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Heat‐Induced Aggregation of Egg White Proteins as Studied by Vertical Flat‐Sheet Polyacrylamide Gel Electrophoresis
Author(s) -
MATSUDA TSUKASA,
WATANABE KENJI,
SATO YASUSHI
Publication year - 1981
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.1365-2621.1981.tb04498.x
Subject(s) - ovotransferrin , egg white , ovalbumin , chemistry , electrophoresis , polyacrylamide gel electrophoresis , egg albumen , chromatography , biophysics , biochemistry , food science , biology , enzyme , immunology , immune system
Heat‐induced aggregation of proteins in egg white was investigated by a vertical flat‐sheet polyacrylamide gel electrophoretic method. The fractional and step‐wise aggregation of egg white proteins was caused by heating. Even with a heating time of 120 min, ovalbumin and globulins Al and A2 failed to aggregate in egg white (pH 7 and 9) at 70°C, and ovotransferrin and ovomucoid also did not aggregate in egg white at 60°C (pH 9) and 76°C (pH 7 and 9), respectively. The ovoinhibitor was much more unstable than ovomucoid under heat‐treatment, and the time dependency of heat‐induced aggregation of flavoprotein was greater than those of the other proteins in egg white.