The denaturation of caseins and whey proteins separated from reconstituted milk, skim milk, pasteurized milk, and ultra-high temperature-treated milk (UM) affecting the functionality of milk was analyzed by gel filtration chromatography(CFC) and polycrylamide gel electrophoresis (PAGE). Whey proteins, bovine serum albumin (BSA), ¥â-lactoglobulin (¥â-LG), ¥á-lactalbumin, immunoglobulin, and non-protein nitrogen, were denatured during various hast treatments. Most of BSA was denatured in pasteurization processing. ¥â-LG was also denatured with BSA in ultra-high temperature treatment. PAGE results showed that caseins from UM had not been denatured much even at high temperature treatments, while most of the whey proteins from UM were denatured as shown in GFC.
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