MXPA99009216A - Cleaning compositions having enhanced enzyme activity - Google Patents
Cleaning compositions having enhanced enzyme activityInfo
- Publication number
- MXPA99009216A MXPA99009216A MXPA/A/1999/009216A MX9909216A MXPA99009216A MX PA99009216 A MXPA99009216 A MX PA99009216A MX 9909216 A MX9909216 A MX 9909216A MX PA99009216 A MXPA99009216 A MX PA99009216A
- Authority
- MX
- Mexico
- Prior art keywords
- percent
- weight
- composition
- surfactant
- carbon atoms
- Prior art date
Links
- 239000000203 mixture Substances 0.000 title claims abstract description 150
- 238000004140 cleaning Methods 0.000 title claims abstract description 37
- 230000024881 catalytic activity Effects 0.000 title description 4
- 239000004094 surface-active agent Substances 0.000 claims abstract description 75
- 102000004190 Enzymes Human genes 0.000 claims abstract description 56
- 108090000790 Enzymes Proteins 0.000 claims abstract description 56
- 229940088598 Enzyme Drugs 0.000 claims abstract description 38
- 108091005771 Peptidases Proteins 0.000 claims abstract description 33
- 239000004365 Protease Substances 0.000 claims abstract description 31
- 102000004882 lipase Human genes 0.000 claims abstract description 31
- 108090001060 lipase Proteins 0.000 claims abstract description 31
- 239000004367 Lipase Substances 0.000 claims abstract description 30
- 235000019421 lipase Nutrition 0.000 claims abstract description 30
- -1 alkyl ether sulfate Chemical class 0.000 claims abstract description 20
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 claims abstract description 20
- 235000000346 sugar Nutrition 0.000 claims abstract description 20
- 102000035443 Peptidases Human genes 0.000 claims abstract description 10
- 102000013142 Amylases Human genes 0.000 claims abstract description 9
- 108010065511 Amylases Proteins 0.000 claims abstract description 9
- 108010084185 Cellulases Proteins 0.000 claims abstract description 9
- 102000005575 Cellulases Human genes 0.000 claims abstract description 9
- 108090000437 Peroxidases Proteins 0.000 claims abstract description 9
- 102000003992 Peroxidases Human genes 0.000 claims abstract description 9
- 235000019418 amylase Nutrition 0.000 claims abstract description 9
- 229940025131 Amylases Drugs 0.000 claims abstract description 7
- 125000000217 alkyl group Chemical group 0.000 claims description 42
- 238000000034 method Methods 0.000 claims description 40
- 125000004432 carbon atoms Chemical group C* 0.000 claims description 37
- 102000033147 ERVK-25 Human genes 0.000 claims description 23
- 229940106157 CELLULASE Drugs 0.000 claims description 21
- 108010059892 Cellulase Proteins 0.000 claims description 21
- 229940040461 Lipase Drugs 0.000 claims description 19
- 239000003599 detergent Substances 0.000 claims description 14
- RTZKZFJDLAIYFH-UHFFFAOYSA-N diethyl ether Chemical compound CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 claims description 13
- 235000014113 dietary fatty acids Nutrition 0.000 claims description 11
- 239000000194 fatty acid Substances 0.000 claims description 11
- 150000004665 fatty acids Chemical class 0.000 claims description 11
- QAOWNCQODCNURD-UHFFFAOYSA-L sulfate Chemical compound [O-]S([O-])(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-L 0.000 claims description 11
- 240000007170 Cocos nucifera Species 0.000 claims description 10
- 235000013162 Cocos nucifera Nutrition 0.000 claims description 10
- 239000003795 chemical substances by application Substances 0.000 claims description 10
- 239000000758 substrate Substances 0.000 claims description 10
- 239000007788 liquid Substances 0.000 claims description 9
- IAYPIBMASNFSPL-UHFFFAOYSA-N oxane Chemical compound C1CO1 IAYPIBMASNFSPL-UHFFFAOYSA-N 0.000 claims description 9
- 239000004753 textile Substances 0.000 claims description 9
- 239000003945 anionic surfactant Substances 0.000 claims description 5
- 239000007844 bleaching agent Substances 0.000 claims description 5
- 230000000875 corresponding Effects 0.000 claims description 5
- 239000000975 dye Substances 0.000 claims description 5
- 239000006260 foam Substances 0.000 claims description 5
- 239000006057 Non-nutritive feed additive Substances 0.000 claims description 4
- 239000012190 activator Substances 0.000 claims description 4
- 239000000654 additive Substances 0.000 claims description 4
- 239000002280 amphoteric surfactant Substances 0.000 claims description 4
- 239000000969 carrier Substances 0.000 claims description 4
- 239000003093 cationic surfactant Substances 0.000 claims description 4
- 239000002738 chelating agent Substances 0.000 claims description 4
- 239000002270 dispersing agent Substances 0.000 claims description 4
- 239000003752 hydrotrope Substances 0.000 claims description 4
- 239000003112 inhibitor Substances 0.000 claims description 4
- 230000002401 inhibitory effect Effects 0.000 claims description 4
- 239000002736 nonionic surfactant Substances 0.000 claims description 4
- 230000003287 optical Effects 0.000 claims description 4
- 239000000049 pigment Substances 0.000 claims description 4
- 239000002689 soil Substances 0.000 claims description 4
- 239000002904 solvent Substances 0.000 claims description 4
- 101710023152 yngHB Proteins 0.000 claims description 4
- 239000002888 zwitterionic surfactant Substances 0.000 claims description 4
- 150000002632 lipids Chemical class 0.000 claims description 3
- 238000004821 distillation Methods 0.000 claims 6
- 125000000837 carbohydrate group Chemical group 0.000 claims 3
- 125000001033 ether group Chemical group 0.000 claims 3
- 230000002087 whitening Effects 0.000 claims 2
- ATVJXMYDOSMEPO-UHFFFAOYSA-N 3-prop-2-enoxyprop-1-ene Chemical compound C=CCOCC=C ATVJXMYDOSMEPO-UHFFFAOYSA-N 0.000 claims 1
- 150000005215 alkyl ethers Chemical class 0.000 claims 1
- 229940110715 ENZYMES FOR TREATMENT OF WOUNDS AND ULCERS Drugs 0.000 description 18
- 238000006116 polymerization reaction Methods 0.000 description 12
- 238000001007 flame atomic emission spectroscopy Methods 0.000 description 8
- 238000010587 phase diagram Methods 0.000 description 7
- 230000000694 effects Effects 0.000 description 5
- 241000233866 Fungi Species 0.000 description 4
- GUBGYTABKSRVRQ-YOLKTULGSA-N Maltose Natural products O([C@@H]1[C@H](O)[C@@H](O)[C@H](O)O[C@H]1CO)[C@@H]1[C@H](O)[C@@H](O)[C@@H](O)[C@@H](CO)O1 GUBGYTABKSRVRQ-YOLKTULGSA-N 0.000 description 4
- 241000209149 Zea Species 0.000 description 4
- 235000002017 Zea mays subsp mays Nutrition 0.000 description 4
- 125000005466 alkylenyl group Chemical group 0.000 description 4
- OKTJSMMVPCPJKN-UHFFFAOYSA-N carbon Chemical group [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 4
- 235000005822 corn Nutrition 0.000 description 4
- 235000005824 corn Nutrition 0.000 description 4
- 238000009472 formulation Methods 0.000 description 4
- 241000196324 Embryophyta Species 0.000 description 3
- 229940072417 Peroxidase Drugs 0.000 description 3
- 125000003342 alkenyl group Chemical group 0.000 description 3
- 230000001580 bacterial Effects 0.000 description 3
- YFMUPHJGWWRKLX-UHFFFAOYSA-N boric acid;propane-1,2-diol Chemical compound OB(O)O.CC(O)CO YFMUPHJGWWRKLX-UHFFFAOYSA-N 0.000 description 3
- 150000001720 carbohydrates Chemical group 0.000 description 3
- 150000001875 compounds Chemical class 0.000 description 3
- 229910001651 emery Inorganic materials 0.000 description 3
- 125000001183 hydrocarbyl group Chemical group 0.000 description 3
- 102000004169 proteins and genes Human genes 0.000 description 3
- 108090000623 proteins and genes Proteins 0.000 description 3
- 235000010339 sodium tetraborate Nutrition 0.000 description 3
- 239000006188 syrup Substances 0.000 description 3
- 235000020357 syrup Nutrition 0.000 description 3
- BSVBQGMMJUBVOD-UHFFFAOYSA-N trisodium borate Chemical compound [Na+].[Na+].[Na+].[O-]B([O-])[O-] BSVBQGMMJUBVOD-UHFFFAOYSA-N 0.000 description 3
- 239000004382 Amylase Substances 0.000 description 2
- 241000193830 Bacillus <bacterium> Species 0.000 description 2
- BJHIKXHVCXFQLS-UYFOZJQFSA-N Fructose Natural products OC[C@@H](O)[C@@H](O)[C@H](O)C(=O)CO BJHIKXHVCXFQLS-UYFOZJQFSA-N 0.000 description 2
- 241000223198 Humicola Species 0.000 description 2
- 229940024999 Proteolytic enzymes for treatment of wounds and ulcers Drugs 0.000 description 2
- 241000191940 Staphylococcus Species 0.000 description 2
- SRBFZHDQGSBBOR-SQOUGZDYSA-N Xylose Natural products O[C@@H]1CO[C@@H](O)[C@@H](O)[C@@H]1O SRBFZHDQGSBBOR-SQOUGZDYSA-N 0.000 description 2
- 239000002585 base Substances 0.000 description 2
- 229910052799 carbon Inorganic materials 0.000 description 2
- 238000006243 chemical reaction Methods 0.000 description 2
- 125000003438 dodecyl group Chemical group [H]C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])* 0.000 description 2
- HZAXFHJVJLSVMW-UHFFFAOYSA-N ethanolamine Chemical compound NCCO HZAXFHJVJLSVMW-UHFFFAOYSA-N 0.000 description 2
- 238000002474 experimental method Methods 0.000 description 2
- 230000002538 fungal Effects 0.000 description 2
- MHAJPDPJQMAIIY-UHFFFAOYSA-N hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 description 2
- 239000004615 ingredient Substances 0.000 description 2
- 125000002496 methyl group Chemical group [H]C([H])([H])* 0.000 description 2
- 210000000056 organs Anatomy 0.000 description 2
- RZVAJINKPMORJF-UHFFFAOYSA-N p-acetaminophenol Chemical compound CC(=O)NC1=CC=C(O)C=C1 RZVAJINKPMORJF-UHFFFAOYSA-N 0.000 description 2
- 239000000843 powder Substances 0.000 description 2
- 235000019833 protease Nutrition 0.000 description 2
- 239000002994 raw material Substances 0.000 description 2
- 150000008163 sugars Chemical class 0.000 description 2
- 238000005406 washing Methods 0.000 description 2
- WQZGKKKJIJFFOK-VFUOTHLCSA-N β-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 2
- 241000607534 Aeromonas Species 0.000 description 1
- 241000228212 Aspergillus Species 0.000 description 1
- 241000193422 Bacillus lentus Species 0.000 description 1
- 235000014469 Bacillus subtilis Nutrition 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 108091005650 Basic proteases Proteins 0.000 description 1
- 210000004369 Blood Anatomy 0.000 description 1
- 210000001124 Body Fluids Anatomy 0.000 description 1
- 241000218236 Cannabis Species 0.000 description 1
- 240000000218 Cannabis sativa Species 0.000 description 1
- GZCGUPFRVQAUEE-KCDKBNATSA-N D-(+)-Galactose Natural products OC[C@@H](O)[C@H](O)[C@H](O)[C@@H](O)C=O GZCGUPFRVQAUEE-KCDKBNATSA-N 0.000 description 1
- WQZGKKKJIJFFOK-GASJEMHNSA-N D-Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 1
- WQZGKKKJIJFFOK-QTVWNMPRSA-N D-mannopyranose Chemical compound OC[C@H]1OC(O)[C@@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-QTVWNMPRSA-N 0.000 description 1
- 241000237379 Dolabella Species 0.000 description 1
- 108010035722 EC 1.11.1.10 Proteins 0.000 description 1
- 108010073997 EC 1.11.1.18 Proteins 0.000 description 1
- 239000005715 Fructose Substances 0.000 description 1
- 210000000514 Hepatopancreas Anatomy 0.000 description 1
- 240000005979 Hordeum vulgare Species 0.000 description 1
- 235000007340 Hordeum vulgare Nutrition 0.000 description 1
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 1
- 241001480714 Humicola insolens Species 0.000 description 1
- GUBGYTABKSRVRQ-UUNJERMWSA-N Lactose Natural products O([C@@H]1[C@H](O)[C@H](O)[C@H](O)O[C@@H]1CO)[C@H]1[C@@H](O)[C@@H](O)[C@H](O)[C@H](CO)O1 GUBGYTABKSRVRQ-UUNJERMWSA-N 0.000 description 1
- 240000008415 Lactuca sativa Species 0.000 description 1
- 235000003228 Lactuca sativa Nutrition 0.000 description 1
- 241000237852 Mollusca Species 0.000 description 1
- 241000187479 Mycobacterium tuberculosis Species 0.000 description 1
- 229940010383 Mycobacterium tuberculosis Drugs 0.000 description 1
- 240000007594 Oryza sativa Species 0.000 description 1
- 235000007164 Oryza sativa Nutrition 0.000 description 1
- 235000019482 Palm oil Nutrition 0.000 description 1
- 210000001819 Pancreatic Juice Anatomy 0.000 description 1
- 240000002834 Paulownia tomentosa Species 0.000 description 1
- 235000010678 Paulownia tomentosa Nutrition 0.000 description 1
- 241000589516 Pseudomonas Species 0.000 description 1
- 241000221662 Sclerotinia Species 0.000 description 1
- 206010070834 Sensitisation Diseases 0.000 description 1
- 240000006394 Sorghum bicolor Species 0.000 description 1
- 102000005158 Subtilisins Human genes 0.000 description 1
- 108010056079 Subtilisins Proteins 0.000 description 1
- 231100000765 Toxin Toxicity 0.000 description 1
- 240000008529 Triticum aestivum Species 0.000 description 1
- 229960003487 Xylose Drugs 0.000 description 1
- 241000235015 Yarrowia lipolytica Species 0.000 description 1
- 150000001298 alcohols Chemical class 0.000 description 1
- 229910052783 alkali metal Inorganic materials 0.000 description 1
- 150000001340 alkali metals Chemical group 0.000 description 1
- 229910052784 alkaline earth metal Chemical group 0.000 description 1
- 150000001342 alkaline earth metals Chemical group 0.000 description 1
- 150000003973 alkyl amines Chemical class 0.000 description 1
- 125000005233 alkylalcohol group Chemical group 0.000 description 1
- 108090000637 alpha-Amylases Proteins 0.000 description 1
- 102000004139 alpha-Amylases Human genes 0.000 description 1
- 230000003625 amylolytic Effects 0.000 description 1
- 230000001851 biosynthetic Effects 0.000 description 1
- 238000004061 bleaching Methods 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 239000010839 body fluid Substances 0.000 description 1
- 235000009120 camo Nutrition 0.000 description 1
- 238000006555 catalytic reaction Methods 0.000 description 1
- 235000013339 cereals Nutrition 0.000 description 1
- 235000005607 chanvre indien Nutrition 0.000 description 1
- 238000000354 decomposition reaction Methods 0.000 description 1
- 230000003247 decreasing Effects 0.000 description 1
- 238000001212 derivatisation Methods 0.000 description 1
- 239000008121 dextrose Substances 0.000 description 1
- 230000001079 digestive Effects 0.000 description 1
- 235000013399 edible fruits Nutrition 0.000 description 1
- 125000001495 ethyl group Chemical group [H]C([H])([H])C([H])([H])* 0.000 description 1
- 239000004744 fabric Substances 0.000 description 1
- 239000003925 fat Substances 0.000 description 1
- 235000013305 food Nutrition 0.000 description 1
- 239000008103 glucose Substances 0.000 description 1
- 125000002791 glucosyl group Chemical group C1([C@H](O)[C@@H](O)[C@H](O)[C@H](O1)CO)* 0.000 description 1
- 150000004676 glycans Polymers 0.000 description 1
- 150000002338 glycosides Chemical class 0.000 description 1
- 125000003630 glycyl group Chemical group [H]N([H])C([H])([H])C(*)=O 0.000 description 1
- 239000011487 hemp Substances 0.000 description 1
- 235000012765 hemp Nutrition 0.000 description 1
- 235000019534 high fructose corn syrup Nutrition 0.000 description 1
- 125000002887 hydroxy group Chemical group [H]O* 0.000 description 1
- 230000000977 initiatory Effects 0.000 description 1
- GUBGYTABKSRVRQ-XLOQQCSPSA-N lactose Chemical compound O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@H]1O[C@@H]1[C@@H](CO)O[C@H](O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-XLOQQCSPSA-N 0.000 description 1
- 239000008101 lactose Substances 0.000 description 1
- 108010062085 ligninase Proteins 0.000 description 1
- 235000012766 marijuana Nutrition 0.000 description 1
- 230000002906 microbiologic Effects 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- 235000019713 millet Nutrition 0.000 description 1
- 238000000199 molecular distillation Methods 0.000 description 1
- PMZURENOXWZQFD-UHFFFAOYSA-L na2so4 Chemical compound [Na+].[Na+].[O-]S([O-])(=O)=O PMZURENOXWZQFD-UHFFFAOYSA-L 0.000 description 1
- 235000014571 nuts Nutrition 0.000 description 1
- 239000003921 oil Substances 0.000 description 1
- 235000019198 oils Nutrition 0.000 description 1
- MYMOFIZGZYHOMD-UHFFFAOYSA-N oxygen Chemical compound O=O MYMOFIZGZYHOMD-UHFFFAOYSA-N 0.000 description 1
- 229910052760 oxygen Inorganic materials 0.000 description 1
- 239000001301 oxygen Substances 0.000 description 1
- 239000002540 palm oil Substances 0.000 description 1
- PNIJRIIGBGFYHF-UHFFFAOYSA-N perborate(2-) Chemical compound O[B-]1(O)OO[B-](O)(O)OO1 PNIJRIIGBGFYHF-UHFFFAOYSA-N 0.000 description 1
- JRKICGRDRMAZLK-UHFFFAOYSA-L peroxydisulfate Chemical compound [O-]S(=O)(=O)OOS([O-])(=O)=O JRKICGRDRMAZLK-UHFFFAOYSA-L 0.000 description 1
- 229920001282 polysaccharide Polymers 0.000 description 1
- 239000005017 polysaccharide Substances 0.000 description 1
- 150000004804 polysaccharides Polymers 0.000 description 1
- 230000017854 proteolysis Effects 0.000 description 1
- 230000002797 proteolythic Effects 0.000 description 1
- 239000011541 reaction mixture Substances 0.000 description 1
- 230000002829 reduced Effects 0.000 description 1
- 235000009566 rice Nutrition 0.000 description 1
- 230000008313 sensitization Effects 0.000 description 1
- 230000001235 sensitizing Effects 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 229910052938 sodium sulfate Inorganic materials 0.000 description 1
- 235000011152 sodium sulphate Nutrition 0.000 description 1
- MWNQXXOSWHCCOZ-UHFFFAOYSA-L sodium;oxido carbonate Chemical compound [Na+].[O-]OC([O-])=O MWNQXXOSWHCCOZ-UHFFFAOYSA-L 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 241000894007 species Species 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 230000002195 synergetic Effects 0.000 description 1
- 108010075550 termamyl Proteins 0.000 description 1
- 239000003053 toxin Substances 0.000 description 1
- 108020003112 toxins Proteins 0.000 description 1
- 150000003626 triacylglycerols Chemical class 0.000 description 1
- 235000013311 vegetables Nutrition 0.000 description 1
- 235000021307 wheat Nutrition 0.000 description 1
- WQZGKKKJIJFFOK-PHYPRBDBSA-N α-D-galactose Chemical compound OC[C@H]1O[C@H](O)[C@H](O)[C@@H](O)[C@H]1O WQZGKKKJIJFFOK-PHYPRBDBSA-N 0.000 description 1
Abstract
A cleaning composition containing:(a) from about 1 to about 60%by weight of a surfactant component consisting essentially of:(i) a fatty alkyl ether sulfate;(ii) a linear alcohol ethoxylate;and (iii) a nonionic sugar surfactant, having a ratio by weight of (i):(ii):(iii) in a range of about 0.5 to 1.0:1.5 to 2.5:0.5 to 1.5;and (b) from about 0.1 to about 10%by weight of an enzyme component selected from the group consisting of proteases, amylases, lipases, cellulases, peroxidases, and mixturesthereof, all weights being based on the weight of the compositon.
Description
"CLEANSING COMPOSITIONS THAT HAVE IMPROVED ENZYME ACTIVITY"
FIELD OF THE INVENTION
The present invention relates generally to a cleaning composition having improved enzyme activity and stability. More particularly, by adding an effective amount of alkyl polyglycoside to a cleaning composition having a predetermined amount of enzyme contained therein, the enzyme activity and stability of the cleaning composition is improved.
BACKGROUND OF THE INVENTION
Enzymes have long been used in the detergent field to improve the cleaning of textile substrates. Specific stains on dirty fabrics respond with particularity to enzymes that leave specific bonds in the molecules of the stain. For example, enzymes such as proteases and lipases are effective in removing stains, such as blood and oils from textile substrates. These spots are fractions of protein and lipid from food and fats such -
as those deposited from the dirt of the body. The action of the enzyme in the specific spot helps the surfactant to be a total cleaning improvement. A specific difficulty associated with working with enzymes is that when they occur in the form of powders, there have been cases of sensitization to the enzyme in selected people ^. To avoid contact with enzymes, it has been proposed that detergent products containing the same are prepared in the form of a lipid, thereby minimizing the presence of any fine powder containing the enzyme. However, liquid detergent formulations containing enzymes cause problems related to the stability of the enzyme. The problem associated with placing the enzymes in a liquid environment is that they are subject to decomposition, either by denaturing the surfactant or by self-digestion
(proteolysis). Therefore, it is a program to stabilize the enzymes over extended periods of time, particularly when exposed to heat which also reduces the stability of the enzyme. It is therefore desirable to obtain a cleaning composition in a solid liquid form in which the enzyme contained therein is stabilized in such a way that an improved synergistic cleaning operation is obtained.
COMPENDIUM OF THE INVENTION
The present invention provides a cleaning composition containing: (a) from about 1 percent to about 60 percent by weight of a mixture of the surfactant, the mixture containing: (i) an alkyl ether sulfate surfactant; (ii) a linear alcohol ethoxylate surfactant; and (ii) a sugar-nonionic surfactant, wherein the surfactants (i) - (iii) are present in the mixture in one of a weight ratio of
(i): (ii): (iii) of about 1: 2: 1; and (b) from about 0.1 percent to about 10 percent by weight of an enzyme that is selected from the group consisting of protease, amylase, lipase, cellulase, peroxidase, and mixtures thereof, all weights being weight-based of the composition.
- -
The present invention also provides a process for cleaning textile substrates which involves contacting the textile substrates with the cleaning composition disclosed above. The present invention also provides a process for making a cleaning composition having improved enzyme stability which involves: (a) providing from about 1 percent to about 60 percent by weight of a mixture of the surfactant, -the mixture contains: (i) a sulfate-alkyl ether surfactant; (ii) a linear alcohol ethoxylate surfactant; and (ii) a nonionic sugar surfactant, wherein the surfactants (i) - (iii) are present in the mixture in one of a weight ratio of
(i): (ii): (iii) of about 1: 2: 1; (b) providing from about 0.01 percent to about 10 weight percent of an enzyme that is selected from the group consisting of protease, amylase, lipase, cellulase, peroxidase and mixtures thereof; and (c) combining (a) and (b) to form the composition, all weights being based on the weight of the composition.
BRIEF DESCRIPTION OF THE DRAWINGS "" "
Figure 1 is a phase diagram showing the stability in the protease in a cleaning composition according to the present invention, then-28 days at 40 ° C. Figure 2 is a phase diagram showing the stability of the lipase in a cleaning composition, in accordance with the present invention, after 28 days at 40 ° C. Figure 3 is a phase diagram showing the stability of the cellulase in a cleaning composition, in accordance with the present invention, after 28 days at 40 ° C. Figure 4 is a phase diagram showing the stability of a protease and lipase in a cleaning composition, in accordance with the present invention, after 28 days at 40 ° C. Figure 5 is a phase diagram showing the stability of a protease and cellulase in a cleaning composition, in accordance with the present invention, after 28 days at 40 ° C. Figure 6 is a phase diagram showing the stability of a lipase and cellulase in a cleaning composition, in accordance with the present invention, after 28 days at 40 ° C. Figure 7 is a phase diagram showing the stability of the protease, lipase and cellulase in a cleaning composition, in accordance with the present invention, after 28 days at 40 ° C.
DESCRIPTION OF THE INVENTION
In another part other than the working examples or when indicated otherwise, all numbers expressing amounts of ingredients or reaction conditions used herein must be understood as having been modified in all cases by the term "approximately". Suitable nonionic sugar surfactants include, for example, alkyl polyglycosides and polyhydroxy fatty acid amides ("glucamides"). The polyhydroxy fatty acid amides which can be used in the present invention correspond to the form I:
Rl o
R - C - N - Y (I)
wherein Rj_ is H, hydrocarbyl of 1 to 4 carbon atoms, ethyl of 2-hydroxy, propyl of 2-hydroxy, or a mixture thereof, preferably alkyl of 1 to 4 carbon atoms, more preferably alkyl of 1 or 2 carbon atoms, and more preferably alkyl of 1 carbon atom (i.e., methyl); and R2 is a hydrocarbyl residue of 5 to 31 carbon atoms, preferably alkyl or alkenyl of 7 to 19 carbon atoms straight chain, more preferably alkyl or alkenyl of 9 to 17 straight carbon atoms, so especially preferred straight-chained alkyl or alkenyl of 11 to 19 carbon atoms, or a mixture thereof; and Y is a polyhydroxyhydrocarbyl residue having a linear hydrocarbyl chain with at least 3 hydroxyls directly connected to the chain, or an alkoxylated derivative (preferably ethoxylated or propoxylated) thereof. And, preferably it will be derived from a reducing sugar in a reductive animation reaction; more preferably Y is a residue is glycityl. Suitable reducing sugars include glucose, fructose, maltose, lactose, galactose, mannose and xylose. As raw materials, high dextrose corn syrup, high fructose corn syrup and high maltose corn syrup, as well as the individual sugars mentioned above may be used. These corn syrups can yield a mixture of sugar components for Y. It should be understood that in no way is it intended to exclude other suitable raw materials. And, preferably it will be selected from the group consisting of -CH - (CHOH) n-CH OH, -CH (CH 0 H) - (CHOH) n _? - CH 2? H / -CH 2 - (CHOH) (CHOR ') ( CHOH) -CH2OH, wherein n is an integer from 3 to 5, inclusive and R 'is H or a cyclic mono- or poly-saccharide, and alkoxylated derivatives thereof. glycyls are particularly preferred wherein n is 4, particularly -CH - (CHOH) 4 ~ CH2OH. The compounds of the formula I are also known as glucamides. Therefore, for example, when R] _ is methyl, R2 is dodecyl; and Y is -CH2- (CHOH) 4 ~ CH2OH, the compound in question is referred to as dodecyl N-methylglucamide. Methods for making the polyhydroxy fatty acid amides are known in the art. In general, the polyhydroxy fatty acid amides can be made by reductively aminating a reducing sugar which reacts with an alkyl amine to form a corresponding N-alkyl polyhydroxy ina, and then - -
by reacting the N-alkyl polyhydroxyamine with a fatty aliphatic ester or triglyceride to form the N-alkyl polyhydroxy fatty acid amide. The alkyl polyglycosides that can be used in the cleaning compositions according to the invention correspond to formula II: RiO (R20) b (Z) to (II) wherein R] _ is a monovalent organic radical having about 6 at about 30 carbon atoms; R2 is a divalent alkylene radical having from 2 to 4 carbon atoms; Z is a saccharide residue having 5 or 6 carbon atoms; b is a number having a value from 0 to about 12; a is a number having a value from 1 to about 6. Preferred alkyl polyglycosides that can be used in the compositions according to the invention have the formula I, wherein Z is a glucose residue and b is zero. These alkyl polyglycosides can be obtained commercially, for example, as APG®, GLUCOPON® or PLANTAREN® surfactants from Henkel Corporation, of Ambler, PA 19002. Examples of these surfactants include, but are not limited to: 1. Surfactant GLUCOPON® 220 - an alkyl polyglycoside wherein the alkyl group contains from 8 to 10 carbon atoms and has an average degree of polymerization of 1.5. 2. GLUCOPON® surfactant 225 - an alkyl polyglycoside wherein the alkyl group contains from 8 to 10 carbon atoms and has an average degree of polymerization of 1.7. 3. GLUCOPON® 600 surfactant - an alkyl polyglycoside wherein the alkyl group contains from 12 to 16 carbon atoms and has an average degree of polymerization of 1.4. 4. GLUCOPON® 625 surfactant - an alkyl polyglycoside wherein the alkyl group contains from 12 to 16 carbon atoms and has an average degree of polymerization of 1.4. 5. APG® 325 surfactant - an alkyl polyglycoside wherein the alkyl group contains from 9 to 11 carbon atoms and has an average degree of polymerization of 1.6. 6. PLANTAREN® 2000 surfactant - an alkyl polyglycoside wherein the alkyl group contains from 8 to 16 carbon atoms and has an average degree of polymerization of 1.4. 7. PLANTAREN® 1300 surfactant - an alkyl polyglycoside wherein the alkyl group contains from 12 to 16 - -
carbon atoms and has an average degree of polymerization of 1.6. 8. AGRIMUL® PG 2067 surfactant - an alkyl polyglycoside wherein the alkyl group contains from 8 to 10 carbon atoms and has an average degree of polymerization of 1.7. Other examples include the alkyl polyglycoside surfactant compositions comprising mixtures of compounds of the formula I, wherein Z represents a reducing tm_ saccharide-derived residue containing 5 or 6 carbon atoms; a is a number that has a value from 1 to approximately 6; b is zero; and R] _ is an alkyl radical having from 8 to 20 carbon atoms. The compositions are characterized in that they have increased surfactant properties and an HLB within the scale of about 10 about 16, and a non-Flory distribution of glycosides. which consists of a mixture of an alkyl monoglycoside and a mixture of alkyl polyglycosides having varying degrees of polymerization of 2 and higher, in progressively decreasing amounts, wherein the amount by weight of the polyglycoside having the degree of polymerization of 2, or mixtures thereof with the polyglycoside having a degree of polymerization of 3, predominate in relation to the amount of monoglycoside, said composition having a -
average polymerization degree of about 1.8 to about 3. These compositions, also known as alkyl maximal polyglycosides, can be prepared by removing the monoglycoside from the original reaction mixture of alkyl monoglycoside and alkyl polyglycosides after the alcohol removal. . This separation can be carried out by molecular distillation and normally results in the removal of about 70 percent to 95 percent by weight of the alkyl monoglycoside. After the removal of the alkyl monoglycosides, the relative distribution of the different components, mono- and polyglycosides in the resulting product, changes and the concentration in the product of the polyglycosides in relation to the monoglycoside increases as well as the concentration of the individual polyglycosides to the total, that is, the DP2 fractions and DP3 in relation to the sum of all DP fractions. These compositions are disclosed in U.S. Patent Number 5,266,690, the total content of which is incorporated herein by reference. Other alkyl polyglycosides that may be used in the compositions according to the invention are those wherein the alkyl residue contains from 6 to 18 carbon atoms, wherein the average length of the carbon chain of the composition is from about 9 to about 14, comprising a mixture of 2 or more of at least binary alkyl polyglycoside components, wherein each binary component is present in the mixture in relation to its average carbon chain length in an amount effective to provide the composition surfactant with the average length of the carbon chain from about 9 to about 14, and wherein at least one or both of the binary components comprise a distribution of Flory polyglycosides which are derived from an acid-catalyzed reaction of the alcohol containing 6 to 20 carbon atoms and an appropriate saccharide of -where the excess alcohol has separated. In a particularly preferred embodiment, the nonionic sugar surfactant is an alkyl polyglycoside corresponding to formula 117 wherein R] _ is a monovalent organic radical having from about 8 to about 16 carbon atoms, b is zero and is a number having a value of from 1 to about 3. The alkyl ether sulfates which can be used in the present invention correspond to formula III: Ri - (CH2CH20) n-S03X (III) - -
wherein R] _ is a linear or branched alkyl or alkenyl radical having from about 8 to about 16 carbon atoms, n is a number from 1 to 10, and X is an alkali metal or alkaline earth metal. A particularly preferred alkyl ether sulfate for use in the present invention is SULFOTEX® NL60-S, a semi-cut coconut ether sulfate having 2 moles of ethylene oxide.The linear alcohol ethoxylates which can be employed in the present invention can be either straight chain or branched chain alcohols having from 8 to 16 carbon atoms which are ethoxylated with from about 1 to about 10 moles of ethylene oxide.Their derivatization is well known in the art. Particularly preferred embodiment of the present invention, the linear alcohol ethoxylate is an ethoxylated straight chain 12 to 16 carbon alcohol with from about 6 to about 7 moles of ethylene oxide The cleaning composition of the present invention also contains from about 0.1 to about 10 percent by weight, and preferably from about 0.5 percent to about 1.5 percent by weight of u n detergent enzyme component. Suitable enzymes include proteases, amylases, dipases, cellulases, peroxidase, as well as mixtures thereof all of which are employed on a pure enzyme basis. In a preferred embodiment, however, bacterial enzymes such as amylases and proteases and fungal enzymes such as cellulase, are employed in the cleaning composition. In a particularly preferred embodiment, the cleaning composition contains an enzyme component that contains a mixture of a protease, cellulase and lipase. Examples of lipases suitable for use herein include those of animal, plant and microbiological origin. Although only limited studies have been carried out on the distribution of lipase in plants, the appropriate lipase enzymes are present in "cambium", bark and in the roots of the plant. In addition, lipases have been found in fruit seeds, palm oil, lettuce, rice, bran, barley and malt, wheat, oatmeal and oatmeal, tung grains, corn, millet, coconuts, nuts, hemp, cannabis and cucurbit. Suitable lipases are also found in many strains of bacteria and fungi, for example, lipases suitable for use herein may be derived from Pseudomonas, Aspergillus, Pneumococcus, Staphylococcus and Staphylococcus Toxins, Mycobacterium Tuberculosis, Mycotorula Lipolytica and Sclerotinia microorganisms.
The appropriate animal lipases are found in the body fluids and organs of many species. Most mammalian organs contain lipases, but in addition, enzymes are found in various digestive juices as well as in pancreatic juice. Amylases suitable for use in the present cleaning composition include, for example, alpha-amylases obtained from a special strain of B. licheniforms. The amylolytic proteins include, for example, RAPIDASE®, obtainable from International Bio-Synthetics, Inc. and TERMAMYL®, obtainable from Novo Industries. Cellulases that can be employed herein include both bacterial and fungal cellulases. Examples include cellulases produced by a strain of Humicola insolens (Humicola grísea var. - thermoidea), particularly the strain Humicola DSM 1800, and cellulases produced by a fungus of Bacillus N or a cellulase-producing fungus 212 belonging to the genus Aeromonas, and the cellulase extracted from the hepatopancreas of a marine mollusk (Dolabella Auricle Solander). Peroxidase enzymes are used in combination with oxygen sources e.g. percarbonate, perborate, persulfate, hydrogen peroxide, etc. They are typically used for "solution bleaching", that is, to prevent the
transfer of dyes or pigments_ removed from textile substrates during washing operations to other substrates in the washing solution. Peroxidase enzymes are known in the art and include, for example, strong horseradish peroxidase, ligninase and haloperoxidase such as chloro- and bromo-peroxidase. Suitable proteolytic enzymes for use in the cleaning composition of the present invention are of vegetable, animal, bacterial, mold and fungus origin. Examples of proteases that can be employed in the cleansing composition of the present invention are the subtilisins that are obtained from specific strains of B. subtilis and B. lincheni forms. Another appropriate protease is obtained from a Bacillus strain, which has maximum activity through the pH scale of 8 to 12, developed and sold by Novo Industries A / S, under the registered trade name ESPERASE®. Of specific interest in the category of proteolytic enzymes are the alkaline proteases derived from Bacillus lentus, which is referred to herein as BLAP, as disclosed in US Pat. No. 5,352,604, all the contents of which are incorporated herein by reference. the present by reference. The mixture of the surfactant, as discussed above, is used in the composition - -
present in an amount of about 1 percent to about 60 percent by weight, and preferably about 5 percent to about 50 percent by weight, and especially preferably about 15 percent to about 30 percent by weight based on the weight of the cleaning composition. The weight ratio of the alkyl alcohol: ethoxylated linear alcohol: sulfate: nonionic sugar sulfate surfactant is within the range of about 0.5 to 1.0: 1.5 to 2.5: 0.5 to 1.5. In a particularly preferred embodiment, the weight ratio is about 1: 2: 1. The enzyme component employed herein is present in the cleaning composition in an amount of from about 0.1 percent to about 10 percent, and preferably from about 0.5 percent to about 1.5 percent by weight based on the weight of the composition . The enzyme component preferably consists of a mixture of protease, lipase and cellulase. According to one embodiment of the inven there is provided a cleaning composition containing: (a) from about 15 percent to about 30 percent by weight of a surfactant component consisting esselly of (i) a fatty alkyl ether sulfate, (ii) a linear alcohol ethoxylate, and (iii) a -
alkyl polyglycosides, in a weight ratio of (i): (ii): (iii) of about 1: 2: 1; and (b) from about 0.5 percent to about 1.5 weight percent of an enzyme component consisting esselly of a mixture of a protease, a lipase and a cellulase. The cleaning composition of the present inven may also contain auxiliary components which are selected from the group consisting of other anionic surfactants, other nonionic detergent surfactants, cationic surfactants, amphoteric and zwitterionic surfactants, detergent additives, agents bleaches, bleach activators, polymeric soil release agents, chelating agents, aredeposition agents, polymeric dispersing agents, optical brighteners, foam inhibitors, carriers, hydrotropes, processing aids ^ dyes, pigments, solvents for liquid formulations and mixtures thereof. The present inven also provides a process for cleaning textile substrates that involve contacting textile substrates with the cleaning composition disclosed above.
-
The present inven also provides a process for making a cleaning composition having improved cleaning properties that involves: (a) providing from about 1 percent to about 60 percent by weight, preferably from about 5 percent to about 50 percent by weight, and more preferably from about 15 percent to about 30 percent by weight of a surfactant mixture, the mixture contains: (i) an alkyl ether sulfate surfactant, (ii) a surfactant of ethoxylated linear alcohol; Y
(iii) a nonionic sugar surfactant, wherein the weight ratio of (i): (ii): (iii) is about
1: 2: 1; and (b) providing from about 0.5 percent to about 1.5 weight percent of an enzyme component consisting esselly of a mixture of a protease, a lipase and a cellulase; and (c) combine (a) and
(b) to form the composition, all weights being based on the weight of the composition. The present inven will be better understood from the examples which will be given below, all of which are intended to be illustrative only and are not intended to unduly limit the scope of the inven. Unless stated otherwise, the percentages are on a weight-in-weight basis.
EXAMPLES
To test the effect of the different surfactants on the long-term stability of the enzyme in a formulated liquid detergent, an experimental design approach was used. The detergent samples were prepared using a combination of different surfactants that keep the activities of the surfactant constant at 26 percent. In this work, three different types of enzymes were used. The activity of each enzyme in the formulation was determined for a zero time and as a function of time at elevated temperature (40 ° C). The stability of each enzyme was expressed in units of percent based on the initial activity of the enzyme. The formulation and scale for each component is given in Table 1, which is presented below. EMERY® 625 is a coconut fatty acid that is used for foam control. Monoethanolamine was used to neutralize the fatty acid and as a source of alkalinity. Propylene glycol / sodium borate was added to help stabilize the enzymes. Enzymes were added to the propylene glycol / sodium borate mixture before addition to the detergent base. The pH of the formulated detergent is adjusted to 8.5 before the enzymes are added.
-
Table 1. Formulation of Liquid Detergent for Experimental Design Experiments
Ingredients Weight Percent SULFOTEX® NL60-S 0 - 19 percent BIOSOFT® D-40 0 - 19 percent NEODOL® 25-7 0 - 13 percent GLUCOPON® 600 UP 0 - 13 percent EMERY® 625 4.0 percent Monoethanolamine 1.0 percent Sodium Sulfate 0.1 percent Ethanol 4.5 percent Propylene Glycol / Sodium Borate (7/1) 15 percent SAVINASE® 16L 0.75 percent LIPOLASE® 100L 0.75 percent CAREZYME® 0.75 percent
SULFOTEX® NL60-S 0 percent FAES supplied by Henkel Corp. BIOSOFT® D-40 = 40 percent LAS supplied from Stepan. NEODOL® 25-7 100 percent LAE supplied by Shell Chemical.
- -
GLUCOPON® 600 UP 50 percent APG supplied by Henkel Corp. EMERY® 625 a coconut fatty acid supplied by Henkel Corp. SAVINASE® 16L solution quality protease supplied by Novo Nordisk. LIPOLASE® 100L solution quality lipase supplied by Novo Nordisk. CAREZYME® solution quality cellulase supplied by Novo Nordisk.
The stability of the protease after 28 days at 40 ° C is shown in Figure 1. The stability of the enzyme is provided along the z axis, while the base plane xy provides the surfactant composition. For protease, the activity of the enzyme increases with the increased concentration of FAES and decreases with the increased concentration of LAS. Increasing the concentration of GLUCOPON® 600UP in the mixture provides a slight improvement in the stability of the enzyme. The stability of the lipase after 28 days at 40 ° C is shown in Figure 2. For this system the stability of the enzyme increases with the increased concentration of LAE and APG and decreases with the increased concentration of FAES and LAS. It seems that the agents -
Anionic surfactants are effective in denaturing the protein. The stability of the cellulase at 28 days at 40 ° C is shown in Figure 3. For this system, the stability of the enzyme increases with the increased concentration of
FAES, LAE and APG and decreases with the increased concentration of LAS in the formulation. To determine the optimal surfactant composition for multiple enzyme systems, the data from the design experiments was solved simultaneously. The optimal surfactant composition for protease and lipase is shown in Figure 4. The unshaded area represents the ratio of the surfactant mixture, providing good stability for both enzymes. Based on this work, the optimal mix consists of
FAES / LAE / APG = 25 percent / 50 percent / 25 percent. The optimum surfactant composition for .protease and cellulase is provided in Figure 5. Again, the non-shaded region represents regions with good stability for both enzymes. Based on this work, the optimal surfactant mixture ratio consists of
FAES / LAE / APG / LAS = 30 percent / 50 percent / 10 percent / 10 percent. The optimal surfactant composition for lipase and cellulase is provided in Figure 6. The ratio of the -
optimum surfactant mixture consists of
FAES / LAE / APG / LAS = 10 percent / 50 percent / 35 percent / 5 percent. The optimal surfactant composition for protease, lipase and cellulase is provided in Figure 7. The ratio of the optimal mixture consists of FAES / LAE / APG = 25 percent / 50 percent / 25 percent.
Claims (48)
1. A lipid composition comprising: (a) from about 1 percent to about 60 percent by weight of a surfactant component, which consists essentially of: (i) a fatty alkyl ether sulfate; (ii) a linear alcohol ethoxylate; and (iii) a nonionic sugar surfactant having a weight ratio of (i): (ii): (iii) within the range of about 0.5 to 1.0: 1.5 to 2.5: 0.5 to 1.5; and (b) from about 0.1 percent to about 10 percent by weight of an enzyme component that is selected from the group consisting of proteases, amylases, lipases, cellulases, peroxidases and mixtures thereof, all weights being based on the weight of the composition. -
2. The composition of claim 1, wherein the nonionic sugar surfactant is selected from the group consisting of an alkyl polyglycoside corresponding to formula I: R! (R20) b (Z) to (I) wherein R] _ is a monovalent organic radical having from about 6 to about 30 carbon atoms; - R2 is a divalent alkylene radical having from 2 to 4 carbon atoms; Z is a saccharide residue having 5 or 6 carbon atoms; b is a number having a value from 0 to about 12; a is a number having a value of 1 to about 6, a polyhydroxy fatty acid amide and mixtures thereof.
The composition of claim 2, wherein the nonionic sugar surfactant is an alkyl polyglycoside of the formula I, wherein R] _ is a monovalent organic radical having from about 8 to about 16 carbon atoms, b is zero is already a number having a value from 1 to about 3.
The composition of claim 1, wherein the surfactant component is present in the composition in an amount from about 15 percent to about 30 percent by weight. weight, based on the weight of the composition.
The composition of claim 1, wherein the weight ratio of (i): (ii): (iii) is about 1: 2: 1.
The composition of claim 1, wherein the enzyme component consists essentially of a protease, a lipase and a cellulase.
The composition of claim 1, wherein the enzyme component is present in the composition in an amount of about 0.5 percent to about 1.5 percent by weight, based on the weight of the composition.
The composition of claim 1, wherein the composition further comprises an auxiliary component that is selected from the group consisting of other anionic surfactants, other nonionic surfactants, cationic surfactants, amphoteric and zwitterionic surfactants, detergent additives. , bleaching agents, whitening activators, polymeric soil release agents, chelating agents, anti-redeposition agents, polymeric dispersing agents, optical brighteners, foam inhibitors, carriers, hydrotropes, processing aids, dyes, pigments, solvents for liquid formulations and mixtures thereof.
The composition of claim 1, wherein (i) is present in the surfactant mixture in an amount of about 25 weight percent, (ii) is present in the surfactant mixture in an amount of about 50 percent by weight, and (iii) is present in a mixture of the surfactant in an amount of about 25 - per cent by weight, all weights being based on the total weight of the surfactant mixture.
The composition of claim 1, wherein the protease is BLAP.
The composition of claim 1, wherein the diallyl ether ether sulfate is ether sulfate of coconut medium distillation fraction having approximately two moles of ethylene oxide.
12. The composition of claim 1, wherein the linear alcohol ethoxylate is ether sulfate of coconut medium distillation fraction having about 7 moles of ethylene oxide.
13. A process for cleaning a textile substrate comprising contacting the textile substrate, the cleaning composition comprising: (a) from about 1-percent to about 60 percent by weight of a surfactant component, consisting essentially of: (i) a fatty alkyl ether sulfate; (ii) a linear alcohol ethoxylate; and (iii) a nonionic sugar surfactant having a weight ratio of (i): (ii): (iii) within the range of about 0.5 to 1.0: 1.5 to 2.5: 0.5 to 1.5; Y - - (b) from about 0.1 percent to about 10 weight percent of an enzyme component that is selected from the group consisting of proteases, amylases, lipases, cellulases, peroxidases and mixtures thereof, all weights being based on the weight of the composition.
The process of claim 13, wherein the nonionic sugar surfactant is selected from the group consisting of an alkyl polyglycoside corresponding to formula I: R! (R20) b (Z) a (I) wherein R] _ is a monovalent organic radical having from about 6 to about 30 carbon atoms; R2 is a divalent alkylene radical having from 2 to 4 carbon atoms; Z is a saccharide residue having 5 or 6 carbon atoms; b is a number having a value from 0 to about 12; a is a number having a value of 1 to about 6, a polyhydroxy fatty acid amide and mixtures thereof. -
15. The process of claim 14, wherein the nonionic sugar surfactant is an alkyl polyglycoside of the formula I, wherein R] _ is a monovalent organic radical having from about 8 to about 16 carbon atoms. , b is zero is already a number that has a value of 1 to about 3.
16. The process of claim 13, wherein the surfactant component is present in the composition in an amount of about 15 percent to about 30 percent. percent in weight, based on the weight of the composition. ,
17. The process of claim 13, wherein the weight ratio of (i): (ii): (iii) is about 1: 2: 1.
18. The process of claim 13, wherein the enzyme component consists essentially of a protease, a lipase and a cellulase.
The process of claim 13, wherein the enzyme component is present in the composition in an amount of about 0.5 percent to about 1.5 percent by weight, based on the weight of the composition.
The process of claim 13, wherein the composition further comprises an auxiliary component that is selected from the group consisting of other anionic surfactants, other nonionic surfactants, cationic surfactants, amphoteric and zwitterionic surfactants, detergent additives , bleaching agents, bleach activators, polymeric soil release agents, chelating agents, anti-redeposition agents, polymeric dispersing agents, optical brighteners, foam inhibitors, carriers, hydrotropes, processing aids, dyes, pigments, solvents for formulations liquid and mixtures thereof.
The process of claim 13, wherein (i) is present in the surfactant mixture in an amount of about 25 weight percent, (ii) is present in the surfactant mixture in an amount of about 50. percent by weight, and (iii) is present in the surfactant mixture in an amount of about 25 weight percent, all weights being based on the total weight of the surfactant mixture.
22. The process of claim 13, wherein the protease is BLAP.
23. The process of claim 13, wherein the fatty alkyl ether sulfate is ether sulfate of coconut medium distillation fraction having about two moles of ethylene oxide.
The process of claim 13, wherein the linear alcohol ethoxylate is an ether sulfate of - medium distillation fraction of coconut having approximately 7 moles of ethylene oxide.
25. A process for making a cleaning composition having improved enzyme stability comprising: (a) providing from about 1 percent to about 60 percent by weight of a surfactant component, consisting essentially of: (i) a sulfate of fatty alkyl ether; (ii) a linear alcohoi ethoxylate; and (iii) a nonionic sugar surfactant having a weight ratio of (i): (ii): (iii) within the range of about 0.5 to 1.0: 1.5 to 2.5: 0.5 to 1.5; (b) providing from about 0.1 percent to about 10 percent by weight of an enzyme component that is selected from the group consisting of proteases, amylases, lipases, cellulases, peroxidases and mixtures thereof, all weights being based on in the weight of the composition; and (c) mixing (a) and (b) to form the composition.
26. The process of claim 25, wherein the nonionic sugar surfactant is selected from the group consisting of an alkyl polyglycoside corresponding to formula I: R! (R20) b (Z) a (I) wherein R _ is a monovalent organic radical having from about 6 to about 30 carbon atoms; R2 is a divalent alkylene radical having from 2 to 4 carbon atoms; Z is a saccharide residue having 5 or 6 carbon atoms; b is a number having a value from 0 to about 12; a is a number having a value of 1 to about 6, a polyhydroxy fatty acid amide and mixtures thereof.
The process of claim 26, wherein the nonionic sugar surfactant is an alkyl polyglycoside of the formula I, wherein R] _ is a monovalent organic radical having from about 8 to about 16 carbon atoms, b is zero is already a number having a value from 1 to about 3.
The process of claim 25, wherein the surfactant component is present in the composition in an amount of from about 15 percent to about 30 percent in weight, based on the weight of the composition. - -
29. The process of claim 25, wherein the weight ratio of (i): (ii): (iii) is about 1: 2: 1.
30. The process of claim 25, wherein the enzyme component consists essentially of a protease, a lipase and a cellulase.
The process of claim 25, wherein the enzyme component is present in the composition in an amount of from about 0.5 percent to about 1.5 percent by weight, based on the weight of the composition.
32. The process of claim 25, wherein the composition further comprises an auxiliary component that is selected from the group consisting of other anionic surfactants, other nonionic surfactants, other cationic surfactants, other amphoteric and zwitterionic surfactants, additives detergents, bleaching agents, whitening activators, polymeric soil release agents, chelating agents, anti-redeposition agents, polymeric dispersing agents, optical brighteners, foam inhibitors, carriers, hydrotropes, processing aids, dyes, pigments , solvents for liquid formulations and mixtures thereof. -
33. The process of claim 25, wherein (i) is present in the surfactant mixture in an amount of about 25 weight percent, (ii) is present in the surfactant mixture in an amount of about 50 percent in weight, and (iii) is present in the surfactant mixture in an amount of about 25 weight percent, all weights being based on the total weight of the surfactant mixture.
34. The process of claim 25, wherein the protease is BLAP.
35. The process of claim 25, wherein the fatty alkyl ether sulfate is an ether sulfate of coconut medium distillation fraction having approximately two moles of ethylene oxide.
36. The process of claim 25, wherein the linear alcohol ethoxylate is an ether sulfate of the average coconut distillation fraction having about 7 moles of ethylene oxide. - -
37. The product of the claim process
25.
38. The product of the claim process
26.
39. The product of the process of claim 27
40. The product of the claim process 28
41. The product of the claim process
29.
42. The product of the claim process 30
43. The product of the claim process 31
44. The product of the process of claim 32
45. The product of the claim process
33.
46. The product of the claim process 34,
47. The product of the claim process
35.
48. The product of the claim process _
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US08833878 | 1997-04-10 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| MXPA99009216A true MXPA99009216A (en) | 2001-05-17 |
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