The properties of
Schizosacch. pombe α-glucosidase have been studied.
The preparation of α-glucosidase from
Schizosacch. pombe was fractionated into three fractions of peak I, II and III by DEAE-cel-lulose column chromatography, but in this experiments Peak III was used as enzyme.
The range of pH-optimum was 4.0_??_4.4 and optimal temperature was 45°C, The enzyme lost almost all the enzymatic activity at 55°C for 15min. and the range of pH-stability was 3.2_??_6.8 at 30°C for 20 hours.
The enzyme was capable of hydrolyzing more readily malto-oligosaccharides in comparison with other various saccharides, and even malto-heptaose and -octaose were attacked feebly. The rate of hydrolysis decreased in the followihg order: maltose, isomaltose, phenyl-α-glucoside, panose and turanose.
Accordingly, it was suggested that the sub-strate specificity of this enzyme was quite different from that of brewer's yeast (
Sacch. cerevisiae) α-glucosidase,
7) and it was similar to that of crystalline mold α-glucosidase.
8)
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