抄録
1. The hydrolytic reaction of phenyl β-maltoside catalyzed by saccharifying α-amylase [EC 3. 2. 1. 1] of Bacillus subtilis was studied at 25°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 β-maltoside at the glucosidic linkage between the two glu-cose residues to form D-glucose and phenyl β-D-glucoside. Besides these products, maltose, maltotriose, and phenyl β-maltotrioside were also observed as reaction products. The identifi-cation of phenyl β-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.
