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Binding of Alcohols by Soy Protein in Aqueous Solutions
Author(s) -
CHUNG S.,
VILLOTA R.
Publication year - 1989
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.1365-2621.1989.tb05170.x
Subject(s) - chemistry , soy protein , hydrogen bond , denaturation (fissile materials) , aqueous solution , hydrophobic effect , chromatography , organic chemistry , biochemistry , molecule , nuclear chemistry
Interactions of alcohols with soy protein isolate were investigated using an equilibrium dialysis method. It was found that interactions may involve hydrophobic association and, to some degree, hydrogen bonding. Studies with soy protein with various levels of denaturation indicated that denaturation of the protein by heating may limit its ability for the formation of hydrogen bonds with alcohols. The proteins under investigation exhibited practically unlimited binding capacity for alcohols.