Quantitative Determination of Anomeric Forms of Sugar Produced by Amylases

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  • HIROMI KEITARO
    Laboratory of Biophysical Chemistry, College of Agriculture, University of Osaka Prefecture
  • SHIBAOKA TOSHIO
    Laboratory of Biophysical Chemistry, College of Agriculture, University of Osaka Prefecture
  • FUKUBE HIROYUKI
    Laboratory of Biophysical Chemistry, College of Agriculture, University of Osaka Prefecture
  • ONO SÔZABURO
    Laboratory of Biophysical Chemistry, College of Agriculture, University of Osaka Prefecture

Description

The anomer form of product maltose formed in the hydrolytic reaction of phenyl α-maltoside into phenol and maltose catalyzed by crystalline saccharifying α-amylase [EC 3.2. 1. 1] from Bacillus subtilis was determined quantitatively under the condition that the alternative pathway (hydrolysis into glucose and phenyl α-glucoside (1)) could be ignored.<br> The procedure involved continuous measurements of optical rotation change and of simultaneous phenol production during the reaction, which was carried out at 24.7°C, pH 5.4 and at 0.478mM substrate concentration.<br> It was quantitatively demonstrated that-fnaltose released from phenyl α-maltoside was exclusively of α-form, indicating that the configuration of the substrate linkage between glucose and phenyl residues was retained during the hydrolysis catalyzed by this enzyme.

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