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Journal of Dairy Science Vol. 59 No. 2 203-206
© 1976 by American Dairy Science Association ®
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Comparison of Calcium Sensitivities of {alpha}s1-B, ß-A2, and {gamma}-A2 Caseins and Their Stabilization by K-Casein A1

W. N. Eigel2 and H. E. Randolph

Department of Animal Science, Texas A&M University, College Station 77843

ABSTRACT

Increasing concentrations of calcium increased precipitation of {alpha}s1-B, ß-A2, and {gamma}-A2 caseins. However, differences occurred at various concentrations of added calcium. At low calcium (<4mM), {gamma}-casein A2 was more calcium-sensitive than either {alpha}s1-B or ß-A2 casein. At high added calcium (15mM), only 55% of the {gamma}-casein A2 precipitated compared to 94 and 80% of the {alpha}s1-B and ß-A2 caseins. Variations in calcium sensitivity were attributed to differences in average hydrophobicity and in phosphorus content of the three caseins. Solubilities of {alpha}s1-B, ß-A2, and {gamma}-A2 caseins in the presence of 10 mM calcium increased with increasing concentrations of {kappa}-casein A. In each case, the maximum solubility was near a {kappa}-casein/calcium-sensitive casein ratio of .10. At ratios of {kappa}-casein A/ß-casein A2 and {kappa}-casein A/{gamma}-casein A2 of .04 and greater, the solubility curves were similar. The ability of {kappa}-casein to stabilize ß- and {gamma}-caseins against precipitation by calcium was attributed primarily to hydrophobic interactions. Further work on {gamma}-casein is needed.


FOOTNOTES

1 Technical article 11692 of the Texas Agricultural Experiment Station, College Station.

2 Food Sciences Institute, Purdue University, Lafayette, IN 47907.







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