Premium
Heat‐Induced Aggregation and Denaturation of Egg White Proteins in Acid Media
Author(s) -
WATANABE KENJI,
MATSUDA TSUKASA,
NAKAMURA RYO
Publication year - 1985
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.1365-2621.1985.tb13438.x
Subject(s) - ovotransferrin , egg white , chemistry , denaturation (fissile materials) , ovalbumin , electrophoresis , globulin , protein aggregation , chromatography , biochemistry , biophysics , nuclear chemistry , biology , immune system , immunology
Heat‐induced aggregation and denaturation of egg white proteins adjusted to pH 5.5, 4.5, 3.5 and 2.5 were investigated by vertical flat‐sheet polyacrylamide gel electrophoretic and differential scanning calorimetric methods. The fractional and step‐wise aggregation of egg white proteins was caused by heating. As the acidity was increased from pH 5.5 to 2.5, ovotransferrin, ovomacroglobulin, globulin G3A, globulins A1 and A2, and ovalbumin became much more unstable to heat. However, ovomucoid and ovoinhibitor did not aggregate in the acidified egg white under heat treatments of 3 min at 90°C or 20 min at 74°C. The heat‐induced aggregation of flavoprotein was slightly greater at pH 4.5 and 3.5 than at pH 5.5 and 2.5.