MilliporeSigma
  • Home
  • Search Results
  • Characterization of alditol oxidase from Streptomyces coelicolor and its application in the production of rare sugars.

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

Bioorganic & medicinal chemistry (2020-04-07)
Zhou Chen, Zijie Li, Fen Li, Ning Wang, Xiao-Dong Gao
ABSTRACT

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 (AldOS.coe) was expressed in E. coli and the purified AldOS.coe was characterized. Furthermore, a recombinant E. coli strain overexpressing six enzymes including AldOS.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.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
D-(+)-Glyceraldehyde, ≥98.0% (HPLC), viscous
Sigma-Aldrich
Nitrilotriacetic acid disodium salt, Sigma Grade, ≥99%
Sigma-Aldrich
D-Psicose, ≥95%