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

✍ Scribed by Vaintraub, I. A. ;Seliger, P. ;Shutov, A. D.

• Publisher: John Wiley and Sons
• Year: 1979
• Tongue: English
• Weight: 398 KB
• Volume: 23
• Category: Article
• ISSN: 0027-769X
• DOI: 10.1002/food.19790230104

✦ Synopsis

The action of pepsin on the 1 I-S and 7-S proteins of vetch, 1 I-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 proteip 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.