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Abstract
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Article Information:
Overexpression of D-psicose 3-epimerase from Clostridium cellulolyticum H10 in Bacillus subtilis and its Prospect for D-psicose Production
Xiaobo Li, Yueming Zhu, Yan Zeng, Tongcun Zhang and Yuanxia Sun
Corresponding Author: Yuanxia Sun
Submitted: September 13, 2012
Accepted: December 17, 2012
Published: March 15, 2013 |
Abstract:
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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.
Key words: 3-epimerase, Bacillus subtilis, Clostridium cellulolyticum , D-psicose, D-psicose food-grade, ,
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Abstract
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Cite this Reference:
Xiaobo Li, Yueming Zhu, Yan Zeng, Tongcun Zhang and Yuanxia Sun, . Overexpression of D-psicose 3-epimerase from Clostridium cellulolyticum H10 in Bacillus subtilis and its Prospect for D-psicose Production. Advance Journal of Food Science and Technology, (03): 264-269.
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ISSN (Online): 2042-4876
ISSN (Print): 2042-4868 |
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