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-casein and ß-lactoglobulin 1Department of Dairy and Poultry Science, Kansas Agricultural Experiment Station, Manhattan
ABSTRACT
Polyacrylamide disc electrophoresis patterns were used to study the effect of 0.10% hydrogen peroxide on the interaction between ß-lactoglobulin and
-casein when heated to 85 C for 30 min. The ß-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
-casein, although the ß-casein contaminant appeared to have been affected. Apparently, the hydrogen peroxide modified ß-lactoglobulin retarded formation of the complex with
-casein; however, it did not completely prevent the interaction.
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