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Thermal Denaturation of Hen Egg White Studied by Chromatographic and Immunochemical Techniques
Author(s) -
SAJDOK JIR̂Í,
POŽÁRKOVÁ DANA,
RAUCH PAVEL,
KÁŠ JAN
Publication year - 1989
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.1365-2621.1989.tb07910.x
Subject(s) - ovalbumin , egg white , chromatography , chemistry , denaturation (fissile materials) , biochemistry , biology , antigen , nuclear chemistry , genetics
The course of thermal denaturation of hen egg white at 70°C was studied in detail by fast gel chromatography on Superose 12 and by immunochemical techniques. The mechanism of thermal denaturation differed depending on the pH of the environment. The aggregation of protein at the beginning of heat treatment was typical at pH 5 while at pH 9 the breakdown to smaller fragments prevailed. The chromatographic method for the determination of thermally undamaged (native) ovalbumin correlated well with the immunochemical method.