Heat-Induced Aggregation of Egg White Proteins as Studied by Vertical Flat-Sheet Polyacrylamide Gel Electrophoresis |
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| Authors: | TSUKASA MATSUDA KENJI WATANABE YASUSHI SATO |
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| Affiliation: | Authors Matsuda, Watanabe, and Sato are affiliated with the Dept of Food Science &Technology, Faculty of Agriculture. Nagoya Univ., Chikusa-ku, Nagoya 464, Japan. |
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| Abstract: | 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. |
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