Hostname: page-component-77c89778f8-rkxrd Total loading time: 0 Render date: 2024-07-22T00:22:06.975Z Has data issue: false hasContentIssue false

Mode of binding of ionic materials to casein micelles

Published online by Cambridge University Press:  01 June 2009

Margaret L Green
Affiliation:
National Institute for Research in Dairying, Shinfield, Reading R02 9 AT, UK

Summary

The proportion of materials which adsorb to casein micelles and accelerate milk coagulation, and remain bound on dilution of the micelle suspension with milk dialysate was determined. This was higher than expected from the postulate that equilibration took place between the solution and many equivalent binding sites on the micelle. This suggests that binding involved either or both hydrophobic interactions and multipoint attachment to charged groups. The location of the additive binding sites in the micelle was investigated using models Na caseinate and hydroxyapatite at pH 6·6. Materials which accelerated coagulation bound to either or both models. Those with the greatest effect on milk coagulation probably bound primarily to the casein rather than to the colloidal calcium phosphate moiety of casein micelles.

Type
Original Articles
Copyright
Copyright © Proprietors of Journal of Dairy Research 1982

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

REFERENCES

Davibs, D. T. & White, J. C. D. 1960 The use of ultrafiltration and dialysis in isolating the aqueous phase of milk and in determining the partition of milk constituents between the aqueous and disperse phases. Journal of Dairy Research 27 171190Google Scholar
Green, M. L. 1971 The specificity for κ-casein as the stabiliser of αs-casein and β-casein. II. Replacement of κ-casein by detergents and water-soluble polymers. Journal of Dairy Research 38 2532CrossRefGoogle Scholar
Green, M. L. 1982 Effect on the composition and properties of casein micelles of interaction with ionic materials. Journal of Dairy Research 49 8798CrossRefGoogle Scholar
Green, M. L. & Marshall, R. J. 1977 The acceleration by cationic materials of the coagulation of casein micelles by rennet. Journal of Dairy Research 44 521531CrossRefGoogle Scholar
Hummel, J. P. & Dreyer, W. J. 1962 Measurement of protein-binding phenomena by gel filtration. Biochimica ei Biophysica Ada 63 530532CrossRefGoogle ScholarPubMed
Jenness, R. 1970 Protein Composition Of Milk. In Milk Proteins: Chemistry and Molecular Biology Vol. 1 pp. 1743 (Ed. McKenzie, H. A.). New York and London: Academic PressCrossRefGoogle Scholar
Knoop, A. M., Knoop, E., Frede, E., Preoht, D. & Wiechen, A. 1979 [The submicroscopic structure of natural and artifical casein micelles]. Milchwissenschaft 34 129131Google Scholar
Lin, C. F. 1977 Interaction of sulfated polysaccharides with proteins. In Food Colloids pp. 320346 (Ed. Graham, H. D.) Westport, Conn: Avi Publishing Co.Google Scholar
Marshall, R. J. & Green, M. L. 1980 The effect of the chemical structure of additives on the coagulation of casein micelle suspensions by rennet. Journal of Dairy Research 47 359369CrossRefGoogle Scholar
MoMeekin, T. L. & Groves, M. L. 1965 Physical equilibria in milk: protein. In Fundamentals of Dairy Chemistry pp. 374402 (Eds Webb, B. H. and Johnson, A. H.). Westport, Conn: Avi Publishing Co.Google Scholar
Ntailianas, H. A. & Whitney, R. McL. 1964 Calcein as an indicator for the determination of total calcium and magnesium and calcium alone in the same aliquot of milk. Journal of Dairy Science 47 1927CrossRefGoogle Scholar
Simonsen, D. G., Wertman, M., Westover, L. M. & Mehl, J. W. 1946 The determination of serum phosphate by the molybdivanadate method. Journal of Biological Chemistry 166 747755CrossRefGoogle ScholarPubMed
Tiselius, A., Hjertėn, S. & Levin, Ö. 1956 Protein chromatography on calcium phosphate columns. Archives of Biochemistry and Biophysics 65 132155CrossRefGoogle Scholar
Waugh, D. F., Slattery, C. W. & Creamer, L. K. 1971 Binding of cations to caseins. Site binding, Donnan binding and system characteristics. Biochemistry 10 817823CrossRefGoogle ScholarPubMed