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Journal of Dairy Science Vol. 50 No. 7 1045-1048
© 1967 by American Dairy Science Association ®
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Effect of Hydrogen Peroxide on Whey Protein Nitrogen Value of Heated Skimmilk1

Nancy L. Fish and R. Mickelsen

Department of Dairy and Poultry Science, Kansas State University, Manhattan

ABSTRACT

The effect on the whey protein nitrogen value of skimmilk treated with different concentrations of hydrogen peroxide in the skimmilk 10 min before it was heated at 85 C for 30 min was determined. Hydrogen peroxide decreased denaturation of skimmilk.

Disc electrophoresis patterns were compared for normal, heated, hydrogen peroxide-heated and hydrogen peroxide-heated-catalase-treated samples of {alpha}-lactalbumin, bovine serum albumin (BSA), ß-lactoglobulin, and acid whey. The {alpha}-lactalbumin band was lighter in the hydrogen peroxide-treated sample than in the normal or heated sample. Bovine serum albumin was denatured by heat treatment. Hydrogen peroxide prevented total denaturation of BSA. ß-lactoglobulin was denatured by heat treatment and extensively modified by hydrogen peroxide. The electrophoretic pattern of hydrogen peroxide-heated acid whey had a darker band in the position normally occupied by {alpha}-lactalbumin. Hydrogen peroxide modified ß-lactoglobulin to form a band in the same position. A component not found in hydrogen peroxide-heated acid whey was in the electrophoretic pattern of acid whey from hydrogen peroxide-heated skimmilk, possibly from a reaction of hydrogen peroxide with a casein protein to form a product not precipitated with the casein.

FOOTNOTES

1 Contribution no. 651, Kansas Agricultural Experiment Station, Manhattan.






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Copyright © 1967 by the American Dairy Science Association ®.