JPH0523753B2 - - Google Patents
Info
- Publication number
- JPH0523753B2 JPH0523753B2 JP2511985A JP2511985A JPH0523753B2 JP H0523753 B2 JPH0523753 B2 JP H0523753B2 JP 2511985 A JP2511985 A JP 2511985A JP 2511985 A JP2511985 A JP 2511985A JP H0523753 B2 JPH0523753 B2 JP H0523753B2
- Authority
- JP
- Japan
- Prior art keywords
- cgtase
- enzyme
- amount
- adsorbed
- contact time
- 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
- 108010025880 Cyclomaltodextrin glucanotransferase Proteins 0.000 claims description 23
- 108010093096 Immobilized Enzymes Proteins 0.000 claims description 16
- 229920002472 Starch Polymers 0.000 claims description 13
- 235000019698 starch Nutrition 0.000 claims description 13
- 239000008107 starch Substances 0.000 claims description 13
- 239000003957 anion exchange resin Substances 0.000 claims description 12
- 229920000858 Cyclodextrin Polymers 0.000 claims description 6
- HFHDHCJBZVLPGP-UHFFFAOYSA-N schardinger α-dextrin Chemical compound O1C(C(C2O)O)C(CO)OC2OC(C(C2O)O)C(CO)OC2OC(C(C2O)O)C(CO)OC2OC(C(O)C2O)C(CO)OC2OC(C(C2O)O)C(CO)OC2OC2C(O)C(O)C1OC2CO HFHDHCJBZVLPGP-UHFFFAOYSA-N 0.000 claims description 6
- 238000004519 manufacturing process Methods 0.000 claims description 4
- 241000178960 Paenibacillus macerans Species 0.000 claims description 2
- 108090000790 Enzymes Proteins 0.000 description 19
- 102000004190 Enzymes Human genes 0.000 description 19
- 239000000243 solution Substances 0.000 description 16
- 239000011347 resin Substances 0.000 description 11
- 229920005989 resin Polymers 0.000 description 11
- 230000000694 effects Effects 0.000 description 9
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 6
- 238000000034 method Methods 0.000 description 6
- 102000004169 proteins and genes Human genes 0.000 description 6
- 108090000623 proteins and genes Proteins 0.000 description 6
- 230000007423 decrease Effects 0.000 description 5
- 239000003456 ion exchange resin Substances 0.000 description 5
- 229920003303 ion-exchange polymer Polymers 0.000 description 5
- 239000002245 particle Substances 0.000 description 5
- 238000001179 sorption measurement Methods 0.000 description 5
- MYRTYDVEIRVNKP-UHFFFAOYSA-N 1,2-Divinylbenzene Chemical compound C=CC1=CC=CC=C1C=C MYRTYDVEIRVNKP-UHFFFAOYSA-N 0.000 description 4
- 125000002791 glucosyl group Chemical group C1([C@H](O)[C@@H](O)[C@H](O)[C@H](O1)CO)* 0.000 description 4
- NWUYHJFMYQTDRP-UHFFFAOYSA-N 1,2-bis(ethenyl)benzene;1-ethenyl-2-ethylbenzene;styrene Chemical compound C=CC1=CC=CC=C1.CCC1=CC=CC=C1C=C.C=CC1=CC=CC=C1C=C NWUYHJFMYQTDRP-UHFFFAOYSA-N 0.000 description 3
- NBIIXXVUZAFLBC-UHFFFAOYSA-N Phosphoric acid Chemical compound OP(O)(O)=O NBIIXXVUZAFLBC-UHFFFAOYSA-N 0.000 description 2
- PPBRXRYQALVLMV-UHFFFAOYSA-N Styrene Chemical compound C=CC1=CC=CC=C1 PPBRXRYQALVLMV-UHFFFAOYSA-N 0.000 description 2
- HFHDHCJBZVLPGP-RWMJIURBSA-N alpha-cyclodextrin Chemical compound OC[C@H]([C@H]([C@@H]([C@H]1O)O)O[C@H]2O[C@@H]([C@@H](O[C@H]3O[C@H](CO)[C@H]([C@@H]([C@H]3O)O)O[C@H]3O[C@H](CO)[C@H]([C@@H]([C@H]3O)O)O[C@H]3O[C@H](CO)[C@H]([C@@H]([C@H]3O)O)O3)[C@H](O)[C@H]2O)CO)O[C@@H]1O[C@H]1[C@H](O)[C@@H](O)[C@@H]3O[C@@H]1CO HFHDHCJBZVLPGP-RWMJIURBSA-N 0.000 description 2
- WHGYBXFWUBPSRW-FOUAGVGXSA-N beta-cyclodextrin Chemical compound OC[C@H]([C@H]([C@@H]([C@H]1O)O)O[C@H]2O[C@@H]([C@@H](O[C@H]3O[C@H](CO)[C@H]([C@@H]([C@H]3O)O)O[C@H]3O[C@H](CO)[C@H]([C@@H]([C@H]3O)O)O[C@H]3O[C@H](CO)[C@H]([C@@H]([C@H]3O)O)O[C@H]3O[C@H](CO)[C@H]([C@@H]([C@H]3O)O)O3)[C@H](O)[C@H]2O)CO)O[C@@H]1O[C@H]1[C@H](O)[C@@H](O)[C@@H]3O[C@@H]1CO WHGYBXFWUBPSRW-FOUAGVGXSA-N 0.000 description 2
- 239000000969 carrier Substances 0.000 description 2
- 229920001429 chelating resin Polymers 0.000 description 2
- 238000006243 chemical reaction Methods 0.000 description 2
- 229920001577 copolymer Polymers 0.000 description 2
- 238000005859 coupling reaction Methods 0.000 description 2
- 238000000354 decomposition reaction Methods 0.000 description 2
- 239000012458 free base Substances 0.000 description 2
- GDSRMADSINPKSL-HSEONFRVSA-N gamma-cyclodextrin Chemical compound OC[C@H]([C@H]([C@@H]([C@H]1O)O)O[C@H]2O[C@@H]([C@@H](O[C@H]3O[C@H](CO)[C@H]([C@@H]([C@H]3O)O)O[C@H]3O[C@H](CO)[C@H]([C@@H]([C@H]3O)O)O[C@H]3O[C@H](CO)[C@H]([C@@H]([C@H]3O)O)O[C@H]3O[C@H](CO)[C@H]([C@@H]([C@H]3O)O)O[C@H]3O[C@H](CO)[C@H]([C@@H]([C@H]3O)O)O3)[C@H](O)[C@H]2O)CO)O[C@@H]1O[C@H]1[C@H](O)[C@@H](O)[C@@H]3O[C@@H]1CO GDSRMADSINPKSL-HSEONFRVSA-N 0.000 description 2
- 238000003756 stirring Methods 0.000 description 2
- 238000006276 transfer reaction Methods 0.000 description 2
- 239000004382 Amylase Substances 0.000 description 1
- 102000013142 Amylases Human genes 0.000 description 1
- 108010065511 Amylases Proteins 0.000 description 1
- 229920002261 Corn starch Polymers 0.000 description 1
- 229920001503 Glucan Polymers 0.000 description 1
- 102000004157 Hydrolases Human genes 0.000 description 1
- 108090000604 Hydrolases Proteins 0.000 description 1
- DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 1
- 102000004195 Isomerases Human genes 0.000 description 1
- 108090000769 Isomerases Proteins 0.000 description 1
- 108090000992 Transferases Proteins 0.000 description 1
- 102000004357 Transferases Human genes 0.000 description 1
- NIXOWILDQLNWCW-UHFFFAOYSA-N acrylic acid group Chemical group C(C=C)(=O)O NIXOWILDQLNWCW-UHFFFAOYSA-N 0.000 description 1
- 230000002411 adverse Effects 0.000 description 1
- 239000012670 alkaline solution Substances 0.000 description 1
- 229910000147 aluminium phosphate Inorganic materials 0.000 description 1
- 235000019418 amylase Nutrition 0.000 description 1
- 239000002585 base Substances 0.000 description 1
- 239000007853 buffer solution Substances 0.000 description 1
- 239000003054 catalyst Substances 0.000 description 1
- 238000010924 continuous production Methods 0.000 description 1
- 239000008120 corn starch Substances 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 238000010438 heat treatment Methods 0.000 description 1
- 108010063993 lens intrinsic protein MP 64 Proteins 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 230000010534 mechanism of action Effects 0.000 description 1
- 229920001542 oligosaccharide Polymers 0.000 description 1
- 150000002482 oligosaccharides Chemical class 0.000 description 1
- ISWSIDIOOBJBQZ-UHFFFAOYSA-N phenol group Chemical group C1(=CC=CC=C1)O ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 1
- 229920000768 polyamine Polymers 0.000 description 1
- 239000011148 porous material Substances 0.000 description 1
- 229920001592 potato starch Polymers 0.000 description 1
- 150000003141 primary amines Chemical class 0.000 description 1
- 230000035484 reaction time Effects 0.000 description 1
- 238000007363 ring formation reaction Methods 0.000 description 1
- 150000003335 secondary amines Chemical class 0.000 description 1
- 238000007086 side reaction Methods 0.000 description 1
- 229910052708 sodium Inorganic materials 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- 239000007974 sodium acetate buffer Substances 0.000 description 1
- 239000001488 sodium phosphate Substances 0.000 description 1
- 229910000162 sodium phosphate Inorganic materials 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 235000000346 sugar Nutrition 0.000 description 1
- 150000008163 sugars Chemical class 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 150000003512 tertiary amines Chemical class 0.000 description 1
- RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
Landscapes
- Immobilizing And Processing Of Enzymes And Microorganisms (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP2511985A JPS61185196A (ja) | 1985-02-14 | 1985-02-14 | サイクロデキストリンの生成方法 |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP2511985A JPS61185196A (ja) | 1985-02-14 | 1985-02-14 | サイクロデキストリンの生成方法 |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JPS61185196A JPS61185196A (ja) | 1986-08-18 |
| JPH0523753B2 true JPH0523753B2 (enrdf_load_stackoverflow) | 1993-04-05 |
Family
ID=12157042
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2511985A Granted JPS61185196A (ja) | 1985-02-14 | 1985-02-14 | サイクロデキストリンの生成方法 |
Country Status (1)
| Country | Link |
|---|---|
| JP (1) | JPS61185196A (enrdf_load_stackoverflow) |
Families Citing this family (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2610452B2 (ja) * | 1987-10-23 | 1997-05-14 | 株式会社ホーネンコーポレーション | 高分子分岐デキストリン組成物の製造法 |
| JPH01319501A (ja) * | 1988-05-25 | 1989-12-25 | Uop Inc | シクロデキストリンの製造法 |
| JPH0771489B2 (ja) * | 1989-06-29 | 1995-08-02 | 農林水産省食品総合研究所長 | 転移糖の製造法 |
| JP6093938B2 (ja) * | 2012-11-15 | 2017-03-15 | 公立大学法人 富山県立大学 | チューリッパリン類の製造方法 |
-
1985
- 1985-02-14 JP JP2511985A patent/JPS61185196A/ja active Granted
Also Published As
| Publication number | Publication date |
|---|---|
| JPS61185196A (ja) | 1986-08-18 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US4808232A (en) | Separation and purification of cyclodextrins | |
| Ettalibi et al. | Sucrose hydrolysis by thermostable immobilized inulinases from Aspergillus ficuum | |
| EP0220719B1 (en) | Cyclodextrin absorbing material and its use | |
| Guerrero et al. | Effect of the type of immobilization of β-galactosidase on the yield and selectivity of synthesis of transgalactosylated oligosaccharides | |
| Bodalo et al. | A comparison of different methods of β-galactosidase immobilization | |
| JPS638749B2 (enrdf_load_stackoverflow) | ||
| Campbell et al. | The recycling of NAD+ (free and immobilized) within semipermeable aqueous microcapsules containing a multi-enzyme system | |
| Yun et al. | Continuous production of inulo-oligosaccharides from chicory juice by immobilized endoinulinase | |
| JPH0338B2 (enrdf_load_stackoverflow) | ||
| Erhardt et al. | Immobilization of dextranase from Chaetomium erraticum | |
| Hill et al. | Immobilization and stabilization of levansucrase biocatalyst of high interest for the production of fructooligosaccharides and levan | |
| JPH0523753B2 (enrdf_load_stackoverflow) | ||
| JPS6219835B2 (enrdf_load_stackoverflow) | ||
| Caldwell et al. | Immobilization of enzymes based on hydrophobic interaction. II. Preparation and properties of an amyloglucosidase adsorbate | |
| Berger et al. | Immobilization of β-galactosidases from Thermus aquaticus YT-1 for oligosaccharides synthesis | |
| OKOS et al. | Hydrolysis of lactose in acid whey using β‐galactosidase adsorbed to a phenol formaldehyde resin | |
| JPS61185188A (ja) | 固定化酵素 | |
| Tomotani et al. | Screening of Dowex® anion-exchange resins for invertase immobilization | |
| JP2595004B2 (ja) | 酵素固定化用担体とその酵素固定化方法および酵素脱着方法 | |
| CN115058412A (zh) | 一种多酶包埋共固定化方法 | |
| Ivanova | Immobilization of cyclodextrin glucanotransferase from Paenibacillus macerans ATCC 8244 on magnetic carriers and production of cyclodextrins | |
| JPH0716411B2 (ja) | 固定化酵素 | |
| WO2004099260A1 (ja) | ß-サイクロデキストリンの製造法 | |
| JP2524984B2 (ja) | 固定化酵素 | |
| US5543310A (en) | Immobilized phosphorylase |