A novel metalloprotease from banana peel and its biochemical characterization.

Protein cleaving enzymes, called proteases are one of the most commercially used enzymes possessing extensive applications in various industries. The present study was focused on screening, extraction, purification and characterization of protease from banana peel. Twelve different varieties of banana peels were screened for the protease activity. The maximum activity of the isolated enzyme was 230.4 CDU/mg from Nendran banana. The crude enzyme was purified up to 8.1 fold with the yield of 61.34%. The molecular weight of the purified fraction was found to be 40 kDa. The optimum conditions for maximum protease activity were achieved at 30 °C and pH 7. The Lineweaver-Burk plot exhibited the kinetic parameters of the enzyme such as V_max and K_m as 588.4 CDU/mg and 15.2 mg/ml respectively. The influence of different inhibitors, metal ions, organic solvents, detergents, oxidising agents and salinity were examined. The collagenolytic activity was tested with purified type I collagen as a substrate. The enzyme was tested for cell cytotoxicity, detection of apoptosis using fluorescent dyes and antitumor activity. The results demonstrated that protease from banana peel was of high significance and potential for usage in therapeutic for breaking down collagen/peptide bonds.