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Effect of heat induced interaction between β-lactoglobulin and κ-casein on syneresis

Published online by Cambridge University Press:  01 June 2009

Martin J. Pearse ,
Peter M. Linklater ,
Robert J. Hall  and
Antony G. Mackinlay
Martin J. Pearse
Affiliation:
Schools of Biochemistry
Peter M. Linklater
Affiliation:
Chemical Engineering. University of New South Wales, Kensington, New South Wales 2033, Australia
Robert J. Hall
Affiliation:
Chemical Engineering. University of New South Wales, Kensington, New South Wales 2033, Australia
Antony G. Mackinlay
Affiliation:
Schools of Biochemistry
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Summary

The effect of preheating skim milk and artificial micelle milk on curd syneresis was studied. The inhibition of syneresis caused by heat was dependent on the presence of β-lactoglobulin (β-lg) and to a lesser extent α-lactalbumin. The degree of inhibition increased with increasing amounts of added β-lg and preheating temperature. This agrees with the hypothesis that the detrimental effect of preheating on syneresis is due to complex formation between β-lg and κ-casein. This complex appeared to be mediated via thiol–disulphide exchange and its formation appeared to interfere with the micelle–micelle interactions responsible for syneresis.

Type
Original Articles
Information
Journal of Dairy Research , Volume 52 , Issue 1 , February 1985 , pp. 159 - 165
Copyright
Copyright © Proprietors of Journal of Dairy Research 1985

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References

REFERENCES

Crestfield, A. M., Moore, S. & Stein, W. N. 1963 The preparation and enzymatic hydrolysis of reduced and S-carboxymethylated proteins. Journal of Biological Chemistry 238 622–627CrossRefGoogle ScholarPubMed
Elfagm, A. A. & Wheelock, J. V. 1977 Effect of heat on α-lactalbumin and β-lactoglobulin in bovine milk. Journal of Dairy Research 44 367–371CrossRefGoogle Scholar
Hindle, E. J. & Wheelock, J. V. 1970 The release of peptides and glycopeptides by the action of heat on cow's milk. Journal of Dairy Research 37, 397–405CrossRefGoogle Scholar
Kannan, A. & Jenness, R. 1961 Relation of milk serum proteins and milk salts to the effects of heat.treatment on clotting time. Journal of Dairy Science 44 802–822CrossRefGoogle Scholar
McKenzie, H. A. & Wake, R. G. 1961 An improved method for the isolation of κ-casein. Biochimica et Biophysica Acta 47 240–242CrossRefGoogle Scholar
Morrissey, P. A. 1969 The rennet hysteresis of heated milk. Journal of Dairy Research 36 333–341CrossRefGoogle Scholar
Pearse, M. J., Mackinlay, A. G., Hall, R. J. & Linklater, P. M. 1984 A microassay for the syneresis of cheese curd. Journal of Dairy Research 51 131–139CrossRefGoogle Scholar
Sawyer, W. H. 1969 Complex between β-lactoglobulin and κ-casein. A review. Journal of Dairy Science 52 1347–1355CrossRefGoogle ScholarPubMed
Sawyer, W. H., Coulter, S. T. & Jenness, R. 1963 Role of sulfhydryl groups in the interaction of κ-casein and β-lactoglobulin. Journal of Dairy Science 46 564–565CrossRefGoogle Scholar
Schmidt, D. G., Both, P. & Koops, J. 1979 Properties of artificial casein micelles. 3. Relationship between salt composition, size and stability towards ethanol, dialysis and heat. Netherlands Milk and Dairy Journal 33 40–49Google Scholar
Schmidt, D. G. & Koops, J. 1977 Properties of artificial casein micelles. 2. Stability towards ethanol, dialysis pressure and heat in relation to casein composition. Netherlands Milk and Dairy Journal 31 342–357Google Scholar
Schmidt, D. G., Koops, J. & Westerbeek, D. 1977 Properties of artificial casein micelles. 1. Preparation, size distribution and composition. Netherlands Milk and Dairy Journal 31 328–341Google Scholar
Shalabi, S. I. & Wheelock, J. V. 1976 The role of α-lactalbumin in the primary phase of chymosin action on heated casein micelles. Journal of Dairy Research 43 331–335CrossRefGoogle Scholar
Smits, P. & Van Brouwershaven, J. H. 1980 Heat-induced association of β-lactoglobulin and casein micelles. Journal of Dairy Research 47 313–325CrossRefGoogle ScholarPubMed
Snoeren, T. H. M. & Van Der Spek, C. A. 1977 The isolation of a heat-induced complex from UHTST milk. Netherlands Milk and Dairy Journal 31 352–355Google Scholar
Tessier, H. & Rose, D. 1964 Influence of κ-casein and β-lactoglobulin on the heat stability of skimmilk. Journal of Dairy Science 47 1047–1051CrossRefGoogle Scholar
Tessier, H., Yaguchi, M. & Rose, D. 1969 Zonal ultracentrifugation of β-laetoglobulin and κ-casein complexes induced by heat. Journal of Dairy Science 52 139–145CrossRefGoogle Scholar
Waugh, D. F. 1971 In Milk Proteins (Ed. McKenzie, H. A.) Vol. 2 pp. 3–79. New York: Academic PressCrossRefGoogle Scholar
Wheelock, J. V. & Kirk, A. 1974 The role of β-lactoglobulin in the primary phase of rennin action on heated casein micelles and heated milk. Journal of Dairy Research 41 367–372CrossRefGoogle ScholarPubMed
Wilson, G. A. & Wheelock, J. V. 1972 Factors affecting the action of rennin in heated milk. Journal of Dairy Research 39 413–419CrossRefGoogle Scholar
Zittle, C. A., Thompson, M. P., Custer, J. H. & Cerbulis, J. 1962 κ-Casein- β-lactoglobulin interaction in solution when heated. Journal of Dairy Science 45 807–810CrossRefGoogle Scholar