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Physical Changes in Milk Proteins at Elevated Temperatures as Determined by Light Scattering. II. Interaction between ß-Lactoglobulin and Whole, -, and -Casein in Buffer¹

Departments of Dairy Technology and Chemistry, The Ohio State University, Columbus

ABSTRACT

Application of the technique of light scattering to the study of heat-induced bovine milk casein interactions with ß-lactoglobulin was made. Marked aggregation of ß-lactoglobulin was observed at 70 and 90 C. Interaction of both -casein and -casein with ß-lactoglobulin was observed at 90 C, but not with -casein at 30 C. The addition of para-hydroxymercuribenzoate appeared to inhibit the stabilizing interaction at elevated temperatures between whole casein and ß-lactoglobulin. Covering the air surface of ß-lactoglobulin solutions and ß-lactoglobulin-casein mixtures with mineral oil prevented the appearance of a precipitate at the surface.

¹ Technical article 14:63. The Department of Dairy Technology. Supported by a grant from the National Institutes of Health.

² Present address: Department of Chemistry, Cornell University, Ithaca, New York.