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Sulfhydryl Groups Changes in Heat‐induced Soluble Egg White Aggregates in Relation to Molecular Size
Author(s) -
MINE YOSHINORI
Publication year - 1992
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.1365-2621.1992.tb05468.x
Subject(s) - egg white , chemistry , disulfide bond , polymerization , white (mutation) , biophysics , biochemistry , polymer , organic chemistry , biology , gene
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.