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Changes in Mixtures of Whey Protein and -Casein Due to Heat Treatments

Department of Dairy and Food Industries, The University of Wisconsin, Madison

ABSTRACT

Polyacrylamide disc electrophoresis developed by Davis (4) was investigated to determine its effectiveness in resolving whey proteins and for assessing the effect of heat on milk proteins. This technique was chosen because of its high resolution properties with protein solutions. The major whey protein bands are identified as ß-lactoglobulin A and B, -lactalbumin, bovine serum albumin (BSA), and the immune globulins in decreasing order of mobility.

A complex begins to occur between -casein and ß-lactoglobulin when they are mixed in equal parts by weight in a solution of milk salts and heated to 74.5 C for 30 min. They interact completely when heated to 85 C under the same conditions. This complex did not occur with -lactalbumin or BSA when heated with -casein at 74.5 or 85 C for 30 min.

One common electrophoretic band was formed by heating ß-lactoglobulin A and B to 74.5 or 85 C for 30 min. It had a slower electrophoretic mobility which may be due to increased molecular size or a change in molecular configuration during heating. This protein does not occur naturally in milk whey.