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Keywords:

  • Egg-white;
  • albumin;
  • aggregates;
  • sulfhydryls

ABSTRACT

The sulfhydryl content of heat-induced soluble egg white aggregates gradually decreased in proportion to standing time at room temperature, and the molecular size of the aggregates continued to increase at least 4 days. The progress of soluble egg white aggregates was much inhibited by N-ethylmaleimide. Soluble egg white aggregates are polymerized through a mechanism involving sulfhydryl-disulfide interchange and sulfhydryl oxidation during standing.