Abstract
AbstractTwo particular fractions of the soluble proteins were consistently reduced by heating liquid egg for 5 min at 150°F. These fractions were quantitatively greater in the soluble proteins from frozen egg. The soluble proteins appeared to be more stable to heat in eggs that had been stored for 15 days at 70°F than in new‐laid eggs. Unfrozen new‐laid and stale egg and frozen new‐laid egg all showed an increase in insoluble material after pasteurisation, and frozen egg contained more insoluble materials than unfrozen egg. Gel filtration showed that the proportion of compounds of high molecular weight in the insoluble proteins was markedly increased by pasteurisation and even more markedly increased by freezing.
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