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Characterization of ribose-5-phosphate isomerase converting d-psicose to d-allose from Thermotoga lettingae TMO

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Abstract

The gene coding for ribose-5-phosphate isomerase (Rpi) from Thermotoga lettingae TMO was cloned and expressed in E. coli. The recombinant enzyme was purified by Ni-affinity chromatography. It converted d-psicose to d-allose maximally at 75 °C and pH 8.0 with a 32 % conversion yield. The k m, turnover number (k cat), and catalytic efficiency (k cat k −1m ) for substrate d-psicose were 64 mM, 6.98 min−1 and 0.11 mM−1 min−1 respectively.

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Acknowledgments

This work was supported by the 973 Project (No. 2012CB720802), NSFC Project (No. 31171705 and 21276001), the 863 Project (No. 2011AA100904), and the Support Project of Jiangsu Province (No. BE2010678 and BE2010626).

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Authors and Affiliations

  1. State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, 214122, China

    Zaiping Feng, Wanmeng Mu & Bo Jiang

  2. School of Life Science and Engineering, Lanzhou University of Technology, Lanzhou, 730050, China

    Zaiping Feng

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  1. Zaiping Feng
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  2. Wanmeng Mu
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  3. Bo Jiang
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Correspondence to Bo Jiang.

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Feng, Z., Mu, W. & Jiang, B. Characterization of ribose-5-phosphate isomerase converting d-psicose to d-allose from Thermotoga lettingae TMO. Biotechnol Lett 35, 719–724 (2013). https://doi.org/10.1007/s10529-013-1136-3

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  • DOI: https://doi.org/10.1007/s10529-013-1136-3

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