Purification and Properties of β-Glucosidase from Aspergillus terreus

摘要: A β-glucosidase (EC 3.2.1.21) from the fungus Aspergillus terreus was purified to homogeneity as indicated by disc acrylamide gel electrophoresis. Optimal activity observed at pH 4.8 and 50°C. The had Km values of 0.78 0.40 mM for p-nitrophenyl-β-d-glucopyranoside cellobiose, respectively. Glucose a competitive inhibitor, with Ki 3.5 when used substrate. specific enzyme found be 210 IU 215 U per mg protein on cellobiose substrates, Cations, proteases, inhibitors little or no effect activity. glycoprotein containing 65% carbohydrate weight. It Stokes radius 5.9 nm an approximate molecular weight 275,000. affinity that isolated exhibited compared favorably obtained β-glucosidases other organisms being studied use in industrial cellulose saccharification.