Abstract
The substrate specificity of purified Taka-maltase I was studied. The relative rates of hydrolysis of Taka-maltase I on maltose, α-methyl-D-glucoside, α-phenyl-D-glucoside, α-methyl-maltoside and α-phenyl-maltoside were 1, 0.0048, 0.092 0.0096 and 0.54, respectively. Amylose, sucrose, raffinose, trehalose, cellobiose and lactose were not attacked by this enzyme.
Taka-maltase I also showed the transglucosylase activity. Downward mutarotation of glucose produced by hydrolysis of maltose by this enzyme was observed.
The author wishes to express his gratitude to Prof. S. Akabori for his kind guidance throughout the study, and also wishes to thank the Sankyo Co. Ltd. for their kind supply of “Takadiastase Sankyo”.
