CS252472B2 - Method of b-carboxypeptidase's enzyme insulation - Google Patents
Method of b-carboxypeptidase's enzyme insulation Download PDFInfo
- Publication number
- CS252472B2 CS252472B2 CS842361A CS236184A CS252472B2 CS 252472 B2 CS252472 B2 CS 252472B2 CS 842361 A CS842361 A CS 842361A CS 236184 A CS236184 A CS 236184A CS 252472 B2 CS252472 B2 CS 252472B2
- Authority
- CS
- Czechoslovakia
- Prior art keywords
- enzyme
- centrifuged
- suspension
- carboxypeptidase
- allowed
- Prior art date
Links
- 238000000034 method Methods 0.000 title claims abstract description 23
- 102000004190 Enzymes Human genes 0.000 title claims description 46
- 108090000790 Enzymes Proteins 0.000 title claims description 46
- 238000009413 insulation Methods 0.000 title 1
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 claims abstract description 49
- 229910052921 ammonium sulfate Inorganic materials 0.000 claims abstract description 49
- 235000011130 ammonium sulphate Nutrition 0.000 claims abstract description 49
- 210000000496 pancreas Anatomy 0.000 claims abstract description 42
- 102000003670 Carboxypeptidase B Human genes 0.000 claims abstract description 26
- 108090000087 Carboxypeptidase B Proteins 0.000 claims abstract description 26
- 239000000725 suspension Substances 0.000 claims description 60
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 47
- 239000002244 precipitate Substances 0.000 claims description 42
- 239000006228 supernatant Substances 0.000 claims description 32
- 239000000203 mixture Substances 0.000 claims description 23
- 102000005367 Carboxypeptidases Human genes 0.000 claims description 12
- 108010006303 Carboxypeptidases Proteins 0.000 claims description 12
- 238000010438 heat treatment Methods 0.000 claims description 6
- 239000007853 buffer solution Substances 0.000 claims description 5
- 239000007788 liquid Substances 0.000 claims description 3
- 238000005119 centrifugation Methods 0.000 claims description 2
- 238000002955 isolation Methods 0.000 claims description 2
- 230000000694 effects Effects 0.000 abstract description 50
- 239000000843 powder Substances 0.000 abstract description 10
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 abstract description 7
- 239000012530 fluid Substances 0.000 abstract description 3
- 238000005194 fractionation Methods 0.000 abstract description 3
- 239000007858 starting material Substances 0.000 abstract description 3
- 150000001718 carbodiimides Chemical class 0.000 abstract 1
- 229920000642 polymer Polymers 0.000 abstract 1
- 238000007669 thermal treatment Methods 0.000 abstract 1
- 239000000243 solution Substances 0.000 description 49
- 229940088598 enzyme Drugs 0.000 description 43
- 102000004169 proteins and genes Human genes 0.000 description 31
- 108090000623 proteins and genes Proteins 0.000 description 31
- 239000000872 buffer Substances 0.000 description 27
- 235000015277 pork Nutrition 0.000 description 20
- 235000013372 meat Nutrition 0.000 description 19
- 238000000502 dialysis Methods 0.000 description 18
- 239000008057 potassium phosphate buffer Substances 0.000 description 15
- 229920006395 saturated elastomer Polymers 0.000 description 14
- 150000003839 salts Chemical class 0.000 description 13
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 12
- CSCPPACGZOOCGX-UHFFFAOYSA-N Acetone Chemical compound CC(C)=O CSCPPACGZOOCGX-UHFFFAOYSA-N 0.000 description 10
- 239000000047 product Substances 0.000 description 10
- 239000008363 phosphate buffer Substances 0.000 description 9
- 238000000746 purification Methods 0.000 description 9
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 8
- 239000012153 distilled water Substances 0.000 description 8
- GFLCPYUSPYXNBV-NSHDSACASA-N (2s)-2-[(2-benzamidoacetyl)amino]-5-(diaminomethylideneamino)pentanoic acid Chemical compound NC(N)=NCCC[C@@H](C(O)=O)NC(=O)CNC(=O)C1=CC=CC=C1 GFLCPYUSPYXNBV-NSHDSACASA-N 0.000 description 7
- RTZKZFJDLAIYFH-UHFFFAOYSA-N Diethyl ether Chemical compound CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 description 6
- 238000003756 stirring Methods 0.000 description 6
- 239000007864 aqueous solution Substances 0.000 description 5
- 239000001913 cellulose Substances 0.000 description 5
- 229920002678 cellulose Polymers 0.000 description 5
- 210000000056 organ Anatomy 0.000 description 5
- 238000002360 preparation method Methods 0.000 description 5
- QGZKDVFQNNGYKY-UHFFFAOYSA-O Ammonium Chemical compound [NH4+] QGZKDVFQNNGYKY-UHFFFAOYSA-O 0.000 description 4
- ODKSFYDXXFIFQN-UHFFFAOYSA-N Arginine Chemical compound OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 4
- 101100536354 Drosophila melanogaster tant gene Proteins 0.000 description 4
- QAOWNCQODCNURD-UHFFFAOYSA-L Sulfate Chemical compound [O-]S([O-])(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-L 0.000 description 4
- 239000000284 extract Substances 0.000 description 4
- KDXKERNSBIXSRK-UHFFFAOYSA-N lysine Chemical compound NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 4
- 238000004519 manufacturing process Methods 0.000 description 4
- 230000035484 reaction time Effects 0.000 description 4
- 239000011780 sodium chloride Substances 0.000 description 4
- 239000000126 substance Substances 0.000 description 4
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 3
- 241000283707 Capra Species 0.000 description 3
- YXFVVABEGXRONW-UHFFFAOYSA-N Toluene Chemical compound CC1=CC=CC=C1 YXFVVABEGXRONW-UHFFFAOYSA-N 0.000 description 3
- 239000006286 aqueous extract Substances 0.000 description 3
- 239000000758 substrate Substances 0.000 description 3
- 241000283690 Bos taurus Species 0.000 description 2
- 108010093096 Immobilized Enzymes Proteins 0.000 description 2
- 229920005654 Sephadex Polymers 0.000 description 2
- 239000012507 Sephadex™ Substances 0.000 description 2
- 239000008351 acetate buffer Substances 0.000 description 2
- 239000001166 ammonium sulphate Substances 0.000 description 2
- 239000007900 aqueous suspension Substances 0.000 description 2
- RQPZNWPYLFFXCP-UHFFFAOYSA-L barium dihydroxide Chemical compound [OH-].[OH-].[Ba+2] RQPZNWPYLFFXCP-UHFFFAOYSA-L 0.000 description 2
- 229910001863 barium hydroxide Inorganic materials 0.000 description 2
- 238000006243 chemical reaction Methods 0.000 description 2
- 230000006378 damage Effects 0.000 description 2
- 229940110377 dl- arginine Drugs 0.000 description 2
- 230000003100 immobilizing effect Effects 0.000 description 2
- 239000012535 impurity Substances 0.000 description 2
- 238000005342 ion exchange Methods 0.000 description 2
- 102000004196 processed proteins & peptides Human genes 0.000 description 2
- 108090000765 processed proteins & peptides Proteins 0.000 description 2
- 229910021653 sulphate ion Inorganic materials 0.000 description 2
- ZSOMKTOYRKMTJS-YFKPBYRVSA-N (2S)-5-(diaminomethylideneamino)-2-(fluoromethylamino)pentanoic acid Chemical compound FCN[C@@H](CCCNC(N)=N)C(=O)O ZSOMKTOYRKMTJS-YFKPBYRVSA-N 0.000 description 1
- WNWVKZTYMQWFHE-UHFFFAOYSA-N 4-ethylmorpholine Chemical group [CH2]CN1CCOCC1 WNWVKZTYMQWFHE-UHFFFAOYSA-N 0.000 description 1
- JCLFHZLOKITRCE-UHFFFAOYSA-N 4-pentoxyphenol Chemical compound CCCCCOC1=CC=C(O)C=C1 JCLFHZLOKITRCE-UHFFFAOYSA-N 0.000 description 1
- 241000238876 Acari Species 0.000 description 1
- 208000035404 Autolysis Diseases 0.000 description 1
- 206010057248 Cell death Diseases 0.000 description 1
- GUBGYTABKSRVRQ-WFVLMXAXSA-N DEAE-cellulose Chemical compound OC1C(O)C(O)C(CO)O[C@H]1O[C@@H]1C(CO)OC(O)C(O)C1O GUBGYTABKSRVRQ-WFVLMXAXSA-N 0.000 description 1
- 108090000371 Esterases Proteins 0.000 description 1
- 241000124008 Mammalia Species 0.000 description 1
- 229930006000 Sucrose Natural products 0.000 description 1
- CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 description 1
- 241000282887 Suidae Species 0.000 description 1
- NIXOWILDQLNWCW-UHFFFAOYSA-N acrylic acid group Chemical group C(C=C)(=O)O NIXOWILDQLNWCW-UHFFFAOYSA-N 0.000 description 1
- 230000003213 activating effect Effects 0.000 description 1
- 229940024606 amino acid Drugs 0.000 description 1
- 150000001413 amino acids Chemical class 0.000 description 1
- 238000012870 ammonium sulfate precipitation Methods 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 150000007942 carboxylates Chemical class 0.000 description 1
- 125000002057 carboxymethyl group Chemical group [H]OC(=O)C([H])([H])[*] 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 238000004440 column chromatography Methods 0.000 description 1
- 238000001816 cooling Methods 0.000 description 1
- 230000007423 decrease Effects 0.000 description 1
- 238000011033 desalting Methods 0.000 description 1
- 239000000385 dialysis solution Substances 0.000 description 1
- 229940079919 digestives enzyme preparation Drugs 0.000 description 1
- 230000008030 elimination Effects 0.000 description 1
- 238000003379 elimination reaction Methods 0.000 description 1
- 150000002148 esters Chemical class 0.000 description 1
- 239000002360 explosive Substances 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 235000013861 fat-free Nutrition 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 238000002523 gelfiltration Methods 0.000 description 1
- 231100001261 hazardous Toxicity 0.000 description 1
- 230000007062 hydrolysis Effects 0.000 description 1
- 238000006460 hydrolysis reaction Methods 0.000 description 1
- 239000004615 ingredient Substances 0.000 description 1
- 150000007522 mineralic acids Chemical class 0.000 description 1
- 235000014594 pastries Nutrition 0.000 description 1
- XNGIFLGASWRNHJ-UHFFFAOYSA-L phthalate(2-) Chemical compound [O-]C(=O)C1=CC=CC=C1C([O-])=O XNGIFLGASWRNHJ-UHFFFAOYSA-L 0.000 description 1
- LWIHDJKSTIGBAC-UHFFFAOYSA-K potassium phosphate Substances [K+].[K+].[K+].[O-]P([O-])([O-])=O LWIHDJKSTIGBAC-UHFFFAOYSA-K 0.000 description 1
- 229910000160 potassium phosphate Inorganic materials 0.000 description 1
- 235000011009 potassium phosphates Nutrition 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 230000028043 self proteolysis Effects 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 239000005720 sucrose Substances 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
- C12N11/00—Carrier-bound or immobilised enzymes; Carrier-bound or immobilised microbial cells; Preparation thereof
- C12N11/02—Enzymes or microbial cells immobilised on or in an organic carrier
- C12N11/04—Enzymes or microbial cells immobilised on or in an organic carrier entrapped within the carrier, e.g. gel or hollow fibres
-
- 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)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
-
- 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
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S435/00—Chemistry: molecular biology and microbiology
- Y10S435/814—Enzyme separation or purification
-
- 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
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S435/00—Chemistry: molecular biology and microbiology
- Y10S435/814—Enzyme separation or purification
- Y10S435/816—Enzyme separation or purification by solubility
Landscapes
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Organic Chemistry (AREA)
- Zoology (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Wood Science & Technology (AREA)
- Microbiology (AREA)
- Biotechnology (AREA)
- Biomedical Technology (AREA)
- Biochemistry (AREA)
- General Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Molecular Biology (AREA)
- Medicinal Chemistry (AREA)
- Dispersion Chemistry (AREA)
- Enzymes And Modification Thereof (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CS853128A CS252482B2 (cs) | 1983-07-11 | 1984-03-29 | Způsob imobilizace enzymu karboxypeptidázy |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| HU832469A HU190129B (en) | 1983-07-11 | 1983-07-11 | Process for the isolation of carboxypeptidase b enzyme from mammal pancreas |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| CS236184A2 CS236184A2 (en) | 1987-01-15 |
| CS252472B2 true CS252472B2 (en) | 1987-09-17 |
Family
ID=10959530
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CS842361A CS252472B2 (en) | 1983-07-11 | 1984-03-29 | Method of b-carboxypeptidase's enzyme insulation |
Country Status (9)
| Country | Link |
|---|---|
| US (1) | US4650762A (ro) |
| CS (1) | CS252472B2 (ro) |
| CU (1) | CU21674A3 (ro) |
| DD (2) | DD220334A5 (ro) |
| DE (1) | DE3412669A1 (ro) |
| HU (1) | HU190129B (ro) |
| RO (1) | RO88619A (ro) |
| RU (1) | RU1769763C (ro) |
| SU (1) | SU1487817A3 (ro) |
Families Citing this family (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5278284A (en) * | 1992-05-14 | 1994-01-11 | Miller Brewing Company | Protein purification method |
| IL116696A (en) * | 1995-01-25 | 1999-08-17 | Bio Technology General Corp | Production of enzymatically active recombinant carboxypeptidase b |
| PL325017A1 (en) * | 1995-08-16 | 1998-07-06 | Zeneca Ltd | Chemical compounds |
| RU2177997C1 (ru) * | 2000-05-12 | 2002-01-10 | Институт биоорганической химии имени М.М. Шемякина и Ю.А. Овчинникова РАН | Способ выделения карбоксипептидазы в |
| RU2354696C1 (ru) * | 2007-08-07 | 2009-05-10 | Федеральное государственное учреждение науки Государственный научный центр прикладной микробиологии и биотехнологии (ФГУН ГНЦ ПМБ) | Способ получения карбоксипептидазы b из поджелудочной железы свиньи |
Family Cites Families (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US3260654A (en) * | 1963-03-22 | 1966-07-12 | Ormonoterapia Richter Spa | Method for the preparation of a pancreas extract having a high proteolytic activity |
| FR3071M (fr) * | 1963-10-18 | 1965-01-18 | Centre Nat Rech Scient | Nouvelles protéases pancréatiques, utilisables notamment en gastro-entérologie. |
| DK124483B (da) * | 1967-12-04 | 1972-10-23 | Bayer Ag | Fremgangsmåde til rensning af carboxypeptidase B. |
| JPS57150384A (en) * | 1981-03-12 | 1982-09-17 | Eisai Co Ltd | Carboxypeptidase ar and its preparation |
| US4532214A (en) * | 1982-06-03 | 1985-07-30 | Reanal Finomvegyszergyar | Method for isolation of aminoacylase |
-
1983
- 1983-07-11 HU HU832469A patent/HU190129B/hu not_active IP Right Cessation
-
1984
- 1984-03-29 CS CS842361A patent/CS252472B2/cs unknown
- 1984-04-02 US US06/595,767 patent/US4650762A/en not_active Expired - Fee Related
- 1984-04-04 DE DE19843412669 patent/DE3412669A1/de not_active Ceased
- 1984-04-05 RO RO84114181A patent/RO88619A/ro unknown
- 1984-04-06 DD DD84261731A patent/DD220334A5/de not_active IP Right Cessation
- 1984-04-06 DD DD84270845A patent/DD222632A5/de not_active IP Right Cessation
- 1984-04-16 SU SU843731150A patent/SU1487817A3/ru active
- 1984-07-11 CU CU832469/83A patent/CU21674A3/es unknown
-
1987
- 1987-01-13 RU SU874028800A patent/RU1769763C/ru active
Also Published As
| Publication number | Publication date |
|---|---|
| HU190129B (en) | 1986-08-28 |
| US4650762A (en) | 1987-03-17 |
| DD222632A5 (de) | 1985-05-22 |
| RO88619A (ro) | 1986-02-28 |
| CS236184A2 (en) | 1987-01-15 |
| SU1487817A3 (ru) | 1989-06-15 |
| CU21674A3 (en) | 1987-10-12 |
| DE3412669A1 (de) | 1985-01-24 |
| HUT34234A (en) | 1985-02-28 |
| DD220334A5 (de) | 1985-03-27 |
| RU1769763C (ru) | 1992-10-15 |
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