Characterization of ribose-5-phosphate isomerase converting d-psicose to d-allose from Thermotoga lettingae TMO |
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| Authors: | Zaiping Feng Wanmeng Mu Bo Jiang |
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| Institution: | 1. State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, 214122, China
2. School of Life Science and Engineering, Lanzhou University of Technology, Lanzhou, 730050, China
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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 m ?1 ) for substrate d-psicose were 64 mM, 6.98 min?1 and 0.11 mM?1 min?1 respectively. |
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