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Biotechnol Lett. 2013 May;35(5):719-24. doi: 10.1007/s10529-013-1136-3. Epub 2013 Feb 6.

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

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

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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