ANTIBACTERIAL ACTIVITY OF A TRYPSIN-CHYMOTRYPSIN-ELASTASE INHIBITOR ISOLATED FROM LAVATERA CASHMERIANA CAMB.SEEDS

Authors: S. Rakashanda, M. Ishaq, A. Masood, S. Amin
Journal: Journal of Animal and Plant Sciences (JAPS)
ISSN: 1018-7081 (Print), 2309-8694 (Online)
Volume: 22  Issue: 4  Pages: 983-986
Year: 2012
DOI: NA
URL: https://doi.org/NA
Publisher: Pakistan Agricultural Scientists Forum

Abstract:
<p>Protease inhibitors were extracted from the seeds of&nbsp;<em>Lavatera cashmeriana</em>&nbsp;Cambby ammonium sulphate precipitation and purified by chromatography on DEAE-cellulose and Sephadex G-100 column. The bound protein eluted into four major peaks which we named as LC-pi I, II, III and IV, all showing strong anti protease activity against trypsin, chymotrypsin and elastase. LC-pi I was screened for antibacterial activity against&nbsp;<em>Klebsiella pnuemoniae, &nbsp;Escherichia coli</em>&nbsp;and&nbsp;<em>Pseudomonas aeruginosa</em>. The protease inhibitor showed strong antibacterial activity against&nbsp;<em>Klebsiella pnuemoniae &nbsp;</em>and&nbsp;<em>Pseudomonas aeruginosa</em>&nbsp;but was less active against&nbsp;<em>&nbsp;Escherichia&nbsp; coli</em>.</p>

Keywords: Lavatera cashmeriana Camb, antibacterial activity, LC-pi I, nutrient agar.