Kinetics and Mechanism of Hydrolysis of Phenyl a-Maltoside by Saccharifying a-Amylase of Bacillus subtilis

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Abstract
1. The hydrolytic reaction of phenyl cr-maltoside catalyzed by crystalline saccharifying α-amylase [EC 3.2.1.1] of B. subtilis was studied at 25° and pH 5.4 by the measurements of total reducing value and the amounts of phenol produced and also by thin-layer chromato-graphy. 2. The hydrolytic reaction was found to involve two parallel processes; first, the hydrolysis between phenol and glucose residues to produce phenol and maltose, and the second, the hydrolysis between two glucose residues to produce glucose and phenyl α-glucoside. At lower substrate concentration, the first process is predominant, while the second becomes evident at higher substrate concentrations. 3. At higher substrate concentrations, the intermedial production of maltotriose was shown by thin-layer and paper chromatography. The maltotriose was also identified by optical rotatory dispersion, rates of hydrolyses by gluc-amylase and Taka-amylase A. A possibility of transglucosidation of this enzyme was suggested.

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