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J. Biochem, 1970, Vol. 68, No. 1 91-96
© 1970 Japanese Biochemical Society

research-article

Studies on the Substrate Specificity of Taka-amylase A

IV. The Mode of Action of Take-amylase A on Modified Pheny1{alpha}-Maltoside

Hitoshi ARITA, Mamoru ISEMURA, Tokuji IKENAKA and Yoshio MATSUHIMA

The Department of Chemistry, Osaka University College of Science Toyonaka

The action of Taka-amylase A [EC 3. 2.1.1] on the several derivatives of phenyl {alpha}maltoside was investigated and the comparative rates of the hydrolysis were determined by analyzing the reaction products. The enzymatic reaction products were detected by thin layer- and gas liquid chromatography. Any of the hydroxyl groups in the reducing-end glucose residue of phenyl a-maltoside, when modified as described in the text, made the enzymatic reaction inaccessible. Some information on the role of 6-position of the non reducing-end glucose residue was also obtained. The steric requirement of the 6-position of the reducing-end glucose residue seemed to be rather strict in comparison with that of the non reducing-end glucose residue.


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