Properties of maltose phosphorylase from Propionibacterium freudenreichii

Abstract Maltose phosphorylase (EC 2.4.1.8) from Propionibacterium freudenreichii was purified and characterized. The enzyme ctalyzed both the phosphorolysis and the synthesis of maltose. In particular, in the synthetic reaction, the enzyme could use any of nine sugars other than d -glucose as a sugar acceptor, which resulted in the formation of new disaccharides, in which the first carbon of d -glucose and the fourth carbon of the other sugar were connected by an α-glycosidic linkage.