ES2697675T3 - Formulación enzimática líquida y su procedimiento de preparación - Google Patents
Formulación enzimática líquida y su procedimiento de preparación Download PDFInfo
- Publication number
- ES2697675T3 ES2697675T3 ES12788227T ES12788227T ES2697675T3 ES 2697675 T3 ES2697675 T3 ES 2697675T3 ES 12788227 T ES12788227 T ES 12788227T ES 12788227 T ES12788227 T ES 12788227T ES 2697675 T3 ES2697675 T3 ES 2697675T3
- Authority
- ES
- Spain
- Prior art keywords
- transglutaminase
- formulation
- polyol
- enzyme
- activity
- 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.)
- Active
Links
- 239000000203 mixture Substances 0.000 title claims abstract description 57
- 238000009472 formulation Methods 0.000 title claims abstract description 53
- 239000007788 liquid Substances 0.000 title claims abstract description 45
- 230000002255 enzymatic effect Effects 0.000 title claims abstract description 34
- 238000000034 method Methods 0.000 title claims description 32
- 238000002360 preparation method Methods 0.000 title description 81
- 108060008539 Transglutaminase Proteins 0.000 claims abstract description 99
- 102000003601 transglutaminase Human genes 0.000 claims abstract description 99
- 102000004190 Enzymes Human genes 0.000 claims abstract description 89
- 108090000790 Enzymes Proteins 0.000 claims abstract description 89
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 claims abstract description 60
- 239000007900 aqueous suspension Substances 0.000 claims abstract description 47
- 102000014171 Milk Proteins Human genes 0.000 claims abstract description 38
- 108010011756 Milk Proteins Proteins 0.000 claims abstract description 38
- 235000021239 milk protein Nutrition 0.000 claims abstract description 38
- 238000004132 cross linking Methods 0.000 claims abstract description 37
- 102000009127 Glutaminase Human genes 0.000 claims abstract description 31
- 108010073324 Glutaminase Proteins 0.000 claims abstract description 31
- 102000003425 Tyrosinase Human genes 0.000 claims abstract description 30
- 108060008724 Tyrosinase Proteins 0.000 claims abstract description 30
- 229920005862 polyol Polymers 0.000 claims abstract description 18
- 150000003077 polyols Chemical class 0.000 claims abstract description 18
- FBPFZTCFMRRESA-FSIIMWSLSA-N D-Glucitol Natural products OC[C@H](O)[C@H](O)[C@@H](O)[C@H](O)CO FBPFZTCFMRRESA-FSIIMWSLSA-N 0.000 claims abstract description 14
- 239000000600 sorbitol Substances 0.000 claims abstract 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 abstract description 7
- 230000000694 effects Effects 0.000 claims description 64
- 239000000725 suspension Substances 0.000 claims description 32
- 239000003755 preservative agent Substances 0.000 claims description 21
- 230000008569 process Effects 0.000 claims description 19
- 230000002335 preservative effect Effects 0.000 claims description 17
- 239000003607 modifier Substances 0.000 claims description 12
- 235000013305 food Nutrition 0.000 claims description 11
- 108010029541 Laccase Proteins 0.000 claims description 10
- 239000002253 acid Substances 0.000 claims description 8
- 150000007513 acids Chemical class 0.000 claims description 3
- 229940088598 enzyme Drugs 0.000 description 82
- JVTAAEKCZFNVCJ-UHFFFAOYSA-N lactic acid Chemical compound CC(O)C(O)=O JVTAAEKCZFNVCJ-UHFFFAOYSA-N 0.000 description 48
- CMDGQTVYVAKDNA-UHFFFAOYSA-N propane-1,2,3-triol;hydrate Chemical compound O.OCC(O)CO CMDGQTVYVAKDNA-UHFFFAOYSA-N 0.000 description 30
- 239000004310 lactic acid Substances 0.000 description 24
- 235000014655 lactic acid Nutrition 0.000 description 24
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 22
- 230000000813 microbial effect Effects 0.000 description 21
- 230000002906 microbiologic effect Effects 0.000 description 21
- 238000003860 storage Methods 0.000 description 12
- WXMKPNITSTVMEF-UHFFFAOYSA-M sodium benzoate Chemical compound [Na+].[O-]C(=O)C1=CC=CC=C1 WXMKPNITSTVMEF-UHFFFAOYSA-M 0.000 description 8
- 239000004299 sodium benzoate Substances 0.000 description 8
- 235000010234 sodium benzoate Nutrition 0.000 description 8
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-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
- 102000003992 Peroxidases Human genes 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
- 238000004519 manufacturing process Methods 0.000 description 6
- 108090000623 proteins and genes 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
- 230000015572 biosynthetic process Effects 0.000 description 5
- 229940116332 glucose oxidase Drugs 0.000 description 5
- 235000019420 glucose oxidase Nutrition 0.000 description 5
- 239000012669 liquid formulation Substances 0.000 description 5
- 235000018102 proteins Nutrition 0.000 description 5
- 102000004169 proteins and genes Human genes 0.000 description 5
- 108010001535 sulfhydryl oxidase 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
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 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
- 230000003647 oxidation Effects 0.000 description 4
- 238000007254 oxidation reaction Methods 0.000 description 4
- 108040007629 peroxidase activity proteins Proteins 0.000 description 4
- 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
- 235000010469 Glycine max Nutrition 0.000 description 3
- 235000015173 baked goods and baking mixes Nutrition 0.000 description 3
- 235000021028 berry Nutrition 0.000 description 3
- 235000012180 bread and bread product Nutrition 0.000 description 3
- 235000013399 edible fruits Nutrition 0.000 description 3
- 235000013601 eggs 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
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 3
- 235000015250 liver sausages Nutrition 0.000 description 3
- 235000013372 meat Nutrition 0.000 description 3
- 235000015927 pasta Nutrition 0.000 description 3
- 239000000843 powder Substances 0.000 description 3
- 230000009467 reduction Effects 0.000 description 3
- 235000013311 vegetables Nutrition 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
- QGZKDVFQNNGYKY-UHFFFAOYSA-N Ammonia Chemical compound N QGZKDVFQNNGYKY-UHFFFAOYSA-N 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
- 108010024636 Glutathione Proteins 0.000 description 2
- MHAJPDPJQMAIIY-UHFFFAOYSA-N Hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 description 2
- 235000011054 acetic acid Nutrition 0.000 description 2
- 230000009471 action Effects 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
- 150000001491 aromatic compounds Chemical class 0.000 description 2
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 2
- 235000015165 citric acid Nutrition 0.000 description 2
- 230000000052 comparative effect Effects 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
- 235000006408 oxalic acid Nutrition 0.000 description 2
- 239000001301 oxygen Substances 0.000 description 2
- 229910052760 oxygen Inorganic materials 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
- 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 class 0.000 description 2
- 241000894006 Bacteria Species 0.000 description 1
- 241000249126 Chryseobacterium proteolyticum Species 0.000 description 1
- 239000004971 Cross linker Substances 0.000 description 1
- 241000233866 Fungi 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
- 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
- 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
- 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
- 241000490025 Schefflera digitata Species 0.000 description 1
- 241000218483 Streptomyces lydicus Species 0.000 description 1
- 241000222357 Trametes hirsuta Species 0.000 description 1
- 125000000539 amino acid group Chemical group 0.000 description 1
- 229910021529 ammonia Inorganic materials 0.000 description 1
- 150000001720 carbohydrates Chemical class 0.000 description 1
- 235000014633 carbohydrates Nutrition 0.000 description 1
- 235000013339 cereals Nutrition 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 235000018417 cysteine Nutrition 0.000 description 1
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 1
- 230000006240 deamidation Effects 0.000 description 1
- 230000001419 dependent effect Effects 0.000 description 1
- 235000019688 fish Nutrition 0.000 description 1
- 235000015219 food category Nutrition 0.000 description 1
- 238000001879 gelation Methods 0.000 description 1
- 235000021474 generally recognized As safe (food) Nutrition 0.000 description 1
- 235000021472 generally recognized as safe 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
- 239000000383 hazardous chemical Substances 0.000 description 1
- 231100000206 health hazard Toxicity 0.000 description 1
- 239000006194 liquid suspension Substances 0.000 description 1
- 235000013336 milk Nutrition 0.000 description 1
- 239000008267 milk Substances 0.000 description 1
- 210000004080 milk Anatomy 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 230000001590 oxidative effect Effects 0.000 description 1
- 150000002989 phenols Chemical class 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- -1 tyrosine Chemical class 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
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)
- Genetics & Genomics (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- General Engineering & Computer Science (AREA)
- Microbiology (AREA)
- Medicinal Chemistry (AREA)
- Biomedical Technology (AREA)
- Molecular Biology (AREA)
- Biotechnology (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 (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| FI20116074A FI126442B (en) | 2011-11-01 | 2011-11-01 | Liquid enzyme preparation and process for its preparation |
| PCT/FI2012/051048 WO2013064736A1 (en) | 2011-11-01 | 2012-10-31 | A liquid enzyme formulation and a process for its preparation |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| ES2697675T3 true ES2697675T3 (es) | 2019-01-25 |
Family
ID=47215584
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| ES12788227T Active ES2697675T3 (es) | 2011-11-01 | 2012-10-31 | Formulación enzimática líquida y su procedimiento de preparación |
Country Status (19)
| Country | Link |
|---|---|
| US (1) | US20140287098A1 (enExample) |
| EP (1) | EP2773753B1 (enExample) |
| JP (1) | JP6297979B2 (enExample) |
| KR (1) | KR101998182B1 (enExample) |
| CN (2) | CN104024406A (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) |
Families Citing this family (21)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP6341091B2 (ja) | 2012-10-17 | 2018-06-13 | 味の素株式会社 | 化粧料組成物 |
| CN107177567B (zh) * | 2016-02-16 | 2018-07-03 | 上海青瑞食品科技有限公司 | 一种液体酶制剂及制备方法 |
| KR102512028B1 (ko) | 2016-04-01 | 2023-03-20 | 오틀리 아베 | 증가된 점도의 귀리 베이스 및 발효된 귀리 베이스 제품 |
| 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 |
| JP7501357B2 (ja) | 2018-03-23 | 2024-06-18 | 味の素株式会社 | トランスグルタミナーゼを含有する液体製剤 |
| CN122278976A (zh) * | 2020-03-17 | 2026-06-26 | 天野酶制品株式会社 | 蛋白质的交联方法 |
| EP4150062A4 (en) * | 2020-05-13 | 2024-08-14 | Curie Co. Inc. | TRANSGLUTAMINASE VARIANTS AND METHODS OF USE THEREOF |
| CN116057184A (zh) * | 2020-09-10 | 2023-05-02 | 天野酶制品株式会社 | 加工蛋白质的制造方法 |
| US20230329292A1 (en) * | 2020-09-10 | 2023-10-19 | Amano Enzyme Inc. | Tofu production method |
| JP7829496B2 (ja) * | 2020-12-04 | 2026-03-13 | 天野エンザイム株式会社 | 液体酵素製剤 |
| EP4414450A4 (en) * | 2021-10-04 | 2025-07-02 | Amano Enzyme Inc | LIQUID TRANSGLUTAMINASE ENZYME PREPARATION |
| 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 |
| AU2024303157A1 (en) | 2023-06-14 | 2026-01-08 | Amano Enzyme Inc. | Liquid enzyme preparation |
| CN121620590A (zh) | 2023-09-01 | 2026-03-06 | 诺维信公司 | 稳定的液体脱酰胺酶组合物 |
| EP4777622A1 (en) * | 2023-09-13 | 2026-07-22 | 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 |
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| 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 |
| US5340734A (en) * | 1992-11-25 | 1994-08-23 | Biosource Genetics Corporation | Method for making stable, extracellular tyrosinase and synthesis of polyphenolic polymers therefrom |
| FI955962L (fi) * | 1994-04-18 | 1995-12-13 | Gist Brocades Bv | Stabiilit vesi-öljyemulsiot |
| EP0777726B1 (en) | 1994-08-26 | 2006-06-07 | Novozymes A/S | Microbial transglutaminases, their production and use |
| CN1167791C (zh) * | 1997-03-12 | 2004-09-22 | 诺沃奇梅兹有限公司 | 包含漆酶的耐贮存液体制剂 |
| 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 |
| CN100448366C (zh) * | 2002-09-26 | 2009-01-07 | 味之素株式会社 | 酶制剂及用其生产食品的方法 |
| 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 |
| CN101945995B (zh) * | 2008-02-13 | 2013-06-12 | 天野酶株式会社 | 稳定型转谷氨酰胺酶及其制造法 |
| US20110064847A1 (en) * | 2008-03-14 | 2011-03-17 | Ajinomoto Co., Inc. | Method of denaturing protein with enzymes |
| NZ589121A (en) * | 2008-06-09 | 2012-10-26 | Danisco Us Inc | Recovery of insoluble enzyme from fermentation broth and formulation of insoluble enzyme |
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