Efficient biosynthesis of uridine diphosphate glucose from maltodextrin by multiple enzymes immobilized on magnetic nanoparticles.
Uridine diphosphate glucose (UDP-Glc) serves as a glucosyl donor in many enzymatic glycosylation processes.This paper describes a multiple enzyme, one-pot, biocatalytic system for the synthesis of UDP-Glc from low cost raw materials: maltodextrin and uridine triphosphate. Three enzymes needed for the synthesis of UDP-Glc (maltodextrin phosphorylase, glucose-1-phosphate thymidylytransferase, and pyrophosphatase)were expressed in Escherichia coli and then immobilized individually on aminofunctionalized magnetic nanoparticles. The conditions for biocatalysis were optimized and the immobilized multiple-enzyme biocatalyst could be easily recovered and reused up to five times in repeated syntheses of UDP-Glc. After a simple purification, approximately 630 mg of crystallized UDP-Glc was obtained from 1 l of reaction mixture, for a moderate yield of around 50% (UTP conversion) at very low cost.
Dong
Qing
Q
Laboratory of Biocatalysis and Bioprocessing, State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, 130 Meilong Road, Shanghai, PR China.
Ouyang
Li-Ming
LM
Yu
Hui-Lei
HL
Xu
Jian-He
JH
D004800:Enzymes, Immobilized / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics; D007700:Kinetics; D008280:Magnetics; D053758:Nanoparticles / Q000737:chemistry*; D011134:Polysaccharides / Q000378:metabolism*; D014532:Uridine Diphosphate Glucose / Q000096:biosynthesis*
D004800:Enzymes, Immobilized; D011134:Polysaccharides; C008315:maltodextrin; D014532:Uridine Diphosphate Glucose