Biochemical identification of D-mannose 2-epimerase from Cytophagaceae bacterium SJW1-29 for efficient bioconversion of D-glucose to D-mannose.

Enzymatic production of D-mannose attracts increasing attention because of the health effects and commercial values of D-mannose. Several kinds of epimerases or isomerases have been used for enzymatic production of D-mannose from D-glucose or D-fructose. D-Mannose epimerase (MEase), belonging to N-acyl-D-glucosamine 2-epimerase superfamily enzymes, catalyzes the C-2 epimerization between D-glucose and D-mannose. In this study, a novel MEase was identified from Cytophagaceae bacterium SJW1-29. Sequence and structure alignments indicate that it is highly conserved with the reported R. slithyformis MEase with the known crystal structure. It was a metal-independent enzyme, with an optimal pH of 8.0 and an optimal temperature of 40 °C. The specific activities on D-glucose and D-mannose were 2.90 and 2.96 U/mg, respectively. The K _m , k _cat , and k _cat /K _m on D-glucose were measured to be 194.9 mM, 2.72 s ^-1 , and 0.014 mM ^-1 s ^-1 , respectively. The purified enzyme produced 23.15 g/L of D-mannose from 100 g/L of D-glucose at pH 8.0 and 40 °C for 8 h, with a conversion rate of 23.15 %.
Competing Interests: Declaration of Competing Interest The authors declare that they have no known financial interests or personal relationships that could have influenced the work reported in this paper.
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