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^ß-Lactoglobulin--Casein Interaction in Various Salt Solutions¹

Department of Animal and Range Sciences, Montana State University, Bozeman 59715

ABSTRACT

Mixtures of 2% each of ß-lactoglobulin ABC and -casein AB were heated at 110 C for 30 min in solutions containing de-ionized water, .02 M calcium, 5% -lactose, .035% phosphorous, .2% citrate, .14% chlorine, synthetic ultra-filtrate, and milk dialysate. Differences in composition of interaction products were shown qualitatively by zone electrophoresis and quantitatively by preparative electrophoresis. A minimum interaction of 13.8% ß-lactoglobulin with 17.1% -casein occurred in de-ionized water while a maximum of 76.6% ß-lactoglobulin interacted with 83.3% -casein in milk dialysate. Rates of interactions for other reaction solutions varied between the two. Zonal electrophoresis of individual ß-lactoglobulin and -casein treated similarly showed that some interaction products may ensue from the effect of neating on these proteins.

¹ Contribution from Montana State University, Agricultural Experiment Station, Project No. 168, Paper No. 533.