Partial Purification and Characterization of β-glucosidase from Monascus sanguineus

The aim of the present work was to study the production and characterization of beta-glucosidase from Monascus sanguineus. Agro-waste residues were screened to obtain the maximum yield of enzyme. Jack fruit seed was the best substrate for enzyme production. Studies on the optimization of pH and temperature showed acidic pH favorable for enzymatic activity, whereas the optimum temperature was 60 degrees C. Enzyme kinetics studies with different concentration of pNPG showed the calculated value of Km approximately 0.89 mM with the non-linear regression and 0.98 mM with the linear regression techniques. The enzyme was predominantly inhibited by KCl (69.8%) and moderately inhibited by CaCl2 (14.8%). Studies on the sensitivity for glucose showed that after 100 mM concentration of glucose, inhibition in pNPG hydrolysis took place. The molecular weight of the protein was estimated as 116 and 66 kDa with SDS-PAGE and zymography was carried out to verify the specific activity.