures is limited. As a consequence bleach activators, such as TAED (tetra acetyl ethylene diamine) , are added. These activators are not needed in case percarbonate is being used as a bleaching agent. However percarbonate is not stable in detergents, unless EDTA (ethylene diamine tetra acetic acid)
(significant quantities, non-biodegradable) as a stabiliser is added. From this summary it is clear that not only the environmental bio burden, related to extremely large scale production levels of these ingredients are troublesome, but also their biodegradability is under continuous debate and worry, and that less environmentally harmful alternatives will be most welcomed.
As mentioned above, today an average heavy duty laundry detergent is composed of as many as 15 - 20 ingredients, chosen by the manufacturer to optimize the performance as much as (economically) possible, each ingredient having its own specific function. On a weight basis, surfactants, builders and bleaching components comprise the vast majority of these formulations. This is
basically due to their performance profile, which is typical for chemical activities i.e. at low concentrations a rather poor performance, at a certain concentration a dramatic increase in performance and beyond that concentration no 5 significant increase in performance.
Bleaching components such as sodium perborate and percarbonate are also needed in high concentrations due to their chemical action mechanisms, which are dependent on the type of stain, the type of fabric, the temperature the pH 0 and the concentration of specific bi-valent metal ions. For instance, the mechanism is strongly inhibited by lowering the wash temperature; from 80°C to 20°C the bleaching reaction kinetics are slowed down by a factor 1000. Instability of the bleaching agents, as a results of the s presence of certain bi-valent metal ions is also an issue and reason to relatively overdose the bleach or to add chelaters such as EDTA or activators such as manganese porphyrins or manganese diols/polyols. An alternative to the activation of persalts is the in situ generation of peracids 0 via bleach activators such as TAED, TAGU and SNOBS. This approach requires a relatively high pH and requires (again) stabilisers to prevent the formation of highly active radicals that may cause dye and fabric damage. All in all chemical bleaching is rather complex, does have limitations 5 in terms of type of fabric and (low) temperature and pH applications, and is most certainly not free from risks concerning fabric color and fabric care.
Moreover, basically, bleaching is the destruction of chromophores in highly conjugated organic bio macro- o molecules such as anthocyanins (fruit stains) , tannins (tea stains) and chlorophyllins (grass stains) via oxidation of a number of double bonds in these molecules, which causes a shift in the absorption profiles of the chromophores from visible (on the fabric) to less visible or unvisible, (but 5 still present) on the fabric. In other words the stains are not really being removed from the textile, but only seem to
be removed, because after oxidation they are no longer visible.
In contrast to chemical bleaching, bleaching processes that operate via an enzymatic mechanism are described.
But although enzymatic bleaching was already described in the early seventies (US 3640877) , until now there are no detergent compositions comprising an enzymatic bleaching system. This will probably be due to the incompatibility of enzymatic bleach compositions with other detergent ingredients. The enzymes are not stable when formulated with other detergent ingredients.
Summary of the invention It has been found that chemical bleach, in the application of bleaches in washing and cleaning procedures, can be substituted by an enzymatic bleach booster composition.
Accordingly, the present invention relates to enzymatic bleach booster compositions, which compositions are capable of exerting a bleaching effect on objects to be bleached, washed or cleaned. The enzymatic bleach booster compositions comprise at least an enzyme and a substrate for this enzyme, which substrate can be converted by the enzyme in a bleach active compound.
Another object of the invention is a method of bleaching, washing or cleaning a soiled object in which the method is characterized by the following steps: a) supplying an enzymatic bleach booster composition and optionally a washing or cleaning composition to the soiled object; and b) washing or cleaning the soiled object.
Still another object of the invention is a bleach protector composition, which is capable of increasing the effectiveness of bleach, when applied in laundry washing.
Detailed description of the invention
Enzymatic bleach booster compositions of the invention are compositions which mainly consist of an enzyme and a substrate for this enzyme, which substrate can be converted by the enzyme in a bleach active compound.
Contrary to prior art detergents comprising an enzymatic bleach system in which the enzymes are not stable, the enzymatic bleach booster compositions according to the invention comprise very little surfactants and/or builders. The amount of surfactants and/or builders is preferably below 5%. In one embodiment of the invention the enzymatic bleach booster composition comprises no surfactants and/or builders at all.
Enzymes that could be used in enzymatic bleach booster compositions are for example oxidases, such as oxido-reductases and peroxidases. As a substrate for these enzymes short-chain alcohols, sugars etc. could be used. For example glucose oxidase, ribose oxidase, methanol oxidase or ethanol oxidase and their respective substrates glucose, ribose, methanol and ethanol could be used.
Bleach active compounds are for example hydrogen peroxide, peracids, etc.
Enzymatic bleach booster compositions of the invention may further comprise bleach activators. Bleach activators are substances which react with oxygen-molecules
(originating) from persalts, to form bleach active peracids.
Surprisingly, it has been found that the addition of bleach activators like TAED, TAGU (tetra acetyl glycol Uril) , PAG
(penta acetyl glucose) , SNOBS (sodium nonaoyl oxibenzene sulphonate) and ISONOBS (sodium isononaoyl oxibenzene sulphonate) will result in a better performance.
Furthermore, enzymatic bleach booster compositions of the invention may comprise so-called bleach protectors. Bleach protectors are substances that protect the bleaching active compound from attack of bleach destroying substances. For example catalase which is present on laundry is able to degrade hydrogen peroxide rapidly, which will reduce the
bleaching effect of the bleaching composition. Incorporating substances like a bleach stable protease which will degrade the catalase, or hydroxyl ammonium sulphate, which inhibits the catalase, in the enzymatic bleach booster composition will protect the bleach from degradation.
Bleach protectors will increase the bleaching effectiveness of the enzymatic bleach booster composition.
Bleach protector compositions comprising a bleach stable protease and/or a catalase-inhibitor, like hydroxyl ammonium sulphate are also part of the invention. These compositions may be incorporated in the enzymatic bleach booster composition or may be used seperately. Bleach protector compositions which may comprise other enzymes (e.g. amylase, cellulase or lipase) are also capable of protecting chemical bleach.
The enzymatic bleach booster composition may further comprise, depending on the formulation type, minor quantities of e.g. processing aids and stabilisers.
This way of enzymatic bleaching has several advantages both in terms of cleaning capabilities as well as in terms of economic- and environmental issues. For instance it can be demonstrated that enzymes generate significant performance levels at rather moderate concentrations of typically 0.2 - 1.0 % on a weight basis, but fully substitute or even surpass the performance of current chemical cleaners (such as bleaching salts) , at higher enzyme dosages viz: 1.0-5.0 % on a weight basis. This is found to be also true at moderate till low washing temperatures and in moderate till high water hardnesses. Apparently the use of enzymes in cleaning will facilitate the bleaching process thus avoiding the use of aggressive chemicals and costly high washing temperatures, demonstrating their specific cleaning benefits.
Also from a manufacturing point of view, the use of enzymes in bleaching is beneficial. Enzymes are being recovered from large scale fermentation of naturally occurring micro-organisms that produce these enzymes quite
effectively. Since these micro organisms are being grown on naturally occurring nutrients, such as organic nitrogen- and carbon sources, the bioburden, caused by the manufacturing of the raw materials is in comparison to that of chemicals s negligibly low. Also the energy required for production of enzymatic bleach is extremely low relative to the chemical alternative (apprx. 25 MJ/kg vs 60 MJ/kg) , which in the light of lowest possible resources consumption is clearly in favour of the enzymatic rather than the chemical product. o Because enzymes are being produced by naturally occurring micro-organisms, their origin is fully biological, and therefore their biodegradability is 100 %. This in contrast to the biodegradability of at least some chemical bleaching agents. From this comparison it is clear that the s bio-burden of enzymatic bleaching is absolutely negligible, demonstrating their full environmental compatibility/ superiority over chemical alternatives.
Basically enzymes, to be used in the enzymatic bleach booster composition or bleach protector composition, 0 are being produced by large scale fermentation of micro¬ organisms like bacteria, such as Baccilli, Streptomyces, Pseudomonas, or yeasts or fungi, etc. Typically the production is started by pumping in nutrients comprising sugars, proteins, salts, etc. into the fermenter (> 100 m3) , 5 which is then (steam) sterilised at a temperature of approx. 120°C for several hours. Meanwhile a preculture of a selected micro-organism is prepared (small culture flask, containing broth, grown for 24-48 hours) , which culture is used for inoculation of the fermenter, usually via a small o fermenter as an intermediate step. In order to get optimal growth vigorous stirring is necessary to assure good nutrient distribution and good oxygen dissolution. This stirring and also as a result of nutrient consumption
(combustion) , the heat, which is released, is absorbed via s cooling coils. During the fermentation (48-100 hours at approx. 40°C) several parameters are monitored to check pure microbial growth and enzyme production, and to automatically
adjust nutrient levels, oxygen uptake, pH, temperature, etc. After the fermentation, the broth is treated with chemicals and solvents to kill the production micro-organisms, filtered to remove germs and stored to cool down. With the aid of inorganic salts and organic solvents the enzyme is precipitated from the clear liquid, filtered and washed, dried and finally sieved. During all these processes the enzyme activity and purity is checked. Finally the enzyme is suitably formulated to liquids, slurries or (dust free) granulates. These granulates may be of the type to contain various types of enzymes in various overlayers to allow for so-called sequential release of the enzymes upon application.
Subsequently, or during enzyme formulation, an enzymatic bleach booster formulation can be produced by mixing a selection of enzymes and their substrates plus minor quantities of activator and/or stabiliser, processing aids etc, to be contained in a useful deliverance system such as a bottle, a sachet, an ampoule, a tablet or the like, depending on the physical appearance of the (concentrated) enzyme mixture.
Due to their nature enzymes act as biochemical catalysts i.ed. they facilitate a certain reaction drastically, without really being an active participant, which is being transformed or "consumed" by that reaction. By this invention it has been found, that upon application of enzymes, as the main ingredient in enzymatic bleach boosting processes, these enzymes apparently do act, and therefore give good performances, under moderate till very 0 low temperatures, at which chemical bleaching usually is rather poor. Also in the absence of builders, which are normally necessary to constitute low water hardness conditions to allow sufficient performance of the chemical ingredients, it is found that enzymes do perform s excellently. By this invention it is specifically demonstrated that in the absence of chemical bleach, sufficient bleaching activity can be obtained, provided the
proper enzyme mixture is being applied. Surprisingly it was also found that, in the absence of anti-redeposition agents and optical brighteners, with certain enzyme cocktails an unexpectedly high whiteness level of the fabrics can be reached. Apparently enzymes are particularly active and stable under application conditions to allow for the use of only moderate enzyme concentrations whilst still getting good performance results.
Another object of the invention is a method of bleaching, washing or cleaning a soiled object in which the method is characterized by the following steps: a) supplying an enzymatic bleach booster composition and optionally a washing or cleaning composition to the soiled object; and b) washing or cleaning the soiled object.
The soiled object can be anything that needs to be bleached, washed or cleaned. For example the soiled object can be laundry, china, glasses, kitchen or sanitary floors and so on. The soiled objects can be found in households, institutions (like hospitals) and in industrial environments.
The washing or cleaning composition may comprise a detergent composition (that is suitable for application in which it will be used) . The enzymatic bleach booster composition is added to the washing or cleaning composition to provide a bleaching activity for the thus obtained composition.
The enzymatic bleach booster composition can also be used after dissolution in water or when it is formulated as a liquid, it could be used non-diluted.
A big advantage of the enzymatic bleach booster composition is that it can be dosed in an amount that is needed for the job to be done. Furthermore it can be used seperately, e.g. in the bleaching of white fabrics that appeared to have become yellowish.
The invention further relates to a broad field of applications, because the soils and stains that can be removed are quite universal.
Soils and stains may vary considerably in terms of their composition, most of them are fully natural due to the fact that they are derived after spillage of all kinds of natural substances such as for instance food and drinks, or are the results of contact with the body. Therefore most stains may considered to be a mixture of bio-macromolecules and other particular soil, most of the time significantly denatured and (therefore) firmly attached to the surface (fabric, dish, etc) , and consequently very difficult to remove. By using enzymatic bleach booster compositions it is found that all kinds of natural occurring soils can be removed rather easily, even at low temperatures, most specifically stains that are sensitive to biochemical hydrolases, oxidases, and lyases. Surprisingly other soils are being removed concomitantly, giving an extremely white appearance of the enzymatically bleach boosted, washed textile or other surface. In other words it does not really matter where the soil and stain is coming from, nor where it is sitting. As long as sufficient quantities of bleach boosting enzymes plus stabilisers are present in the enzymatic bleach booster composition the removal of soil and 5 stains will be carried out quite effectively, provided some mechanical force and some rinsing with water is carried out, either in typically designed equipment or by hand. Therefore the field of application may be the area of textile care and cleaning i.e. the field of household laundry cleaning in 0 washing machines, or via manual cleaning. Another field of application may be the area of industrial and institutional cleaning as superior alternative for the rather aggressive chemical cleaning processes that are currently being applied. Another field of application may be the area of dry s cleaning which is currently being performed with basically very versatile and therefore strongly air polluting chemicals. Again another field of application may be the
area of either ADD's (automatic dishwash detergents) or HDD's (hand dishwash detergents), as a better performing alternative, which is also more compatible with for instance delicate china or silver cutlery, due to its less aggressive s nature, and therefore more friendly to the end-user i.e. the consumer as well as to the environment. Other examples of field of application are equipment cleaning, hardsurface cleaning, such as tiles, toiletbowls, and the like, which nowadays is done mainly via strong alkali, hypochlorite and o hot water. It must be clear that all the area's described, are just some examples of fields of application of the current invention, and may not be considered as a limitation whatsoever.
As already mentioned in the previous section, one of s the great advantages of enzymatic bleach boosting is that unexpected cleaning results can be obtained at relatively low enzyme concentrations and rather low washing temperatures. Washing at low enzyme concentrations, as compared to the rather high concentrations needed in o chemical bleaching processes, will lead to significant savings in production energy/ environmental bio burden, for virtually the same cleaning results. For the sake of illustration; a change from washing at 60°C, (for proper chemical bleaching) , to 40°C for excellent enzymatic s bleaching, will save an amount of energy, that can be estimated to be approx. 0.5 kWh or 1800 kJ per wash. Therefore the energy spent on the production of an enzymatic bleach booster corresponds to less than 10 % of the energy savings by using these boosters (at low wash temperature) . o From a biodegradability point of view, it may be stated, that enzymes are fully biodegradable and do not form an environmental risk, whatsoever. Over the last 15 years large quantities of enzymes have been produced and used as additives in a wide variety of applications, without any 5 adverse effects on the health of the end-users, and/or the environment, and in this respect most certainly are better
alternatives for many chemicals, that currently are being used.
Another benefit of the use of enzymatic bleach booster compositions is that the enzymes contained in these compositions generate their bleaching activity in situ, which means at the place and time needed, rather than having the bleach already available in the dry (synthetic) detergent matrix, which asks for extra stability measures upon manufacturing, packaging and storage of the detergents. All in all it can be said that the use of enzymatic bleach booster compositions is a better alternative relative to chemical bleaching in terms of: better performance, better for the environment, and with better economic results (lower production and application energy) .
Examples
A test system for the enzymatic bleach booster composition was developed. This test system was based on the ability of the compositions to remove stains from either indicator swatches (e.g. commercially available swatches from EMPA (Swiss federal laboratories for materials testing & research, St. Gallen, Switzerland)) or household worn textiles, which were washed in a Miele type washing machine (W701) under fully controlled conditions. The performance of the enzymes was conveniently determined by reflectance measurements (on the textiles) which is well known to those skilled in the art.
In some cases the results of the washing experiments were evaluated through a panel evaluation in which individuals had to judge the results visually.
Example 1
As mentioned before, conventional powder detergents do contain either perborate or percarbonate as the most important bleaching agent. A drawback of conventional chemical bleaching is that its efficiency is significantly
slowed down at low temperatures e.g. at 40°C and lower, due to the rather poor solubility of the chemical bleaching system. In order to overcome this inefficiency, we successfully designed an enzymatic alternative, which is a combination of a suitable enzyme, a suitable substrate and an activator. As a typical example, which should not be considered as a limitation of the invention, of such an enzymatic bleach booster composition, we disclose the results obtained with: glucose oxidase (as the bleaching enzyme) , glucose (as the substrate) and TAED (as the activator) .
Test conditions:
Washing at 50, 40 and 30°C for 30 min. Test swatches: A) Red wine on cotton (EMPA art.nr. 114)
B) Blood on cotton (EMPA art.nr. Ill) Results (% soil removal) :
The % soil removal was calculated from the reflectance measurements, using the following formula:
^soiled, and washed " ^soiled, not washed % soil removal = 100%
Knot soiled " ^soiled, not washed
(R denoting the reflectance)
50 °C 40 °C 30 °C
A B A B A B
Detergent 37 80 37 79 30 76
Detergent + PB4 60 73 52 71 34 72
Detergent + PB4 + TAED 81 72 75 72 52 74
Detergent + GOX 43 81 39 80 49 79
Detergent + GOX + TAED 70 85 67 86 65 84
Detergent = IEC (zeolite containing test detergent obtained from WFK Krefeld, Germany) detergent without bleach : 5 g/1 sud
PB4 = sodium perborate tetra hydrate : 12 % (w/w) TAED = tetra acetyl ethylene diamine: 2% (w/w) GOX = Glucose/Glucose oxidase (1:1) : 5% (w/w) MAXAZYME GO* glucose oxidase (purchased from Gist-Brocades B.V.) with 2500 Sarrett Units/g was used.
From these results it is clear that the enzymatic bleach booster composition, specifically at low temperatures, performs better than current days chemical bleach compositions. Surprisingly this performance is significantly enhanced by the addition of TAED. Apparently the best low temperature bleaching activity can be obtained by a mixture of enzymes, substrates and an activator.
Example 2 One reason for rapid degradation of bleach activity is supposed to be the potential presence of e.g. catalases in textiles. These catalases are secreted by the human body upon perspiration and therefore are most commonly present in heavily worn socks, sport shirts and bedsheets. In order to overcome this bleach degradation, we have successfully designed specific enzyme mixtures comprising suitable proteolytic enzymes in combination with suitable stabilisers, able to suppress catalase activity released from the textile and therefore able to significantly boost the bleaching capacity. As a typical example, which should not be considered as a limitation of the invention, of such a bleach protector composition, we disclose the results obtained with MAXAPEM* CX20-protease, with 20 Maxapem Units/g, (as the bleach stable proteolytic enzyme obtainable from Genencor International Inc.) and hydroxylammonium- sulphate.
Test conditions:
Washing at 40°C
Test swatches: A) Red wine on cotton (EMPA ART. NR 114)
B) Blood on cotton (EMPA ART. NR 111)
C) Cocoa on cotton (EMPA ART. NR 112) Results (% soil removal) :
B
Det + PB4 + TAED 100 (*) 100 (*) 100 (*)
Det + PB4 + TAED + socks 62 80 46 0 Det + PB4 + TAED + socks + Mix 85 100 91
Det = IEC detergent without bleach : 5 g/1 sud PB4 = sodium perborate tetra hydrate : 12 % (w/w) TAED = tetra acetyl ethylene diamine : 2 % (w/w) s Mix = MAXAPEM® protease/hydroxylammoniumsulphate (2:1) : 3 % (w/w) (*) = set at 100 by definition
The above presented results show that the mixture of MAXAPEM® protease/hydroxyl ammonium sulphate restore most of 0 the bleaching capacity of chemical bleach.
Example 3
Based on the results described in the previous two examples we have also tested the outcome of combinations of s the enzymatic bleach booster composition and the bleach protector composition.
Testconditions : Washing at 30 and 40°C 0 Test swatches: A) Red wine on cotton (EMPA ART. NR 114)
B) Blood on cotton (EMPA ART.NR 111) Results (% soil removal) :
40°C 30°C
A B
A
B
Det + PB4 + TAED 74 73 50 72
Det + PB4 + TAED + socks 44 58 31 58
Det + PB4 + TAED + socks + mix 63 74 42 73
Det + GOX + TAED + socks 42 60 47 55
Det + GOX + TAED + socks + mix 61 90 66 92
Det = IEC detergent without bleach : 5 g/1 sud PB4 = sodium perborate tetra hydrate : 12% (w/w) TAED = tetra acetyl ethylene diamine: 2% (w/w) Mix = MAXAPEM® protease/hydroxylammoniumsulphate
(2:1) : 3% (w/w) GOX = Glucose/MAXAZYME GO® Glucose oxidase (2500 SU/g)
(1:1) : 5% (w/w)
Surprisingly, since it was expected that the glucose oxidase would be affected by the protease, we found that the combination of GOX (Glucose/Glucose oxidase) and the protease containing bleach protector composition resulted in the best bleaching performance, especially at low temperatures .
Example 4
Alternatively we checked the results of the bleach protector composition by a panel analysis. For that reason a random selection was made amongst sufficient families to compose a group of 125 families, which was very heterogenous in washing habits, 80% of them having children, of which 50 % being younger than 12 years old. The group was asked to run house-hold washings for 3 periods of 3 weeks each, with the detergents the family was familiar with (test sample A) , this detergent plus a bleach protector composition (test sample B) and this detergent plus a placebo (test sample C) .
The bleach protector composition (dosed per wash) consisted of bleach stable MAXAPEM® CX 20 protease prills
(20 Maxapem U/g) (purchased from Genencor International Inc . ) : 1.0 g
MAXAMYL® CXT 5000 amylase prills (5000 TAU/g)
(purchased from Genencor International Inc.) : 0.4 g and hydroxylammoniumsulphate crystals : 0.5 g
The placebo consisted of empty prills.
o Based on a total of about 4000 house-hold washes, the results read as follows:
Preference; Test sample A 21% s Test sample B 54% Test sample C 22% No difference 3%
Looking in more detail at the cleaning power, on a o scale ranging from 1 = excellent, 2 = good, 3 = fair and 4 = bad, the results read as follows:
Whiteness Dirt removal Overall
Test sample A 3.10 2.09 2.58
Test sample B 1.39 1.70 1.57 5 Test sample C 3.23 2.51 2.88
From these results it is clear that the addition of a bleach protector composition will boost up general detergency (best score in dirt removal) , and surprisingly 0 has also an enormous beneficial effect on fabric whiteness (best score on whiteness) , which may be considered as a unexpected bonus, that allows for the reduction in use of optical brighteners.
Claims
1. An enzymatic bleach booster composition comprising at least
5 an enzyme and a substrate for this enzyme, which substrate can be converted by this enzyme in a bleach active compound.
2. An enzymatic bleach booster composition according o to claim 1, which comprises very little builders and surfactants .
3. An enzymatic bleach booster composition according to claim 1 or 2, which further comprises a bleach activator. 5
4. An enzymatic bleach booster composition according to claim 1-3, which further comprises a bleach protector composition.
0 5. An enzymatic bleach booster composition according to claims 1-4, in which the enzyme is selected from glucose oxidase, ribose oxidase, methanol oxidase or ethanol oxidase.
5 6. An enzymatic bleach booster composition according to claim 1-4 in which the substrate is selected from glucose, ribose, methanol or ethanol.
7. An enzymatic bleach booster composition according o to claim 3, in which the bleach activator is selected from
TAED, TAGU, SNOBS, ISONOBS or PAG.
8. An enzymatic bleach booster composition according to claim 4, in which the bleach protector composition 5 comprises a protease and/or a catalase inhibitor.
9. An enzymatic bleach booster composition according to claim 8 in which the catalase inhibitor is hydroxyl ammonium sulphate .
s
10. A method of bleaching, washing or cleaning a soiled object in which the method is characterized by the following steps: a) supplying an enzymatic bleach booster composition and optionally a washing or cleaning composition to the o soiled object; and b) washing or cleaning the soiled object.
11. A method according to claim 10 in which the enzymatic bleach booster composition is defined in one of s claims 1-9.
12. Use of a bleach protector composition capable of increasing the effectiveness of bleach in bleaching, washing or cleaning processes. 0
13. Use of a bleach protector composition according to claim 12, in which the bleach is obtained from an enzymatic bleach booster composition.
s 14. Use of a bleach activator capable of increasing the bleaching, washing or cleaning performance of enzymactic bleach booster compositions.
15. A bleach protector composition capable of 0 increasing the effectiveness of bleach in bleaching, washing or cleaning processes which composition comprises a protease and hydroxylammonium sulphate .
Applications Claiming Priority (3)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
EP94202101 | 1994-07-18 | ||
EP94202101 | 1994-07-18 | ||
PCT/EP1995/002875 WO1996002623A1 (en) | 1994-07-18 | 1995-07-18 | Enzymatic bleach booster compositions |
Publications (2)
Publication Number | Publication Date |
---|---|
AU3163195A true AU3163195A (en) | 1996-02-16 |
AU701937B2 AU701937B2 (en) | 1999-02-11 |
Family
ID=8217049
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
AU31631/95A Ceased AU701937B2 (en) | 1994-07-18 | 1995-07-08 | Enzymatic bleach booster compositions |
Country Status (4)
Country | Link |
---|---|
EP (1) | EP0745118A1 (en) |
AU (1) | AU701937B2 (en) |
CA (1) | CA2186498A1 (en) |
WO (1) | WO1996002623A1 (en) |
Families Citing this family (4)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US6569286B1 (en) | 1998-09-30 | 2003-05-27 | Warwick International Group Limited | Method for the alkaline bleaching of pulp with a peroxyacid based oxygen bleaching species using an agglomerated bleach activator |
DE102006037440A1 (en) * | 2006-08-09 | 2008-02-14 | Henkel Kgaa | Detergents and cleaners containing oxidoreductases and bleach activators |
DE102007040326A1 (en) * | 2007-08-24 | 2009-02-26 | Henkel Ag & Co. Kgaa | Laundry pre-treatment agent and method |
KR20210136009A (en) | 2019-01-31 | 2021-11-16 | 펄스테라 코포레이션 | Sterilization method and composition |
Family Cites Families (7)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US3640877A (en) * | 1969-04-17 | 1972-02-08 | Michael R R Gobert | Detergent |
US4421668A (en) * | 1981-07-07 | 1983-12-20 | Lever Brothers Company | Bleach composition |
JPS6460693A (en) * | 1987-08-28 | 1989-03-07 | Amano Pharma Co Ltd | Detergent containing oxidase and protease |
DE4231767A1 (en) * | 1992-09-23 | 1994-03-24 | Henkel Kgaa | Bleaching or washing compsns. contg. no bleach activators - contain hydrogen peroxide source comprising oxidase enzyme and substrate |
JPH06315907A (en) * | 1993-05-06 | 1994-11-15 | Amano Pharmaceut Co Ltd | Decolor processing agent and decolor processing method for wood |
US5601750A (en) * | 1993-09-17 | 1997-02-11 | Lever Brothers Company, Division Of Conopco, Inc. | Enzymatic bleach composition |
JPH0797597A (en) * | 1993-09-29 | 1995-04-11 | Sekisui Chem Co Ltd | Composition for decomposing mold pigment |
-
1995
- 1995-07-08 AU AU31631/95A patent/AU701937B2/en not_active Ceased
- 1995-07-18 EP EP95927685A patent/EP0745118A1/en not_active Withdrawn
- 1995-07-18 CA CA002186498A patent/CA2186498A1/en not_active Abandoned
- 1995-07-18 WO PCT/EP1995/002875 patent/WO1996002623A1/en not_active Application Discontinuation
Also Published As
Publication number | Publication date |
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WO1996002623A1 (en) | 1996-02-01 |
EP0745118A1 (en) | 1996-12-04 |
AU701937B2 (en) | 1999-02-11 |
CA2186498A1 (en) | 1996-02-01 |
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