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Role of Sulfhydryl Groups in the Interaction of -Casein and ß-Lactoglobulin¹

Department of Dairy Industries

Robert Jenness

Department of Biochemistry, University of Minnesota, St. Paul

ABSTRACT

Recently, Zittle and coworkers (19) have demonstrated that heat treatment induces the formation of a complex between -casein and ß-lactoglobulin. This confirms suggestions by others (3, 6, 10, 11, 12, 15, 16) that -casein and ß-lactoglobulin interact when heated together. The complex has an electrophoretic mobility at pH 2.1, µ = 0.01, intermediate between those of the two proteins heated singly. Zittle et al. (19) suggested that the reaction may involve exposure of the sulfhydryl groups in the ß-lactoglobulin, but presented no evidence for this idea. Trautman and Swanson (15, 16) had earlier shown that the presence of sulfhydryl blocking agents during heating of skimmilk prevented (a) the transformation of ß-lactoglobulin into a form (possibly a complex) which moved electrophoretically with -casein at pH 6.8, µ = 0.1, and (b) the well-known stabilization of evaporated milk by forewarming.

The present experiments were undertaken to clarify the role of —SH groups in this reaction by blocking sulfhydryls during heating and by reducing following heating in systems similar to those employed by Zittle et al. (19).

¹ Paper No. 5067, Scientific Journal Series, Minnesota Agricultural Experiment Station.