Proteinaceous Protease Inhibitor from Lawsonia inermis: Purification, Characterization and Antibacterial Activity

作者：Dabhade Arvind; Patel Priti; Patil Ulhas^*

来源：Natural Product Communications, 2013, 8(10): 1467-1470.

• Staphylococcus aureus
• Pseudomonas aeruginosa
• Papain
• Trypsin
• Pepsin
• Metallo-protease

A thermo-stable, proteinaceous protease inhibitor (LPI) from Lawsonia inermis is reported. The LPI was purified from Lawsonia inermis seeds by subsequent ammonium sulfate precipitation, ion exchange chromatography (DEAE-Cellulose) and gel permeation chromatography (Sephadex-50). The purified protease inhibitor is effective against a wide range of proteases viz. papain, trypsin, pepsin and metallo-protease. The apparent molecular weight of the protease inhibitor is 19 kDa, determined by SDS-PAGE electrophoresis. The protease inhibitor was found to be stable at 70 degrees C for 30 min. It was also examined for antibacterial activity against Pseudomonas aeruginosa MTCC 7926 and Staphylococcus aureus NCIM 2079; the IC50 values of the purified LPI were 11.4 mu g/mL and 16.6 mu g/mL respectively.

• 出版日期2013-10