Biochemical Characterization Of A Partially Purified Protease Fromaspergillus Terreus7461 And Its Application As An Environmentally Friendly Dehairing Agent For Leather Industry

Proteases can be used in several biotechnological processes including detergent, food and leather industries. In the leather industry, dehairing is carried out by chemicals, which pollute the environment. Therefore, to make the hair removal process environmentally friendly, a protease produced byAspergillus terreushas been purified, biochemically characterized and had an efficient ability to remove hair from bovine leather. The protease was produced using 1% wheat bran and was purified 2.3-fold using two chromatographic steps showing a molecular weight of 90 kDa. Optimal temperature and pH were 50 degrees C and 6.5, respectively. Thermal stability was up to 1 h at 50 degrees C. Protease was stable to detergents like Tween 80 and to organic solvents. The activity was activated by Ca(2+)and inhibited by Hg(2+)and Cu2+. The enzyme was classified as serine protease, by the inhibition by PMSF and was stable to reducing agents. It hydrolyzed casein, azocasein, BSA, egg albumin and BTpNA. The Km and Vmax values were 0.65 +/- 0.03 mg/mL and 3.66 +/- 0.18 mu mol/min, respectively. Remarkable properties about temperature, pH, stability to detergents and reducing agents ensure that the protease fromA. terreuscan be an excellent candidate for industrial applications, particularly in the leather industry.