Characterization of alditol oxidase from Streptomyces coelicolor and its application in the production of rare sugars

A synthetic platform for the cascade synthesis of rare sugars using Escherichia coli whole cells was established. In the cascade, the donor substrate dihydroxyacetone phosphate (DHAP) was generated from glycerol by glycerol kinase (GK) and glycerol phosphate oxidase (GPO). The acceptor D-glyceraldehyde was directly produced from glycerol by an alditol oxidase. Then, the aldol reaction between DHAP and D-glyceraldehyde was performed by L-rhamnulose-1 -phosphate aldolase (RhaD) to generate the corresponding sugar-1-phosphate. Finally, the phosphate group was removed by fructose-1-phosphatase (YqaB) to obtain the rare sugars D-sorbose and D-psicose. To accomplish this goal, the alditol oxidase from Streptomyces coelicolor (AldO(S)(.coe)) was expressed in E. coli and the purified AldO(S)(.coe) was characterized. Furthermore, a recombinant E. coli strain overexpressing six enzymes including AldO(S)(.coe) was constructed. Under the optimized conditions, it produced 7.9 g/L of D-sorbose and D-psicose with a total conversion rate of 17.7% from glycerol. This study provides a useful and cost-effective method for the synthesis of rare sugars.