Effect of Hydrogen Peroxide Treatment on Heat Induced Interaction of κ-casein and β-lactoglobulin

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Abstract
Poly-acrylamide disc electrophoresis patterns were used to study the effect of 0.10% hydrogen peroxide on the interaction between [beta]-lactoglobulin and K-casein when heated to 85[degree]C for 30 min. The [beta]-lactoglobulin was modified by treatment with hydrogen peroxide to form an electro-phoretic component of reduced mobility that appeared as a diffuse band. There was no observable change in the electrophoretic pattern of the K-casein, although the [beta]-casein contaminant appeared to have been affected. Apparently, the hydrogen peroxide modified [beta]-lactoglobulin retarded formation of the complex with K-casein; however, it did not completely prevent the interaction.