Premium
Surface Active Properties of Proteins: Effects of Progressive Succinylation 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.tb14077.x
Subject(s) - succinylation , chemistry , viscosity , chemical engineering , amino acid , biophysics , chromatography , materials science , biochemistry , lysine , composite material , biology , engineering
Succinylation of glycinin at 25, 50, 70, and 98% of available amino groups progressively increased hydrophobicity, viscosity and exposure of aromatic amino acids. Maxima in surface pressure (at pH 4–8), film‐yield stress, and film elasticity were observed at 25% succinylation where the maximum in foam stability was also observed. Excessive succinylation (>50%) reduced these parameters because the high net negative charges may have impaired protein:protein interactions in films.