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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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Matsuda et al. (1981) studied this question.
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