Purification and Biochemical Characterization of a β-glucosidase from Penicillium commune ITV01

glucosidases have attracted considerable attention in recent years due to their important roles in various biotechnological processes such as hydrolysis of isoflavone glucosides, the production of fuel ethanol from agricultural residues, the release of aromatic compounds from flavorless precursors, among others. In this study, extracellular -glucosidase induced by cellulose from Penicillium commune IT 01 was purified to homogeneity by electrofocusing (IEF) and Sephadex G-100 gel filtration. The enzyme was characterized and the molecular weight was 144.2 kDa as estimated by SDS-PAGE. The isoelectric point determined by IEF was 4.73 and the enzyme was able to hydrolyze cellobiose and cellulose to glucose but not laminarine, xylan, starch, pullulan, colloidal chitin and carboxymethyl-cellulose. Optimal pH and temperature were detected at 5.0 and 50°C, respectively. Stability was observed at temperatures 30 to 50°C and pH values between 5 and 7 for 24 h. Enzyme activity was activated by K+, Cu+, Mn++, Fe++, Cu++, Ca++ ions and significantly by Co++. -glucosidase was completely inhibited by Hg++. In conclusion, the novel -glucosidase purified from P. commune shows great potential for biotechnological uses.