Characterization of Protease Inhibitors from the Seeds of Adenanthera Pavonina

摘要

Enzyme inhibitors such as protease inhibitors are widely distributed in nature inhibit the catalytic activity of proteolytic enzymes. They involved in variety of proteolytic process of biological/physiological significance. The protease inhibitors, APPI-1, APPI-2and APPI-3 have been isolated and purified from the seeds of Adenanthera pavonina employing salt fractionation, Sephadex G-10 and Sepahdex G-50 gel-permeation chromatography and RP-HPLC. The APPI-1, APPI-2and APPI-3 was purified to 31.24, 36.02 and 19.21 fold with a recovery of 41.10%, 51% and 43.28%, respectively. Further, APPI-1, APPI-2and APPI-3 showed a specific inhibitor activity of 16.15, 20.43 and 11.06, respectively. The purified APPI-1, APPI-2and APPI-3 showed a molecular weight of7 - 8 kDa, 11 -12 kDa and 13-14 kDa (approximately) as determined by gel filtration chromatography. All the three purified inhibitors are both pH and temperature stable. The APPI-1, APPI-2and APPI-3 showed antimicrobial activity on E.coli and streptococcus species.