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Thermal denaturation of soy proteins as related to their dye‐binding characteristics and functionality
Author(s) -
Lin Shaowen,
Lakin Alan Llyods
Publication year - 1990
Publication title -
journal of the american oil chemists' society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.512
H-Index - 117
eISSN - 1558-9331
pISSN - 0003-021X
DOI - 10.1007/bf02540509
Subject(s) - chemistry , denaturation (fissile materials) , urea , orange (colour) , soy protein , urease , chromatography , lysine , biochemistry , amino acid , food science , nuclear chemistry
The binding of Cresol Red and of Acid Orange 10 (in the absence and presence of urea) to unheated and progressively heated, defatted soy meal was compared with their NSI values, urease activities, in vitro digestibilities, unreactive lysine contents, and foaming and emulsifying capacities. These results suggested that increased amounts of Cresol Red and of Acid Orange 10 (in the presence of urea) bound to the heated samples were due to the progressive exposure of hydrophobic residues caused thermal denaturation. High statistical correlations were obtained between dye‐binding, the duration of heating, and functional properties. Our results indicate that dye‐binding has potential for predicting certain functional properties as well as for monitoring thermal denaturation of soy proteins.