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Surface Active Properties of Food Proteins: Effects of Reduction of Disulfide Bonds on Film Properties and Foam Stability of Glycinin
Author(s) -
KIM S.H.,
KINSELLA J.E.
Publication year - 1987
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.1365-2621.1987.tb13987.x
Subject(s) - dithiothreitol , chemistry , disulfide bond , chemical engineering , viscosity , soy protein , elasticity (physics) , biophysics , materials science , food science , organic chemistry , biochemistry , composite material , biology , engineering , enzyme
Reduction of soy glycinin with 5 mM and 10 mM dithiothreitol resulted in molecular conformational changes which enhanced molecular hydrophobicity and increased viscosity. These changes were associated with significant improvement increases in surface active properties of the reduced proteins. The surface yield stress and elasticity of surface films were increased. The stability of foams as reflected in drainage time was improved especially at pH 6 and 7.0.