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Immobilization of α-Chymotrypsin and Other Enzymes on Acylchitosan
https://doi.org/10.57375/00001763
https://doi.org/10.57375/000017631a837ecf-14ef-4026-9db1-5e774168a5e6
| 名前 / ファイル | ライセンス | アクション |
|---|---|---|
KJ00002498530.pdf (472.7 kB)
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| Item type | 紀要論文 / Departmental Bulletin Paper(1) | |||||
|---|---|---|---|---|---|---|
| 公開日 | 2009-04-10 | |||||
| タイトル | ||||||
| タイトル | Immobilization of α-Chymotrypsin and Other Enzymes on Acylchitosan | |||||
| 言語 | ||||||
| 言語 | eng | |||||
| 資源タイプ | ||||||
| 資源タイプ識別子 | http://purl.org/coar/resource_type/c_6501 | |||||
| 資源タイプ | departmental bulletin paper | |||||
| ID登録 | ||||||
| ID登録 | 10.57375/00001763 | |||||
| ID登録タイプ | JaLC | |||||
| 著者 |
KUSAOKE, Hideo
× KUSAOKE, Hideo |
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| 抄録 | ||||||
| 内容記述タイプ | Abstract | |||||
| 内容記述 | α-Chymotrypsin has been immobilized on acylchitosan, a chitosan derivative, using glutaraldehyde as an intermediate reagent ; the activity of the immobilized enzyme on acylchitosan was much higher than that on chitosan. The increase of the degree of substitution of acyl groups in acylchitosan as support was effective for the enzyme activity. The retained maximum activity of immobilized α-chymotrypsin was approximately 60% that of the native enzyme, obtained by the use of the butyrylchitosan with the degree of substitution of butyryl groups of 0.87. Immobilized α-chymotrypsin showed a significant changes in optimal temperature and heat stability. The pH optimum of the fixed α-chymotrypsin was simillar to that of native enzyme. Immobilized α-amylase and invertase on acylchitosan also showed a slight higher enzyme activity than that on chitosan. | |||||
| 書誌情報 |
福井工業大学研究紀要 号 16, p. 197-205, 発行日 1986 |
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| 出版者 | ||||||
| 出版者 | 福井工業大学 | |||||
| ISSN | ||||||
| 収録物識別子タイプ | ISSN | |||||
| 収録物識別子 | 2868571 | |||||
| 書誌レコードID | ||||||
| 識別子タイプ | NCID | |||||
| 関連識別子 | TF00011822 | |||||
| 著者版フラグ | ||||||
| 出版タイプ | VoR | |||||
| 出版タイプResource | http://purl.org/coar/version/c_970fb48d4fbd8a85 | |||||
