The interaction between micellar kappa-casein and beta-lactoglobulin in cow's milk

Imm, J.Y.; Kim, Y.K.

Korean Journal of Animal Science 35(3): 237-243

1993


Accession: 009592878

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Abstract
The effect of micelle size on heat-induced interaction between beta-lactoglobulin and kappa-casein was studied. beta-lactoglobulin was isolated from fresh bovine milk and various size of casein pellets were obtained by ultracentrifugation at 100,000 times g for 10, 30 and 60 min. The mixture of beta-lactoglobulin and casein pellet were heated at 65, 75, 85 and 95 degree C for 30 min, respectively prior to analysing by means of Sepharose 6B column chromatography, ultracentrifugation and polyacrylamide gel electrophoresis. Heating beta-lactoglobulin alone (85 degree C) showed formation of large molecular weight polymer of beta-lactoglobulin in Sepharose chromatography. After heating mixtures containing beta-lactoglobulin and casein pellet at 85 degree C beta-lactoglobulin peak decreased while casein pellet peak increased. Electrophoretic analysis also showed interaction of beta-lactoglobulin with casein micelle occurred during heat treatment. As the heating temperature increase the protein content of the ultracentrifugal supernatant decreased. Smallest protein content was also found in the small micelle (casein pellet 3). These results indicate that the interaction of beta-lactoglobulin and kappa-casein was affected micelle size ascribed to variation in the kappa-casein content of micelles.