The action of pepsin on the reserve proteins of some leguminous seeds

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Abstract
The action of pepsin on the 11‐S and 7‐S proteins of vetch, 11‐S protein of soybean and 7‐S protein of Phaseolus vulgaris was investigated. The first three proteins are hydrolyzed almost completely, the rate of hydrolysis being close to that of hemoglobin, while the hydrolysis of Ph. vulgaris 7‐S protein stops after the cleavage of only 2,4% of peptide bonds. The nonhydrolyzable high molecular weight core makes up to 87% of the initial protein and differs from the latter in its electrophoretic mobility and sedimentation coefficient. The action of pepsin does not increase the digestibility of Ph. vulgaris 7‐S protein by trypsin. After the consecutive action of these enzymes about two thirds of the protein remain unhydrolyzed. The digestion of Ph. vulgaris 7‐S protein by pepsin is completed only after its denaturation by heat treatment or by the action of 6 M guanidine hydrochloride.