Abstract
The rpiB gene, encoding ribose-5-phosphate isomerase (RpiB) from Clostridium thermocellum, was cloned and expressed in Escherichia coli. RpiB converted d-psicose into d-allose but it did not convert d-xylose, l-rhamnose, d-altrose or d-galactose. The production of d-allose by RpiB was maximal at pH 7.5 and 65°C for 30 min. The half-lives of the enzyme at 50°C and 65°C were 96 h and 4.7 h, respectively. Under stable conditions of pH 7.5 and 50°C, 165 g d-allose l−1 was produced without by-products from 500 g d-psicose l−1 after 6 h.
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This study was supported by the Second Phase of Brain Korea 21 Project (Ministry of Education & Human Resources Development) and by Grant R01-2004-000-10012-0 from the Basic Research Program of the Korea Science & Engineering Foundation (KOSEF).
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Park, CS., Yeom, SJ., Kim, HJ. et al. Characterization of ribose-5-phosphate isomerase of Clostridium thermocellum producing d-allose from d-psicose. Biotechnol Lett 29, 1387–1391 (2007). https://doi.org/10.1007/s10529-007-9393-7
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DOI: https://doi.org/10.1007/s10529-007-9393-7