Protease inhibitors from broad bean isolation and purification |
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Authors: | A.S. Warsy G. Norton M. Stein |
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Affiliation: | Department of Applied Biochemistry and Nutrition, University of Nottingham School of Agriculture, Sutton Bonington, Loughborough, Leics. LE12 5RD U.K. |
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Abstract: | Four protease inhibitors were demonstrated and two, BBPI-1 and BBPI-2, were purified from broad bean seeds using a combination of (NH4)2SO4 fractionation, ion-exchange chromatography on CM 52-cellulose and CM 50 Sephadex. BBPI-1 and 2 had broad specificity and inhibited trypsin, chymotrypsin, thrombin, pronase and papain. Both inhibitors were heat stable, had a wide pH tolerance, a MW of approximately 11 000 and contained 14·5% N. BBPI-1 and 2 had a pI of 8·5 and 7·5 respectively. |
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Keywords: | Leguminosae broad bean protease inhibitors isolation purification properties. |
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