Efficient biosynthesis of uridine diphosphate glucose from maltodextrin by multiple enzymes immobilized on magnetic nanoparticles

被引：22

作者：

Dong, Qing ^{[1
]}

Ouyang, Li-Ming ^{[1
]}

Yu, Hui-Lei ^{[1
]}

Xu, Jian-He ^{[1
]}

机构：

[1] E China Univ Sci & Technol, Lab Biocatalysis & Bioproc, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China

来源：

CARBOHYDRATE RESEARCH | 2010年 / 345卷 / 11期

关键词：

UDP-Glc; Biocatalytic synthesis; One-pot; Magnetic nanoparticles; Immobilized biocatalyst; LIPASE;

D O I：

10.1016/j.carres.2010.04.025

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 amino-functionalized 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 1l of reaction mixture, for a moderate yield of around 50% (UTP conversion) at very low cost. (C) 2010 Elsevier Ltd. All rights reserved.

引用

页码：1622 / 1626

页数：5

共 20 条

[1] Facile synthesis of glucose-1-phosphate from starch by Thermus caldophilus GK24 α-glucan phosphorylase [J].