K. Aisaka et al., PROPERTIES OF MALTOSE PHOSPHORYLASE FROM PROPIONIBACTERIUM-FREUDENREICHII, Journal of fermentation and bioengineering, 82(2), 1996, pp. 171-173
Maltose phosphorylase (EC 2.4.1.8) from Propionibacterium freudenreich
ii was purified and characterized. The enzyme catalyzed both the phosp
horolysis and the synthesis of maltose. In particular, in the syntheti
c reaction, the enzyme could use any of nine sugars other than D-gluco
se as a sugar acceptor, which resulted in the formation of new disacch
arides, in which the first carbon of D-glucose and the fourth carbon o
f the other sugar were connected by an a-glycosidic linkage.