JPH0327198B2 - - Google Patents
Info
- Publication number
- JPH0327198B2 JPH0327198B2 JP62175747A JP17574787A JPH0327198B2 JP H0327198 B2 JPH0327198 B2 JP H0327198B2 JP 62175747 A JP62175747 A JP 62175747A JP 17574787 A JP17574787 A JP 17574787A JP H0327198 B2 JPH0327198 B2 JP H0327198B2
- Authority
- JP
- Japan
- Prior art keywords
- chitosan
- gel
- aldehyde
- enzymes
- enzyme
- 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
- 102000004190 Enzymes Human genes 0.000 claims description 40
- 108090000790 Enzymes Proteins 0.000 claims description 40
- 238000000034 method Methods 0.000 claims description 24
- 244000005700 microbiome Species 0.000 claims description 12
- 229920001661 Chitosan Polymers 0.000 claims description 11
- 230000000813 microbial effect Effects 0.000 claims description 11
- SXRSQZLOMIGNAQ-UHFFFAOYSA-N Glutaraldehyde Chemical compound O=CCCCC=O SXRSQZLOMIGNAQ-UHFFFAOYSA-N 0.000 claims description 9
- 238000004132 cross linking Methods 0.000 claims description 8
- 230000003100 immobilizing effect Effects 0.000 claims description 7
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 7
- 150000001299 aldehydes Chemical class 0.000 claims description 6
- 239000002262 Schiff base Substances 0.000 claims description 2
- 150000004753 Schiff bases Chemical class 0.000 claims description 2
- 125000003277 amino group Chemical group 0.000 claims description 2
- 125000004435 hydrogen atom Chemical group [H]* 0.000 claims description 2
- 239000011347 resin Substances 0.000 claims 1
- 229920005989 resin Polymers 0.000 claims 1
- 229940088598 enzyme Drugs 0.000 description 32
- 239000000499 gel Substances 0.000 description 30
- 230000000694 effects Effects 0.000 description 20
- 230000001580 bacterial effect Effects 0.000 description 18
- 108010093096 Immobilized Enzymes Proteins 0.000 description 12
- 102000005936 beta-Galactosidase Human genes 0.000 description 12
- 108010005774 beta-Galactosidase Proteins 0.000 description 12
- 108700040099 Xylose isomerases Proteins 0.000 description 9
- 238000006243 chemical reaction Methods 0.000 description 7
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 6
- 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 6
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 6
- 239000012153 distilled water Substances 0.000 description 6
- WSFSSNUMVMOOMR-UHFFFAOYSA-N formaldehyde Substances O=C WSFSSNUMVMOOMR-UHFFFAOYSA-N 0.000 description 6
- 239000008103 glucose Substances 0.000 description 6
- GUBGYTABKSRVRQ-QKKXKWKRSA-N Lactose Natural products OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 description 5
- 239000008101 lactose Substances 0.000 description 5
- 239000000243 solution Substances 0.000 description 5
- 241000187411 Streptomyces phaeochromogenes Species 0.000 description 3
- -1 aliphatic aldehyde Chemical class 0.000 description 3
- 230000014759 maintenance of location Effects 0.000 description 3
- MSWZFWKMSRAUBD-IVMDWMLBSA-N 2-amino-2-deoxy-D-glucopyranose Chemical compound N[C@H]1C(O)O[C@H](CO)[C@@H](O)[C@@H]1O MSWZFWKMSRAUBD-IVMDWMLBSA-N 0.000 description 2
- 241000186361 Actinobacteria <class> Species 0.000 description 2
- 241000228212 Aspergillus Species 0.000 description 2
- 241000894006 Bacteria Species 0.000 description 2
- ZTQSAGDEMFDKMZ-UHFFFAOYSA-N Butyraldehyde Chemical compound CCCC=O ZTQSAGDEMFDKMZ-UHFFFAOYSA-N 0.000 description 2
- 241000238557 Decapoda Species 0.000 description 2
- 108090000769 Isomerases Proteins 0.000 description 2
- 102000004195 Isomerases Human genes 0.000 description 2
- CSNNHWWHGAXBCP-UHFFFAOYSA-L Magnesium sulfate Chemical compound [Mg+2].[O-][S+2]([O-])([O-])[O-] CSNNHWWHGAXBCP-UHFFFAOYSA-L 0.000 description 2
- NBBJYMSMWIIQGU-UHFFFAOYSA-N Propionic aldehyde Chemical compound CCC=O NBBJYMSMWIIQGU-UHFFFAOYSA-N 0.000 description 2
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 2
- MSWZFWKMSRAUBD-UHFFFAOYSA-N beta-D-galactosamine Natural products NC1C(O)OC(CO)C(O)C1O MSWZFWKMSRAUBD-UHFFFAOYSA-N 0.000 description 2
- 239000006285 cell suspension Substances 0.000 description 2
- 238000012258 culturing Methods 0.000 description 2
- 229930182830 galactose Natural products 0.000 description 2
- 229960002442 glucosamine Drugs 0.000 description 2
- 238000006317 isomerization reaction Methods 0.000 description 2
- 239000000203 mixture Substances 0.000 description 2
- 239000008363 phosphate buffer Substances 0.000 description 2
- 230000008961 swelling Effects 0.000 description 2
- 241001446247 uncultured actinomycete Species 0.000 description 2
- FHVDTGUDJYJELY-UHFFFAOYSA-N 6-{[2-carboxy-4,5-dihydroxy-6-(phosphanyloxy)oxan-3-yl]oxy}-4,5-dihydroxy-3-phosphanyloxane-2-carboxylic acid Chemical compound O1C(C(O)=O)C(P)C(O)C(O)C1OC1C(C(O)=O)OC(OP)C(O)C1O FHVDTGUDJYJELY-UHFFFAOYSA-N 0.000 description 1
- 108091005508 Acid proteases Proteins 0.000 description 1
- 229920001817 Agar Polymers 0.000 description 1
- 108090000145 Bacillolysin Proteins 0.000 description 1
- 108091005658 Basic proteases Proteins 0.000 description 1
- 108010084185 Cellulases Proteins 0.000 description 1
- 102000005575 Cellulases Human genes 0.000 description 1
- 229920002101 Chitin Polymers 0.000 description 1
- 108090000317 Chymotrypsin Proteins 0.000 description 1
- 229930091371 Fructose Natural products 0.000 description 1
- 239000005715 Fructose Substances 0.000 description 1
- RFSUNEUAIZKAJO-ARQDHWQXSA-N Fructose Chemical compound OC[C@H]1O[C@](O)(CO)[C@@H](O)[C@@H]1O RFSUNEUAIZKAJO-ARQDHWQXSA-N 0.000 description 1
- 102000002464 Galactosidases Human genes 0.000 description 1
- 108010093031 Galactosidases Proteins 0.000 description 1
- 108010073178 Glucan 1,4-alpha-Glucosidase Proteins 0.000 description 1
- 102100022624 Glucoamylase Human genes 0.000 description 1
- 108010028688 Isoamylase Proteins 0.000 description 1
- 239000004367 Lipase Substances 0.000 description 1
- 108090001060 Lipase Proteins 0.000 description 1
- 102000004882 Lipase Human genes 0.000 description 1
- 102000035092 Neutral proteases Human genes 0.000 description 1
- 108091005507 Neutral proteases Proteins 0.000 description 1
- 108090000526 Papain Proteins 0.000 description 1
- 108010073038 Penicillin Amidase Proteins 0.000 description 1
- 102000057297 Pepsin A Human genes 0.000 description 1
- 108090000284 Pepsin A Proteins 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 241000187747 Streptomyces Species 0.000 description 1
- 102000003990 Urokinase-type plasminogen activator Human genes 0.000 description 1
- 108090000435 Urokinase-type plasminogen activator Proteins 0.000 description 1
- ZNOZWUKQPJXOIG-XSBHQQIPSA-L [(2r,3s,4r,5r,6s)-6-[[(1r,3s,4r,5r,8s)-3,4-dihydroxy-2,6-dioxabicyclo[3.2.1]octan-8-yl]oxy]-4-[[(1r,3r,4r,5r,8s)-8-[(2s,3r,4r,5r,6r)-3,4-dihydroxy-6-(hydroxymethyl)-5-sulfonatooxyoxan-2-yl]oxy-4-hydroxy-2,6-dioxabicyclo[3.2.1]octan-3-yl]oxy]-5-hydroxy-2-( Chemical compound O[C@@H]1[C@@H](O)[C@@H](OS([O-])(=O)=O)[C@@H](CO)O[C@H]1O[C@@H]1[C@@H]2OC[C@H]1O[C@H](O[C@H]1[C@H]([C@@H](CO)O[C@@H](O[C@@H]3[C@@H]4OC[C@H]3O[C@H](O)[C@@H]4O)[C@@H]1O)OS([O-])(=O)=O)[C@@H]2O ZNOZWUKQPJXOIG-XSBHQQIPSA-L 0.000 description 1
- IKHGUXGNUITLKF-XPULMUKRSA-N acetaldehyde Chemical compound [14CH]([14CH3])=O IKHGUXGNUITLKF-XPULMUKRSA-N 0.000 description 1
- 239000008272 agar Substances 0.000 description 1
- 229940023476 agar Drugs 0.000 description 1
- 230000002776 aggregation Effects 0.000 description 1
- 238000004220 aggregation Methods 0.000 description 1
- 229940072056 alginate Drugs 0.000 description 1
- 229920000615 alginic acid Polymers 0.000 description 1
- 235000010443 alginic acid Nutrition 0.000 description 1
- 108090000637 alpha-Amylases Proteins 0.000 description 1
- 102000004139 alpha-Amylases Human genes 0.000 description 1
- WQZGKKKJIJFFOK-PHYPRBDBSA-N alpha-D-galactose Chemical compound OC[C@H]1O[C@H](O)[C@H](O)[C@@H](O)[C@H]1O WQZGKKKJIJFFOK-PHYPRBDBSA-N 0.000 description 1
- 102000005840 alpha-Galactosidase Human genes 0.000 description 1
- 108010030291 alpha-Galactosidase Proteins 0.000 description 1
- 229940024171 alpha-amylase Drugs 0.000 description 1
- 108010003977 aminoacylase I Proteins 0.000 description 1
- 108010019077 beta-Amylase Proteins 0.000 description 1
- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 1
- 108010051210 beta-Fructofuranosidase Proteins 0.000 description 1
- 229960002376 chymotrypsin Drugs 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- 229940079593 drug Drugs 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 238000001035 drying Methods 0.000 description 1
- 230000007613 environmental effect Effects 0.000 description 1
- 238000006911 enzymatic reaction Methods 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 238000005189 flocculation Methods 0.000 description 1
- 230000016615 flocculation Effects 0.000 description 1
- 235000013305 food Nutrition 0.000 description 1
- 150000004676 glycans Chemical class 0.000 description 1
- 108010002430 hemicellulase Proteins 0.000 description 1
- 230000007062 hydrolysis Effects 0.000 description 1
- 238000006460 hydrolysis reaction Methods 0.000 description 1
- 230000003834 intracellular effect Effects 0.000 description 1
- 239000001573 invertase Substances 0.000 description 1
- 235000011073 invertase Nutrition 0.000 description 1
- 235000019421 lipase Nutrition 0.000 description 1
- 229910052943 magnesium sulfate Inorganic materials 0.000 description 1
- 235000019341 magnesium sulphate Nutrition 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- WSFSSNUMVMOOMR-NJFSPNSNSA-N methanone Chemical compound O=[14CH2] WSFSSNUMVMOOMR-NJFSPNSNSA-N 0.000 description 1
- 229940055729 papain Drugs 0.000 description 1
- 235000019834 papain Nutrition 0.000 description 1
- 229940111202 pepsin Drugs 0.000 description 1
- 229920002401 polyacrylamide Polymers 0.000 description 1
- 229920001282 polysaccharide Polymers 0.000 description 1
- 239000005017 polysaccharide Substances 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 239000007974 sodium acetate buffer Substances 0.000 description 1
- 238000001179 sorption measurement Methods 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 238000011282 treatment Methods 0.000 description 1
- 229960005356 urokinase Drugs 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
Landscapes
- Immobilizing And Processing Of Enzymes And Microorganisms (AREA)
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP17574787A JPS6420087A (en) | 1987-07-13 | 1987-07-13 | Immobilization of enzyme or bacterium cell using chitosan-aldehyde gel as carrier |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP17574787A JPS6420087A (en) | 1987-07-13 | 1987-07-13 | Immobilization of enzyme or bacterium cell using chitosan-aldehyde gel as carrier |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JPS6420087A JPS6420087A (en) | 1989-01-24 |
| JPH0327198B2 true JPH0327198B2 (da) | 1991-04-15 |
Family
ID=16001545
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP17574787A Granted JPS6420087A (en) | 1987-07-13 | 1987-07-13 | Immobilization of enzyme or bacterium cell using chitosan-aldehyde gel as carrier |
Country Status (1)
| Country | Link |
|---|---|
| JP (1) | JPS6420087A (da) |
Families Citing this family (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| IL100096A (en) * | 1991-11-20 | 1996-03-31 | Univ Ramot | Method for entrapment of active materials in chitosan |
| CN1312991C (zh) * | 2005-10-19 | 2007-05-02 | 中国科学院海洋研究所 | 一种农业杀菌剂 |
Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS5745555A (en) * | 1980-09-01 | 1982-03-15 | Hitachi Metals Ltd | Electric charge type magnetic toner |
| JPS5849234A (ja) * | 1981-09-18 | 1983-03-23 | Bridgestone Corp | タイヤ成形機 |
| JPS5849234U (ja) * | 1981-09-30 | 1983-04-02 | 株式会社日立製作所 | マルチスリツト分光光度計 |
| JPS59213390A (ja) * | 1983-05-19 | 1984-12-03 | Asahi Denka Kogyo Kk | 固定化酵素及びその製造方法 |
-
1987
- 1987-07-13 JP JP17574787A patent/JPS6420087A/ja active Granted
Patent Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS5745555A (en) * | 1980-09-01 | 1982-03-15 | Hitachi Metals Ltd | Electric charge type magnetic toner |
| JPS5849234A (ja) * | 1981-09-18 | 1983-03-23 | Bridgestone Corp | タイヤ成形機 |
| JPS5849234U (ja) * | 1981-09-30 | 1983-04-02 | 株式会社日立製作所 | マルチスリツト分光光度計 |
| JPS59213390A (ja) * | 1983-05-19 | 1984-12-03 | Asahi Denka Kogyo Kk | 固定化酵素及びその製造方法 |
Also Published As
| Publication number | Publication date |
|---|---|
| JPS6420087A (en) | 1989-01-24 |
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