English  |  正體中文  |  简体中文  |  全文筆數/總筆數 : 18074/20272 (89%)
造訪人次 : 4074581      線上人數 : 865
RC Version 7.0 © Powered By DSPACE, MIT. Enhanced by NTU 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: https://ir.cnu.edu.tw/handle/310902800/27610


    標題: Enzymatic characterization of Bacillus licheniformis gamma-glutamyltranspeptidase fused with N-terminally truncated forms of Bacillus sp TS-23 alpha-amylase
    作者: Hu, Hui-Yu
    Yang, Jia-Ci
    Chen, Jiau-Hua
    Chi, Meng-Chun
    Lin, Long-Liu
    貢獻者: 食品科技系
    關鍵字: Bacillus Licheniformis
    Gamma-Glutamyltranspeptidase
    Autocatalytic Processing
    Alpha-Amylase
    Starch-Binding Domain
    日期: 2012-07-15
    上傳時間: 2014-03-21 16:15:10 (UTC+8)
    出版者: Elsevier Science Inc
    摘要: Bacillus licheniformis gamma-glutamyltranspeptidase (BIGGT) was fused at its C-terminal end with N-terminally truncated forms of Bacillus sp. TS-23 alpha-amylase. BIGGT and six fusion enzymes, BIGGT/SBD, BIGGT/AMY Delta N476, BIGGT/AMY Delta N443, BIGGT/AMY Delta N376, BIGGT/AMY Delta N195, and BIGGT/AMY Delta N34, were over-expressed in Escherichia coli M15 cells and purified to apparent homogeneity by metal-affinity chromatography. The fusion constructions had no significant effect on the autocatalytic processing of BIGGT. Progressive decrease in the GGT activity of fusion proteins was associated with an increasing level of truncation, and only BIGGT/AMY Delta N34 reserved the amylolytic activity. The protein fusions did not alter the optimal temperature and pH of BIGGT. However, as compared with the parental BIGGT, a significant change in circular dichorism and fluorescence spectra was observed in the fusion enzymes. Thermal unfolding of BIGGT, BIGGT/AMY Delta N476, BIGGT/AMY Delta N443, and BIGGT/AMY Delta N376 followed the two-state unfolding process with a transition point (T-m) of 61.3-63.1 degrees C, whereas BIGGT/AMY Delta N195 and BIGGT/AMY Delta N34 displayed two temperature transitions at 40.6 and 46.7 degrees C as well as at 62.8 and 62.9 degrees C, respectively. All of the fusion enzymes exhibited the raw-starch-binding ability, and the adsorbed proteins could be eluted from the adsorbent by 50 mM Tris-HCl (pH 9.0) containing 2% soluble starch. (c) 2012 Elsevier Inc. All rights reserved.
    關聯: Enzyme And Microbial Technology, 51(2), 86-94
    顯示於類別:[ 食品科技系 ] 期刊論文

    文件中的檔案:

    檔案 描述 大小格式瀏覽次數
    index.html0KbHTML1872檢視/開啟


    在CNU IR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 IR team Copyright ©   - 回饋