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題 名 | 應用殼糖胺多點式結合進行酪胺酸酶之固定化=The Immobilization of Tyrosinase on Chitosan by Multiple Point Attachment |
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作 者 | 吳鴻程; 朱惠鈴; 郭建民; 蕭介夫; | 書刊名 | 中國農業化學會誌 |
卷 期 | 36:4 1998.08[民87.08] |
頁 次 | 頁425-432 |
分類號 | 361.1925 |
關鍵詞 | 洋菇酪胺酸酶; 殼糖胺; 多點式結合; 固定化; Mushroom tyrosinase; Chitosan; Multiple point attachment; Immobilization; |
語 文 | 中文(Chinese) |
中文摘要 | 洋菇之酪胺酸脢以多點式之共價鍵結固定於臺灣盛產之不溶性擔體,即幾丁質之 衍生物殼糖胺, 以殼糖胺 - 碳二醯胺 - 戊二醛( Chitosan-carbodiimide-glutaraldehyde, CN-EDC-GA )系統進行固定化,每克擔體結合相 當 78.8mg 之可溶性酪胺酸脢活性。固定化酪胺酸脢對可溶性酵素之相對比活性,以 L- 酪 胺酸為基質時為 57%,以 L-DOPA 為基質時為 67%。固定化酪胺酸脢安最適 pH 值為 7.5, 比可溶性之酪胺酸脢高出 1.0 單位 pH,且其活性對 pH 變化較溶性酵素不敏感,固定化酪 酸脢之 pH 穩定性亦較溶性酵素為高,固定化之酪胺酸脢其最適之反應溫度為 70 ℃,比可 溶性酵素高出 20 ℃。 固定化酵素及可溶性酵素於 60 ℃時其熱變性速率常數 K, 分別為 0.0053 及 0.0172/h,可知固定化酵素於 60 ℃其熱穩定性為可溶性酵素 3.26 倍,固定化 酵素於 40 ℃時,具有良好之操作穩定性,其操作變性半衰期為 6.25 天。可知殼糖胺多點 式共價鍵結法提供高溫時酵素穩定性及酵素之操作穩定性。 |
英文摘要 | Mushroom tyrosinase was covalently coupled by multiple point attachment on chitosan, the product of which is abundant in Taiwan. The immobilization was performed using the chitosan-carbodiimide glutraldehyde (CN-EDC-GA) system. Saturation of the support was reached at an activity equivalent to 78.8 mg soluble tyrosinase per gram chitosan. The relative specific activity of the immobilized tyrosinase to soluble enzyme with L-tyrosine as the substrate was 57% while that with L-DOPA as the substrat was 67%. The optimal pH of immobilized tyrosinase was 7.5, which was 1.0 pH unit higher than that of the soluble form. The activity of the former was less pH sensitive than that of the latter. The immobilized tyrosinase also exhibited higher pHdtability than did the soluble form. The optimal temperature of immobilized tyrosinase was 70 ℃ ,which was 20 ℃ higher than that of the solubel form. The activity of the former less temperature sensitive than that of the latter. The thermal stability of immobilized tyrosinase was higher than that of the soluble form. The denaturation rate constants of immobilized tyrosinase and the soluble form at 60 ℃ were 0.0053/h and 0.0172/h, respectively. Therfore, the immobilized tyrosinase was 3.26 times more stable than the soulble form at this temperature. Moreover, the immobilized tyrosinase showed the best operation stability with a denaturation half life of 6.25 days at 40 ℃. In conclusion, the multiple attachment of tyrosinase on chitosan greatly enhanced the stability of the enzyme against thermal denaturation. |
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