ISSN: 0973-7510

E-ISSN: 2581-690X

Kempohalli S. Chandrashekharaiah
1Department of Biotechnology, PES Institute of Technology, BSK III Stage, Bangalore – 560 085, India.
J Pure Appl Microbiol. 2013;7(3):2405-2410
© The Author(s). 2013
Received: 25/01/2013 | Accepted: 02/03/2013 | Published: 30/09/2013

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.


Mucuna pruriens, seeds, Trypsin inhibitor, antifungal properties

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