AbstractThe filamentous fungus Aspergillus terreus was cultivated in a 2-L stirred tank bioreactor, and the resulting culture filtrate was used for protein purification. From the cultivation broth, seven crude extracts of glucanase and one of β-glucosidase were purified. A total of eight components were identified, including endoglucanases (Endo I, II, III, and IV), cellobiohydrolases (CBH I, II, and III), and β-glucosidase. The eight major components in the fermentation broth of A. terreus, which most likely constitute the essential enzymes for cellulose hydrolysis, were further purified by a series of column chromatography steps. Interestingly, the β-glucosidase from A. terreus displayed an extremely high activity on p-nitrophenyl-β-D-glucopyranoside (pNPG), which suggests that it is a good candidate enzyme for the conversion of cellobiose to glucose. The temperature and pH ranges for optimal activity of the purified enzyme were 46 to 62 °C and 5.0 to 6.0, respectively.