ISSN:
1750-3841
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
,
Process Engineering, Biotechnology, Nutrition Technology
Notes:
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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1365-2621.1986.tb13839.x
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