Abstract
Coexpression of formate dehydrogenase (FDH) and ribitol dehydrogenase (RDH) in Escherichia coli was used for the synthesis of Allitol from D-psicose. FDH was coexpressed with RDH for continuous NADH regeneration. The results revealed that the optimum conditions for allitol production occurred at pH 7.0 and 30 °C. Allitol reached the maximum yield of 19.2 mg at 2.0% substrate concentration after 48 hours. Using D-psicose as a substrate, allitol was successfully produced using an engineered E. coli coexpressed with RDH and FDH.
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