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The heat stability of milk as affected by variations in pH and milk salts

Published online by Cambridge University Press:  01 June 2009

P. A. Morrissey
P. A. Morrissey
Affiliation:
Dairy Chemistry Department, University College, Cork, Irish Republic
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Summary

The maximum and minimum heat stability exhibited by most milks over a relatively narrow range of pH values is shown also by synthetic colloidal calcium caseinate-calcium phosphate systems and even by simple caseinate systems, provided all possess adequate contents of β-lactoglobulin, soluble calcium and phosphate. The phenomenon is not, however, dependent on the presence of the characteristic micellar structure of the casein of milk. The minimum stability observed, usually around pH 6·9, is the most characteristic feature of the phenomenon and arises from heat induced deposition of calcium phosphate on a caseinate/β-lactoglobulin complex. This reaction, which tends to occur to a marked degree at relatively high pH values and calcium ion concentrations, sensitizes the complex to precipitation by calcium ions. The precise pH values at which the maximum and minimum stabilities occur can vary depending on the salt composition of the serum, since the latter can influence the solubility of calcium phosphate.

Type
Original Articles
Information
Journal of Dairy Research , Volume 36 , Issue 3 , October 1969 , pp. 343 - 351
Copyright
Copyright © Proprietors of Journal of Dairy Research 1969

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References

REFERENCES

McGann, T. C. A. & Pyne, G. T. (1960). J. Dairy Res. 27, 403.CrossRefGoogle Scholar
Morrissey, P. A. (1969). J. Dairy Res. 36, 333.CrossRefGoogle Scholar
Pyne, G. T. (1958). J. Dairy Res. 25, 467.CrossRefGoogle Scholar
Pyne, G. T. (1959) 15th Int. Dairy Congr., London, vol. III. p. 1673.Google Scholar
Pyne, G. T. & McHenry, K. A. (1955). J. Dairy Res. 22, 60.CrossRefGoogle Scholar
Rose, D. (1961 a). J. Dairy Sci. 44, 430.CrossRefGoogle Scholar
Rose, D. (1961 b). J. Dairy Sci. 44, 1405.CrossRefGoogle Scholar
Rose, D. (1962). J. Dairy Sci. 45, 1305.CrossRefGoogle Scholar
Rose, D. (1963). Dairy Sci. Abstr. 25, 45.Google Scholar
Rose, D. (1965). J. Dairy Sci. 48, 139.CrossRefGoogle Scholar
Rose, D. & Tessier, H. (1959). J. Dairy Sci. 42, 989.CrossRefGoogle Scholar
Sommer, H. H. & Hart, E. B. (1919). J. biol. Chem. 40, 137.CrossRefGoogle Scholar
Sommer, H. H. & Hart, E. B. (1922). J. Dairy Sci. 5, 525.CrossRefGoogle Scholar
Sommer, H. H. & Hart, E. B. (1926). Res. Bull, agric. Exp. Stn Univ. Wis. no. 67.Google Scholar
Tessier, H. & Rose, D. (1964). J. Dairy Sci. 47, 1047.CrossRefGoogle Scholar