Abstract: α-D-Glucose-1-phosphate (Glc-1-P) is an expensive intermediate in the biosynthesis of nucleotide glucose. This paper describes a biocatalytic system for the efficient synthesis of Glc-1-P from the low cost raw materials: maltodextrin and phosphate at ordinary tempera-tures. After molecular cloning and the expression of a maltodextrin phosphorylase (MalPase) gene from E. coli (Escherichia coli) K12, the resultant recombinant enzyme was immobilized on amino-functionalized magnetic nanoparticles for recycling and repeated use. Conditions for the biocatalytic reaction were optimized and the immobilized MalPase could be easily recovered and reused over eight cycles in the re-peated synthesis of Glc-1-P. After simple purification steps approximately 440 mg of crude product was obtained with a moderate isolation yield of 70.5%.

Key words: α-D-Glucose-1-phosphate, maltodextrin phosphorylase, maltodextrin, magnetic nanoparticle, immobilized biocatalyst