In Vitro Digestibility of Dry Bean (Phaseolus Vulgaris L.) Proteins: The Role of Heat‐Stable Protease Inhibitors

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Abstract
In vitro susceptibility to trypsin of whole bean extracts, and waterand salt‐soluble proteins of 11 dry bean (Phaseolus vulgaris L.) varieties were investigated. Whole bean proteins were rapidly digested at a 10:l protein:trypsin ratio. Salt‐soluble proteins of beans were more readily and completely hydrolyzed by trypsin than their watersoluble proteins. Of the 8 fractions obtained by DEAE‐cellulose column chromatography of Great Northern bean albumins, three were identified to contain heat‐stable trypsin and chymotrypsin inhibitory activity. Proteins in these fractions seemed to protect phaseolin from rapid hydrolysis by proteases by virtue of both their inhibitory activity as well as protein:protein interactions.
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