Purification and characterization of the intracellular beta-glucosidase from Aureobasidium sp ATCC 20524

beta-Glucosidase hydrolyzing cellobiose was extracted from Aureobasidiom sp ATCC 20524 and purified to homogeneity. The molecular mass was estimated t o be about 331 kDa. The enzyme contained 26.5% (w/w) carbohydrate. The opti mum pH and temperature for the enzyme reaction were pH 4 and 80 degrees C, respectively. The enzyme was stable at a wide range of pH, 2.2-9.8, after 3 h and at 75 degrees C for 15 min. The kinetic parameters were determined. The enzyme was relatively stable against typical organic enzyme inhibitors. The enzyme also hydrolyzed gentiobiose, p-nitrophenyl-beta-glucoside and s alicin.