Comparative studies of three exo-beta-glycosidases of Aspergillus oryzae.
beta-Glucosidase [beta-D-glucoside glucohydrolase EC 3.2.1.21] and beta-galactosidase [beta-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 beta-glucosidase was 218,000 by sedimentation equilibrium and 110,000-116,000 by SDS-disc electrophoresis. Molecular weight of the beta-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-beta-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.
D000118:Acetylglucosaminidase / Q000378:metabolism*; D000596:Amino Acids / Q000032:analysis; D001230:Aspergillus / Q000201:enzymology*; D001236:Aspergillus oryzae / Q000201:enzymology*; D005696:Galactosidases / Q000378:metabolism*; D005959:Glucosidases / Q000378:metabolism*; D006596:Hexosaminidases / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008970:Molecular Weight; D013379:Substrate Specificity; D001616:beta-Galactosidase / Q000302:isolation & purification / Q000378:metabolism*; D001617:beta-Glucosidase / Q000302:isolation & purification / Q000378:metabolism*
D000596:Amino Acids; D005696:Galactosidases; D005959:Glucosidases; D006596:Hexosaminidases; D001617:beta-Glucosidase; D001616:beta-Galactosidase; D000118:Acetylglucosaminidase