CN116731797A - Complex enzyme preparation and application thereof in oil stain cleaning - Google Patents
Complex enzyme preparation and application thereof in oil stain cleaning Download PDFInfo
- Publication number
- CN116731797A CN116731797A CN202310564449.XA CN202310564449A CN116731797A CN 116731797 A CN116731797 A CN 116731797A CN 202310564449 A CN202310564449 A CN 202310564449A CN 116731797 A CN116731797 A CN 116731797A
- Authority
- CN
- China
- Prior art keywords
- enzyme preparation
- activity
- compound enzyme
- enzyme
- lysozyme
- 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.)
- Pending
Links
- 102000004190 Enzymes Human genes 0.000 title claims abstract description 90
- 108090000790 Enzymes Proteins 0.000 title claims abstract description 90
- 238000002360 preparation method Methods 0.000 title claims abstract description 40
- 238000004140 cleaning Methods 0.000 title claims abstract description 10
- 229940088598 enzyme Drugs 0.000 claims abstract description 89
- 150000001875 compounds Chemical class 0.000 claims abstract description 34
- 102000016943 Muramidase Human genes 0.000 claims abstract description 15
- 108010014251 Muramidase Proteins 0.000 claims abstract description 15
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 claims abstract description 15
- 239000004325 lysozyme Substances 0.000 claims abstract description 15
- 229960000274 lysozyme Drugs 0.000 claims abstract description 15
- 235000010335 lysozyme Nutrition 0.000 claims abstract description 15
- 108010059892 Cellulase Proteins 0.000 claims abstract description 14
- 108091005804 Peptidases Proteins 0.000 claims abstract description 14
- 102000004139 alpha-Amylases Human genes 0.000 claims abstract description 14
- 108090000637 alpha-Amylases Proteins 0.000 claims abstract description 14
- 229940024171 alpha-amylase Drugs 0.000 claims abstract description 14
- 229940106157 cellulase Drugs 0.000 claims abstract description 14
- 239000003995 emulsifying agent Substances 0.000 claims abstract description 14
- 230000007935 neutral effect Effects 0.000 claims abstract description 14
- 239000003381 stabilizer Substances 0.000 claims abstract description 14
- 239000004365 Protease Substances 0.000 claims abstract description 13
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 claims abstract description 13
- 102000004882 Lipase Human genes 0.000 claims abstract description 12
- 108090001060 Lipase Proteins 0.000 claims abstract description 12
- 239000004367 Lipase Substances 0.000 claims abstract description 11
- 235000019421 lipase Nutrition 0.000 claims abstract description 11
- 239000000022 bacteriostatic agent Substances 0.000 claims abstract description 6
- 230000000694 effects Effects 0.000 claims description 49
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 12
- LZZYPRNAOMGNLH-UHFFFAOYSA-M Cetrimonium bromide Chemical group [Br-].CCCCCCCCCCCCCCCC[N+](C)(C)C LZZYPRNAOMGNLH-UHFFFAOYSA-M 0.000 claims description 10
- CHHHXKFHOYLYRE-UHFFFAOYSA-M 2,4-Hexadienoic acid, potassium salt (1:1), (2E,4E)- Chemical compound [K+].CC=CC=CC([O-])=O CHHHXKFHOYLYRE-UHFFFAOYSA-M 0.000 claims description 8
- 239000004302 potassium sorbate Substances 0.000 claims description 8
- 235000010241 potassium sorbate Nutrition 0.000 claims description 8
- 229940069338 potassium sorbate Drugs 0.000 claims description 8
- 229920001214 Polysorbate 60 Polymers 0.000 claims description 7
- 239000001818 polyoxyethylene sorbitan monostearate Substances 0.000 claims description 7
- 235000010989 polyoxyethylene sorbitan monostearate Nutrition 0.000 claims description 7
- 229940113124 polysorbate 60 Drugs 0.000 claims description 7
- 239000000843 powder Substances 0.000 claims description 7
- RTZKZFJDLAIYFH-UHFFFAOYSA-N Diethyl ether Chemical compound CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 claims description 4
- 229910052708 sodium Inorganic materials 0.000 claims description 4
- 239000011734 sodium Substances 0.000 claims description 4
- WXMKPNITSTVMEF-UHFFFAOYSA-M sodium benzoate Chemical compound [Na+].[O-]C(=O)C1=CC=CC=C1 WXMKPNITSTVMEF-UHFFFAOYSA-M 0.000 claims description 3
- 235000010234 sodium benzoate Nutrition 0.000 claims description 3
- 239000004299 sodium benzoate Substances 0.000 claims description 3
- QAOWNCQODCNURD-UHFFFAOYSA-L Sulfate Chemical compound [O-]S([O-])(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-L 0.000 claims description 2
- SZYSLWCAWVWFLT-UTGHZIEOSA-N [(2s,3s,4s,5r)-3,4-dihydroxy-5-(hydroxymethyl)-2-[(2r,3r,4s,5s,6r)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxyoxolan-2-yl]methyl octadecanoate Chemical compound O([C@@H]1[C@@H]([C@@H](O)[C@H](O)[C@@H](CO)O1)O)[C@]1(COC(=O)CCCCCCCCCCCCCCCCC)O[C@H](CO)[C@@H](O)[C@@H]1O SZYSLWCAWVWFLT-UTGHZIEOSA-N 0.000 claims description 2
- 238000010790 dilution Methods 0.000 claims description 2
- 239000012895 dilution Substances 0.000 claims description 2
- 239000002552 dosage form Substances 0.000 claims description 2
- 150000002191 fatty alcohols Chemical class 0.000 claims description 2
- 235000019626 lipase activity Nutrition 0.000 claims description 2
- 239000008297 liquid dosage form Substances 0.000 claims description 2
- -1 sodium alkyl sulfate Chemical class 0.000 claims description 2
- 230000009471 action Effects 0.000 abstract description 3
- 230000001804 emulsifying effect Effects 0.000 abstract description 3
- 238000000034 method Methods 0.000 abstract description 3
- 230000008569 process Effects 0.000 abstract description 3
- 230000003197 catalytic effect Effects 0.000 abstract description 2
- 231100000956 nontoxicity Toxicity 0.000 abstract description 2
- 230000000052 comparative effect Effects 0.000 description 16
- 238000005260 corrosion Methods 0.000 description 9
- 239000004033 plastic Substances 0.000 description 8
- 229920003023 plastic Polymers 0.000 description 8
- 238000005238 degreasing Methods 0.000 description 7
- 238000001035 drying Methods 0.000 description 7
- 239000000463 material Substances 0.000 description 7
- 239000000203 mixture Substances 0.000 description 6
- 239000000243 solution Substances 0.000 description 6
- 230000000844 anti-bacterial effect Effects 0.000 description 5
- 230000007797 corrosion Effects 0.000 description 5
- XEEYBQQBJWHFJM-UHFFFAOYSA-N Iron Chemical compound [Fe] XEEYBQQBJWHFJM-UHFFFAOYSA-N 0.000 description 4
- 229920002472 Starch Polymers 0.000 description 4
- MYSWGUAQZAJSOK-UHFFFAOYSA-N ciprofloxacin Chemical compound C12=CC(N3CCNCC3)=C(F)C=C2C(=O)C(C(=O)O)=CN1C1CC1 MYSWGUAQZAJSOK-UHFFFAOYSA-N 0.000 description 4
- 239000003921 oil Substances 0.000 description 4
- 235000019198 oils Nutrition 0.000 description 4
- 238000011056 performance test Methods 0.000 description 4
- 239000008107 starch Substances 0.000 description 4
- 235000019698 starch Nutrition 0.000 description 4
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
- 210000002421 cell wall Anatomy 0.000 description 3
- 238000001514 detection method Methods 0.000 description 3
- 229940079919 digestives enzyme preparation Drugs 0.000 description 3
- 230000002255 enzymatic effect Effects 0.000 description 3
- 239000001963 growth medium Substances 0.000 description 3
- 239000008363 phosphate buffer Substances 0.000 description 3
- 229910000838 Al alloy Inorganic materials 0.000 description 2
- 241000894006 Bacteria Species 0.000 description 2
- 241000607142 Salmonella Species 0.000 description 2
- 238000002835 absorbance Methods 0.000 description 2
- XAGFODPZIPBFFR-UHFFFAOYSA-N aluminium Chemical compound [Al] XAGFODPZIPBFFR-UHFFFAOYSA-N 0.000 description 2
- 229910052782 aluminium Inorganic materials 0.000 description 2
- 230000001580 bacterial effect Effects 0.000 description 2
- 229960003405 ciprofloxacin Drugs 0.000 description 2
- 239000012459 cleaning agent Substances 0.000 description 2
- 239000011248 coating agent Substances 0.000 description 2
- 238000000576 coating method Methods 0.000 description 2
- 238000010411 cooking Methods 0.000 description 2
- 238000012258 culturing Methods 0.000 description 2
- 235000014113 dietary fatty acids Nutrition 0.000 description 2
- 239000000194 fatty acid Substances 0.000 description 2
- 229930195729 fatty acid Natural products 0.000 description 2
- 150000004665 fatty acids Chemical class 0.000 description 2
- 235000013305 food Nutrition 0.000 description 2
- 150000004676 glycans Chemical class 0.000 description 2
- 239000004519 grease Substances 0.000 description 2
- 229910052742 iron Inorganic materials 0.000 description 2
- 150000002632 lipids Chemical class 0.000 description 2
- 238000002156 mixing Methods 0.000 description 2
- 229920001282 polysaccharide Polymers 0.000 description 2
- 239000005017 polysaccharide Substances 0.000 description 2
- 229920000136 polysorbate Polymers 0.000 description 2
- 229950008882 polysorbate Drugs 0.000 description 2
- 102000004196 processed proteins & peptides Human genes 0.000 description 2
- 108090000765 processed proteins & peptides Proteins 0.000 description 2
- 238000002791 soaking Methods 0.000 description 2
- 239000002904 solvent Substances 0.000 description 2
- 239000008223 sterile water Substances 0.000 description 2
- 239000000126 substance Substances 0.000 description 2
- 230000002195 synergetic effect Effects 0.000 description 2
- 238000005303 weighing Methods 0.000 description 2
- OWEGMIWEEQEYGQ-UHFFFAOYSA-N 100676-05-9 Natural products OC1C(O)C(O)C(CO)OC1OCC1C(O)C(O)C(O)C(OC2C(OC(O)C(O)C2O)CO)O1 OWEGMIWEEQEYGQ-UHFFFAOYSA-N 0.000 description 1
- RYGMFSIKBFXOCR-UHFFFAOYSA-N Copper Chemical compound [Cu] RYGMFSIKBFXOCR-UHFFFAOYSA-N 0.000 description 1
- 239000004375 Dextrin Substances 0.000 description 1
- 229920001353 Dextrin Polymers 0.000 description 1
- 241000588724 Escherichia coli Species 0.000 description 1
- 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 description 1
- 229920002488 Hemicellulose Polymers 0.000 description 1
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 1
- GUBGYTABKSRVRQ-PICCSMPSSA-N Maltose Natural products O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@@H](CO)OC(O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-PICCSMPSSA-N 0.000 description 1
- 241000192041 Micrococcus Species 0.000 description 1
- OVRNDRQMDRJTHS-UHFFFAOYSA-N N-acelyl-D-glucosamine Natural products CC(=O)NC1C(O)OC(CO)C(O)C1O OVRNDRQMDRJTHS-UHFFFAOYSA-N 0.000 description 1
- MNLRQHMNZILYPY-MDMHTWEWSA-N N-acetyl-alpha-D-muramic acid Chemical compound OC(=O)[C@@H](C)O[C@H]1[C@H](O)[C@@H](CO)O[C@H](O)[C@@H]1NC(C)=O MNLRQHMNZILYPY-MDMHTWEWSA-N 0.000 description 1
- OVRNDRQMDRJTHS-FMDGEEDCSA-N N-acetyl-beta-D-glucosamine Chemical compound CC(=O)N[C@H]1[C@H](O)O[C@H](CO)[C@@H](O)[C@@H]1O OVRNDRQMDRJTHS-FMDGEEDCSA-N 0.000 description 1
- MBLBDJOUHNCFQT-LXGUWJNJSA-N N-acetylglucosamine Natural products CC(=O)N[C@@H](C=O)[C@@H](O)[C@H](O)[C@H](O)CO MBLBDJOUHNCFQT-LXGUWJNJSA-N 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 1
- 229910000831 Steel Inorganic materials 0.000 description 1
- DPXJVFZANSGRMM-UHFFFAOYSA-N acetic acid;2,3,4,5,6-pentahydroxyhexanal;sodium Chemical compound [Na].CC(O)=O.OCC(O)C(O)C(O)C(O)C=O DPXJVFZANSGRMM-UHFFFAOYSA-N 0.000 description 1
- 239000003513 alkali Substances 0.000 description 1
- 239000000956 alloy Substances 0.000 description 1
- 150000001413 amino acids Chemical class 0.000 description 1
- 239000003242 anti bacterial agent Substances 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- 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 1
- GUBGYTABKSRVRQ-QUYVBRFLSA-N beta-maltose Chemical compound OC[C@H]1O[C@H](O[C@H]2[C@H](O)[C@@H](O)[C@H](O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@@H]1O GUBGYTABKSRVRQ-QUYVBRFLSA-N 0.000 description 1
- 239000001768 carboxy methyl cellulose Substances 0.000 description 1
- 239000005018 casein Substances 0.000 description 1
- BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical compound NCCCCC(C(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(CC(C)C)N=C(O)C(CCC(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(C(C)O)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(COP(O)(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(N)CC1=CC=CC=C1 BECPQYXYKAMYBN-UHFFFAOYSA-N 0.000 description 1
- 235000021240 caseins Nutrition 0.000 description 1
- 239000003093 cationic surfactant Substances 0.000 description 1
- 210000004027 cell Anatomy 0.000 description 1
- 239000001913 cellulose Substances 0.000 description 1
- 229920002678 cellulose Polymers 0.000 description 1
- 239000000919 ceramic Substances 0.000 description 1
- 239000002131 composite material Substances 0.000 description 1
- 239000010949 copper Substances 0.000 description 1
- 229910052802 copper Inorganic materials 0.000 description 1
- 238000000354 decomposition reaction Methods 0.000 description 1
- 230000000593 degrading effect Effects 0.000 description 1
- 235000019425 dextrin Nutrition 0.000 description 1
- 238000007865 diluting Methods 0.000 description 1
- 238000004090 dissolution Methods 0.000 description 1
- 239000012153 distilled water Substances 0.000 description 1
- 239000000295 fuel oil Substances 0.000 description 1
- 239000008103 glucose Substances 0.000 description 1
- 230000007062 hydrolysis Effects 0.000 description 1
- 238000006460 hydrolysis reaction Methods 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 230000002401 inhibitory effect Effects 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 229950006780 n-acetylglucosamine Drugs 0.000 description 1
- 239000013642 negative control Substances 0.000 description 1
- 229920001542 oligosaccharide Polymers 0.000 description 1
- 150000002482 oligosaccharides Chemical class 0.000 description 1
- 239000008055 phosphate buffer solution Substances 0.000 description 1
- 239000002504 physiological saline solution Substances 0.000 description 1
- 229920001184 polypeptide Polymers 0.000 description 1
- 239000013641 positive control Substances 0.000 description 1
- 230000007065 protein hydrolysis Effects 0.000 description 1
- 235000018102 proteins Nutrition 0.000 description 1
- 102000004169 proteins and genes Human genes 0.000 description 1
- 108090000623 proteins and genes Proteins 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 235000019812 sodium carboxymethyl cellulose Nutrition 0.000 description 1
- 229920001027 sodium carboxymethylcellulose Polymers 0.000 description 1
- 239000010959 steel Substances 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 239000004094 surface-active agent Substances 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 230000001988 toxicity Effects 0.000 description 1
- 231100000419 toxicity Toxicity 0.000 description 1
- UFTFJSFQGQCHQW-UHFFFAOYSA-N triformin Chemical compound O=COCC(OC=O)COC=O UFTFJSFQGQCHQW-UHFFFAOYSA-N 0.000 description 1
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 1
- 235000015112 vegetable and seed oil Nutrition 0.000 description 1
- 239000008158 vegetable oil Substances 0.000 description 1
- 238000005406 washing Methods 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
- C11D3/38627—Preparations containing enzymes, e.g. protease or amylase containing lipase
-
- 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
- C11D1/00—Detergent compositions based essentially on surface-active compounds; Use of these compounds as a detergent
- C11D1/66—Non-ionic compounds
- C11D1/835—Mixtures of non-ionic with cationic compounds
-
- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
- C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
- C11D3/16—Organic compounds
- C11D3/20—Organic compounds containing oxygen
- C11D3/2075—Carboxylic acids-salts thereof
- C11D3/2079—Monocarboxylic acids-salts thereof
-
- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
- C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
- C11D3/16—Organic compounds
- C11D3/26—Organic compounds containing nitrogen
- C11D3/30—Amines; Substituted amines ; Quaternized amines
-
- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
- C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
- C11D3/16—Organic compounds
- C11D3/38—Products with no well-defined composition, e.g. natural products
- C11D3/386—Preparations containing enzymes, e.g. protease or amylase
-
- C—CHEMISTRY; METALLURGY
- 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
- C11D3/38636—Preparations containing enzymes, e.g. protease or amylase containing enzymes other than protease, amylase, lipase, cellulase, 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
- C11D3/16—Organic compounds
- C11D3/38—Products with no well-defined composition, e.g. natural products
- C11D3/386—Preparations containing enzymes, e.g. protease or amylase
- C11D3/38645—Preparations containing enzymes, e.g. protease or amylase containing cellulase
-
- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
- C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
- C11D3/48—Medical, disinfecting agents, disinfecting, antibacterial, germicidal or antimicrobial compositions
-
- 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
- C11D1/00—Detergent compositions based essentially on surface-active compounds; Use of these compounds as a detergent
- C11D1/38—Cationic compounds
- C11D1/62—Quaternary ammonium compounds
-
- 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
- C11D1/00—Detergent compositions based essentially on surface-active compounds; Use of these compounds as a detergent
- C11D1/66—Non-ionic compounds
- C11D1/74—Carboxylates or sulfonates esters of polyoxyalkylene glycols
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
- Y02A—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE
- Y02A20/00—Water conservation; Efficient water supply; Efficient water use
- Y02A20/20—Controlling water pollution; Waste water treatment
- Y02A20/204—Keeping clear the surface of open water from oil spills
Landscapes
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Engineering & Computer Science (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Oil, Petroleum & Natural Gas (AREA)
- Wood Science & Technology (AREA)
- Organic Chemistry (AREA)
- Health & Medical Sciences (AREA)
- Emergency Medicine (AREA)
- Enzymes And Modification Thereof (AREA)
Abstract
The invention provides a compound enzyme preparation, which comprises the following components in parts by weight: 28-65.5% of lipase, 10-20% of protease, 10-15% of neutral cellulase, 5-15% of alpha-amylase, 5-15% of lysozyme, 1.0-2.0% of bacteriostatic agent, 2.0-5.0% of emulsifying agent and 0.5-1% of stabilizing agent. The compound enzyme preparation has the characteristics of high catalytic efficiency, high specificity, mild action condition, strong emulsifying capacity, no toxicity, no harm and the like, has excellent comprehensive performance in the oil stain cleaning process, and has better performance on bacteriostasis, corrosiveness and detergency.
Description
Technical Field
The invention belongs to the field of biological enzyme preparations, and particularly relates to a compound enzyme preparation and application thereof in oil stain cleaning.
Background
A large amount of greasy dirt can be generated in the food cooking process, the greasy dirt is easy to rancidity after being oxidized at high temperature and is attached to kitchen tiles, gas stoves, range hoods, electromagnetic ovens, microwave ovens, air fryers and the like, so that the food cooking process is difficult to clean, and a large amount of bacteria and peculiar smell are easy to breed. For heavy oil areas such as kitchens, the cleaning agents currently in general use are of the following three types: (1) Strong alkali, although having strong detergency, has strong corrosiveness; (2) Solvent type, which uses solvent with good solubility to achieve the degreasing effect, but has the risk of inflammability and explosiveness and toxicity; (3) The surfactant is a type of cleaning agent which is most widely used and studied at present, has mild effect and lower cost, but has the problems of weak emulsifying capacity and incomplete cleaning.
Disclosure of Invention
In view of the above, the invention provides a compound enzyme preparation and application thereof in oil stain cleaning.
In order to achieve the above purpose, the invention adopts the following technical scheme:
the compound enzyme preparation comprises the following components in parts by weight: 28-65.5% of lipase, 10-20% of protease, 10-15% of neutral cellulase, 5-15% of alpha-amylase, 5-15% of lysozyme, 1.0-2.0% of bacteriostatic agent, 2.0-5.0% of emulsifying agent and 0.5-1% of stabilizing agent.
Preferably, the compound enzyme preparation comprises the following components in parts by weight: 50% of lipase, 16.2% of protease, 10% of neutral cellulase, 10% of alpha-amylase, 10% of lysozyme, 1% of bacteriostat, 2% of emulsifier and 0.8% of stabilizer.
Further, the compound enzyme preparation comprises a liquid dosage form and a powder dosage form.
Further, the pH of the compound enzyme preparation is 6.0-8.0.
Further, the lipase activity is 40000-100000U/g or 40000-100000U/mL, the protease activity is 50000-100000U/g or 50000-100000U/mL, the neutral cellulase activity is 6000-9000U/g or 6000-9000U/mL, the alpha-amylase activity is 5000-15000U/g or 5000-15000U/mL, and the lysozyme activity is 2000-6000U/g or 2000-6000U/mL.
Further, the bacteriostatic agent is cetyl trimethyl ammonium bromide.
Further, the emulsifier comprises polysorbate-60, sucrose stearate, sodium alkyl sulfate, sodium fatty alcohol ether sulfate.
Further, the stabilizer is any one of three parts per thousand by mass of sodium benzoate and two parts per thousand by mass of potassium sorbate.
The application of the compound enzyme preparation in oil stain cleaning.
In the application, the compound enzyme preparation and water are mixed according to the mass ratio of 1: (0-10) dilution.
Compared with the prior art, the invention has the beneficial effects that:
(1) The compound enzyme preparation provided by the invention contains a plurality of enzymes, wherein lipase has affinity of an oil-water interface, can efficiently catalyze and hydrolyze water-insoluble lipid substances on the oil-water interface, and can gradually hydrolyze triglyceride into glycerol and fatty acid; proteases are capable of catalyzing the hydrolysis of proteins and polypeptides into small peptides and amino acids; the neutral cellulase can promote the dissolution of plant cell walls while improving the decomposition of cellulose and hemicellulose so as to dissolve out more plant cell inner solubles and degrade nondigestible macromolecular polysaccharide, protein and lipid into micromolecular substances; alpha-amylase hydrolyzes alpha-1, 4-glucosidic bond in starch molecular chain, cuts the starch chain into short-chain dextrin, oligosaccharide and a small amount of maltose and glucose, and rapidly reduces the viscosity of the starch to achieve the purpose of liquefaction; lysozyme can catalyze the hydrolysis of β -glycosidic bonds between C1 of N-acetylmuramic acid and C4 of N-acetylglucosamine in bacterial cell walls, thereby rapidly dissolving polysaccharide components in the cell walls; the mixing action of the enzymes enables the greasy dirt to be removed easily.
(2) The antibacterial agent cetyl trimethyl ammonium bromide in the compound enzyme preparation provided by the invention belongs to a cationic surfactant, has good surface activity, stability, bactericidal property and biodegradability, and can play a role in synergy with lysozyme, a stabilizer and an emulsifier in the compound enzyme preparation;
(3) The compound enzyme preparation provided by the invention has the characteristics of high catalytic efficiency, high specificity, mild action condition, strong emulsifying capability, no toxicity, no harm and the like.
Detailed Description
The present invention will be described in further detail with reference to specific examples so as to more clearly understand the present invention by those skilled in the art.
Key test material sources and physicochemical parameters:
lipase, protease, neutral cellulase, alpha-amylase, lysozyme were purchased from Wuhan Xinhua Yangrong Co., ltd
The specific enzyme activities in the following examples are defined as follows:
lipase enzyme activity unit (U): 1g of enzyme powder or 1mL of enzyme solution is hydrolyzed at 40 ℃ and pH7.5 for 1min to generate 1 mu mol of titratable fatty acid as one enzyme activity unit U.
Protease enzyme activity unit (U): the amount of enzyme required to hydrolyze casein at 40℃and pH3.0 for 1min to produce 1. Mu.g tyrosine is one enzyme activity unit U for 1g of enzyme powder or 1mL of enzyme solution.
Enzymatic activity unit (U) of neutral cellulase: the amount of enzyme required for degrading 1. Mu. Mol of reducing sugar per minute from a sodium carboxymethyl cellulose solution having a concentration of 15mg/mL at 37℃and pH6.0 was one enzyme activity unit U by 1g of enzyme powder or 1mL of enzyme solution.
Enzymatic activity unit of alpha-amylase (U): the amount of enzyme required for liquefying 1g of soluble starch at 60 ℃ for 1h under the condition of pH6.0 by 1g of enzyme powder or 1mL of enzyme solution is one enzyme activity unit U.
Enzymatic activity unit of lysozyme (U): 1g of enzyme powder or 1mL of enzyme solution was subjected to a reduction of absorbance at 450nm per minute by 0.001 in a phosphate buffer (pH 6.2) at 25℃with Micrococcus lyticus as a substrate, and the amount of enzyme required was one enzyme activity unit U.
Other materials or structures not specifically described in the present invention exist in the prior art and are commercially available.
Example 1
The embodiment provides a compound enzyme preparation, which comprises the following specific components in parts by weight: 50% of lipase with an enzyme activity of 50000U/g, 16.2% of protease with an enzyme activity of 60000U/g, 10% of neutral cellulase with an enzyme activity of 9000U/g, 10% of alpha-amylase with an enzyme activity of 10000U/g, 10% of lysozyme with an enzyme activity of 5000U/g, 1% of cetyltrimethylammonium bromide, 60.2% of polysorbate and 0.8% of potassium sorbate.
Example 2
The embodiment provides a compound enzyme preparation, which comprises the following specific components in parts by weight: lipase 60% with an enzyme activity of 70000U/g, protease 10% with an enzyme activity of 80000U/g, neutral cellulase 15% with an enzyme activity of 8000U/g, alpha-amylase 5% with an enzyme activity of 12000U/g, lysozyme 5% with an enzyme activity of 3000U/g, cetyltrimethylammonium bromide 1%, polysorbate-60% and potassium sorbate 1.0%.
Example 3
The embodiment provides a compound enzyme preparation, which comprises the following specific components in parts by weight: 30.5% of lipase with enzyme activity of 90000U/g, 20% of protease with enzyme activity of 90000U/g, 15% of neutral cellulase with enzyme activity of 6000U/g, 15% of alpha-amylase with enzyme activity of 8000U/g, 12% of lysozyme with enzyme activity of 3000U/g, 2% of cetyl trimethyl ammonium bromide, 60% of polysorbate-5%, 0.2% of potassium sorbate and 0.3% of sodium benzoate.
Example 4
The embodiment provides a compound enzyme preparation, which comprises the following specific components in parts by weight: 50% of lipase with an enzyme activity of 50000U/mL, 16.2% of protease with an enzyme activity of 60000U/mL, 10% of neutral cellulase with an enzyme activity of 9000U/mL, 10% of alpha-amylase with an enzyme activity of 10000U/mL, 10% of lysozyme with an enzyme activity of 5000U/mL, 1% of cetyltrimethylammonium bromide, 60-2% of polysorbate and 0.8% of potassium sorbate.
Comparative example 1
The comparative example provides a compound enzyme preparation, which has the same material composition as that of example 1, except that: cetyl trimethylammonium bromide, polysorbate-60 and potassium sorbate were removed.
Comparative example 2
The comparative example provides a compound enzyme preparation, which has the same material composition as that of example 1, except that: polysorbate-60 and potassium sorbate were removed.
Comparative example 3
The comparative example provides a compound enzyme preparation, which has the same material composition as that of example 1, except that: cetyl trimethylammonium bromide and polysorbate-60 were removed.
Comparative example 4
The comparative example provides a compound enzyme preparation, which has the same material composition as that of example 1, except that: polysorbate-60 was removed.
Comparative example 5
The comparative example provides a compound enzyme preparation, which has the same material composition as that of example 1, except that: cetyl trimethylammonium bromide is removed.
The compound enzyme preparations in examples 1-3 and comparative examples 1-5 were subjected to antibacterial effect test, degreasing performance test and corrosion performance test, and the specific operation steps are as follows:
antibacterial effect test: inoculating Escherichia coli and Salmonella respectively into LB culture medium, culturing in incubator at 37deg.C for 12-16 hr, diluting with LB culture medium to make its absorbance at 600nm be 0.30-0.36, adding diluted bacterial suspension into NA culture medium at 50deg.C+ -1deg.C according to 0.1%, mixing thoroughly, sucking 20mL into sterile culture dish with sterile pipette, and solidifying to obtain detection plate.
1g of each compound enzyme preparation is weighed, 99mL of sterilized phosphate buffer solution is added, and the mixture is extracted for 30min at 170rpm of a shaking table and used as a sample for standby.
Oxford cups are placed on a detection plate in a split area by using tweezers, 300uL of the sample groups are respectively added into different oxford cups, ciprofloxacin is used as a positive control, phosphate buffer is used as a negative control, sterile water and normal saline are used as blank controls, a ceramic tile cover is covered, the detection plate is placed in a constant temperature incubator at 37 ℃ for culturing for 18-24 hours, and the diameter of a bacteriostasis ring is measured by using a vernier caliper, wherein the experimental result is shown in table 1.
TABLE 1 antibacterial test results
| Group of | Coli (mm) | Salmonella (mm) |
| Example 1 | 12.56±0.46 | 17.86±0.95 |
| Example 2 | 13.12±0.24 | 18.38±.0.24 |
| Example 3 | 13.66±0.32 | 18.86±0.36 |
| Example 4 | 12.66±0.42 | 17.76±0.48 |
| Comparative example 1 | 8.61±0.56 | 13.75±0.43 |
| Comparative example 2 | 8.91±0.31 | 13.84±0.21 |
| Comparative example 3 | 10.88±0.25 | 16.96±0.36 |
| Comparative example 4 | 11.56±0.21 | 16.54±0.51 |
| Comparative example 5 | 11.87±0.39 | 16.75±0.82 |
| Ciprofloxacin control (3.0 μg/well) | 20.71 | 18.72 |
| Phosphate buffer | 6.92 | 6.78 |
| Sterile water | 6.94 | 6.76 |
| Physiological saline | 6.56 | 6.64 |
As can be seen from the results in table 1: the simple complex enzyme and the single combination or any two combinations of the complex enzyme, the emulsifier, the bacteriostat and the stabilizer have certain bacteriostasis effect, but the effect is optimal only when the complex enzyme, the emulsifier, the bacteriostat and the stabilizer are contained at the same time, and the components have good synergistic effect, so that the bacteriostasis capability is further enhanced.
Degreasing performance test: uniformly coating vegetable oil from a kitchen on a plastic plate, drying, vertically placing the plastic plate in a large-caliber beaker, respectively adding the compound enzyme preparations, adding a proper amount of water, simultaneously taking clear water as a comparison group, vibrating the plastic plate coated with grease at a uniform speed for 10min in a soaking state, taking out the plastic plate, drying in a drying oven, and measuring the detergency F, wherein the calculation formula is as follows:
s in 0 Is the initial weight (g), S of the plastic plate 1 Is the mass (g) of the plastic plate after washing, S 2 The mass (g) of the plastic plate after the coating with the grease was shown in Table 2.
TABLE 2 degreasing test results
From the results in table 2, it can be seen that: the simple complex enzyme and the single combination or any two combinations of the complex enzyme, the emulsifier, the bacteriostat and the stabilizer have certain degreasing effect, but the degreasing effect is optimal only when the complex enzyme, the emulsifier, the bacteriostat and the stabilizer are contained at the same time, and the degreasing effect can reach more than 90% after 60min along with the extension of time; the components can have good synergistic effect, so that the antibacterial capability is further enhanced.
Corrosion performance test: selecting 6 test pieces of plastics, copper, iron, aluminum and aluminum alloy with the dimensions of 40mm multiplied by 20mm multiplied by 5mm, cleaning each test piece with distilled water, drying, weighing, soaking in a compound enzyme preparation for a certain time, taking clear water as a comparison group, taking out, cleaning, drying to constant weight, and calculating the corrosion rate E of each test piece after weighing, wherein the calculation formula is as follows:
c in the formula 0 C is the mass (g) of the test piece after the 1 st drying 1 The test results are shown in Table 3, which are the mass (g) of the test piece weighed after the 2 nd drying.
TABLE 3 Corrosion test results
As can be seen from the results in table 3: compared with the clean water group, the single complex enzyme and the emulsifier, the bacteriostatic agent and the stabilizing agent are singly combined or any two are combined, but have certain anti-corrosion effect; however, the anti-corrosion effect is optimal only when the composite enzyme, the emulsifier, the bacteriostat and the stabilizer are contained at the same time, wherein compared with the clean water group, the anti-corrosion effect on iron, steel, aluminum and aluminum alloy materials is obvious, and the anti-corrosion effect can be improved by about half.
In conclusion, the compound enzyme preparation provided by the invention has excellent comprehensive performance and good effects on removing greasy dirt, inhibiting bacteria and preventing corrosion.
The foregoing is merely a preferred embodiment of the present invention, and is not intended to limit the scope of the present invention. Any modification, equivalent replacement, improvement, etc. made within the spirit and principle of the present invention should be included in the protection scope of the present invention.
Claims (10)
1. The compound enzyme preparation is characterized by comprising the following components in parts by weight: 28-65.5% of lipase, 10-20% of protease, 10-15% of neutral cellulase, 5-15% of alpha-amylase, 5-15% of lysozyme, 1.0-2.0% of bacteriostatic agent, 2.0-5.0% of emulsifying agent and 0.5-1% of stabilizing agent.
2. The compound enzyme preparation according to claim 1, which is characterized by comprising the following components in parts by weight: 50% of lipase, 16.2% of protease, 10% of neutral cellulase, 10% of alpha-amylase, 10% of lysozyme, 1% of bacteriostat, 2% of emulsifier and 0.8% of stabilizer.
3. The compound enzyme preparation according to claim 1, wherein the compound enzyme preparation comprises a liquid dosage form and a powder dosage form.
4. A complex enzyme preparation according to any one of claims 1-3, characterized in that the pH of the complex enzyme preparation is 6.0-8.0.
5. The complex enzyme preparation according to any one of claims 1 to 4, wherein the lipase activity is 40000-100000U/g or 40000-100000U/mL, the protease activity is 50000-100000U/g or 50000-100000U/mL, the neutral cellulase activity is 6000-9000U/g or 6000-9000U/mL, the alpha-amylase activity is 5000-15000U/g or 5000-15000U/mL, the lysozyme activity is 2000-6000U/g or 2000-6000U/mL.
6. The complex enzyme preparation of any one of claims 1-4, wherein the bacteriostatic agent is cetyltrimethylammonium bromide.
7. The built enzyme preparation according to any one of claims 1-4, wherein the emulsifier comprises polysorbate-60, sucrose stearate, sodium alkyl sulfate, sodium fatty alcohol ether sulfate.
8. The compound enzyme preparation according to any one of claims 1 to 4, wherein the stabilizer is any one of three parts per thousand by mass of sodium benzoate and two parts per thousand by mass of potassium sorbate.
9. Use of the complex enzyme preparation of any one of claims 1-8 in oil stain cleaning.
10. The use according to claim 9, wherein the compound enzyme preparation is used with water in a mass ratio of 1: (0-10) dilution.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN202310564449.XA CN116731797A (en) | 2023-05-18 | 2023-05-18 | Complex enzyme preparation and application thereof in oil stain cleaning |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN202310564449.XA CN116731797A (en) | 2023-05-18 | 2023-05-18 | Complex enzyme preparation and application thereof in oil stain cleaning |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CN116731797A true CN116731797A (en) | 2023-09-12 |
Family
ID=87903543
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN202310564449.XA Pending CN116731797A (en) | 2023-05-18 | 2023-05-18 | Complex enzyme preparation and application thereof in oil stain cleaning |
Country Status (1)
| Country | Link |
|---|---|
| CN (1) | CN116731797A (en) |
Citations (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN106164236A (en) * | 2014-04-11 | 2016-11-23 | 诺维信公司 | Composition of detergent |
| CN108841463A (en) * | 2018-07-17 | 2018-11-20 | 广州立白企业集团有限公司 | detergent composition |
| CN110938501A (en) * | 2019-12-12 | 2020-03-31 | 武汉新华扬生物股份有限公司 | Compound enzyme preparation for cleaning crayfish and use method thereof |
| EP3786272A1 (en) * | 2019-09-02 | 2021-03-03 | BlueSun Consumer Brands, S.L. | Unit dose liquid laundry detergent composition |
| US20240132808A1 (en) * | 2019-10-18 | 2024-04-25 | Basf Se | Storage-Stable Hydrolase Containing Liquids |
-
2023
- 2023-05-18 CN CN202310564449.XA patent/CN116731797A/en active Pending
Patent Citations (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN106164236A (en) * | 2014-04-11 | 2016-11-23 | 诺维信公司 | Composition of detergent |
| CN108841463A (en) * | 2018-07-17 | 2018-11-20 | 广州立白企业集团有限公司 | detergent composition |
| EP3786272A1 (en) * | 2019-09-02 | 2021-03-03 | BlueSun Consumer Brands, S.L. | Unit dose liquid laundry detergent composition |
| US20240132808A1 (en) * | 2019-10-18 | 2024-04-25 | Basf Se | Storage-Stable Hydrolase Containing Liquids |
| CN110938501A (en) * | 2019-12-12 | 2020-03-31 | 武汉新华扬生物股份有限公司 | Compound enzyme preparation for cleaning crayfish and use method thereof |
Non-Patent Citations (1)
| Title |
|---|
| 孙平等: "《食品添加剂 第二版》", 31 May 2020, 中国轻工业出版社 * |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| Silva et al. | Purification and characterization of xylanases from Trichoderma inhamatum | |
| Terrasan et al. | Xylanase and β-xylosidase from Penicillium janczewskii: Purification, characterization and hydrolysis of substrates | |
| Akiba et al. | Purification and characterization of a protease-resistant cellulase from Aspergillus niger | |
| Tamaru et al. | Purification and characterization of an extracellular beta-1, 4-mannanase from a marine bacterium, Vibrio sp. strain MA-138 | |
| Niyonzima et al. | Purification and characterization of detergent-compatible protease from Aspergillus terreus gr. | |
| Terrone et al. | Agroindustrial biomass for xylanase production by Penicillium chrysogenum: Purification, biochemical properties and hydrolysis of hemicelluloses | |
| Metin et al. | Purification and characterization of α-amylase produced by Penicillium citrinum HBF62 | |
| Romanowska et al. | Isolation and properties of Aspergillus niger IBT-90 xylanase for bakery | |
| Egbune et al. | Characterization of a surfactant-stable α-amylase produced by solid-state fermentation of cassava (Manihot esculenta Crantz) tubers using Rhizopus oligosporus: Kinetics, thermal inactivation thermodynamics and potential application in laundry industries | |
| Alves et al. | Production and characterization of a thermostable antifungal chitinase secreted by the filamentous fungus Aspergillus niveus under submerged fermentation | |
| CN103865663A (en) | Medical multi-enzyme cleaning agent and preparation method thereof | |
| Deshpande et al. | Chemical modification of xylanases: evidence for essential tryptophan and cysteine residues at the active site | |
| Sindhu et al. | Purification and characterization of α-amylase from Penicillium janthinellum (NCIM 4960) and its application in detergent industry | |
| Terrone et al. | Salt-tolerant α-arabinofuranosidase from a new specie Aspergillus hortai CRM1919: Production in acid conditions, purification, characterization and application on xylan hydrolysis | |
| Ma et al. | Production, purification and characterization of an exo-polygalacturonase from Penicillium janthinellum sw09 | |
| Uzun et al. | Immobilization and some application of α-amylase purified from Rhizoctonia solani AG-4 strain ZB-34 | |
| Coitinho et al. | Characterization of an exoinulinase produced by Aspergillus terreus CCT 4083 grown on sugar cane bagasse | |
| Kim et al. | Substrate specificity and detailed characterization of a bifunctional amylase‐pullulanase enzyme from Bacillus circulans F‐2 having two different active sites on one polypeptide | |
| Lee et al. | Purification and characterization of a thermostable laminarinase from Penicillium rolfsii c3-2 (1) IBRL | |
| Aktuganov et al. | Purification and characterization of exo-β-1, 4-glucosaminidase produced by chitosan-degrading fungus, Penicillium sp. IB-37-2A | |
| CN116731797A (en) | Complex enzyme preparation and application thereof in oil stain cleaning | |
| Hayashida et al. | Occurrence of an affinity site apart from the active site on the raw-starch-digesting but non-raw-starch-adsorbable Bacillus subtilis 65 α-amylase | |
| Koç et al. | Purification and characterization of a thermostable glucoamylase produced by Aspergillus flavus HBF34 | |
| Fawzi | Highly thermostable purified xylanase from Rhizomucor miehei NRRL 3169 | |
| Jiang et al. | Subunit composition of a large xylanolytic complex (xylanosome) from Streptomyces olivaceoviridis E-86 |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| PB01 | Publication | ||
| PB01 | Publication | ||
| SE01 | Entry into force of request for substantive examination | ||
| SE01 | Entry into force of request for substantive examination |