Effect of Hydrogen Peroxide on Whey Protein Nitrogen Value of Heated Skimmilk

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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 degrees 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), [beta]-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. [beta]-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 [beta]-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.