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Casein Micelle Structure, Functions, and Interactions

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Advanced Dairy Chemistry

Abstract

Casein micelles are supramolecule of colloidal size. They are modeled as having a lattice structure in which both casein-calcium phosphate aggregates and casein polymer chains act together to maintain its supramolecular integrity. The interlocked structure and occurrence of multiple interactions produce an open sponge-like particle that is generally resistant to spatial changes. The structural arrangement within the casein supramolecule can be modified by environmental changes that modify hydrophobic interactions and calcium phosphate solubility. This is discussed in relation to microstructure imaging using electron microscopy and changes that occur during acid coagulation, heating, and ethanol addition.

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References

  • Anema, S.G. and Klostermeyer, H. (1997). Heat-induced, pH-dependent dissociation of casein micelles on heating reconstituted skim milk at temperatures below 100°C. J. Agric. Food Chem. 45, 1108–1115.

    CAS  Google Scholar 

  • Anema, S.G. and Li, Y. (2003). Effect of pH on the association of denatured whey proteins with casein micelles in heated reconstituted skim milk. J. Agric. Food Chem. 51, 1640–1646.

    CAS  Google Scholar 

  • Aoki, T., Kako, Y. and Imamura, T. (1986). Separation of casein aggregates cross-linked by colloidal calcium phosphate from bovine casein micelles by high performance gel chromatography in the presence of urea. J. Dairy Res. 53, 53–59.

    CAS  Google Scholar 

  • Aoki, T., Umeda, T. and Kako, Y. (1992). The least number of phosphate groups for crosslinking of casein by colloidal calcium phosphate. J. Dairy Sci. 75, 971–975.

    CAS  Google Scholar 

  • Aoki, T., Yamada, N., Kako, Y. and Imamura, T. (1988). Dissociation during dialysis of casein aggregates cross-linked by colloidal calcium phosphate in bovine casein micelles. J. Dairy Res. 55, 189–195.

    CAS  Google Scholar 

  • Bloomfield, V.A. (1979). Association of proteins. J. Dairy Res. 46, 241–252.

    CAS  Google Scholar 

  • Bloomfield, V.A. and Mead, R.J., Jr. (1975). Structure and stability of casein micelles. J. Dairy Sci. 58, 592–601.

    CAS  Google Scholar 

  • Bloomfield, V.A. and Morr, C.V. (1973). Structure of casein micelles: physical methods. Neth. Milk Dairy J. 27, 103–120.

    CAS  Google Scholar 

  • Bylund, G. et al. (2003). Dairy Processing Handbook, 2nd edn., Tetra Pak Processing Systems AB, Lund, Sweden.

    Google Scholar 

  • Corredig, M. and Dalgleish, D.G. (1996). The binding of α-lactalbumin and β-lactoglobulin to casein micelles in milk treated by different heating systems. Milchwissenschaft 51, 123–127.

    CAS  Google Scholar 

  • Dalgleish, D.G. (2011). On the structural models of bovine casein micelles–review and possible improvements. Soft Matter 7, 2265–2272.

    CAS  Google Scholar 

  • Dalgleish, D.G. and Law, A.J.R. (1988). pH-induced dissociation of bovine casein micelles. I. Analysis of liberated caseins. J. Dairy Res. 55, 529–538.

    CAS  Google Scholar 

  • Dalgleish, D.G. and Parker, T. G. (1979). Quantitation of αS1-casein aggregation by the use of polyfunctional models. J. Dairy Res. 46, 259–263.

    CAS  Google Scholar 

  • Dalgleish, D.G., Spagnuolo, P.A. and Goff, H.D. (2004). A possible structure of the casein micelle based on high-resolution scanning electron microscopy. Int. Dairy J. 14, 1025–1031.

    CAS  Google Scholar 

  • Davies, F.L., Shankar, P.A. and Brooker, B.E. (1977). A heat-induced change in the ultrastructure of milk and its effect on gel formation in yoghurt. J. Dairy Res. 45, 53–58.

    Google Scholar 

  • de Kruif, C.G. (1998). Supra-aggregates of casein micelles as a prelude to coagulation. J. Dairy Sci. 81, 3019–3028.

    Google Scholar 

  • de Kruif, C.G. and Holt, C. (2003). Casein micelle structure, functions, and interactions, in, Advanced Dairy Chemistry Proteins, 3rd edn., Vol. 1A, P.F. Fox and P.L.H. McSweeney, eds., Kluwer Academic/Plenum Publishers, New York. pp. 233–270.

    Google Scholar 

  • Dickinson, E. and Matsumura, Y. (1991). Time-dependent polymerization of β-lactoglobulin through disulfide bonds at the oil-water interface in emulsions. Int. J. Biol. Macromolecules 13, 26–30.

    CAS  Google Scholar 

  • Dosako, S., Kaminogawa, S., Taneya, S. and Yanauchi, K. (1980). Hydrophobic surface areas and net charge of αs1-, κ-casein and αs1-casein:κ -casein complex. J. Dairy Res. 47, 123–137.

    CAS  Google Scholar 

  • Euston, S.R. and Horne, D.S. (2005). Simulating the self-association of caseins. Food Hydrocolloids 19, 379–386.

    CAS  Google Scholar 

  • Farrell, H.M., Jr. (1973). Models for casein micelle formation. J. Dairy Sci. 56, 1195–1206.

    CAS  Google Scholar 

  • Farrell, H.M., Jr., Brown, E.M., Hoagland, P.D. and Malin, E. L. (2003). Higher order structures of caseins: a paradox, in, Advanced Dairy Chemistry Proteins, 3rd edn., Vol. 1A, P.F. Fox and P.L.H. McSweeney, eds., Kluwer Academic/Plenum Publishers, New York. pp. 203–232.

    Google Scholar 

  • Farrer, D. and Lips, A. (1999). On the self-assembly of sodium caseinate. Int. Dairy J. 9, 281–286.

    CAS  Google Scholar 

  • Farrell, H.M., Jr., Malin, E.L., Brown, E.M. and Qi, P.X. (2006a). Casein micelle structure: what can be learned from milk synthesis and structural biology? Curr. Opin. Colloid Interface Sci. 11, 135–147.

    CAS  Google Scholar 

  • Farrell, H.M., Jr., Qi, P.X. and Uversky, V.N. (2006b). New views of protein structure: applications to the caseins: protein structure and functionality, in, Advances in Biopolymers: Molecules, Clusters, Networks, and Interactions. M.L. Fishman, P.X. Qi, and L. Wisker, eds., Am. Chem. Soc., Washington. pp. 52–70.

    Google Scholar 

  • Garnier, J. (1973). Models of casein micelle structure. Neth. Milk Dairy J. 27, 240–248.

    CAS  Google Scholar 

  • Garnier, J. and Ribadeau-Dumas, B. (1970). Structure of the casein micelle: a proposed model. J. Dairy Res. 37,493–504.

    CAS  Google Scholar 

  • Garnier, J., Yon, J. and Mocquot, G. (1964). Contribution to the study of the association between κ- and αs-caseins at neutral pH. Biochimica et Biophyica. Acta 82, 481–493.

    CAS  Google Scholar 

  • Gebhardt, R., Takeda, N., Kulozik, U. and Doster, W. (2011). Structure and stabilizing interactions of casein micelles probed by high-pressure light scattering and FTIR. J. Phys. Chem. B. 115, 349–2359.

    Google Scholar 

  • Heertje, I., Visser, J. and Smits, P. (1985). Structure formation in acid milk gels. Food Microstruct. 4, 267–278.

    CAS  Google Scholar 

  • Helminen, H.J. and Ericsson, J.L.E. (1968). Studies on mammary gland involution. 1. On the ultrastructure of the lactating mammary gland. J. Ultrastruct. Res. 25, 193–213

    CAS  Google Scholar 

  • Hojou, K., Oikawa, T., Kanaya, K., Kimura, T., and Adachi, K. (1977). Some applications of ion beam sputtering to high resolution electron microscopy. Micron 8, 151–170.

    CAS  Google Scholar 

  • Holt, C. (1992). Structure and stability of bovine casein micelles. Adv. Prot. Chem. 43, 63–151.

    CAS  Google Scholar 

  • Holt, C. (1998). Casein micelle substructure and calcium phosphate interactions studied by sephacryl column chromatography. J. Dairy Sci. 81, 2994–3003.

    CAS  Google Scholar 

  • Holt, C. and Horne, D.S. (1996). The hairy casein micelle: evolution of the concept and its implications for dairy technology. Neth. Milk Dairy J. 50, 85–111.

    CAS  Google Scholar 

  • Holt, C. and Sawyer, L. (1993). Caseins as rheomorphic proteins: interpretation of the primary and secondary structures of the αs1-, β-, and κ-caseins. J. Chem. Soc. Faraday Trans. 89, 2683–2692.

    CAS  Google Scholar 

  • Holt, C., Davies, D.T. and 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. J. Dairy Res. 53, 557–572.

    CAS  Google Scholar 

  • Holt, C., de Kruif, C.G., Tunier, R. and Timmons, P.A. (2003). Substructure of bovine casein micelles by small angle X-ray and neutron scattering. Colloids Surf. A 213, 275–284.

    CAS  Google Scholar 

  • Holt, C., Wahlgren, N.M. and Drakenberg, T. (1996). Ability of a β-CN phosphopeptide to modulate the precipitation of calcium phosphate by forming amorphous dicalcium phosphate nanoclusters. Biochem. J. 314, 1035–1039.

    CAS  Google Scholar 

  • Holt, C., Timmis, P.A., Errington, N. and Leaver, J. (1998). A core-shell model of calcium phosphate nanoclusters stabilized by β− casein phosphopeptides, derived from sedimentation equilibrium and small-angle X-ray and neutron-scattering measurements. Eur. J. Biochem. 252, 73–78.

    CAS  Google Scholar 

  • Horne, D.S. (1986). Steric stabilization and casein micelle stability. J. Coll. Interf. Sci. 111, 250–260.

    CAS  Google Scholar 

  • Horne, D.S. (1992) Alcohol stability, in, Advanced Dairy Chemistry Proteins, 2nd edn., Vol. 1, P.F. Fox, ed., Elsevier Applied Science, New York. pp. 657–589.

    Google Scholar 

  • Horne, D.S. (1998). Casein interactions: casting light on the black boxes, the structure of dairy products. Int. Dairy J. 8, 171–177.

    CAS  Google Scholar 

  • Horne, D.S. (2002a). Casein structure, self assembly and gelation. Curr. Opin. Coll. Interf. Sci. 7, 456–461.

    Google Scholar 

  • Horne, D.S. (2002b). Caseins, micellar structure, in, Encyclopaedia of Dairy Sciences, Vol. 3, R. Roginski, P.F. Fox and J.W Fuquay, eds., Academic Press, NY. pp. 1902–1909.

    Google Scholar 

  • Horne, D.S. (2006). Casein micelle structure: models and muddles. Curr. Opin. Coll. Interf. Sci. 11, 148–153.

    CAS  Google Scholar 

  • Horne, D.S. and Davidson, C.M. (1987). Alcohol stability of bovine skim-milk. Anomalous effects with trifluoroethanol. Milchwissenschaft 42, 509–512.

    CAS  Google Scholar 

  • Horne, D.S., Parker, T.G. and Dalgleish, D.G. (1988). Casein micelles, polycondensation, and fractals, in, Food Colloids, R.D. Bee, P. Richmond and J. Mingins, eds, Royal Soc. Chem., London. pp. 400–406.

    CAS  Google Scholar 

  • Kalab, M., Emmons, D.B., and Sargant, A.G. (1976). Milk gel structure: V. Microstructure of yoghurt as related to the heating of milk. Milchwissenschaft 31, 402–408.

    CAS  Google Scholar 

  • Karlsson, A., Ipsen, R. and Ardö, Y. (2007). Observations of casein micelles in skim milk concentrate by transmission electron microscopy. LWT-Food Sci. Technol. 40, 1102–1107.

    CAS  Google Scholar 

  • Kim, B.Y. and Kinsella, J.E. (1989). Effect of temperature and pH on the coagulation of casein. Milchwissenschaft 44, 622–625.

    CAS  Google Scholar 

  • Kirchmeuer, O. (1973). Arrangement of components, electrical charge and interaction energies of casein micelles. Neth. Milk Dairy J. 27, 191–198.

    Google Scholar 

  • Knoop, A.M., Knoop, E. and Wiechen, A. (1979). Sub-structure of synthetic casein micelles. J. Dairy Res. 46, 357–350.

    Google Scholar 

  • Kumosinski, T.P., Pessen, H., Farrell, H.M., Jr. and Brumberger, H. (1988). Determination of the quaternary structure of bovine caseins by small-angle X-ray scattering. Arch. Biochem. Biophys. 266, 548–561.

    CAS  Google Scholar 

  • Lin, S.H.C., Leong, L.S., Dewan, R.K., Bloomfield, V.A. and Morr, C.V. (1972). Effect of calcium ion on the structure of native bovine casein micelles. Biochem. 11, 1818–1821.

    CAS  Google Scholar 

  • Linderstrøm Lang, K. (1929). Studies on casein. III. On the fractionation of casein. Compt. Rend. Trav. Lab. Carlsberg. 36(9), 1.

    Google Scholar 

  • Lucey, J. A. (2002). Formation and physical properties of milk protein gels. J. Dairy Sci. 85, 281–294.

    CAS  Google Scholar 

  • Malin, E.L., Brown, E.M., Wickham, E.D. and Farrell, H.M., Jr. (2005). Contributions of terminal peptides to the associative behavior of αs1-casein. J. Dairy Sci. 88, 2318–2328.

    CAS  Google Scholar 

  • Marchin, S., Putaux, J.-L., Pignon, F. and Léonil, J. (2007). Effects of the environmental factors on the casein micelle structure studied by cryo transmission electron microscopy and small-angle X-ray scattering/ultrasmall-angle X-ray scattering. J. Chem. Phys. 126(4), 045101 (1–10).

    Google Scholar 

  • McMahon, D.J. and Brown, R.J. (1984). Composition, structure, and integrity of casein micelles: a review. J. Dairy Sci. 67, 499–512.

    CAS  Google Scholar 

  • McMahon, D.J. and McManus, W.R. (1998). Rethinking casein micelle structure using electron microscopy. J. Dairy Sci. 81, 2985–2993.

    CAS  Google Scholar 

  • McMahon, D.J. and Oommen, B.S. (2008). Supramolecular structure of the casein micelle. J. Dairy Sci. 91, 1709–1721.

    CAS  Google Scholar 

  • McMahon, D.J., Du, H., McManus, W.R. and Larsen, K.M. (2009). Microstructural changes in casein supramolecules during acidification of skim milk. J. Dairy Sci. 92, 5854–5867.

    CAS  Google Scholar 

  • Meyer, J.L. and Angino, E.E. (1977). The role of trace metals in calcium urolithiasis. Invest. Urol. 14, 347–350.

    CAS  Google Scholar 

  • Morr, C.V. (1967). Effect of oxalate and urea upon ultracentrifugation properties of raw and heated skim milk casein micelles. J. Dairy Sci. 50, 1744–1751.

    CAS  Google Scholar 

  • O’Connell, J.E., Kelly, A.L., Auty, M.A.E., Fox, P.F. and de Kruif, C.G. (2001a). Ethanol-dependent temperature-induced dissociation of casein micelles. J. Agric. Food Chem. 49, 4420–4423.

    Google Scholar 

  • O’Connell, J.E., Kelly, A.L., Fox, P.F. and de Kruif, C.G. (2001b). Mechanism for the ethanol-dependent heat-induced dissociation of casein micelles. J. Agric. Food Chem. 49, 4424–4428.

    Google Scholar 

  • Oommen, B.S. (2004). Casein Supramolecules: Structure and Coagulation Properties, Ph.D. Dissertation, Utah State University, Logan, UT, USA.

    Google Scholar 

  • Payens, T.A.J. (1966). Association of caseins and their possible relation to structure of the casein micelle. J. Dairy Sci. 49, 1317–1324.

    CAS  Google Scholar 

  • Payens, T.A.J. (1968). Self association and complex formation of αs1- and β-caseins. Biochemical J. 108, 14p.

    CAS  Google Scholar 

  • Payens, T.A.J. and Markwijk, V. (1963). Some features of the association of β-casein. Biochimi. Biophys. Acta 71, 517–530.

    Google Scholar 

  • Payens, T.A.J. and Vreeman, H.J. (1982). Casein micelles and micelles of κ- and β-casein, in, Solution Behavior of Surfactants: Theoretical and Applied Aspects, K.L. Mittal and E.J. Fendler, eds., Vol. 1, Perseus Publishing, Cambridge, MA. pp. 543–571.

    Google Scholar 

  • Pessen, H., Kumosinski, T.F. and Farrell, H.M., Jr. (1989). Small-angle x-ray scattering investigation of the micellar and submicellar forms of bovine casein. J. Dairy Res. 56, 443–451.

    Google Scholar 

  • Pierre, A. and Brule, G. (1981). Mineral and protein equilibria between the colloidal and soluble phases of milk at low temperature. J. Dairy Res. 48, 417–428.

    CAS  Google Scholar 

  • Pierre, A., Brule, G. and Fauquant, J. (1983). Etude de la mobilite du calcium dans le lait a l’aide du calcium. Lait. 63, 473–489.

    CAS  Google Scholar 

  • Pignon, F., Belina, G., Narayanan, T., Paubel, X., Magnin, A. and Gésan-Guiziou, G. (2004). Structure and rheological behavior of casein micelle suspensions during ultrafiltration process. J. Chem. Phys. A 121, 8138–8146.

    CAS  Google Scholar 

  • Rasmussen, L.K., Johnsen, L.B., Tsiora, A., Sørenson, E.S., Thomsen, J.K., Nielsen, N.C., Jakobsen, H.J. and Petersen, T.E. (1999). Disulphide-linked caseins and casein micelles. Int. Dairy J. 9, 215–218.

    CAS  Google Scholar 

  • Roefs, S.P.F.M., Walstra, P., Dalgleish, D.G. and Horne, D.S. (1985). Preliminary note on the change in casein micelles caused by acidification. Neth. Milk Dairy J. 39, 119–122.

    CAS  Google Scholar 

  • Rollema, H.S. (1992). Chemistry of milk proteins, in, Developments in Dairy Chemistry Proteins, Vol. 1, P.F. Fox, ed., Applied Science, London. pp. 111–140.

    Google Scholar 

  • Rollema, H.S. and Brinkhuis, J.A. (1989). A 1H-NMR study of bovine casein micelles; influence of pH, temperature and calcium ions on micellar structure. J. Dairy Res. 56, 417–425.

    CAS  Google Scholar 

  • Rose, D. (1969). A proposed model of micelle structure in bovine milk. Dairy Sci. Abstr. 31, 171–175.

    CAS  Google Scholar 

  • Schmidt, D.G. (1980). Colloidal aspects of casein. Neth. Milk Dairy J. 34, 42–64.

    CAS  Google Scholar 

  • Schmidt, D.G. and Payens, T.A.J. (1976). Micellar aspects of casein, in, Surface and Colloid Science, Vol. 9, E. Matijevic, ed., Wiley-Interscience, New York. pp. 165–229.

    Google Scholar 

  • Schmidt, D.G., Koops, J. and Westerbeek, D. (1977). Properties of artificial casein micelles. 1). Preparation, size distribution and composition. Neth. Milk Dairy J. 31, 328–341.

    CAS  Google Scholar 

  • Schmidt, D.G., van der Spek, C.A., Buchheim, W. and Hinz, A. (1974). On the formation of artificial casein micelles. Milchwissenschaft 29, 455–459.

    CAS  Google Scholar 

  • Schmidt, D.G., Walstra, P. and Buchheim, W. (1973). The size distribution of casein micelles in cow’s milk. Neth. Milk Dairy J. 27, 128.

    Google Scholar 

  • Singh, H., Roberts, M.S., Munro, R.A. and Teo, C.T. (1996a). Acid-induced dissociation of casein micelles in milk: effects of heat treatment. J. Dairy Sci. 79, 1340–1346.

    CAS  Google Scholar 

  • Singh, H., Sharma, R., Taylor, M.W. and Creamer, L.K. (1996b). Heat-induced aggregation and dissociation of protein and fat particles in recombined milk. Neth. Milk Dairy J. 50, 149–166.

    CAS  Google Scholar 

  • Slattery, C.W. (1976). Review: casein micelle structure; an examination of models. J. Dairy Sci. 59, 1547–1556.

    CAS  Google Scholar 

  • Slattery, C.W. (1979). A phosphate-induced sub-micelle equilibrium in reconstituted casein micelle systems. J. Dairy Res. 46, 253–258.

    CAS  Google Scholar 

  • Slattery, C.W. and Evard, R. (1973). A model for the formation and structure of casein micelles from subunits of variable composition. Biochim. Biophys. Acta. 317, 529–538.

    CAS  Google Scholar 

  • Smith, E., Clegg, R. and Holt, C. (2004). A biological perspective on the structure and function of caseins and casein micelles. Int. J. Dairy Technol. 57, 121–126.

    Google Scholar 

  • Snøeren, T.H.M., Klok, H.J., van Hooydonk, A.C.M. and Dammam, A.J. (1984). The voluminosity of casein micelles. Milchwissenschaft 39, 461–463.

    Google Scholar 

  • Swaisgood, H.E. (1992). Chemistry of the caseins, in, Advanced Dairy Chemistry Proteins, 3rd edn., Vol. 1A, P.F. Fox and P.L.H. McSweeney, eds., Kluwer Academic/Plenum Publishers, New York. pp. 63–110.

    Google Scholar 

  • Swaisgood, H.E. (2003). Chemistry of the caseins, in, Advanced Dairy Chemistry Proteins, Vol 1A, P.F. Fox and P.L.H. McSweeney, eds., Kluwer Academic/Plenum Publishers, New York. pp. 139–187.

    Google Scholar 

  • Swaisgood, H.E. and Brunner, J.R. (1973). The caseins. CRC Crit. Rev. Food Technol. 3, 375–414.

    Google Scholar 

  • Thompson, M.P., and Farrell, H.M., Jr. (1973). The casein micelle-the forces contributing to its integrity. Neth. Milk Dairy J. 27, 220–239.

    CAS  Google Scholar 

  • Thurn, A., Buchard, W. and Niki R. (1987). Structure of casein micelles 2. as1-. Coll. Poylmer Sci. 265, 653–666.

    CAS  Google Scholar 

  • Trejo, R., Dokland, T., Jurat-Fuentes, J. and Harte, F. (2011). Cryo-transmission electron tomography of native milk casein micelles. J. Dairy Sci. 94, 5770–5775.

    Google Scholar 

  • Tuiner, R. and de Kruif, C.G. (2002). Stability of casein micelles in milk. J. Chem. Phys. 117, 1290–1295.

    Google Scholar 

  • Udabage, P., McKinnon, I.R. and Augustin, M.A. (2003). The use of sedimentation field flow fractionation and photon correlation spectroscopy in the characterization of casein micelles. J. Dairy Res. 70, 453–459

    CAS  Google Scholar 

  • van Hooydonk, A.C.M., Boerrigter, I.J. and Hagedoorn, H.G. (1986). pH-induced physico-chemical changes of casein micelles in milk and their effect on renneting: 2. Effect of pH on renneting of milk. Neth. Milk Dairy J. 40, 297–313.

    Google Scholar 

  • Walstra, P. (1990). On casein micelles. J. Dairy Sci. 73, 1965–1979.

    CAS  Google Scholar 

  • Walstra, P. (1999). Casein sub-micelles: do they exist? Int. Dairy. J. 9, 189–192.

    CAS  Google Scholar 

  • Waugh, D.F. and Noble, R.W. (1965). Casein micelles: formation and structure. J. Am. Chem. Soc. 78, 2246–2257.

    Google Scholar 

  • Yoshikawa, M., Sasaki, R. and Chiba, H. (1981). Effects of chemical phosphorylation of bovine casein components on the properties related to casein micelle formation. Agric. Biol. Chem. 45, 909–914.

    CAS  Google Scholar 

  • Zadow, J.G. (1993). Alcohol-mediated temperature-induced reversible dissociation of the casein micelle in milk. Aust. J. Dairy Technol. 48, 78–81.

    CAS  Google Scholar 

  • Zhang, Z.P., Fujii, M. and Aoki, T. (1996). Behavior of calcium and phosphate in artificial casein micelles. J. Dairy Sci. 79, 1722–1727.

    CAS  Google Scholar 

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  1. Western Dairy Center, Utah State University, Logan, UT, USA

    D. J. McMahon

  2. Glanbia Nutritionals Research, Twin Falls, ID, USA

    B. S. Oommen

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  1. School of Food and Nutritional Sciences, University College Cork, Cork, College Ro, Ireland

    Paul L. H. McSweeney

  2. Fac. Food Technology & Nutrition, Dept. Food Science, University College Cork, Cork, Ireland

    Patrick F. Fox

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McMahon, D.J., Oommen, B.S. (2013). Casein Micelle Structure, Functions, and Interactions. In: McSweeney, P., Fox, P. (eds) Advanced Dairy Chemistry. Springer, Boston, MA. https://doi.org/10.1007/978-1-4614-4714-6_6

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