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Disulfide Reduction and Molecular Dissociation Improves the Proteolysis of Soy Glycinin by Pancreatin in vitro
Author(s) -
ROTHENBUHLER E.,
KINSELLA J. E.
Publication year - 1986
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1986.tb13839.x
Subject(s) - dithiothreitol , proteolysis , chemistry , casein , urea , in vitro , biochemistry , dissociation (chemistry) , soy protein , intramolecular force , cysteine , proteostasis , intermolecular force , chromatography , enzyme , organic chemistry , molecule
THE EFFECTS of structural modification by urea and dithiothreitol on the in vitro pancreatin proteolysis of soy glycinin was studied. Urea, up to 4.5M, which causes dissociation of glycinin into subunits and some unfolding of the polypeptides progressively increased proteolysis by pancreatin as measured by the pH‐stat method. Reduction of the intermolecular disulfide bonds with dithiothreitol doubled the rate of proteolysis and when additional intramolecular disulfide bonds of glycinin were cleaved, the rate of digestibility increased approximately threefold becoming equivalent to casein in its susceptibility to proteolysis by pancreatin.