JPH0525479B2 - - Google Patents
Info
- Publication number
- JPH0525479B2 JPH0525479B2 JP57010337A JP1033782A JPH0525479B2 JP H0525479 B2 JPH0525479 B2 JP H0525479B2 JP 57010337 A JP57010337 A JP 57010337A JP 1033782 A JP1033782 A JP 1033782A JP H0525479 B2 JPH0525479 B2 JP H0525479B2
- Authority
- JP
- Japan
- Prior art keywords
- atp
- reactor
- kinase
- enzyme
- present
- 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 - Lifetime
Links
- 238000006243 chemical reaction Methods 0.000 claims description 36
- UDMBCSSLTHHNCD-KQYNXXCUSA-N adenosine 5'-monophosphate Chemical compound C1=NC=2C(N)=NC=NC=2N1[C@@H]1O[C@H](COP(O)(O)=O)[C@@H](O)[C@H]1O UDMBCSSLTHHNCD-KQYNXXCUSA-N 0.000 claims description 33
- 108010092060 Acetate kinase Proteins 0.000 claims description 13
- 108020000543 Adenylate kinase Proteins 0.000 claims description 11
- 102000002281 Adenylate kinase Human genes 0.000 claims description 10
- 241000193385 Geobacillus stearothermophilus Species 0.000 claims description 9
- 238000000034 method Methods 0.000 claims description 8
- 229910019142 PO4 Inorganic materials 0.000 claims description 7
- 239000012528 membrane Substances 0.000 claims description 7
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 claims description 7
- 239000010452 phosphate Substances 0.000 claims description 7
- ZKHQWZAMYRWXGA-KQYNXXCUSA-J ATP(4-) Chemical compound C1=NC=2C(N)=NC=NC=2N1[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)[C@H]1O ZKHQWZAMYRWXGA-KQYNXXCUSA-J 0.000 claims 4
- ZKHQWZAMYRWXGA-UHFFFAOYSA-N Adenosine triphosphate Natural products C1=NC=2C(N)=NC=NC=2N1C1OC(COP(O)(=O)OP(O)(=O)OP(O)(O)=O)C(O)C1O ZKHQWZAMYRWXGA-UHFFFAOYSA-N 0.000 claims 4
- UDMBCSSLTHHNCD-UHFFFAOYSA-N Coenzym Q(11) Natural products C1=NC=2C(N)=NC=NC=2N1C1OC(COP(O)(O)=O)C(O)C1O UDMBCSSLTHHNCD-UHFFFAOYSA-N 0.000 claims 3
- LNQVTSROQXJCDD-UHFFFAOYSA-N adenosine monophosphate Natural products C1=NC=2C(N)=NC=NC=2N1C1OC(CO)C(OP(O)(O)=O)C1O LNQVTSROQXJCDD-UHFFFAOYSA-N 0.000 claims 3
- 238000001914 filtration Methods 0.000 claims 2
- 238000000108 ultra-filtration Methods 0.000 claims 1
- 102000004190 Enzymes Human genes 0.000 description 29
- 108090000790 Enzymes Proteins 0.000 description 29
- 239000000243 solution Substances 0.000 description 9
- 239000000126 substance Substances 0.000 description 9
- 239000011521 glass Substances 0.000 description 7
- LIPOUNRJVLNBCD-UHFFFAOYSA-N acetyl dihydrogen phosphate Chemical compound CC(=O)OP(O)(O)=O LIPOUNRJVLNBCD-UHFFFAOYSA-N 0.000 description 6
- 239000000872 buffer Substances 0.000 description 6
- 244000005700 microbiome Species 0.000 description 6
- 230000000694 effects Effects 0.000 description 5
- TWRXJAOTZQYOKJ-UHFFFAOYSA-L Magnesium chloride Chemical compound [Mg+2].[Cl-].[Cl-] TWRXJAOTZQYOKJ-UHFFFAOYSA-L 0.000 description 4
- PXIPVTKHYLBLMZ-UHFFFAOYSA-N Sodium azide Chemical compound [Na+].[N-]=[N+]=[N-] PXIPVTKHYLBLMZ-UHFFFAOYSA-N 0.000 description 4
- 239000012510 hollow fiber Substances 0.000 description 4
- 239000000047 product Substances 0.000 description 4
- JDIIGWSSTNUWGK-UHFFFAOYSA-N 1h-imidazol-3-ium;chloride Chemical compound [Cl-].[NH2+]1C=CN=C1 JDIIGWSSTNUWGK-UHFFFAOYSA-N 0.000 description 3
- 238000009739 binding Methods 0.000 description 3
- 230000000052 comparative effect Effects 0.000 description 3
- 238000005516 engineering process Methods 0.000 description 3
- 241000588724 Escherichia coli Species 0.000 description 2
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 2
- 108010093096 Immobilized Enzymes Proteins 0.000 description 2
- 102000001253 Protein Kinase Human genes 0.000 description 2
- OIRDTQYFTABQOQ-KQYNXXCUSA-N adenosine Chemical compound C1=NC=2C(N)=NC=NC=2N1[C@@H]1O[C@H](CO)[C@@H](O)[C@H]1O OIRDTQYFTABQOQ-KQYNXXCUSA-N 0.000 description 2
- 239000007853 buffer solution Substances 0.000 description 2
- 229920001577 copolymer Polymers 0.000 description 2
- 238000004128 high performance liquid chromatography Methods 0.000 description 2
- 229910001629 magnesium chloride Inorganic materials 0.000 description 2
- 238000004519 manufacturing process Methods 0.000 description 2
- 230000000813 microbial effect Effects 0.000 description 2
- 230000001172 regenerating effect Effects 0.000 description 2
- 230000008929 regeneration Effects 0.000 description 2
- 238000011069 regeneration method Methods 0.000 description 2
- 238000000926 separation method Methods 0.000 description 2
- 239000000758 substrate Substances 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
- 229920000936 Agarose Polymers 0.000 description 1
- 241000193830 Bacillus <bacterium> Species 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- BTBUEUYNUDRHOZ-UHFFFAOYSA-N Borate Chemical compound [O-]B([O-])[O-] BTBUEUYNUDRHOZ-UHFFFAOYSA-N 0.000 description 1
- 239000002126 C01EB10 - Adenosine Substances 0.000 description 1
- 229920002307 Dextran Polymers 0.000 description 1
- 239000004952 Polyamide Substances 0.000 description 1
- 229920000805 Polyaspartic acid Polymers 0.000 description 1
- 239000004793 Polystyrene Substances 0.000 description 1
- 229920002684 Sepharose Polymers 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 230000003213 activating effect Effects 0.000 description 1
- 229960005305 adenosine Drugs 0.000 description 1
- PNEYBMLMFCGWSK-UHFFFAOYSA-N aluminium oxide Inorganic materials [O-2].[O-2].[O-2].[Al+3].[Al+3] PNEYBMLMFCGWSK-UHFFFAOYSA-N 0.000 description 1
- 229940024606 amino acid Drugs 0.000 description 1
- 150000001413 amino acids Chemical class 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 230000001851 biosynthetic effect Effects 0.000 description 1
- 230000015572 biosynthetic process Effects 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
- 239000006227 byproduct Substances 0.000 description 1
- 239000003054 catalyst Substances 0.000 description 1
- 229920002678 cellulose Polymers 0.000 description 1
- 239000001913 cellulose Substances 0.000 description 1
- 239000007795 chemical reaction product Substances 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 238000013461 design Methods 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 210000000744 eyelid Anatomy 0.000 description 1
- 239000012527 feed solution Substances 0.000 description 1
- 238000000855 fermentation Methods 0.000 description 1
- 230000004151 fermentation Effects 0.000 description 1
- 238000011049 filling Methods 0.000 description 1
- 239000012847 fine chemical Substances 0.000 description 1
- 229960002989 glutamic acid Drugs 0.000 description 1
- 150000004676 glycans Chemical class 0.000 description 1
- 230000034659 glycolysis Effects 0.000 description 1
- 229910052588 hydroxylapatite Inorganic materials 0.000 description 1
- 150000002460 imidazoles Chemical class 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- 238000006317 isomerization reaction Methods 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 230000007774 longterm Effects 0.000 description 1
- 210000003205 muscle Anatomy 0.000 description 1
- 230000007935 neutral effect Effects 0.000 description 1
- XYJRXVWERLGGKC-UHFFFAOYSA-D pentacalcium;hydroxide;triphosphate Chemical compound [OH-].[Ca+2].[Ca+2].[Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O XYJRXVWERLGGKC-UHFFFAOYSA-D 0.000 description 1
- 238000010647 peptide synthesis reaction Methods 0.000 description 1
- 230000002572 peristaltic effect Effects 0.000 description 1
- 229920002401 polyacrylamide Polymers 0.000 description 1
- 229920002647 polyamide Polymers 0.000 description 1
- 108010064470 polyaspartate Proteins 0.000 description 1
- 229920001282 polysaccharide Polymers 0.000 description 1
- 239000005017 polysaccharide Substances 0.000 description 1
- 229920002223 polystyrene Polymers 0.000 description 1
- 238000001243 protein synthesis Methods 0.000 description 1
- 108090000623 proteins and genes Proteins 0.000 description 1
- 239000002994 raw material Substances 0.000 description 1
- 239000011541 reaction mixture Substances 0.000 description 1
- 238000004064 recycling Methods 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 238000012552 review Methods 0.000 description 1
- 238000007086 side reaction Methods 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 230000008961 swelling Effects 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 230000014616 translation Effects 0.000 description 1
- 125000000391 vinyl group Chemical group [H]C([*])=C([H])[H] 0.000 description 1
- 229920002554 vinyl polymer Polymers 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- 229920003169 water-soluble polymer Polymers 0.000 description 1
Landscapes
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Saccharide Compounds (AREA)
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP57010337A JPS58129992A (ja) | 1982-01-26 | 1982-01-26 | アデノシン一リン酸をアデノシン三リン酸へ変換する方法 |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP57010337A JPS58129992A (ja) | 1982-01-26 | 1982-01-26 | アデノシン一リン酸をアデノシン三リン酸へ変換する方法 |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JPS58129992A JPS58129992A (ja) | 1983-08-03 |
| JPH0525479B2 true JPH0525479B2 (sv) | 1993-04-13 |
Family
ID=11747375
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP57010337A Granted JPS58129992A (ja) | 1982-01-26 | 1982-01-26 | アデノシン一リン酸をアデノシン三リン酸へ変換する方法 |
Country Status (1)
| Country | Link |
|---|---|
| JP (1) | JPS58129992A (sv) |
Families Citing this family (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| SG11201707370WA (en) | 2015-03-30 | 2017-10-30 | Greenlight Biosciences Inc | Cell-free production of ribonucleic acid |
| KR102536687B1 (ko) * | 2016-04-06 | 2023-05-25 | 그린라이트 바이오사이언시스, 아이엔씨. | 리보핵산의 무세포 생산 |
Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP0029976A1 (en) * | 1979-11-22 | 1981-06-10 | Unitika Ltd. | A biologically pure culture of strain IFO 14093 and a process for producing an intracellular component herefrom |
-
1982
- 1982-01-26 JP JP57010337A patent/JPS58129992A/ja active Granted
Patent Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP0029976A1 (en) * | 1979-11-22 | 1981-06-10 | Unitika Ltd. | A biologically pure culture of strain IFO 14093 and a process for producing an intracellular component herefrom |
Also Published As
| Publication number | Publication date |
|---|---|
| JPS58129992A (ja) | 1983-08-03 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| Marconi et al. | Industrial applications of fiber-entrapped enzymes | |
| JPH0521553B2 (sv) | ||
| EP0125105B1 (en) | Immobilization of catalytically active microorganisms in agar gel fibers | |
| EP0385486A1 (en) | Process for producing fructose-1,6-diphosphate | |
| JPH0525479B2 (sv) | ||
| CA1179283A (en) | SUCROSE MUTASE, IMMOBILISED SUCROSE MUTASE AND THE USE OF THIS IMMOBILISED SUCROSE MUTASE FOR THE PREPARATION OF ISOMALTULOSE (6-0-.alpha.-D- GLUCOPYRANOSIDO-D-FRUCTOSE) | |
| Chibata et al. | Immobilized cells: Historical background | |
| JPS58209990A (ja) | アデノシン一リン酸のアデノシン三リン酸への変換方法 | |
| EP0050007B1 (en) | A heat-resistant adenylate kinase, a stable immobilized adenylate kinase composite material, and processes for their production | |
| US4113566A (en) | Process for preparing 6-aminopenicillanic acid | |
| JPS5934354B2 (ja) | 固定化耐熱性酢酸キナ−ゼ | |
| Stöcklein et al. | Conversion of L-phenylalanine to L-tyrosine by immobilized bacteria | |
| Lee et al. | Evaluation of immobilization methods for cyclodextrin glucanotransferase and characterization of its enzymatic properties | |
| Chibata | Production of useful chemicals using cells immobilized with polyacrylamide and carrageenan | |
| JPH01132394A (ja) | 固定化菌体の熱処理方法 | |
| Lee et al. | Performance of column type bioreactor packed with immobilized cyclodextrin glucanotransferase for cyclodextrin production | |
| JPS6031474B2 (ja) | バイオリアクタ−に使用する酵素の製造法 | |
| JPS5933355B2 (ja) | 固定化耐熱性酢酸キナ−ゼ | |
| JPS5876097A (ja) | 固定化微生物によるグルコン酸の製造法 | |
| Chibata et al. | Immobilized cells | |
| JP2764084B2 (ja) | Ｌ―トリプトファンの製造方法 | |
| RU2420581C1 (ru) | Способ получения биокатализатора, обладающего активностью в отношении синтеза цефалоспоринов-кислот | |
| JPH0521554B2 (sv) | ||
| GB2102005A (en) | Process for synthesis of polydeoxynucleotides | |
| JPH0616706B2 (ja) | 固定化酵素の製造法 |