Whole Cell Catalytic Synthesis of D-glyceraldehyde by Recombinant Escherichia Coli
D-glyceraldehyde plays an important role in the synthesis of pharmaceuticals,agrochemicals,and natural products.By transforming the alditol oxidase gene of Streptomyces coelicolor,the recombinant expression was carried out in E.coli Rosetta(DE3)strain,and glycerol was converted into D-glyceraldehyde by whole-cell catalysis.Compared with the traditional method,this method is green,safe and efficient.The induction conditions affecting protein expression were optimized by single factor.The reac-tion conditions affecting whole cell catalysis were also studied.The results showed that the relative enzyme activity of the engi-neered E.coli pET-28a(+)-aldO strain was the highest at an inducer IPTG concentration of 0.2 mmol/L,induction temperature of 28℃,and induction time of 6 h.When the bacterial optical density(OD600)is 10,the buffer pH is 7.5,the reaction temperature is 30℃,and the reaction time is 60 minutes,the conversion rate of glycerol can reach 46%,laying the foundation for the biosynthe-sis of D-glyceraldehyde.