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Effect of casein micelle composition and casein dephosphorylation on coagulation and syneresis

Published online by Cambridge University Press:  01 June 2009

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

Summary

The effect of varying the casein composition of artificial micelle milk on rennet coagulation time and syneresis was examined in order to determine whether either of these processes is dependent on the concentration of particular casein components. It was found that the levels of κ-and β-caseins had a significant effect on coagulation, whereas syneresis was only affected by the level of β-casein. Partial dephosphorylation of preformed micelles or the incorporation of dephosphorylated or partly dephosphorylated β-casein into artificial micelle milk was found to have an adverse effect on both coagulation and syneresis. It was concluded that the phosphate groups of casein, particularly those of β-casein, are directly involved in the micelle-micelle interactions which occur during coagulation and syneresis.

Type
Original Articles
Copyright
Copyright © Proprietors of Journal of Dairy Research 1986

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References

REFERENCES

Andrews, A. T. 1976 Further studies on acid phosphatase of leucocyte origin in normal and mastitic bovine milks. Journal of Dairy Research 43 127131CrossRefGoogle ScholarPubMed
Andrews, A. T. & Alichanidis, E. 1975 The acid phosphatases of bovine leucocytes, plasma and milk of healthy and mastitic cows. Journal of Dairy Research 42 391400CrossRefGoogle Scholar
Andrews, A. T. & Pallavicini, C. 1973 Bovine milk acid phosphatase. I. Some kinetic studies and other properties using a partially purified preparation. Biochimica et Biophysica Acta 321 197209CrossRefGoogle ScholarPubMed
Ali, A. E., Andrews, A. T. & Cheeseman, G. C. 1980 Factors influencing casein distribution in cold-stored milk and their effects on cheese-making parameters. Journal of Dairy Research 47 383391CrossRefGoogle Scholar
Bargoni, N. 1963 Studies on the action mechanism of rennin. Enzymologia 26 108112Google ScholarPubMed
Bingham, E. W., Farrell, H. M. & Carroll, R. J. 1972 Properties of dephosphorylated αs1-casein. Precipitation by calcium ions and micelle formation. Biochemistry 11 24502453CrossRefGoogle Scholar
Crestfield, A. M., Moore, S. & Stein, W. H. 1963 The preparation and enzymatic hydrolysis of reduced and S-carboxymethylated proteins. Journal of Biological Chemistry 238 622627CrossRefGoogle ScholarPubMed
Davies, D. T. & Law, A. J. R. 1977 The composition of whole casein from the milk of Ayrshire cows. Journal of Dairy Research 44 447454CrossRefGoogle Scholar
Grindrod, P. E., Price, W. & Sommer, H. H. 1956 Synthetic milk for the study of cheese making. I. Preparation of a casein sol in semblance of skimmilk. Journal of Dairy Science 39 499507CrossRefGoogle Scholar
Hill, R. 1970 The effect of the modification of arginine side chains in casein on the coagulation of rennin-altered casein. Journal of Dairy Research 37 187192CrossRefGoogle Scholar
Hill, R. D. & Craker, B. A. 1968 The role of lysine residues in the coagulation of casein. Journal of Dairy Research 35 1318CrossRefGoogle Scholar
Hill, R. D. & Laing, R. R. 1965 The action of rennin on casein: the effect of modifying functional groups on the casein. Journal of Dairy Research 32 193201CrossRefGoogle Scholar
Hsu, R. Y. H., Anderson, L., Baldwin, R. L., Ernstrom, C. A. & Swanson, A. M. 1958 Rennin coagulation of enzymatically dephosphorylated casein. Nature 182 798799CrossRefGoogle ScholarPubMed
Itzhaki, R. F. & Gill, D. M. 1964 A micro-biuret method for estimating proteins. Analytical Biochemistry 9 401410CrossRefGoogle ScholarPubMed
Lorient, D. & Linden, G. 1976 Dephosphorylation of bovine casein by milk alkaline phosphatase. Journal of Dairy Research 43 1926CrossRefGoogle ScholarPubMed
McKenzie, H. A. & Wake, R. G. 1961 An improved method for the isolation of κ-casein. Biochimica et Biophysica Acta 47 240242CrossRefGoogle Scholar
Manson, W. & Annan, W. 1971 The structure of a phosphopeptide derived from β-casein. Archives of Biochemistry and Biophysics 145 1626CrossRefGoogle Scholar
Melnychyn, P. & Wolcott, J. M. 1967 Simple procedure for the isolation of alphas-casein. Journal of Dairy Science 50 18631867CrossRefGoogle 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 131139CrossRefGoogle Scholar
Reimerdes, E. H. & Roooenbuck, G. 1980 [Chemistry and technology of milk proteins. 1. Modification of β-casein and casein micelles by acid phosphatase from potatoes.] Milchwissenschaft 35 195201Google 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 328341Google Scholar
Shahani, K. M. 1966 Milk enzymes: their role and significance. Journal of Dairy Science 49 907920CrossRefGoogle ScholarPubMed
Swaisgood, H. E. 1973 The caseins. CRC Critical Reviews in Food Technology 4 375414CrossRefGoogle Scholar
Taussky, H. H. & Shorr, E. 1953 A microcolorimetric method for the determination of inorganic phosphorus. Journal of Biological Chemistry 202 675685CrossRefGoogle ScholarPubMed
Yamauchi, K. & Yoneda, Y. 1978 Effect of dephosphorylation of casein on its coagulation and proteolysis by chymosin. Agricultural and Biological Chemistry 42 10311035Google Scholar
Yun, S., Ohmiya, K. & Shimizu, S. 1982 Role of the phosphoryl group of β-casein in milk curdling. Agricultural and Biological Chemistry 46 15051511Google Scholar