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：3
页码：264-269
DOI：10.19026/ajfst.5.3255
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 Co2+, can make the enzyme more thermostable. The Michaelis-Menten constant (K m ) 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.
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