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- W2004236007 abstract "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." @default.
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- W2004236007 date "1986-11-01" @default.
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- W2004236007 title "Disulfide Reduction and Molecular Dissociation Improves the Proteolysis of Soy Glycinin by Pancreatin in vitro" @default.
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- W2004236007 doi "https://doi.org/10.1111/j.1365-2621.1986.tb13839.x" @default.
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