JPS6123994B2 - - Google Patents
Info
- Publication number
- JPS6123994B2 JPS6123994B2 JP3683482A JP3683482A JPS6123994B2 JP S6123994 B2 JPS6123994 B2 JP S6123994B2 JP 3683482 A JP3683482 A JP 3683482A JP 3683482 A JP3683482 A JP 3683482A JP S6123994 B2 JPS6123994 B2 JP S6123994B2
- Authority
- JP
- Japan
- Prior art keywords
- aqualysin
- heat
- stable
- enzyme
- thermus
- 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.)
- Expired
Links
- 108091005804 Peptidases Proteins 0.000 claims description 16
- 241000589596 Thermus Species 0.000 claims description 10
- 239000004365 Protease Substances 0.000 claims description 9
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 claims description 9
- 241000589500 Thermus aquaticus Species 0.000 claims description 9
- 102000011632 Caseins Human genes 0.000 claims description 8
- 108010076119 Caseins Proteins 0.000 claims description 8
- 239000005018 casein Substances 0.000 claims description 8
- 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 claims description 8
- 235000021240 caseins Nutrition 0.000 claims description 8
- 102000035195 Peptidases Human genes 0.000 claims description 7
- MUCZHBLJLSDCSD-UHFFFAOYSA-N diisopropyl fluorophosphate Chemical compound CC(C)OP(F)(=O)OC(C)C MUCZHBLJLSDCSD-UHFFFAOYSA-N 0.000 claims description 6
- 229960005051 fluostigmine Drugs 0.000 claims description 6
- 235000018102 proteins Nutrition 0.000 claims description 4
- 102000004169 proteins and genes Human genes 0.000 claims description 4
- 108090000623 proteins and genes Proteins 0.000 claims description 4
- 239000000126 substance Substances 0.000 claims description 4
- 150000001413 amino acids Chemical class 0.000 claims description 3
- 239000003112 inhibitor Substances 0.000 claims description 3
- 150000002500 ions Chemical class 0.000 claims description 3
- 238000004519 manufacturing process Methods 0.000 claims description 3
- YNJBWRMUSHSURL-UHFFFAOYSA-N trichloroacetic acid Chemical compound OC(=O)C(Cl)(Cl)Cl YNJBWRMUSHSURL-UHFFFAOYSA-N 0.000 claims description 3
- 108010038807 Oligopeptides Proteins 0.000 claims description 2
- 102000015636 Oligopeptides Human genes 0.000 claims description 2
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 claims description 2
- 239000003381 stabilizer Substances 0.000 claims description 2
- 238000012258 culturing Methods 0.000 claims 1
- 229910021645 metal ion Inorganic materials 0.000 claims 1
- 102000004190 Enzymes Human genes 0.000 description 23
- 108090000790 Enzymes Proteins 0.000 description 23
- 229940088598 enzyme Drugs 0.000 description 23
- 239000000243 solution Substances 0.000 description 13
- 239000000872 buffer Substances 0.000 description 9
- 239000008363 phosphate buffer Substances 0.000 description 8
- 230000000694 effects Effects 0.000 description 7
- 239000002609 medium Substances 0.000 description 7
- BTBUEUYNUDRHOZ-UHFFFAOYSA-N Borate Chemical compound [O-]B([O-])[O-] BTBUEUYNUDRHOZ-UHFFFAOYSA-N 0.000 description 5
- 239000000203 mixture Substances 0.000 description 5
- 239000000758 substrate Substances 0.000 description 5
- WCUXLLCKKVVCTQ-UHFFFAOYSA-M Potassium chloride Chemical compound [Cl-].[K+] WCUXLLCKKVVCTQ-UHFFFAOYSA-M 0.000 description 4
- 239000007853 buffer solution Substances 0.000 description 4
- 238000006243 chemical reaction Methods 0.000 description 4
- 238000010586 diagram Methods 0.000 description 4
- 238000000034 method Methods 0.000 description 4
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
- DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 3
- 229940041514 candida albicans extract Drugs 0.000 description 3
- 238000005119 centrifugation Methods 0.000 description 3
- 238000009630 liquid culture Methods 0.000 description 3
- 239000000843 powder Substances 0.000 description 3
- 239000002244 precipitate Substances 0.000 description 3
- 239000006228 supernatant Substances 0.000 description 3
- 239000012138 yeast extract Substances 0.000 description 3
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 2
- 241000589501 Thermus caldophilus Species 0.000 description 2
- 238000010521 absorption reaction Methods 0.000 description 2
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 2
- 229910052921 ammonium sulfate Inorganic materials 0.000 description 2
- 235000011130 ammonium sulphate Nutrition 0.000 description 2
- 230000001580 bacterial effect Effects 0.000 description 2
- 108010092440 caldolysin Proteins 0.000 description 2
- 239000001913 cellulose Substances 0.000 description 2
- 229920002678 cellulose Polymers 0.000 description 2
- 238000000502 dialysis Methods 0.000 description 2
- 238000001962 electrophoresis Methods 0.000 description 2
- 238000010828 elution Methods 0.000 description 2
- 244000005700 microbiome Species 0.000 description 2
- BASFCYQUMIYNBI-UHFFFAOYSA-N platinum Chemical compound [Pt] BASFCYQUMIYNBI-UHFFFAOYSA-N 0.000 description 2
- 239000001103 potassium chloride Substances 0.000 description 2
- 235000011164 potassium chloride Nutrition 0.000 description 2
- 229940024999 proteolytic enzymes for treatment of wounds and ulcers Drugs 0.000 description 2
- 150000003839 salts Chemical class 0.000 description 2
- XPFJYKARVSSRHE-UHFFFAOYSA-K trisodium;2-hydroxypropane-1,2,3-tricarboxylate;2-hydroxypropane-1,2,3-tricarboxylic acid Chemical compound [Na+].[Na+].[Na+].OC(=O)CC(O)(C(O)=O)CC(O)=O.[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O XPFJYKARVSSRHE-UHFFFAOYSA-K 0.000 description 2
- 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 1
- 241000193830 Bacillus <bacterium> Species 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 1
- 102000003846 Carbonic anhydrases Human genes 0.000 description 1
- 108090000209 Carbonic anhydrases Proteins 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
- 244000068988 Glycine max Species 0.000 description 1
- 235000010469 Glycine max Nutrition 0.000 description 1
- 108010058846 Ovalbumin Proteins 0.000 description 1
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
- 241000187747 Streptomyces Species 0.000 description 1
- 241000868182 Thermus thermophilus HB8 Species 0.000 description 1
- 241000006364 Torula Species 0.000 description 1
- 101710162629 Trypsin inhibitor Proteins 0.000 description 1
- 229940122618 Trypsin inhibitor Drugs 0.000 description 1
- 239000000654 additive Substances 0.000 description 1
- 238000005273 aeration Methods 0.000 description 1
- KGBXLFKZBHKPEV-UHFFFAOYSA-N boric acid Chemical compound OB(O)O KGBXLFKZBHKPEV-UHFFFAOYSA-N 0.000 description 1
- 239000004327 boric acid Substances 0.000 description 1
- 229940098773 bovine serum albumin Drugs 0.000 description 1
- 238000001816 cooling Methods 0.000 description 1
- 239000003599 detergent Substances 0.000 description 1
- 239000000706 filtrate Substances 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 235000013373 food additive Nutrition 0.000 description 1
- 239000002778 food additive Substances 0.000 description 1
- 238000001502 gel electrophoresis Methods 0.000 description 1
- 239000008103 glucose Substances 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 239000013028 medium composition Substances 0.000 description 1
- 235000015097 nutrients Nutrition 0.000 description 1
- 229940092253 ovalbumin Drugs 0.000 description 1
- 238000010647 peptide synthesis reaction Methods 0.000 description 1
- 229910052697 platinum Inorganic materials 0.000 description 1
- 229920002401 polyacrylamide Polymers 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 238000011218 seed culture Methods 0.000 description 1
- CIJQGPVMMRXSQW-UHFFFAOYSA-M sodium;2-aminoacetic acid;hydroxide Chemical compound O.[Na+].NCC([O-])=O CIJQGPVMMRXSQW-UHFFFAOYSA-M 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 239000002753 trypsin inhibitor Substances 0.000 description 1
- 235000013343 vitamin Nutrition 0.000 description 1
- 229940088594 vitamin Drugs 0.000 description 1
- 229930003231 vitamin Natural products 0.000 description 1
- 239000011782 vitamin Substances 0.000 description 1
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 1
Landscapes
- Enzymes And Modification Thereof (AREA)
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP3683482A JPS58152482A (ja) | 1982-03-08 | 1982-03-08 | 耐熱性蛋白分解酵素アクアライシンｉおよびその製造法 |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP3683482A JPS58152482A (ja) | 1982-03-08 | 1982-03-08 | 耐熱性蛋白分解酵素アクアライシンｉおよびその製造法 |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JPS58152482A JPS58152482A (ja) | 1983-09-10 |
| JPS6123994B2 true JPS6123994B2 (es) | 1986-06-09 |
Family
ID=12480768
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP3683482A Granted JPS58152482A (ja) | 1982-03-08 | 1982-03-08 | 耐熱性蛋白分解酵素アクアライシンｉおよびその製造法 |
Country Status (1)
| Country | Link |
|---|---|
| JP (1) | JPS58152482A (es) |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO1994010290A1 (en) * | 1992-10-30 | 1994-05-11 | Gomei Kaisha Nakamura Sangyo | Thermophilic cellulose-decomposing bacterium and utilization thereof |
Families Citing this family (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2639803B2 (ja) * | 1987-03-02 | 1997-08-13 | オリエンタル酵母工業株式会社 | 耐熱性イソクエン酸脱水素酵素の製法 |
-
1982
- 1982-03-08 JP JP3683482A patent/JPS58152482A/ja active Granted
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO1994010290A1 (en) * | 1992-10-30 | 1994-05-11 | Gomei Kaisha Nakamura Sangyo | Thermophilic cellulose-decomposing bacterium and utilization thereof |
Also Published As
| Publication number | Publication date |
|---|---|
| JPS58152482A (ja) | 1983-09-10 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| EP0024182B1 (en) | Thermo-stable micro-organism and proteolytic enzyme prepared therefrom, and processes for the preparation of the micro-organism and the proteolytic enzyme | |
| US5827699A (en) | Strain of Rhodococcus rhodochrous as a producer of nitrile hydratase | |
| KR960014702B1 (ko) | 산성 우레아제 및 그의 제조방법 | |
| US4542098A (en) | Production of glucose dehydrogenase and use of the resultant enzyme in the enzymatic synthesis of L-carnitine | |
| Griffiths et al. | Properties of a thermostable β‐galactosidase from a thermophilic Bacillus: Comparison of the enzyme activity of whole cells, purified enzyme and immobilised whole cells | |
| US4315988A (en) | Thermophilic collagenases, thermophilic bacteria capable of producing thermophilic collagenases, and process for producing said collagenases | |
| EP0954571B1 (en) | Biocatalysts with amine acylase activity | |
| US3669843A (en) | Process for the production of uricase | |
| JPS611384A (ja) | Ｎ−アセチルノイラミン酸リア−ゼの製法 | |
| JPS6123994B2 (es) | ||
| Kagayama et al. | Purification and properties of an aromatic amidase from Pseudomonas sp. GDI 211 | |
| JP2882652B2 (ja) | アルカリプロテアーゼ及びその生産性微生物 | |
| EP0206595B1 (en) | Thermally stable tryptophanase process for producing the same, and thermally stable tryptophanase-producing microorganism | |
| JPH0440988B2 (es) | ||
| JPH07108219B2 (ja) | Ｎａｄｈオキシダ−ゼの製造法 | |
| JPH0147150B2 (es) | ||
| JPS6248380A (ja) | セフアロスポリンｃアシラ−ゼの製造法 | |
| JPH0239237B2 (ja) | Shusanokishidaazenoseizoho | |
| JPH0616704B2 (ja) | フッ化物イオンに耐性な細菌カタラーゼ及びそれを生産するミクロコッカスｓｐ．ｋｗｉ‐５菌株 | |
| JPH07289256A (ja) | アミノペプチダーゼおよびその生産方法 | |
| JP3125954B2 (ja) | 新規なホスホエノールピルビン酸カルボキシラーゼ及びその製法 | |
| JPS6248379A (ja) | セフアロスポリンｃアシラ−ゼの製造法 | |
| Kittelmann et al. | Isolation and characterization of N-acetyldehydroleucine acylase, a new enzyme from Zoogloea ramigera | |
| JPH0630572B2 (ja) | Ｌ−フエニルアラニン脱水素酵素 | |
| JPS6147194A (ja) | Ｎ−カルバモイル−ｄ−バリンまたはｄ−バリンの製造法 |