Efficient biosynthesis of uridine diphosphate glucose from maltodextrin by multiple enzymes immobilized on magnetic nanoparticles.
Carbohydr Res
; 345(11): 1622-6, 2010 Jul 19.
Article
en En
| MEDLINE
| ID: mdl-20627237
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.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Polisacáridos
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Uridina Difosfato Glucosa
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Enzimas Inmovilizadas
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Nanopartículas
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Magnetismo
Idioma:
En
Revista:
Carbohydr Res
Año:
2010
Tipo del documento:
Article
Pais de publicación:
Países Bajos