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Journal of Dairy Science Vol. 50 No. 2 142-146
© 1967 by American Dairy Science Association ®
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Changes in Milk Proteins Treated with Hydrogen Peroxide1

Jean Grindrod and T. A. Nickerson

Department of Food Science and Technology, University of California, Davis

ABSTRACT

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

FOOTNOTES

1 This work was supported by Grant EF-00094 of Division of Environmental Engineering and Food Protection, USPHS, and the Dairy Council of California.






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Copyright © 1967 by the American Dairy Science Association ®.