Comparative Studies of Three Exo-β-Glycosidases of Aspergillus oryzae
1979 Volume 85 Issue 2 Pages 335-341
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1979 Volume 85 Issue 2 Pages 335-341
β-Glucosidase [β-D-glucoside glucohydrolase EC 3. 2. 1. 21] and β-galactosidase [β-D-galactoside galactohydrolase, EC 3. 2. 1. 23] of Takadiastase were purified by acetone fractionation, DEAE-cellulose, and hydroxylapatite chromatography.
Purity was confirmed by disc electrophoresis, ultracentrifugation and measurement of other glycosidase activities which coexisted in Takadiastase.
Molecular weight of the β-glucosidase was 218, 000 by sedimentation equilibrium and 110, 000-116, 000 by SDS-disc electrophoresis. Molecular weight of the β-galactosidase was 112, 000 by sedimentation and 56, 000-59, 000 by SDS-disc electrophoresis. These values showed that both enzymes consisted of two subunits. Taka-β-N-acetylglucosaminidase also consisted of two subunits.
Both enzymes were glycoproteins containing glucosamine and neutral sugar. Stability, pH optima, isoelectric points, and some specificities were observed.
