Antimicrobial Activity of Trypsin-Chymotrypsin Inhibitor from the Seeds of Mucuna pruriens

Protease inhibitors are proteins or peptides capable of inhibiting the catalytic activity of proteolytic enzymes and plants are the most abundant sources of which most of them studied and characterized were serine protease inhibitors. Protease inhibitors have been studied with a focus on their potential for biotechnology based pest control for agriculture. The trypsin -chymotrypsin inhibitor has been purified from the seeds of Mucuna pruriens employing ammonium sulfate fractionation, CM-cellulose chromatography and Sephadex G-100 chromatography. The purified Mucuna pruriens trypsin-chymotrypsin inhibitor showed a specific inhibitor activity of 474.66, fold purity of 99.51 and the yield obtained was 22.08%. The Mucuna pruriens trypsin-chymotrypsin inhibitor was inhibited both trypsin and chymotrypsin showing the double headed nature. Antifungal studies showed inhibitory activity against Aspergillus niger and Trichoderma viridae.