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Casein Micelle Structure, Functions and Interactions

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Advanced Dairy Chemistry—1 Proteins

Abstract

In this chapter, we aim to present a consistent description of the structure and functions of caseins and the casein micelle. Function, it must be stressed, is interpreted here to mean both the biological functions of casein in the mammary gland and milk and the function in dairy foods. Thus, we tread a variation of a well-worn path in biology by exploring a structure-function trichotomy.

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References

  • Alaimo, M.H., Wickham, E.D. and Farrell, H.M., Jr. (1999a) Effect of self association of αs1-casein and its cleavage fractions αs1-casein (136-96) and αs1-casein (1-197) on aromatic circular dichroic spectra: comparison with predicted models. Biochim. Biophys. Acta, 1431, 395–409.

    Article  CAS  Google Scholar 

  • Alaimo, M.H., Farrell, H.M., Jr. and Germann, M.W. (1999b) Conformation of the hydrophobic peptide αs1-casein (136-196). Biochim. Biophys. Acta, 1431, 410–20.

    Article  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, 53–9.

    Article  CAS  Google Scholar 

  • Aoki, T., Yamada, N., Tomita, I., Kako, Y. and Imamura, T. (1987) Caseins are cross-linked through their ester phosphate groups by colloidal calcium phosphate. Biochim. Biophys. Acta, 911, 238–43.

    Article  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, 189–95.

    Article  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, 971–5.

    Article  CAS  Google Scholar 

  • Baxter, R.J. (1968) Percus-Yevick equation for hard spheres with surface adhesion. J. Chem. Phys., 49, 2770–4.

    Article  CAS  Google Scholar 

  • Baranyi, M., Brignon, G., Anglade, P. and Ribadeau Dumas, B. (1995) New data on the milk of rabbit (Oryctolagus cuniculus). Comp. Biochem. Physiol., 111B, 407–15.

    CAS  Google Scholar 

  • Berry, G.P. and Creamer, L.K. (1975) The association of β-casein. The importance of the C-terminal region. Biochemistry, 14, 3542–5.

    Article  CAS  Google Scholar 

  • Belton, P.S., Lyster, R.L.J. and Richards, C.P. (1985) The 31P nuclear magnetic resonance spectrum of cows’ milk. J. Dairy Res., 52, 47–54.

    Article  CAS  Google Scholar 

  • Bigelow C.C. (1967) On the average hydrophobicity of proteins and the relation between it and protein structure. J. Theor. Biol. 16, 187–211.

    Article  CAS  Google Scholar 

  • Blanch, E.W., Syme, CD., Holt, C, Goedert, M., Hecht, L. and Barron, L.D. (2002) A Raman optical activity study of rheomorphism in milk and brain proteins: Implications for fibrillogenic propensity. Eur. J. Biochem., 269, 148–56.

    Article  Google Scholar 

  • Brignon, G., Mahé, M.-F., Ribadeau Dumas, B., Mercier, J.-C. and Grosclaude, F. (1990) Two of the three genetic variants of goat αs1-casein which are synthesized at a reduced level have an internal deletion possibly due to altered RNA splicing. Eur. J. Biochem., 193, 237–41.

    Article  CAS  Google Scholar 

  • Creamer, L.K., Berry, G.P. and Mills, O.E. (1977) A study of the dissociation of β-casein from the bovine casein micelle at low temperature. N.Z. J. Dairy Sci. Technol, 12, 58–66.

    CAS  Google Scholar 

  • Cross, K.J., Huq, N.L., Bicknell, W. and Reynolds, E.C. (2001) Cation-dependent structural features of β-casein-(l-25). Biochem. J., 356, 277–86.

    Article  CAS  Google Scholar 

  • Cuilliére, M.L., Trégoat, V., Béné, M.C, Faure, G. and Montagne, P. (1999) Changes in the κ-casein and β-casein concentrations in human milk during lactation. J. Clin. Lab. Anal, 13, 213–8.

    Article  Google Scholar 

  • Dalgleish, D.G. (1983) Coagulation of renneted bovine casein micelles: dependence on temperature, calcium ion concentration and ionic strength. J. Dairy Res., 50, 331–40.

    Article  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, 529–38.

    Article  CAS  Google Scholar 

  • Dalgleish, D.G. and Law, A.J.R. (1989) pH-induced dissociation of bovine casein micelles. II. Mineral solubilization and its relation to casein release. J. Dairy Res., 56, 727–35.

    Article  Google Scholar 

  • Dalgleish, D.G., Home, D.S. and Law, A.J.R. (1989) Size related differences in bovine casein micelles. Biochim. Biophys. Acta, 991, 383–7.

    Article  CAS  Google Scholar 

  • Davies, D.T. and Law, A.J.R. (1977) The composition of whole casein from the milk of Ayrshire cows. J. Dairy Res., 44, 447–54.

    Article  CAS  Google Scholar 

  • Davies, D.T. and 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. J. Dairy Res., 50, 67–75.

    Article  CAS  Google Scholar 

  • De Kruif, CG. (1992) Casein micelles: diffusivity as a function of renneting time. Langmuir, 8, 2932–7.

    Article  Google Scholar 

  • De Kruif, C.G. (1998) Supra-aggregates of casein micelles as a prelude to coagulation. J. Dairy Sci., 81, 3019–28.

    Article  Google Scholar 

  • De Kruif, C.G. (1999) Casein micelle interactions. Int. Dairy J., 9, 183–8.

    Article  Google Scholar 

  • De Kruif, C.G. and Van Miltenburg, J.C (1990) Phase transitions in sterically stabilized silica colloids studied by adiabatic calorimetry. J. Chem. Phys., 93, 6865–9.

    Article  Google Scholar 

  • De Kruif, C.G. and Roefs, S.P.F.M. (1996) Skim milk acidification at low temperatures: a model for the stability of casein micelles. Neth. Milk Dairy J., 50, 113–20.

    Google Scholar 

  • De Kruif, C.G. and Zhulina, E.B. (1996) κ-Casein as a polyelectrolyte brush on the surface of casein micelles. Colloid Surface A: 117, 151–9.

    Article  Google Scholar 

  • De Kruif, C.G., Jeurnink, T.J.M. and Zoon, P. (1992) The viscosity of milk during the initial stages of renneting. Neth. Milk Dairy J., 46, 123–37.

    Google Scholar 

  • Dev, B.C., Sood, S.M., De Wind, S. and Slattery, C.W. (1994) κ-Casein and β-caseins in human milk micelles. Arch. Biochem. Biophys., 314, 329–36.

    Article  CAS  Google Scholar 

  • Dhont, J.K.G. (1996) An Introduction to Dynamics of Colloids, Elsevier Science, Amsterdam.

    Google Scholar 

  • Dickinson, E. (2000) Structure and rheology of simulated gels formed from aggregated colloidal particles. J. Colloid. Interf. Sci., 225, 2–15.

    Article  CAS  Google Scholar 

  • Donnelly, W.J, McNeill, G.P., Buchheim, W. and McGann, T.C.A. (1984) A comprehensive study of the relationship between size and protein composition in natural bovine casein micelles. Biochim. Biophys. Acta, 789, 136–43.

    Article  CAS  Google Scholar 

  • Ellegård, K.H., Gammelgård-Larsen, C, Sørensen, E.S. and Fedosov, S. (1999) Process scale Chromatographic isolation, characterization and identification of tryptic bioactive casein phosphopeptides. Int. Dairy J., 9, 639–52.

    Article  Google Scholar 

  • Evans, M.T.A., Phillips, M.C. and Jones, M.N. (1979) The conformation and aggregation of bovine β-casein A. II. Thermodynamics of thermal association and the effects of changes in polar and apolar interactions on micellization. Biopolymers, 18, 1123–40.

    Article  CAS  Google Scholar 

  • Greenberg, R., Groves, M.L. and Dower, H.J. (1984) Human β-casein amino acid sequence and identification of phosphorylation sites. J. Biol. Chem., 259, 5132–8.

    CAS  Google Scholar 

  • Griffin, M.C.A. (1987) Structural studies of casein micelles using photon correlation spectroscopy. J. Colloid. Interf. Sci., 115, 499–506.

    Article  CAS  Google Scholar 

  • Griffin, M.C.A. and Roberts, G.C.K. (1985) A 1H-n.m.r. study of casein micelles. Biochem. J., 228, 273–6.

    CAS  Google Scholar 

  • Griffin, M.C.A., Lyster, R.L.J. and Price, J.C. (1988) The disaggregation of calcium-depleted casein micelles. Eur. J. Biochem., 174, 339–43.

    Article  CAS  Google Scholar 

  • Groves, M.L., Dower, H.J. and Farrell, H.M., Jr. (1992) Reexamination of the polymeric distributions of κ-casein isolated from bovine milk. J. Protein Chem., 11, 21–8.

    Article  CAS  Google Scholar 

  • Hambraeus, L. (1992) Nutritional aspects of milk proteins. In Advanced Dairy Chemistry, Volume 1, 2nd edn., (P.F. Fox ed.) Elsevier Applied Science, Barking, Essex, UK, pp. 457–90.

    Google Scholar 

  • Hansen, S., Bauer, R., Lomholt, S.B., Bruun Qvist, K., Pedersen, J.S. and Mortensen, K. (1996) Structure of casein micelles studied by small-angle neutron scattering. Eur. Biophys. J., 24, 143–7.

    Article  CAS  Google Scholar 

  • Holt, C. (1985) The size distribution of bovine casein micelles. Food Microstruct., 4, 1–10.

    CAS  Google Scholar 

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

    Article  CAS  Google Scholar 

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

    Article  CAS  Google Scholar 

  • Holt, C. and Dalgleish, D.G. (1986) Electrophoretic and hydrodynamic properties of bovine casein micelles interpreted in terms of particles with an outer hairy layer. J. Colloid Interf. Sci., 114, 513–24.

    Article  CAS  Google Scholar 

  • Holt, C. and Home, D.S. (1996) The hairy casein micelle: Evolution of the concept and its implications for dairy processing. Neth. Milk Dairy J., 50, 1–27.

    Google Scholar 

  • Holt, C. and Hukins, D.W.L. (1991) Structural analysis of the environment of calcium ions in crystalline and amorphous calcium phosphates by X-ray absorption spectroscopy and a hypothesis concerning the biological function of the casein micelle. Int. Dairy J., 1, 151–65.

    Article  CAS  Google Scholar 

  • Holt, C. and Jenness, R. (1984) Interrelationships of constituents and partition of salts in milk samples from eight species. Comp. Biochem. Physiol., 77A, 275–82.

    Article  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, 2683–92.

    Article  CAS  Google Scholar 

  • Holt, C. and Van Kemenade, M.J.J.M. (1989) Interaction of phosphoproteins with calcium phosphates. In Calcified Tissue, (D.W.L. Hukins ed.) Macmillan, London, pp. 175–213.

    Google Scholar 

  • Holt, C, Davies, D.T. and Law, A.J.R. (1986) The effects of colloidal calcium phosphate content and milk serum free calcium ion concentration on the dissociation of bovine casein micelles. J. Dairy Res., 53, 557–72.

    Article  CAS  Google Scholar 

  • Holt, C, Wahlgren, N.M. and Drakenberg, T. (1996) Ability of a β-casein phosphopeptide to modulate the precipitation of calcium phosphate by forming amorphous dicalcium phosphate nanoclusters. Biochem. J., 314, 1035–9.

    CAS  Google Scholar 

  • Holt, C, Timmins, P.A., Errington, N. and Leaver, J. (1998) A core-shell model of calcium phosphate nanoclusters derived from sedimentation equilibrium and small angle X-ray and neutron scattering measurements. Eur. J. Biochem., 252, 73–8.

    Article  CAS  Google Scholar 

  • Holt, C, Drakenberg, T., Errington, N., De Kruif, C.G., Leaver, J., Timmins, P.A, Tuinier, R. and Wahlgren, N.M. (1999) Effect of pH and calcium, phosphate and phosphopeptide concentrations on the size and substructure of calcium phosphate nanoclusters as determined by X-ray and neutron scattering and circular dichroism spectroscopy. Fibre Diffraction Review, 8, 74–5.

    Google Scholar 

  • Home, D.S. (1992) Ethanol stability. In Advanced Dairy Chemistry, Volume 1, 2nd Edn., (P.F. Fox ed.) Elsevier Applied Science, Barking, Essex, UK, pp. 657–90.

    Google Scholar 

  • Horne, D.S. (1998) Casein interactions: casting light on the black boxes, the structure in dairy products. Int. Dairy J., 8, 171–7.

    Article  CAS  Google Scholar 

  • Home, D.S., Parker, T.G. and Dalgleish, D.G. (1989) Casein micelles, polycondensation and fractals. In Food Colloids, (R.D. Bee, P. Richmond and J. Mingins eds.) Special Publication No. 75, Royal Society of Chemistry, London, pp. 400–5.

    Google Scholar 

  • Huq, N.L., Cross, K.J. and Reynolds, E.C. (1995) A 1H-NMR study of the casein phosphopeptide αs1-casein (59-79). Biochim. Biophys. Acta, 1247, 201–8.

    Article  Google Scholar 

  • Jenness, R. (1979a) Comparative aspects of milk proteins. J. Dairy Res., 46, 197–210.

    Article  CAS  Google Scholar 

  • Jenness, R. (1979b) The composition of milk. In Lactation-A Comprehensive Treatise, Vol. 3, (B.L. Larson and V.R. Smith eds.) Academic Press, New York, pp. 3–37.

    Google Scholar 

  • Jeurnink, T.J.M and De Kruif, C.G. (1993) Changes in milk on heating: viscosity measurements. J. Dairy Res., 60, 139–50.

    Article  Google Scholar 

  • Kent, J.C., Arthur, P.G. and Hartmann, P.E. (1998) Citrate, calcium phosphate and magnesium in cow’s milk at initiation of lactation. J. Dairy Res., 65, 55–68.

    Article  CAS  Google Scholar 

  • Kitts, D.D. and Yuan, Y.V. (1992) Caseinophosphopeptides and calcium bioavailability. Trends Food Sci. Tech., 3, 31–5.

    Article  CAS  Google Scholar 

  • Kroening, T.A., Mukerji, P. and Hards, R.G. (1998) Analysis of β-casein and its phosphoforms in human milk. Nutr. Res., 18, 1175–86.

    Article  CAS  Google Scholar 

  • Kurkela, S. and Frank, M. (1990) Cloning and characterization of a cold-and ABA-inducible Arabidopsis gene. Plant Mol. Biol, 15, 137–44.

    Article  CAS  Google Scholar 

  • Langendorff, V., Cuvelier, G., Launay, B., Michon, C, Parker, A. and De Kruif, C.G. (2000) Effect of carrageenan type on the behaviour of carrageenan/milk mixtures. Food Hydrocolloid, 14, 273–80.

    Article  CAS  Google Scholar 

  • Lekkerkerker, H.N.W., Poon, W.C.K., Pusey, P.N., Stroobants, A. and Warren, P.B. (1992) Phase behaviour of colloid + polymer mixtures. Europhys. Lett., 20, 559–62.

    Article  CAS  Google Scholar 

  • Le Questel, J.Y., Morris, D.G, MacCallum, P.H. and Milner-White, E.J. (1993) Common ring motifs in proteins involving asparagine or glutamine amide groups hydrogen-bonded to main chain atoms. J. Mol. Biol., 231, 888–96.

    Article  Google Scholar 

  • Lieske, B, Faber, W. and Konrad, G. (1999) Effect of pH on results of size fractionation of bovine casein micelles using porous glass chromatography. Milchwissenschaft, 54, 9–13.

    CAS  Google Scholar 

  • Lyster, R.L.J., Mann, S.M., Parker, S.B. and Williams, R.J.P. (1984) Nature of micellar calcium phosphate in cow’s milk as studied by high resolution electron microscopy. Biochim. Biophys. Acta, 801, 315–7.

    Article  CAS  Google Scholar 

  • Martin, P. (1999) Genetic polymorphism of caseins: a tool to investigate casein micelle organisation. Int. Dairy J., 9, 163–71.

    Article  CAS  Google Scholar 

  • Marozine, A. and De Kruif, C.G. (2000) Interaction of pectin and casein micelles. Food Hydrocolloid, 391–4.

    Google Scholar 

  • Mellema, M., Leermakers, F.A.M. and De Kruif, C.G. (1999) Molecular mechanism of the renneting process of skim milk examined by viscosity and light scattering experiments and simulated by SCF calculations. Langmuir, 15, 6304–13.

    Article  CAS  Google Scholar 

  • Mellema, M., van Opheusden, J.H. and van Vliet, T. (1999) Relating colloidal particle interactions to gel structure using Brownian dynamics simulations and the Fuchs stability ratio. J. Chem. Phys., 111, 6129–35.

    Article  CAS  Google Scholar 

  • McGann, T.C.A. and Fox, P.F. (1974) Physico-chemical properties of casein micelles reformed from urea-treated milk. J. Dairy Res., 41, 45–53.

    Article  CAS  Google Scholar 

  • McMahon, D.J. and McManus, W.R. (1998) Rethinking casein micelle structure using electron microscopy. J. Dairy Sci., 81, 2985–93.

    Article  CAS  Google Scholar 

  • Neville, M.C., Keller, R.P., Casey, C. and Allen, J.C. (1994) Calcium partitioning in human and bovine milk. J. Dairy Sci., 77, 1964–75.

    Article  CAS  Google Scholar 

  • Niewold, T.A., Murphy, C.L., Hulskamp-Kloch, C.A.M., Tooten, P.C.J. and Gruys, E. (1999) Casein related amyloid, characterization of a new and unique amyloid protein isolated from bovine corpora amylacea. Amyloid, 6, 244–9.

    CAS  Google Scholar 

  • Ono, T., Ohotawa, T. and Takagi, Y. (1994) Complexes of casein phosphopeptide and calcium phosphate prepared from casein micelles by tryptic digestion. Biosci. Biotech. Biochem., 58, 1376–80.

    Article  CAS  Google Scholar 

  • Payens, T.A.J. and Vreeman, H. (1982) Casein micelles and micelles of β-and κ-casein. In Solution Behaviour of Surfactants, Vol. 1, (K.L. Mittal and E.J. Fendler eds.) Plenum Publishing House, New York, pp. 543–71.

    Chapter  Google Scholar 

  • Pierre, A., Brulé, G. and Fauquant, J. (1983) Study of Ca exchange in milk using 45Ca. Lait, 63, 473–80.

    Article  CAS  Google Scholar 

  • Pierre, A., Michel, F., Le Graët, Y. and Zahoute, L. (1998) Composition of casein micelle size in relation with casein composition and αs1, αS2, β and κ casein contents in goat milk. Lait, 78, 591–605.

    Article  CAS  Google Scholar 

  • Pierre, A., Michel, F. and Zahoute, L. (1999) Composition of casein micelles in relation to size in goat milks with A and null αsl-casein variants. Int. Dairy J., 9, 179–82.

    Article  CAS  Google Scholar 

  • Rasmussen, L.K., Højrup, P. and Petersen, T.E. (1992a) Localisation of two interchain disulfide bridges in dimers of bovine αs2-casein. Parallel and antiparallel alignments of the polypeptide chains. Eur. J. Biochem., 203, 381–6.

    Article  CAS  Google Scholar 

  • Rasmussen, L.K., Højrup, P. and Petersen, T.E. (1992b) The multimeric structure and disulfide bonding pattern of bovine κ-casein. Eur. J. Biochem., 207, 215–22.

    Article  CAS  Google Scholar 

  • Rasmussen, L.K., Johnsen, L.B., Tsiora, A., Sørensen, 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, 215–8.

    Article  CAS  Google Scholar 

  • Rollema, H.S. (1992) Casein association and micelle formation. In Advanced Dairy Chemistry Volume 1, (P.F. Fox ed.) Elsevier Applied Science, Barking, Essex, UK, pp. 111–40.

    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, 417–25.

    Article  CAS  Google Scholar 

  • Rollema, H.S., Brinkhuis, J.A. and Vreeman, H.J. (1988) 1H-NMR studies of bovine κ-casein and casein micelles. Neth. Milk Dairy J., 42, 233–48.

    CAS  Google Scholar 

  • Schmidt, D.G. (1982) Association of caseins and casein micelle structure. In Developments in Dairy Chemistry, (P.F. Fox ed.) Applied Science Publishers, Barking, UK, pp. 61–86.

    Google Scholar 

  • Schweers, O., Schönbrunn-Hanebeck, E., Marx, A. and Mandelkow, E. (1994) Structural studies of tau protein and Alzheimer paired helical filaments show no evidence for β-structure. J. Biol. Chem., 269, 24290–7.

    CAS  Google Scholar 

  • Serpell, L.C., Berriman, J., Jakes, R., Goedert, M. and Crowther, R.A. (2000) Fiber diffraction of synthetic α-synuclein filaments shows amyloid-like cross-β conformation Proc. Natl. Acad. Sci., USA, 97, 4897–902.

    Article  CAS  Google Scholar 

  • Shewry, P.R. and Tatham, A.S. (1990) The prolamin storage proteins of cereal seeds: structure and evolution. Biochem. J., 267, 1–12.

    CAS  Google Scholar 

  • Simon, J-P. and Aunis, D. (1989) Biochemistry of the chromogranin A protein family. Biochemical J., 262, 1–13.

    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, 529–38.

    Article  CAS  Google Scholar 

  • Smyth, E., Syme, CD., Blanch, E.W., Hecht, L., Vašák, M. and Barron, L.D. (2000) Solution structure of native proteins with irregular folds from Raman optical activity. Biopolymers, 58, 138–51.

    Article  Google Scholar 

  • Stenkamp, V.S. and Berg, J.C. (1997) The role of long tails in steric stabilization and hydrodynamic layer thickness. Langmuir, 13, 3827–32.

    Article  CAS  Google Scholar 

  • Stothart, P.H. and Cebula, D.J. (1982) Small-angle neutron scattering study of bovine casein micelles and sub-micelles. J. Mol. Biol., 160, 391–5.

    Article  CAS  Google Scholar 

  • Swaisgood, H.E. (1992) Chemistry of the caseins. In Advanced Dairy Chemistry Volume 1, (P.F. Fox ed.) Elsevier Applied Science, Barking, Essex, UK, pp. 63–110.

    Google Scholar 

  • Syrba, A. (1998) Polymer science concepts in dairy systems-An overview of milk protein and food hydrocolloid interactions. Int. Dairy J., 8, 179–94.

    Article  Google Scholar 

  • Thompson, M.P., Kalan, E.B. and Greenberg, R. (1967) Properties of caseins modified by treatment with carboxypeptidase A. J. Dairy Sci., 50, 767–9.

    Article  CAS  Google Scholar 

  • Tsuda, S., Niki, R., Kuwata, T., Tanaka, I. and Hickichi, K. (1991) Proton NMR study of casein phosphopeptide (1-25): assignment and conformation. Magn. Reson. Chem., 28, 1097–102.

    Article  Google Scholar 

  • Tuinier, R. and De Kruif, CG. (1999) Phase behaviour of casein micelles/ exocellular polysaccharide mixtures: experiment and theory. J. Chem. Phys., 110, 9296.

    Article  CAS  Google Scholar 

  • Tuinier, R., Ten Grotenhuis, E., Holt, C, Timmins, P.A. and De Kruif, CG. (1999a) Depletion interaction of casein micelles and an exocellular polysaccharide. Phys. Rev. E, 60, 848–56.

    Article  CAS  Google Scholar 

  • Tuinier, R., Zoon, P., Olieman, C, Cohen Stuart, M.A., Fleer, G.J. and De Kruif, CG. (1999b) Isolation and physical characterization of an exocellular polysaccharide. Biopolymers, 49, 1–9.

    Article  CAS  Google Scholar 

  • Tuinier, R., Dhont, J.K.G. and De Kruif, CG. (2000a) Depletion induced phase separation of aggregated whey proteins. Langmuir, 16, 1497–507.

    Article  CAS  Google Scholar 

  • Tuinier, R., Ten Grotenhuis, E. and De Kruif, CG. (2000b) The effect of depolymerised guar gum on the stability of skim milk. Food Hydrocolloid, 14, 1–7.

    Article  CAS  Google Scholar 

  • Tziboula, A. and Home, D.S. (1999) The role of αsl-casein in the structure of caprine casein micelles. Int. Dairy J., 9, 173–8.

    Article  CAS  Google Scholar 

  • Van Kemenade, M.J.J.M. (1988) Influence of Casein on Precipitation of Calcium Phosphates, PhD Thesis, van’t Hoff Laboratorium, Rijksuniversiteit Utrecht, The Netherlands.

    Google Scholar 

  • Vreeman, HJ., Brinkhuis, J.A. and Van der Spek, C.A. (1981) Some association properties of SH-κ-casein. Biophys. Chem., 14, 185–93.

    Article  CAS  Google Scholar 

  • Vreeman, H.J., Van Markwijk, B.W. and Both, P. (1989) The structure of casein micelles between pH 5.5 and 6.7 as determined by light scattering, electron microscopy and voluminosity experiments. J. Dairy Res., 56, 463–70.

    Article  Google Scholar 

  • Vrij, A. (1976) Polymers at interfaces and the interactions in colloidal dispersions. Pure Appl. Chem., 48, 471–83.

    Article  CAS  Google Scholar 

  • Wahlgren, N.M., Dejmek, P. and Drakenberg, T. (1990) A 45Ca and 31P NMR study of the calcium and phosphate equilibria in heated milk solutions. J. Dairy Res., 57, 355–64.

    Article  CAS  Google Scholar 

  • Wahlgren, N.M., Léonil, J., Dejmek, P. and Drakenberg, T. (1993) Two dimensional nuclear magnetic resonance study of the β-casein peptide 1-25: resonance assignments and secondary structure. Biochim. Biophys. Acta, 1202, 121–8.

    Article  CAS  Google Scholar 

  • Wahlgren, N.M., Dejmek, P. and Drakenberg, T. (1994) Secondary structures in β-casein peptide 1-42: a two dimensional nuclear magnetic resonance study. J. Dairy Res., 61, 495–506.

    Article  CAS  Google Scholar 

  • Walstra, P. (1999) Casein sub-micelles: do they exist? Int. Dairy J., 9, 189–92.

    Article  CAS  Google Scholar 

  • Walstra, P., Bloomfield, V.A., Wei, G.J. and Jenness, R. (1981) Effect of chymosin action on the hydrodynamic diameter of casein micelles. Biochim. Biophys. Acta, 669, 258–9.

    Article  CAS  Google Scholar 

  • Waugh, D.F. (1971) Formation and structure of casein micelles. In Milk Proteins: Chemistry and Molecular Biology, Vol. 2, (H.A. McKenzie ed.) Academic Press, New York, pp. 3–85.

    Google Scholar 

  • Weinreb, P.H., Zhen, W., Poon, A.W., Conway, K.A. and Lansbury, P.T., Jr. (1996) NACP, a protein implicated in Alzheimer’s disease and learning is natively unfolded. Biochemistry, 35, 13709–15.

    Article  CAS  Google Scholar 

  • Yamauchi, K., Yoneda, Y., Koga, Y. and Tsugo, T. (1969) Exchangeability of colloidal calcium in milk with soluble calcium. Agr. Biol. Chem., 33, 907–14.

    Article  CAS  Google Scholar 

  • Zhang, Z.P. and Aoki, T. (1996) Behaviour of calcium and phosphate in bovine casein micelles. Int. Dairy J., 6, 769–80.

    Article  CAS  Google Scholar 

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Authors
  1. C. G. De Kruif
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  2. C. Holt
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Editors and Affiliations

  1. Department of Food Science, Food Technology and Nutrition, University College, Cork, Ireland

    P. F. Fox  & P. L. H. McSweeney  & 

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De Kruif, C.G., Holt, C. (2003). Casein Micelle Structure, Functions and Interactions. In: Fox, P.F., McSweeney, P.L.H. (eds) Advanced Dairy Chemistry—1 Proteins. Springer, Boston, MA. https://doi.org/10.1007/978-1-4419-8602-3_5

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  • DOI: https://doi.org/10.1007/978-1-4419-8602-3_5

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