CN108676782A - 液体酶制剂及其制备方法 - Google Patents
液体酶制剂及其制备方法 Download PDFInfo
- Publication number
- CN108676782A CN108676782A CN201810281980.5A CN201810281980A CN108676782A CN 108676782 A CN108676782 A CN 108676782A CN 201810281980 A CN201810281980 A CN 201810281980A CN 108676782 A CN108676782 A CN 108676782A
- Authority
- CN
- China
- Prior art keywords
- preparation
- transglutaminase
- enzyme
- polyalcohol
- glutaminase
- 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 112
- 108090000790 Enzymes Proteins 0.000 title claims abstract description 112
- 238000002360 preparation method Methods 0.000 title claims abstract description 108
- 239000007788 liquid Substances 0.000 title claims abstract description 59
- 239000000203 mixture Substances 0.000 title claims abstract description 38
- 238000009472 formulation Methods 0.000 title claims abstract description 34
- 108060008539 Transglutaminase Proteins 0.000 claims abstract description 101
- 102000003601 transglutaminase Human genes 0.000 claims abstract description 101
- 238000000034 method Methods 0.000 claims abstract description 39
- 238000004132 cross linking Methods 0.000 claims abstract description 35
- 239000002002 slurry Substances 0.000 claims description 49
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 46
- 239000000725 suspension Substances 0.000 claims description 42
- 239000003755 preservative agent Substances 0.000 claims description 40
- 230000002335 preservative effect Effects 0.000 claims description 40
- 230000004048 modification Effects 0.000 claims description 38
- 238000012986 modification Methods 0.000 claims description 38
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 claims description 37
- 102000009127 Glutaminase Human genes 0.000 claims description 35
- 108010073324 Glutaminase Proteins 0.000 claims description 35
- 102000003425 Tyrosinase Human genes 0.000 claims description 33
- 108060008724 Tyrosinase Proteins 0.000 claims description 33
- 230000002255 enzymatic effect Effects 0.000 claims description 25
- 150000005846 sugar alcohols Polymers 0.000 claims description 20
- 235000011187 glycerol Nutrition 0.000 claims description 18
- 108010029541 Laccase Proteins 0.000 claims description 15
- 230000000694 effects Effects 0.000 claims description 14
- FBPFZTCFMRRESA-JGWLITMVSA-N D-glucitol Chemical compound OC[C@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-JGWLITMVSA-N 0.000 claims description 11
- 239000002253 acid Substances 0.000 claims description 10
- 210000000481 breast Anatomy 0.000 claims description 3
- 230000009144 enzymatic modification Effects 0.000 abstract description 2
- 229940088598 enzyme Drugs 0.000 description 96
- JVTAAEKCZFNVCJ-UHFFFAOYSA-N lactic acid Chemical compound CC(O)C(O)=O JVTAAEKCZFNVCJ-UHFFFAOYSA-N 0.000 description 46
- CMDGQTVYVAKDNA-UHFFFAOYSA-N propane-1,2,3-triol;hydrate Chemical compound O.OCC(O)CO CMDGQTVYVAKDNA-UHFFFAOYSA-N 0.000 description 31
- 239000004310 lactic acid Substances 0.000 description 23
- 235000014655 lactic acid Nutrition 0.000 description 23
- 230000002906 microbiologic effect Effects 0.000 description 20
- 244000005700 microbiome Species 0.000 description 20
- 238000012544 monitoring process Methods 0.000 description 20
- 238000012360 testing method Methods 0.000 description 20
- 238000003860 storage Methods 0.000 description 13
- 239000000047 product Substances 0.000 description 11
- 102000003992 Peroxidases Human genes 0.000 description 8
- 238000012545 processing Methods 0.000 description 8
- WXMKPNITSTVMEF-UHFFFAOYSA-M sodium benzoate Chemical compound [Na+].[O-]C(=O)C1=CC=CC=C1 WXMKPNITSTVMEF-UHFFFAOYSA-M 0.000 description 8
- 235000010234 sodium benzoate Nutrition 0.000 description 8
- 235000013305 food Nutrition 0.000 description 7
- 239000004299 sodium benzoate Substances 0.000 description 7
- QGZKDVFQNNGYKY-UHFFFAOYSA-N Ammonia Chemical compound N QGZKDVFQNNGYKY-UHFFFAOYSA-N 0.000 description 6
- MUBZPKHOEPUJKR-UHFFFAOYSA-N Oxalic acid Chemical compound OC(=O)C(O)=O MUBZPKHOEPUJKR-UHFFFAOYSA-N 0.000 description 6
- KRKNYBCHXYNGOX-UHFFFAOYSA-N citric acid Chemical compound OC(=O)CC(O)(C(O)=O)CC(O)=O KRKNYBCHXYNGOX-UHFFFAOYSA-N 0.000 description 6
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 6
- 108040007629 peroxidase activity proteins Proteins 0.000 description 6
- 108010015776 Glucose oxidase Proteins 0.000 description 5
- 239000004366 Glucose oxidase Substances 0.000 description 5
- 241001495137 Streptomyces mobaraensis Species 0.000 description 5
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 5
- 229940116332 glucose oxidase Drugs 0.000 description 5
- 235000019420 glucose oxidase Nutrition 0.000 description 5
- 238000004519 manufacturing process Methods 0.000 description 5
- 239000001301 oxygen Substances 0.000 description 5
- 229910052760 oxygen Inorganic materials 0.000 description 5
- 108090000623 proteins and genes Proteins 0.000 description 5
- GHOKWGTUZJEAQD-ZETCQYMHSA-N (D)-(+)-Pantothenic acid Chemical compound OCC(C)(C)[C@@H](O)C(=O)NCCC(O)=O GHOKWGTUZJEAQD-ZETCQYMHSA-N 0.000 description 4
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 4
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 4
- 230000001580 bacterial effect Effects 0.000 description 4
- 230000003197 catalytic effect Effects 0.000 description 4
- 230000008859 change Effects 0.000 description 4
- 239000003795 chemical substances by application Substances 0.000 description 4
- 235000013365 dairy product Nutrition 0.000 description 4
- XBDQKXXYIPTUBI-UHFFFAOYSA-N dimethylselenoniopropionate Natural products CCC(O)=O XBDQKXXYIPTUBI-UHFFFAOYSA-N 0.000 description 4
- RWSXRVCMGQZWBV-WDSKDSINSA-N glutathione Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(=O)NCC(O)=O RWSXRVCMGQZWBV-WDSKDSINSA-N 0.000 description 4
- 239000000843 powder Substances 0.000 description 4
- 235000018102 proteins Nutrition 0.000 description 4
- 102000004169 proteins and genes Human genes 0.000 description 4
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 3
- 241000251468 Actinopterygii Species 0.000 description 3
- PHOQVHQSTUBQQK-SQOUGZDYSA-N D-glucono-1,5-lactone Chemical compound OC[C@H]1OC(=O)[C@H](O)[C@@H](O)[C@@H]1O PHOQVHQSTUBQQK-SQOUGZDYSA-N 0.000 description 3
- 241000233866 Fungi Species 0.000 description 3
- 241000490025 Schefflera digitata Species 0.000 description 3
- 108030003984 Thiol oxidases Proteins 0.000 description 3
- 229910021529 ammonia Inorganic materials 0.000 description 3
- 230000015572 biosynthetic process Effects 0.000 description 3
- 235000008429 bread Nutrition 0.000 description 3
- 235000013399 edible fruits Nutrition 0.000 description 3
- 235000012209 glucono delta-lactone Nutrition 0.000 description 3
- 239000000182 glucono-delta-lactone Substances 0.000 description 3
- 229960003681 gluconolactone Drugs 0.000 description 3
- 235000015250 liver sausages Nutrition 0.000 description 3
- 235000013372 meat Nutrition 0.000 description 3
- 230000003647 oxidation Effects 0.000 description 3
- 238000007254 oxidation reaction Methods 0.000 description 3
- BJEPYKJPYRNKOW-REOHCLBHSA-N (S)-malic acid Chemical compound OC(=O)[C@@H](O)CC(O)=O BJEPYKJPYRNKOW-REOHCLBHSA-N 0.000 description 2
- 108700023418 Amidases Proteins 0.000 description 2
- 241000894006 Bacteria Species 0.000 description 2
- GHOKWGTUZJEAQD-UHFFFAOYSA-N Chick antidermatitis factor Natural products OCC(C)(C)C(O)C(=O)NCCC(O)=O GHOKWGTUZJEAQD-UHFFFAOYSA-N 0.000 description 2
- FBPFZTCFMRRESA-KVTDHHQDSA-N D-Mannitol Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-KVTDHHQDSA-N 0.000 description 2
- 108010024636 Glutathione Proteins 0.000 description 2
- MHAJPDPJQMAIIY-UHFFFAOYSA-N Hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 description 2
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 2
- 229930195725 Mannitol Natural products 0.000 description 2
- 235000010627 Phaseolus vulgaris Nutrition 0.000 description 2
- 244000046052 Phaseolus vulgaris Species 0.000 description 2
- 241000218483 Streptomyces lydicus Species 0.000 description 2
- BJEPYKJPYRNKOW-UHFFFAOYSA-N alpha-hydroxysuccinic acid Natural products OC(=O)C(O)CC(O)=O BJEPYKJPYRNKOW-UHFFFAOYSA-N 0.000 description 2
- 102000005922 amidase Human genes 0.000 description 2
- 235000021028 berry Nutrition 0.000 description 2
- 235000015165 citric acid Nutrition 0.000 description 2
- 239000000428 dust Substances 0.000 description 2
- 229960003180 glutathione Drugs 0.000 description 2
- 235000011868 grain product Nutrition 0.000 description 2
- 239000001630 malic acid Substances 0.000 description 2
- 235000011090 malic acid Nutrition 0.000 description 2
- 239000000594 mannitol Substances 0.000 description 2
- 235000010355 mannitol Nutrition 0.000 description 2
- 235000006408 oxalic acid Nutrition 0.000 description 2
- 230000001590 oxidative effect Effects 0.000 description 2
- 235000019161 pantothenic acid Nutrition 0.000 description 2
- 239000011713 pantothenic acid Substances 0.000 description 2
- 229940055726 pantothenic acid Drugs 0.000 description 2
- 230000008569 process Effects 0.000 description 2
- 235000019260 propionic acid Nutrition 0.000 description 2
- IUVKMZGDUIUOCP-BTNSXGMBSA-N quinbolone Chemical compound O([C@H]1CC[C@H]2[C@H]3[C@@H]([C@]4(C=CC(=O)C=C4CC3)C)CC[C@@]21C)C1=CCCC1 IUVKMZGDUIUOCP-BTNSXGMBSA-N 0.000 description 2
- 150000003839 salts Chemical group 0.000 description 2
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 2
- 235000013311 vegetables Nutrition 0.000 description 2
- 101710128063 Carbohydrate oxidase Proteins 0.000 description 1
- 241000611330 Chryseobacterium Species 0.000 description 1
- 241000249126 Chryseobacterium proteolyticum Species 0.000 description 1
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 1
- 235000010469 Glycine max Nutrition 0.000 description 1
- 244000068988 Glycine max Species 0.000 description 1
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 1
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 1
- 239000004472 Lysine Substances 0.000 description 1
- 108700020962 Peroxidase Proteins 0.000 description 1
- 102100030944 Protein-glutamine gamma-glutamyltransferase K Human genes 0.000 description 1
- 241000222354 Trametes Species 0.000 description 1
- 235000009754 Vitis X bourquina Nutrition 0.000 description 1
- 235000012333 Vitis X labruscana Nutrition 0.000 description 1
- 240000006365 Vitis vinifera Species 0.000 description 1
- 235000014787 Vitis vinifera Nutrition 0.000 description 1
- TVXBFESIOXBWNM-UHFFFAOYSA-N Xylitol Natural products OCCC(O)C(O)C(O)CCO TVXBFESIOXBWNM-UHFFFAOYSA-N 0.000 description 1
- 235000011054 acetic acid Nutrition 0.000 description 1
- 239000007900 aqueous suspension Substances 0.000 description 1
- 150000001491 aromatic compounds Chemical class 0.000 description 1
- 125000003118 aryl group Chemical group 0.000 description 1
- 230000008901 benefit 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
- 150000001720 carbohydrates Chemical class 0.000 description 1
- 235000014633 carbohydrates Nutrition 0.000 description 1
- 238000006555 catalytic reaction Methods 0.000 description 1
- 235000013339 cereals Nutrition 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 235000009508 confectionery Nutrition 0.000 description 1
- 238000005260 corrosion Methods 0.000 description 1
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 1
- 235000018417 cysteine Nutrition 0.000 description 1
- HEBKCHPVOIAQTA-NGQZWQHPSA-N d-xylitol Chemical compound OC[C@H](O)C(O)[C@H](O)CO HEBKCHPVOIAQTA-NGQZWQHPSA-N 0.000 description 1
- 230000007423 decrease Effects 0.000 description 1
- 230000001419 dependent effect Effects 0.000 description 1
- 238000000151 deposition Methods 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 235000012055 fruits and vegetables Nutrition 0.000 description 1
- 238000001879 gelation Methods 0.000 description 1
- 235000021474 generally recognized As safe (food) Nutrition 0.000 description 1
- 235000021473 generally recognized as safe (food ingredients) Nutrition 0.000 description 1
- 108010046301 glucose peroxidase Proteins 0.000 description 1
- 235000013922 glutamic acid Nutrition 0.000 description 1
- 239000004220 glutamic acid Substances 0.000 description 1
- 231100000206 health hazard Toxicity 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- HEBKCHPVOIAQTA-UHFFFAOYSA-N meso ribitol Natural products OCC(O)C(O)C(O)CO HEBKCHPVOIAQTA-UHFFFAOYSA-N 0.000 description 1
- 238000010979 pH adjustment Methods 0.000 description 1
- 150000002989 phenols Chemical class 0.000 description 1
- 230000017854 proteolysis Effects 0.000 description 1
- 230000008439 repair process Effects 0.000 description 1
- 230000000630 rising effect Effects 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 230000002195 synergetic effect Effects 0.000 description 1
- 239000000811 xylitol Substances 0.000 description 1
- 235000010447 xylitol Nutrition 0.000 description 1
- HEBKCHPVOIAQTA-SCDXWVJYSA-N xylitol Chemical compound OC[C@H](O)[C@@H](O)[C@H](O)CO HEBKCHPVOIAQTA-SCDXWVJYSA-N 0.000 description 1
- 229960002675 xylitol Drugs 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/10—Transferases (2.)
- C12N9/1025—Acyltransferases (2.3)
- C12N9/104—Aminoacyltransferases (2.3.2)
- C12N9/1044—Protein-glutamine gamma-glutamyltransferase (2.3.2.13), i.e. transglutaminase or factor XIII
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/96—Stabilising an enzyme by forming an adduct or a composition; Forming enzyme conjugates
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES, NOT OTHERWISE PROVIDED FOR; PREPARATION OR TREATMENT THEREOF
- A23L29/00—Foods or foodstuffs containing additives; Preparation or treatment thereof
- A23L29/06—Enzymes
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/0004—Oxidoreductases (1.)
- C12N9/0055—Oxidoreductases (1.) acting on diphenols and related substances as donors (1.10)
- C12N9/0057—Oxidoreductases (1.) acting on diphenols and related substances as donors (1.10) with oxygen as acceptor (1.10.3)
- C12N9/0059—Catechol oxidase (1.10.3.1), i.e. tyrosinase
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/0004—Oxidoreductases (1.)
- C12N9/0055—Oxidoreductases (1.) acting on diphenols and related substances as donors (1.10)
- C12N9/0057—Oxidoreductases (1.) acting on diphenols and related substances as donors (1.10) with oxygen as acceptor (1.10.3)
- C12N9/0061—Laccase (1.10.3.2)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/78—Hydrolases (3) acting on carbon to nitrogen bonds other than peptide bonds (3.5)
- C12N9/80—Hydrolases (3) acting on carbon to nitrogen bonds other than peptide bonds (3.5) acting on amide bonds in linear amides (3.5.1)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y110/00—Oxidoreductases acting on diphenols and related substances as donors (1.10)
- C12Y110/03—Oxidoreductases acting on diphenols and related substances as donors (1.10) with an oxygen as acceptor (1.10.3)
- C12Y110/03001—Catechol oxidase (1.10.3.1), i.e. tyrosinase
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y110/00—Oxidoreductases acting on diphenols and related substances as donors (1.10)
- C12Y110/03—Oxidoreductases acting on diphenols and related substances as donors (1.10) with an oxygen as acceptor (1.10.3)
- C12Y110/03002—Laccase (1.10.3.2)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y203/00—Acyltransferases (2.3)
- C12Y203/02—Aminoacyltransferases (2.3.2)
- C12Y203/02013—Protein-glutamine gamma-glutamyltransferase (2.3.2.13), i.e. transglutaminase or factor XIII
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y305/00—Hydrolases acting on carbon-nitrogen bonds, other than peptide bonds (3.5)
- C12Y305/01—Hydrolases acting on carbon-nitrogen bonds, other than peptide bonds (3.5) in linear amides (3.5.1)
- C12Y305/01043—Peptidyl-glutaminase (3.5.1.43)
Landscapes
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Engineering & Computer Science (AREA)
- Wood Science & Technology (AREA)
- Genetics & Genomics (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Zoology (AREA)
- General Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Microbiology (AREA)
- Biomedical Technology (AREA)
- Molecular Biology (AREA)
- Biotechnology (AREA)
- Medicinal Chemistry (AREA)
- Nutrition Science (AREA)
- Food Science & Technology (AREA)
- Polymers & Plastics (AREA)
- Enzymes And Modification Thereof (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Food Preservation Except Freezing, Refrigeration, And Drying (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| FI20116074A FI126442B (en) | 2011-11-01 | 2011-11-01 | Liquid enzyme preparation and process for its preparation |
| FI20116074 | 2011-11-01 | ||
| CN201280053784.3A CN104024406A (zh) | 2011-11-01 | 2012-10-31 | 液体酶制剂及其制备方法 |
Related Parent Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN201280053784.3A Division CN104024406A (zh) | 2011-11-01 | 2012-10-31 | 液体酶制剂及其制备方法 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CN108676782A true CN108676782A (zh) | 2018-10-19 |
Family
ID=47215584
Family Applications (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN201810281980.5A Pending CN108676782A (zh) | 2011-11-01 | 2012-10-31 | 液体酶制剂及其制备方法 |
| CN201280053784.3A Pending CN104024406A (zh) | 2011-11-01 | 2012-10-31 | 液体酶制剂及其制备方法 |
Family Applications After (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN201280053784.3A Pending CN104024406A (zh) | 2011-11-01 | 2012-10-31 | 液体酶制剂及其制备方法 |
Country Status (19)
| Country | Link |
|---|---|
| US (1) | US20140287098A1 (enExample) |
| EP (1) | EP2773753B1 (enExample) |
| JP (1) | JP6297979B2 (enExample) |
| KR (1) | KR101998182B1 (enExample) |
| CN (2) | CN108676782A (enExample) |
| AU (1) | AU2012331034B2 (enExample) |
| BR (1) | BR112014010222B1 (enExample) |
| CA (1) | CA2853711C (enExample) |
| CL (1) | CL2014001100A1 (enExample) |
| DK (1) | DK2773753T3 (enExample) |
| ES (1) | ES2697675T3 (enExample) |
| FI (1) | FI126442B (enExample) |
| IL (1) | IL232356B (enExample) |
| IN (1) | IN2014MN00968A (enExample) |
| MX (1) | MX356454B (enExample) |
| PL (1) | PL2773753T3 (enExample) |
| RU (1) | RU2668396C2 (enExample) |
| WO (1) | WO2013064736A1 (enExample) |
| ZA (1) | ZA201403965B (enExample) |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN115605588A (zh) * | 2020-05-13 | 2023-01-13 | 居里公司（Us） | 转谷氨酰胺酶变体及其应用 |
Families Citing this family (20)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN104736135B (zh) * | 2012-10-17 | 2019-07-09 | 味之素株式会社 | 化妆品组合物 |
| CN107245481B (zh) * | 2016-02-16 | 2018-06-01 | 上海青瑞食品科技有限公司 | 一种液体酶制剂及制备方法 |
| SG11201808571XA (en) | 2016-04-01 | 2018-10-30 | Oatly Ab | Enhanced viscosity oat base and fermented oat base product |
| CN105852053A (zh) * | 2016-04-20 | 2016-08-17 | 上海青瑞食品科技有限公司 | 一种液体酶制剂在食品质构改良中的应用 |
| JP6787563B2 (ja) * | 2016-06-30 | 2020-11-18 | 千葉製粉株式会社 | 接着成形食品の製造方法、接着成形食品用の接着成分分散液、および、接着成形食品 |
| CN107897533A (zh) * | 2017-12-10 | 2018-04-13 | 济南诺能生物工程有限公司 | 一种单胃动物液体复合酶的制备方法 |
| EP3770254A4 (en) | 2018-03-23 | 2021-12-29 | Ajinomoto Co., Inc. | Liquid preparation containing transglutaminase |
| US20230114377A1 (en) * | 2020-03-17 | 2023-04-13 | Amano Enzyme Inc. | Protein crosslinking method |
| JP7769616B2 (ja) * | 2020-09-10 | 2025-11-13 | 天野エンザイム株式会社 | 豆腐の製造方法 |
| WO2022054880A1 (ja) * | 2020-09-10 | 2022-03-17 | 天野エンザイム株式会社 | 加工タンパク質の製造方法 |
| JPWO2022118914A1 (enExample) | 2020-12-04 | 2022-06-09 | ||
| JPWO2023058616A1 (enExample) | 2021-10-04 | 2023-04-13 | ||
| WO2023228953A1 (ja) * | 2022-05-23 | 2023-11-30 | 天野エンザイム株式会社 | 液体酵素製剤 |
| CN115380981A (zh) * | 2022-08-09 | 2022-11-25 | 武汉新华扬生物股份有限公司 | 一种用于冷萃咖啡的复配酶制剂及其应用方法 |
| EP4428218A1 (en) * | 2023-03-07 | 2024-09-11 | SkyLab AG | Biodegradable transglutaminase-based detergent composition for regeneration of microdamage and regulation of elasticity of delicate fiber |
| WO2024257876A1 (ja) * | 2023-06-14 | 2024-12-19 | 天野エンザイム株式会社 | 液体酵素製剤 |
| WO2025046140A1 (en) | 2023-09-01 | 2025-03-06 | Novozymes A/S | Stabilized liquid deamidase compositions |
| WO2025056701A1 (en) * | 2023-09-13 | 2025-03-20 | Novozymes A/S | Stabilized deamidase compositions |
| WO2025233391A1 (en) * | 2024-05-09 | 2025-11-13 | Novozymes A/S | Stabilized liquid deamidase compositions |
| EP4650443A1 (en) * | 2024-05-13 | 2025-11-19 | Novozymes A/S | Stabilized liquid deamidase compositions |
Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5340734A (en) * | 1992-11-25 | 1994-08-23 | Biosource Genetics Corporation | Method for making stable, extracellular tyrosinase and synthesis of polyphenolic polymers therefrom |
| CN1684593A (zh) * | 2002-09-26 | 2005-10-19 | 味之素株式会社 | 酶制剂及用其生产食品的方法 |
| EP2251421A1 (en) * | 2008-02-13 | 2010-11-17 | Amano Enzyme Inc. | Stabilized transglutaminase and process for production thereof |
Family Cites Families (11)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPH0665280B2 (ja) | 1987-03-04 | 1994-08-24 | 味の素株式会社 | タンパクゲル化剤及びそれを用いるタンパクのゲル化方法 |
| ATE210386T1 (de) * | 1994-04-18 | 2001-12-15 | Dsm Nv | Stabile wasser-in-oel emulsionen |
| WO1996006931A1 (en) | 1994-08-26 | 1996-03-07 | Novo Nordisk A/S | Microbial transglutaminases, their production and use |
| ATE330004T1 (de) * | 1997-03-12 | 2006-07-15 | Novozymes As | Lagerungsstabile, flüssige zusammensetzung, welche laccase enthalten |
| DE60125805T2 (de) * | 2000-09-28 | 2007-10-11 | Dsm Ip Assets B.V. | Flüssige brotverbesserungsmittel |
| US20030219853A1 (en) * | 2002-03-01 | 2003-11-27 | Szu-Yi Chou | Method of cross-linking a compound |
| JP2005034078A (ja) * | 2003-07-17 | 2005-02-10 | Rengo Co Ltd | タンパク質安定化剤 |
| EP1836897A1 (en) * | 2006-03-22 | 2007-09-26 | Nestec S.A. | A solid product comprising oil-droplets |
| GB2438287A (en) * | 2006-05-19 | 2007-11-21 | Norbrook Lab Ltd | Stable aqueous suspension |
| US20110064847A1 (en) * | 2008-03-14 | 2011-03-17 | Ajinomoto Co., Inc. | Method of denaturing protein with enzymes |
| JP2011523562A (ja) * | 2008-06-09 | 2011-08-18 | ダニスコ・ユーエス・インク | 発酵培養液からの不溶性酵素の回収及び不溶性酵素の製剤 |
-
2011
- 2011-11-01 FI FI20116074A patent/FI126442B/en active IP Right Grant
-
2012
- 2012-10-31 EP EP12788227.2A patent/EP2773753B1/en active Active
- 2012-10-31 WO PCT/FI2012/051048 patent/WO2013064736A1/en not_active Ceased
- 2012-10-31 CN CN201810281980.5A patent/CN108676782A/zh active Pending
- 2012-10-31 AU AU2012331034A patent/AU2012331034B2/en active Active
- 2012-10-31 CN CN201280053784.3A patent/CN104024406A/zh active Pending
- 2012-10-31 JP JP2014539370A patent/JP6297979B2/ja active Active
- 2012-10-31 IN IN968MUN2014 patent/IN2014MN00968A/en unknown
- 2012-10-31 RU RU2014121318A patent/RU2668396C2/ru active
- 2012-10-31 PL PL12788227T patent/PL2773753T3/pl unknown
- 2012-10-31 US US14/353,718 patent/US20140287098A1/en not_active Abandoned
- 2012-10-31 DK DK12788227.2T patent/DK2773753T3/en active
- 2012-10-31 MX MX2014005128A patent/MX356454B/es active IP Right Grant
- 2012-10-31 ES ES12788227T patent/ES2697675T3/es active Active
- 2012-10-31 KR KR1020147014440A patent/KR101998182B1/ko active Active
- 2012-10-31 BR BR112014010222-8A patent/BR112014010222B1/pt active IP Right Grant
- 2012-10-31 CA CA2853711A patent/CA2853711C/en active Active
-
2014
- 2014-04-29 IL IL232356A patent/IL232356B/en active IP Right Grant
- 2014-04-29 CL CL2014001100A patent/CL2014001100A1/es unknown
- 2014-05-29 ZA ZA2014/03965A patent/ZA201403965B/en unknown
Patent Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5340734A (en) * | 1992-11-25 | 1994-08-23 | Biosource Genetics Corporation | Method for making stable, extracellular tyrosinase and synthesis of polyphenolic polymers therefrom |
| CN1684593A (zh) * | 2002-09-26 | 2005-10-19 | 味之素株式会社 | 酶制剂及用其生产食品的方法 |
| EP2251421A1 (en) * | 2008-02-13 | 2010-11-17 | Amano Enzyme Inc. | Stabilized transglutaminase and process for production thereof |
Non-Patent Citations (2)
| Title |
|---|
| SHELBY L. BRADBURY ET AL: "Glycerol as an Enzyme-Stabilizing Agent: Effects on Aldehyde Dehydrogenase", 《PNAS》 * |
| YU-JEN YU ET AL: "Overproduction of soluble recombinant transglutaminase from Streptomyces netropsis in Escherichia coli", 《APPL MICROBIOL BIOTECHNOL》 * |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN115605588A (zh) * | 2020-05-13 | 2023-01-13 | 居里公司（Us） | 转谷氨酰胺酶变体及其应用 |
Also Published As
| Publication number | Publication date |
|---|---|
| KR20140096090A (ko) | 2014-08-04 |
| IL232356A0 (en) | 2014-06-30 |
| RU2668396C2 (ru) | 2018-09-28 |
| CL2014001100A1 (es) | 2014-09-05 |
| RU2014121318A (ru) | 2015-12-10 |
| BR112014010222B1 (pt) | 2022-04-12 |
| AU2012331034A1 (en) | 2014-06-26 |
| PL2773753T3 (pl) | 2019-03-29 |
| JP6297979B2 (ja) | 2018-03-20 |
| MX2014005128A (es) | 2014-07-09 |
| CN104024406A (zh) | 2014-09-03 |
| ZA201403965B (en) | 2015-05-27 |
| CA2853711C (en) | 2019-11-26 |
| FI20116074L (fi) | 2013-05-02 |
| DK2773753T3 (en) | 2018-12-10 |
| US20140287098A1 (en) | 2014-09-25 |
| EP2773753A1 (en) | 2014-09-10 |
| IN2014MN00968A (enExample) | 2015-04-24 |
| MX356454B (es) | 2018-05-30 |
| BR112014010222A2 (pt) | 2017-06-13 |
| ES2697675T3 (es) | 2019-01-25 |
| WO2013064736A1 (en) | 2013-05-10 |
| AU2012331034B2 (en) | 2017-10-19 |
| JP2014532421A (ja) | 2014-12-08 |
| KR101998182B1 (ko) | 2019-10-01 |
| FI126442B (en) | 2016-12-15 |
| IL232356B (en) | 2019-03-31 |
| BR112014010222A8 (pt) | 2017-06-20 |
| CA2853711A1 (en) | 2013-05-10 |
| EP2773753B1 (en) | 2018-10-17 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| CN108676782A (zh) | 液体酶制剂及其制备方法 | |
| Kieliszek et al. | Microbial transglutaminase and its application in the food industry. A review | |
| CN101420861B (zh) | 强化乳清蛋白质的搅拌型发酵乳的制造方法 | |
| Gänzle et al. | Physiology and biochemistry of lactic acid bacteria | |
| KR20190003540A (ko) | 증가된 점도의 귀리 베이스 및 발효된 귀리 베이스 제품 | |
| EP1839490A1 (en) | Method for rapid production and usage of biogenerated flavors | |
| EP2394518B1 (en) | Method for producing noodle, and enzyme preparation for modifying noodle | |
| EP4212626A1 (en) | Method of producing processed protein | |
| CA2617894C (en) | Seed koji for brewing, koji for brewing, brewed foods, and method for producing the same | |
| KR101693315B1 (ko) | 기능성 균주를 이용한 보리 된장의 제조방법 및 상기 방법에 의해 제조된 보리 된장 | |
| US20100323058A1 (en) | Method for producing fish paste product, and enzyme preparation for fish paste products | |
| WO2007024111A1 (en) | A method of producing a solid seasoning using liquid culture of kojic mold from plant protein source, a solid seasoning produced from the same, a general food seasoning, sauce, dressing, soysauce, and processed food | |
| KR101834230B1 (ko) | 저염식 담금 메주 된장의 제조방법 | |
| JP5561579B2 (ja) | 納豆及びその製造方法 | |
| CN116406771B (zh) | 一种发酵鱼干工艺及发酵剂开发技术 | |
| Ahmad | Value Addition and Preservation by Fermentation Technology | |
| Hasan et al. | Enzyme Technology in the Food Industry: Molecular Mechanisms, Applications, and Sustainable Innovations | |
| CN107873894A (zh) | 富硒红茶的加工方法 | |
| JP5181207B2 (ja) | 新規な食品保存料およびその製造方法 | |
| CN120249234A (zh) | 一种耐酒精的可降解生物胺的胺氧化酶lyyobn1制备及其应用 | |
| CN120272451A (zh) | 一种耐酒精的可降解生物胺的胺氧化酶lyyobn2制备及其应用 | |
| JP2013116086A (ja) | 発芽大豆発酵組成物 | |
| CN107712127A (zh) | 富硒红茶的加工方法 |
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 | ||
| WD01 | Invention patent application deemed withdrawn after publication |
Application publication date: 20181019 |
|
| WD01 | Invention patent application deemed withdrawn after publication |