首页    期刊浏览 2024年11月30日 星期六
登录注册

文章基本信息

  • 标题:Overexpression of D-psicose 3-epimerase from Clostridium cellulolyticum H10 in Bacillus subtilis and its Prospect for D-psicose Production
  • 本地全文:下载
  • 作者:Xiaobo Li ; Yueming Zhu ; Yan Zeng
  • 期刊名称:Advance Journal of Food Science and Technology
  • 印刷版ISSN:2042-4868
  • 电子版ISSN:2042-4876
  • 出版年度:2013
  • 卷号:5
  • 期号:03
  • 页码:264-269
  • 出版社:MAXWELL Science Publication
  • 摘要:The aim of this study was to overexpress the D-psicose 3-epimerase from Clostridium cellulolyticum H10 in food-grade microbe. This gene was cloned and expressed in Bacillus subtilis The results showed that the recombinant protein was soluble, bioactive, and expressed at high levels. The optimum pH and temperature of the enzyme were 8.0 and 50°C, respectively. The activity of the enzyme was not dependent on metal ions; however, some metal ions, such as Co, make the enzyme more thermostable. The Michaelis-Menten constant (Km) of the enzyme for D-psicose was much lower than that for D-tagatose, suggesting that the optimum substrate of the enzyme is D-psicose. D-Psicose 3-epimerase expressed in the food-grade B. subtilis may be used for the industrial production of D-psicose.
  • 关键词:3-epimerase; Bacillus subtilis; Clostridium cellulolyticum ; D-psicose; D-psicose food-grade; ;
国家哲学社会科学文献中心版权所有