Protease Inhibitors from the seeds of Senna sophera: Isolation and Properties

Need for protease inhibitors in medicinal and therapeutic applications have been well acknowledged by the research community. The natural flora has always been an extensive contributor for various compounds used in disorder treatment owing to its abundance and ease of isolation and purifications methodologies. Conventional protein purification methods such as salt precipitation, gel filtration chromatography on Sephadex G-10 and G50 and RP-HPLC have been employed for the purification of protease inhibitors from the seeds of Senna sophera. Two protease inhibitors SSPI-1 and SSPI-2 were purified. The protease inhibitor SSPI-1 was purified to 16.11 fold with a recovery of 26.20% and showed a specific inhibitor activity of 31.12. SSPI-2 was purified to 61.08 fold with a recovery of 66.23 and showed a specific inhibitor activity of 24.51. Both the purified inhibitors were found to be stable in the pH range 2 – 10 and temperature between 4 – 65°C.