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

Abstract

Polyacrylamide disc electrophoresis patterns were used to study the effect of 0.10% hydrogen peroxide on the interaction between fl-lactoglobulin and K-casein when heated to 85 C for 30 rain. The fl-lactoglobulin was modified by treatment with hydrogen peroxide to form an electrophoretic 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 flcasein contaminant appeared to have been affected. Apparently, the hydrogen peroxide modified fi-lactoglobulin retarded formation of the complex with K-casein; however, it did not completely prevent the interaction.