Changes in Milk Proteins Treated with Hydrogen Peroxide

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Abstract
The effect of hydrogen peroxide on skimmilk and the individual proteins there from was studied, using electrophoretic mobility on polyacrylamlde gel (PAG) with and without urea and 2-mercaptoethanol (ME). Also measured were whey protein and nonprotein N as a function of concentration and time of exposure to H2O2. A heat-induced [kappa]-casein and [beta]-lactoglobulin complex was examined on PAG with and without urea-ME. Following hydrogen peroxide treatment of individual proteins, the migration rates on PAG electrophoresis were reduced for [alpha]s-casein and [beta]-lactoglobulin, were increased for [beta]-casein and bovine serum albumin, and did not change for [kappa]-casein or [alpha]-lactalbumin. In skimmilk, [beta]-casein migration was slowed. When the samples and the gel both contained urea-ME, [alpha]s and [beta]-casein migration rates were reduced, those of [beta]-lactoglobulln and BSA [bovine serum albumin] were increased, and those of [kappa]-casein and [alpha]-lactalbumin were unchanged. Whey protein N decreased and nonprotein N increased as a function of H2O2 concentration and time. Hydrogen peroxide did not induce complex formation between [beta]-lactoglobulin and [kappa]-casein. The heat-induced complex of these 2 proteins was ruptured by use of urea-ME.