期刊論文
| 學年 | 98 |
|---|---|
| 學期 | 1 |
| 出版（發表）日期 | 2009-12-01 |
| 作品名稱 | Conversion and degradation of shellfish wastes by Serratia sp. TKU016 fermentation for the production of enzymes and bioactive materials |
| 作品名稱（其他語言） | |
| 著者 | Wang, San-Lang; Chang, Tao-Jen; Liang, Tzu-Wen |
| 單位 | 淡江大學生命科學研究所 |
| 出版者 | Dordrecht: Springer Netherlands |
| 著錄名稱、卷期、頁數 | Biodegradation 21(3), pp.321-333 |
| 摘要 | A chitosanase and a protease were purified from the culture supernatant of Serratia sp. TKU016 with shrimp shell as the sole carbon/nitrogen source. The molecular masses of the chitosanase and protease determined by SDS–PAGE were approximately 65 and 53 kDa, respectively. The chitosanase was inhibited completely by Mn2+, but the protease was enhanced by all of tested divalent metals. The optimum pH, optimum temperature, pH stability, and thermal stability of the chitosanase and protease were (pH 7, 50°C, pH 6–7, <50°C) and (pH 8–10, 40°C, pH 5–10, <50°C), respectively. SDS (2 mM) had stimulatory effect on TKU016 protease activity. The result demonstrates that TKU016 protease is SDS-resistant protease and probably has a rigid structure. Besides, TKU016 culture supernatant (2% SPP) incubated for 2 days has the highest antioxidant activity, the DPPH scavenging ability was about 76%. With this method, we have shown that shrimp shell wastes can be utilized and it’s effective in the production of enzymes, antioxidants, peptide and reducing sugar, facilitating its potential use in biological applications and functional foods. |
| 關鍵字 | Antioxidant activity;Chitosanase;Protease;Serratia sp.;Shrimp shell wastes |
| 語言 | en |
| ISSN | 0923-9820 |
| 期刊性質 | 國外 |
| 收錄於 | SCI EI |
| 產學合作 | |
| 通訊作者 | Wang, San-Lang; Liang, Tzu-Wen |
| 審稿制度 | |
| 國別 | NLD |
| 公開徵稿 | |
| 出版型式 | 紙本 |
| 相關連結 |
機構典藏連結 ( http://tkuir.lib.tku.edu.tw:8080/dspace/handle/987654321/61848 ) |