| dc.description.abstract | The inability of the plant and animal proteases to meet current world demands has led to an increased interest in microbial proteases. The purpose of this research was to purify and characterize microbial protease from B19 KUB BPPT CC isolate. The isolate were grown in media containing calcium caseinate agar 0.5%, urea 0.5%, and yeast extract 0.05%. Extracelluler protease from B19 KUB BPPT CC isolate was purified using amonium sulfate precipitation and dialysis. The protease was purified 8.37 fold with a recovery by 60% amonium sulfate precipitation. This thermophilic alkaline protease showed a pH optimum of 9.0 and optimum temperature was 60 °C. Phenylmethanesulfonyl-fluoride (PMSF) completely inhibited the enzyme activity suggesting that it was serine protease. Among metal ions, the Na+ ions enhanced activity up to 119.93%. The Km and Vmax values exhibited by purified protease were 0.021 mM and 90.91 U/mgusing casein as substrate. The molecular weight was estimated to be 33.8 kDa and 19.7 kDa on casein zymography. In addition, this enzyme was capable of hydrolyzing bovine serum albumin (BSA), gelatin, hemoglobin, casein, and collagen | en |
