Characterization of Protease inhibitors from the seeds of Senna alata

Manifestations of metabolic disorders are greatly influenced by proteases in either up or down regulation of related biomarkers. Inhibition of these potential proteases results in better management of systemic disorders. Medicinal plants like Senna alata has been a great source of such protease inhibitors in which the current study was focused to isolate, purify and characterize inhibitors, more specifically, trypsin inhibitors. The protease inhibitors were isolated and purified employing conventional protein purification such as salt precipitation, gel filtration chromatography on Sephadex G-10 and G-50 and RP-HPLC. Two Senna alata protease inhibitors (SAPI-I and SAPI-II) were purified. SAPI-I was purified to 36.11 fold with a recovery of 42.80% and showed a specific inhibitor activity of 12.16. SAPI-II was purified to 41.23 fold with a recovery of 51.26 and showed a specific inhibitor activity of 19.61. Both the purified inhibitors were found to be stable in the pH range 5–8 and temperature between 4–65°C.