Electrophoresis and Chromatography of Heat‐Treated Plain, Sugared and Salted Whole Egg

The effects of heat treatments on the proteins in plain, 10% sugared and 10% salted whole egg were studied by polyacrylamide disc gel electrophoresis and diethylaminoethyl‐Sephacel ion exchange chromatography. Electrophoretograms of products heated from 57–87°C for 3.5 min showed a wide range of protein stability. Livetins and some globulins were most heat sensitive, while conalbumin and ovalbumin were most stable. Sugar and salt increased heat stability of proteins by 1.6 and 7.9°C, respectively. Heat sensitive proteins were most stabilized by sugar and salt. Heating whole egg and sugared whole egg changed the chromatograms substantially, while heating salted whole egg caused fewer changes.