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

β-glucosidases have attracted considerable attention in recent years due to their important roles invarious biotechnological processes such as hydrolysis of isoflavone glucosides, the production of fuelethanol from agricultural residues, the release of aromatic compounds from flavorless precursors, among others.In this study, extracellular β-glucosidase induced by cellulose from Penicillium commune ITV01 was purifiedto homogeneity by electrofocusing (IEF) and Sephadex G-100 gel filtration. The enzyme was characterized andthe molecular weight was 144.2 kDa as estimated by SDS-PAGE. The isoelectric point determined by IEF was4.73 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 and50°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++. -glucosidasewas completely inhibited by Hg++. In conclusion, the novel -glucosidase purified from P. commune showsgreat potential for biotechnological uses.

کلیدواژه ها:

Purification ، Glucosidase ، Peniclillium ، Hydrolase ، Fungi ، Cellulolytic activity