English  |  正體中文  |  简体中文  |  全文筆數/總筆數 : 52047/87178 (60%)
造訪人次 : 8676017      線上人數 : 60
RC Version 7.0 © Powered By DSPACE, MIT. Enhanced by NTU Library & TKU Library IR team.
搜尋範圍 查詢小技巧:
  • 您可在西文檢索詞彙前後加上"雙引號",以獲取較精準的檢索結果
  • 若欲以作者姓名搜尋,建議至進階搜尋限定作者欄位,可獲得較完整資料
  • 進階搜尋
    請使用永久網址來引用或連結此文件: http://tkuir.lib.tku.edu.tw:8080/dspace/handle/987654321/61698


    題名: Purification and Characterization of a Chitosanase and a Protease by Conversion of Shrimp Shell Wastes Fermented by Serratia Marcescens Subsp. Sakuensis TKU019
    作者: Liang, Tzu-Wen;Kuo, Yi-Hsuan;Wu, Pei-Chen;Wang, Chuan-Lu;Dzung, Nguyen Anh;Wang, San-Lang
    貢獻者: 淡江大學化學學系
    關鍵詞: Chitosanase;Protease;Serratia marcescens subsp;Sakuensis;Shrimp shell wastes
    日期: 2010-08-01
    上傳時間: 2013-02-27 09:32:05 (UTC+8)
    出版者: 臺北市:中國化學會
    摘要: A chitosanase and a protease were purified from the culture supernatant of Serratia marcescens subsp. sakuensis TKU019 with shrimp shell as the sole carbon/nitrogen source. The culture condition suitable for production of chitosanase was found to be shaken at 37˚C for 3 days in 100 mL of medium containing 0.5% shrimp shell powder, 0.1% K2HPO4 and 0.05% MgSO4‧7H2O at pH 7. The TKU019 chitosanase was suppressed by the simultaneously existing protease, which also showed the maximum activity at the third day of incubation. The molecular masses of the chitosanase and protease determined by SDS-PAGE were approximately 36 kDa and 58 kDa, respectively. Cu2+, Mn2+ and Zn2+ inhibited the chitosanase activity, and all of
    tested divalent metals inhibited in the protease activity. The optimum pH, optimum temperature, pH stability, and thermal stability of the chitosanase was pH 7, 60˚C, pH 4–7, and < 60˚C, respectively. The optimum pH, optimum temperature, pH stability, and thermal stability of the protease was pH 10, 50˚C, pH 5-10, and < 50˚C, respectively. Tween 40 (2%, v/v) had stimulatory effect on TKU019 protease activity.
    關聯: Journal of the Chinese Chemical Society=中國化學會會誌 57(4)pt.B, pp.857-863
    DOI: 10.1002/jccs.201000119
    顯示於類別:[化學學系暨研究所] 期刊論文

    文件中的檔案:

    檔案 大小格式瀏覽次數
    index.html0KbHTML211檢視/開啟

    在機構典藏中所有的資料項目都受到原著作權保護.

    TAIR相關文章

    DSpace Software Copyright © 2002-2004  MIT &  Hewlett-Packard  /   Enhanced by   NTU Library & TKU Library IR teams. Copyright ©   - 回饋