Hydrolysis of phenyl beta-maltoside catalyzed by saccharifying alpha-amylase from Bacillus subtilis

1. The hydrolytic reaction of phenyl beta-maltoside catalyzed by saccharifying alpha-amylase [EC 3.2.1.1] of Bacillus subtilis was studied at 25 degrees C and pH 5.4, by measuring the total reducing power and the amount of phenol liberated, and by thin layer chromatography. 2. The enzyme hydrolyzed phenyl beta-maltoside at the glucosidic linkage between the two glucose residues to form D-glucose and phenyl beta-D-glucoside. Besides these products, maltose, maltotriose, and phenyl beta-maltotrioside were also observed as reaction products. The identification of phenyl beta-maltotrioside is described in detail. The formation of these products was attributed to the transglycosylation reaction of the enzyme. The time course of reaction as followed by reducing power measurement showed an induction period of several minutes.