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A 1H-NMR study of bovine casein micelles; influence of pH, temperature and calcium ions on micellar structure

Published online by Cambridge University Press:  01 June 2009

Harry S. Rollema
Affiliation:
Netherlands Institute for Dairy Research (NIZO), P.O. Box 20, 6710 BA Ede, The Netherlands
Jan A. Brinkhuis
Affiliation:
Netherlands Institute for Dairy Research (NIZO), P.O. Box 20, 6710 BA Ede, The Netherlands

Summary

The influence of pH, temperature and Ca depletion on bovine casein micelle suspensions in D2O containing simulated milk ultrafiltrate was studied by 1H-NMR spectroscopy.

In the pH range of 5·8–7·5 the spectrum of the micelles showed very little pH dependence, indicating that no changes occurred in the dynamic behaviour of the proteins constituting the micelle.

The NMR spectrum of casein micelles was strongly temperature dependent, particularly in the temperature range of 60–98 °C. Increase in temperature resulted in a strong increase in spectral intensity concomitant with changes in the spectral characteristics. In micelle suspensions these changes were reversible, and indicated that at clevated temperatures the rigid structure of the casein micelle started to melt, leading to an increased mobility of appreciable parts of the proteins in the micelle.

Ca depletion of the casein micelles by addition of EDTA resulted in an increase in spectral intensity, which arose from the presence of casein components in the serum phase, The spectrum of these serum phase particlcs resembled closely the spectrum of a solution of total casein in simulated milk ultrafiltrate and was quite different from the spectrum of casein micelles.

The implications of these results with respect to models of the structure of bovine casein micelles are discussed.

Type
Original Articles
Copyright
Copyright © Proprietors of Journal of Dairy Research 1989

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References

REFERENCES

Britten, M., Boulet, M. & Paquin, P. 1986 Composition and interfacial properties of casein micelle fractions. Journal of Dairy Research 53 573584CrossRefGoogle Scholar
Calapaj, G. G. 1968 An electron microscope study of the ultrastructure of bovine and human casein micelles in fresh and acidified milk. Journal of Dairy Research 35 16CrossRefGoogle Scholar
Davies, D. T. & Law, A. J. R. 1983 Variation in the protein composition of bovine casein micelles and serum casein in relation to micellar size and milk temperature. Journal of Dairy Research 50 6775CrossRefGoogle Scholar
Donnelly, W. J., McNeill, G. P., Buchheim, W. & McGann, T. G. A. 1984 A comprehensive study of the relationship between size and protein composition in natural bovine casein micelles. Biochimica et Biophysica Acta 789 136143CrossRefGoogle ScholarPubMed
Garnier, J. 1973 Models of casein micelle structure. Netherlands Milk and Dairy Journal 27 240248Google Scholar
Griffin, M. G. A. & Roberts, G. C. K. 1985 A 1H-NMR study of casein micelles. Biochemical Journal 228 273276CrossRefGoogle ScholarPubMed
Holt, G., Davies, D. T. & Law, A. J. R. 1986 Effects of colloidal calcium phosphate content and free calcium ion concentration in the milk serum on the dissociation of bovine casein micelles. Journal of Dairy Research 53 557572CrossRefGoogle Scholar
Jardetzky, O. & Roberts, G. C. K. 1981 NMR in Molecular Biology pp. 454–162. New York: Academic Press.Google Scholar
Jenness, R. & Koops, J. 1962 Preparation and properties of a salt solution which simulates milk ultrafiltrate. Netherlands Milk and Dairy Journal 16 153164Google Scholar
Knoop, A. M., Knoop, E. & Wiechen, A. 1973 Electron microseopical investigations on the structure of the casein micelles. Netherlands Milk and Dairy Journal 27 121127Google Scholar
Lin, S. H. C., Leong, S. L., Dewan, R. K., Bloomfield, V. A. & Morr, C. V. 1972 Effect of calcium ion on the structure of native bovine casein micelles. Biochemistry 11 18181821CrossRefGoogle ScholarPubMed
Mcmahon, D. J. & Brown, R. J. 1984 Composition, structure and integrity of easein micelles: a review. Journal of Dairy Science 67 499512CrossRefGoogle Scholar
Rollema, H. S., Brinkhuis, J. A. & Vreeman, H. J. 1988 1H-NMR studies of bovine k−casein and casein micelles. Netherlands Milk and Dairy Journal 42 233248Google Scholar
Rollema, H. S., Vreeman, H. J. & Brinkhuis, J. A. 1984. 1H-NMR spectra of bovine k−casein micelles. In Proceedings XXII Congress Ampère pp. 494495 (Ed. Müller, K. A., Kind, R. and Roos, J.). Zürich: Schippert & Co.Google Scholar
Rose, D. 1968 Relation between micellar and serum casein in bovine milk. Journal of Dairy Science 51 18971902CrossRefGoogle Scholar
Schmidt, D. G. 1982 Association of caseins and casein micelle structure. In Developments in Dairy Chemistry vol. 1 pp. 6186 (Ed. Fox, P. F.). London: Applied Science Publishers.Google Scholar
Schmidt, D. G. & Buchheim, W. 1970 Elektronenmikroskopische Untersuchung der Feinstruktur von Caseinmicellen in Kuhmilch. Milchwissenschaft 25 596600Google Scholar
Shimmin, P. D. & Hill, R. D. 1964 An electron microscope study of the internal structure of casein micelles. Journal of Dairy Research 31 121123CrossRefGoogle Scholar
Slattery, C. W. 1976 Review: casein micelle structure: an examination of models. Journal of Dairy Science 59 15471556CrossRefGoogle ScholarPubMed
Stothart, P. H. & Cebula, D. J. 1982 Small-angle neutron scattering study of bovine casein micelles and sub-micelles. Journal of Molecular Biology 160 391395CrossRefGoogle ScholarPubMed
Van Hooydonk, A. C. M., Hagedoorn, H. G. & Boerrioter, I. J. 1986 pH-induced physico-chemical changes of casein micelles in milk and their effect on renneting. I. Effect of acidification on physico-chemical properties. Netherlands Milk and Dairy Journal 40 281296Google Scholar
Visser, J., Minihan, A., Smits, P., Tjan, S. B. & Heertje, I. 1986 Effects of pH and temperature on the milk salt System. Netherlands Milk and Dairy Journal 40 351368Google Scholar
Waugh, D. F. & Talbot, B. 1971 Equilibrium casein micelle Systems. Biochemistry 10 41534162CrossRefGoogle ScholarPubMed