Binding of Alcohols by Soy Protein in Aqueous Solutions

Abstract
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.