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Volumn 11, Issue 2-3, 2006, Pages 148-153

Casein micelle structure: Models and muddles

Author keywords

Calcium phosphate nanoclusters; Casein micelle models; Casein micelle structure; Caseins; Hydrophobic interactions; Micellar calcium phosphate

Indexed keywords

CALCIUM COMPOUNDS; CONSTRAINT THEORY; HYDROPHOBICITY; MATHEMATICAL MODELS; NANOSTRUCTURED MATERIALS;

EID: 33744991713     PISSN: 13590294     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cocis.2005.11.004     Document Type: Review
Times cited : (341)

References (44)
  • 1
    • 0034942313 scopus 로고    scopus 로고
    • Roads taken by milk proteins in mammary epithelial cells
    • A good summary of casein synthesis and expression.
    • Boisgard R., Chanat E., Lavialle F., Pauloin A., and Ollivier-Bousquet. Roads taken by milk proteins in mammary epithelial cells. Livest Prod Sci 70 (2001) 49-61. A good summary of casein synthesis and expression.
    • (2001) Livest Prod Sci , vol.70 , pp. 49-61
    • Boisgard, R.1    Chanat, E.2    Lavialle, F.3    Pauloin, A.4    Ollivier-Bousquet5
  • 2
    • 0348114294 scopus 로고    scopus 로고
    • Casein micelle structure, functions and interactions
    • Advanced dairy chemistry. 3rd edn. Fox P.F., and McSweeney P.L.H. (Eds), Kluwer Academic/Plenum Publishers, New York. An attempt at justifying the Holt model distinguished by its continuing omission of a role for κ-casein and neglect of casein interactions outwith the phosphoserine cluster.
    • DeKruif C.G., and Holt C. Casein micelle structure, functions and interactions. In: Fox P.F., and McSweeney P.L.H. (Eds). Advanced dairy chemistry. 3rd edn. Proteins vol. 1 (2003), Kluwer Academic/Plenum Publishers, New York 213-276. An attempt at justifying the Holt model distinguished by its continuing omission of a role for κ-casein and neglect of casein interactions outwith the phosphoserine cluster.
    • (2003) Proteins , vol.1 , pp. 213-276
    • DeKruif, C.G.1    Holt, C.2
  • 4
    • 2442701167 scopus 로고    scopus 로고
    • An equilibrium thermodynamic model of the sequestration of calcium phosphate by casein micelles and its application to the calculation of the partition of salts in milk
    • Holt C. An equilibrium thermodynamic model of the sequestration of calcium phosphate by casein micelles and its application to the calculation of the partition of salts in milk. Eur Biophys J 33 (2004) 421-434
    • (2004) Eur Biophys J , vol.33 , pp. 421-434
    • Holt, C.1
  • 5
    • 2442702509 scopus 로고    scopus 로고
    • An equilibrium thermodynamic model of the sequestration of calcium phosphate by casein phosphopeptides
    • Little E.M., and Holt C. An equilibrium thermodynamic model of the sequestration of calcium phosphate by casein phosphopeptides. Eur Biophys J 33 (2004) 435-447
    • (2004) Eur Biophys J , vol.33 , pp. 435-447
    • Little, E.M.1    Holt, C.2
  • 6
    • 2442637545 scopus 로고    scopus 로고
    • A biological perspective on the structure and function of caseins and casein micelles
    • Smyth E., Clegg R.A., and Holt C. A biological perspective on the structure and function of caseins and casein micelles. Int J Dairy Technol 57 (2004) 121-126
    • (2004) Int J Dairy Technol , vol.57 , pp. 121-126
    • Smyth, E.1    Clegg, R.A.2    Holt, C.3
  • 7
    • 27144501029 scopus 로고    scopus 로고
    • Milk proteins; general and historical behaviour
    • Advanced dairy chemistry. 3rd edn. Fox P.F., and McSweeney P.L.H. (Eds), Kluwer Academic/Plenum Publishers, New York. The introductory chapter to the third edition of this 'bible' of dairy chemistry.
    • Fox P.F. Milk proteins; general and historical behaviour. In: Fox P.F., and McSweeney P.L.H. (Eds). Advanced dairy chemistry. 3rd edn. Proteins vol. 1 (2003), Kluwer Academic/Plenum Publishers, New York 1-48. The introductory chapter to the third edition of this 'bible' of dairy chemistry.
    • (2003) Proteins , vol.1 , pp. 1-48
    • Fox, P.F.1
  • 8
    • 0018463650 scopus 로고
    • Comparative aspects of milk proteins
    • Jenness R. Comparative aspects of milk proteins. J Dairy Res 46 (1979) 197-210
    • (1979) J Dairy Res , vol.46 , pp. 197-210
    • Jenness, R.1
  • 9
    • 1642280788 scopus 로고    scopus 로고
    • Non-bovine caseins: quantitative variability and molecular diversity
    • Advanced dairy chemistry. 3rd edn. Fox P.F., and McSweeney P.L.H. (Eds), Kluwer Academic/Plenum Publishers, New York. An authoritative chapter on a wide-ranging subject.
    • Martin P., Ferranti P., Leroux C., and Addeo F. Non-bovine caseins: quantitative variability and molecular diversity. In: Fox P.F., and McSweeney P.L.H. (Eds). Advanced dairy chemistry. 3rd edn. Proteins vol. 1 (2003), Kluwer Academic/Plenum Publishers, New York 277-317. An authoritative chapter on a wide-ranging subject.
    • (2003) Proteins , vol.1 , pp. 277-317
    • Martin, P.1    Ferranti, P.2    Leroux, C.3    Addeo, F.4
  • 10
    • 0032029213 scopus 로고    scopus 로고
    • Casein interactions: casting light on the black boxes, the structure in dairy products
    • The paper which introduced the notion that caseins be treated as block copolymers and applied this to casein self-association and micelle formation.
    • Horne D.S. Casein interactions: casting light on the black boxes, the structure in dairy products. Int Dairy J 8 (1998) 171-177. The paper which introduced the notion that caseins be treated as block copolymers and applied this to casein self-association and micelle formation.
    • (1998) Int Dairy J , vol.8 , pp. 171-177
    • Horne, D.S.1
  • 11
    • 0021760656 scopus 로고
    • A comprehensive study of the relationship between size and protein composition in natural bovine casein micelles
    • Donnelly W.J., McNeill G.P., Buchheim W., and McGann T.C.A. A comprehensive study of the relationship between size and protein composition in natural bovine casein micelles. Biochim Biophys Acta 789 (1984) 136-143
    • (1984) Biochim Biophys Acta , vol.789 , pp. 136-143
    • Donnelly, W.J.1    McNeill, G.P.2    Buchheim, W.3    McGann, T.C.A.4
  • 12
  • 15
    • 0001871181 scopus 로고    scopus 로고
    • The hairy casein micelle: evolution of the concept and its implications for dairy technology
    • A summary of the steric stabilization model as it stood in the mid-nineties.
    • Holt C., and Horne D.S. The hairy casein micelle: evolution of the concept and its implications for dairy technology. Neth Milk Dairy J 50 (1996) 85-111. A summary of the steric stabilization model as it stood in the mid-nineties.
    • (1996) Neth Milk Dairy J , vol.50 , pp. 85-111
    • Holt, C.1    Horne, D.S.2
  • 16
    • 0036441109 scopus 로고    scopus 로고
    • Structure, dynamics and optical properties of concentrated milk suspensions: an analogy to hard-sphere liquids
    • Alexander M., Rojas-Ochoa L.F., Leser M., and Schurtenberger P. Structure, dynamics and optical properties of concentrated milk suspensions: an analogy to hard-sphere liquids. J Colloid Interface Sci 253 (2002) 34-46
    • (2002) J Colloid Interface Sci , vol.253 , pp. 34-46
    • Alexander, M.1    Rojas-Ochoa, L.F.2    Leser, M.3    Schurtenberger, P.4
  • 17
    • 0030588089 scopus 로고    scopus 로고
    • κ-Casein as a polyelectrolyte brush on the surface of casein micelles
    • DeKruif C.G., and Zhulina E.B. κ-Casein as a polyelectrolyte brush on the surface of casein micelles. Colloids Surf A Physicochem Eng Asp 117 (1996) 151-159
    • (1996) Colloids Surf A Physicochem Eng Asp , vol.117 , pp. 151-159
    • DeKruif, C.G.1    Zhulina, E.B.2
  • 18
    • 0037101011 scopus 로고    scopus 로고
    • Stability of casein micelles in milk
    • An attempt to provide an intermicellar potential based on a simple summation of contributions, but neglecting the effects of changes in micellar internal structure.
    • Tuinier R., and DeKruif C.G. Stability of casein micelles in milk. J Chem Phys 117 (2002) 1290-1295. An attempt to provide an intermicellar potential based on a simple summation of contributions, but neglecting the effects of changes in micellar internal structure.
    • (2002) J Chem Phys , vol.117 , pp. 1290-1295
    • Tuinier, R.1    DeKruif, C.G.2
  • 19
    • 0000499218 scopus 로고
    • Ethanol stability
    • Advanced dairy chemistry. 2nd edn. Fox P.F. (Ed), Elsevier Applied Science, London
    • Horne D.S. Ethanol stability. In: Fox P.F. (Ed). Advanced dairy chemistry. 2nd edn. Proteins vol. 1 (1992), Elsevier Applied Science, London 657-681
    • (1992) Proteins , vol.1 , pp. 657-681
    • Horne, D.S.1
  • 20
    • 0012856735 scopus 로고    scopus 로고
    • Ethanol stability
    • Advanced dairy chemistry. 3rd edn. Fox P.F., and McSweeney P.L.H. (Eds), Kluwer Academic/Plenum Publishers, New York
    • Horne D.S. Ethanol stability. In: Fox P.F., and McSweeney P.L.H. (Eds). Advanced dairy chemistry. 3rd edn. Proteins vol. 1 (2003), Kluwer Academic/Plenum Publishers, New York 975-999
    • (2003) Proteins , vol.1 , pp. 975-999
    • Horne, D.S.1
  • 21
    • 0037433089 scopus 로고    scopus 로고
    • Casein micelles as hard spheres: limitations of the model in acidified gel formation
    • Horne D.S. Casein micelles as hard spheres: limitations of the model in acidified gel formation. Colloids Surf A Physicochem Eng Asp 213 (2003) 255-263
    • (2003) Colloids Surf A Physicochem Eng Asp , vol.213 , pp. 255-263
    • Horne, D.S.1
  • 22
    • 0001400692 scopus 로고
    • Measurement of electrophoretic mobilities and zeta potentials of particles from milk using laser Doppler electrophoresis
    • Dalgleish D.G. Measurement of electrophoretic mobilities and zeta potentials of particles from milk using laser Doppler electrophoresis. J Dairy Res 51 (1984) 425-438
    • (1984) J Dairy Res , vol.51 , pp. 425-438
    • Dalgleish, D.G.1
  • 23
    • 0022862357 scopus 로고
    • Electrophoretic and hydrodynamic properties of bovine casein micelles interpreted in terms of particles with an outer hairy layer
    • Holt C., and Dalgleish D.G. Electrophoretic and hydrodynamic properties of bovine casein micelles interpreted in terms of particles with an outer hairy layer. J Colloid Interface Sci 114 (1986) 513-524
    • (1986) J Colloid Interface Sci , vol.114 , pp. 513-524
    • Holt, C.1    Dalgleish, D.G.2
  • 24
    • 0023881538 scopus 로고
    • The disaggregation of calcium-depleted casein micelles
    • Griffin M.C.A., Lyster R.L.J., and Price J.C. The disaggregation of calcium-depleted casein micelles. Eur J Biochem 174 (1988) 339-343
    • (1988) Eur J Biochem , vol.174 , pp. 339-343
    • Griffin, M.C.A.1    Lyster, R.L.J.2    Price, J.C.3
  • 25
    • 0001031111 scopus 로고
    • Effects of colloidal calcium phosphate content and free calcium ion concentration in milk serum on the dissociation of bovine casein micelles
    • Holt C., Davies D.T., and Law A.J.R. Effects of colloidal calcium phosphate content and free calcium ion concentration in milk serum on the dissociation of bovine casein micelles. J Dairy Res 53 (1986) 557-572
    • (1986) J Dairy Res , vol.53 , pp. 557-572
    • Holt, C.1    Davies, D.T.2    Law, A.J.R.3
  • 26
    • 84971758074 scopus 로고
    • pH-induced dissociation of bovine casein micelles: I. Analysis of liberated caseins
    • Dalgleish D.G., and Law A.J.R. pH-induced dissociation of bovine casein micelles: I. Analysis of liberated caseins. J Dairy Res 55 (1988) 529-538
    • (1988) J Dairy Res , vol.55 , pp. 529-538
    • Dalgleish, D.G.1    Law, A.J.R.2
  • 27
    • 0002799525 scopus 로고
    • Physico-chemical properties of casein micelles reformed from urea-treated milk
    • An early paper which indicated that calcium phosphate was not the only 'cement' holding the casein micelle together.
    • McGann T.C.A., and Fox P.F. Physico-chemical properties of casein micelles reformed from urea-treated milk. J Dairy Res 41 (1974) 45-53. An early paper which indicated that calcium phosphate was not the only 'cement' holding the casein micelle together.
    • (1974) J Dairy Res , vol.41 , pp. 45-53
    • McGann, T.C.A.1    Fox, P.F.2
  • 28
    • 3042616948 scopus 로고    scopus 로고
    • Hierarchical networks of casein proteins: an elasticity study based on atomic force microscopy
    • Whatever holds the micelle together when the calcium phosphate bonds are disrupted is demonstrated in this paper to be of significant strength.
    • Uricanu V.I., Duits M.H.G., and Mellema J. Hierarchical networks of casein proteins: an elasticity study based on atomic force microscopy. Langmuir 20 (2004) 5079-5090. Whatever holds the micelle together when the calcium phosphate bonds are disrupted is demonstrated in this paper to be of significant strength.
    • (2004) Langmuir , vol.20 , pp. 5079-5090
    • Uricanu, V.I.1    Duits, M.H.G.2    Mellema, J.3
  • 29
    • 0015902350 scopus 로고
    • A model for the formation and structure of casein micelles from subunits of variable composition
    • Slattery C.W., and Evard R. A model for the formation and structure of casein micelles from subunits of variable composition. Biochim Biophys Acta 317 (1973) 529-538
    • (1973) Biochim Biophys Acta , vol.317 , pp. 529-538
    • Slattery, C.W.1    Evard, R.2
  • 30
    • 0017046277 scopus 로고
    • Model calculations of casein micelle size distribution
    • Slattery C.W. Model calculations of casein micelle size distribution. Biophys Chem 6 (1977) 59-64
    • (1977) Biophys Chem , vol.6 , pp. 59-64
    • Slattery, C.W.1
  • 31
    • 0001776309 scopus 로고
    • Colloidal aspects of the caseins
    • Schmidt D.G. Colloidal aspects of the caseins. Neth Milk Dairy J 34 (1980) 42-64
    • (1980) Neth Milk Dairy J , vol.34 , pp. 42-64
    • Schmidt, D.G.1
  • 32
    • 0019461644 scopus 로고
    • Energy-dependent calcium sequestration activity in a Golgi-apparatus fraction derived from lactating mammary glands
    • West D.W. Energy-dependent calcium sequestration activity in a Golgi-apparatus fraction derived from lactating mammary glands. Biochim Biophys Acta 673 (1981) 374-386
    • (1981) Biochim Biophys Acta , vol.673 , pp. 374-386
    • West, D.W.1
  • 33
    • 0019533702 scopus 로고
    • The influence of calmodulin on calcium accumulation and membrane protein autophosphorylation by Golgi vesicles from lactating rat mammary gland
    • West D.W., and Clegg R.A. The influence of calmodulin on calcium accumulation and membrane protein autophosphorylation by Golgi vesicles from lactating rat mammary gland. Biochem Soc Trans 9 (1981) 77
    • (1981) Biochem Soc Trans , vol.9 , pp. 77
    • West, D.W.1    Clegg, R.A.2
  • 34
    • 0026668858 scopus 로고
    • Structure and stability of bovine casein micelles
    • The introduction of the Holt model, distinguished for its brevity and lack of detail.
    • Holt C. Structure and stability of bovine casein micelles. Adv Protein Chem 43 (1992) 63-151. The introduction of the Holt model, distinguished for its brevity and lack of detail.
    • (1992) Adv Protein Chem , vol.43 , pp. 63-151
    • Holt, C.1
  • 35
    • 0347359172 scopus 로고    scopus 로고
    • Rethinking casein micelle structure using electron microscopy
    • The definitive work on the electron microscopy of the casein micelle.
    • McMahon D.J., and McManus W.R. Rethinking casein micelle structure using electron microscopy. J Dairy Sci 81 (1998) 2985-2993. The definitive work on the electron microscopy of the casein micelle.
    • (1998) J Dairy Sci , vol.81 , pp. 2985-2993
    • McMahon, D.J.1    McManus, W.R.2
  • 36
    • 0000778189 scopus 로고
    • Elektronenmikroskopische untersuchung der feinstruktur von caseinmicellen in kuhmilch
    • Schmidt D.G., and Buchheim W. Elektronenmikroskopische untersuchung der feinstruktur von caseinmicellen in kuhmilch. Milchwiss 25 (1970) 596-600
    • (1970) Milchwiss , vol.25 , pp. 596-600
    • Schmidt, D.G.1    Buchheim, W.2
  • 37
    • 0002616085 scopus 로고
    • Milk gel structure: XIII. Rotary shadowing of casein micelles for electron microscopy
    • Kalab M., Phibbs-Todd B.E., and Allan-Wojtas P. Milk gel structure: XIII. Rotary shadowing of casein micelles for electron microscopy. Milchwiss 37 (1982) 513-518
    • (1982) Milchwiss , vol.37 , pp. 513-518
    • Kalab, M.1    Phibbs-Todd, B.E.2    Allan-Wojtas, P.3
  • 38
    • 4544282070 scopus 로고    scopus 로고
    • A possible structure of the casein micelle based on high-resolution field-emission scanning electron microscopy
    • The latest of the microscopy techniques to be employed to visualise the casein micelle but are its pictures artefactual?
    • Dalgleish D.G., Spagnulo P.A., and Goff H.D. A possible structure of the casein micelle based on high-resolution field-emission scanning electron microscopy. Int Dairy J 14 (2004) 1025-1031. The latest of the microscopy techniques to be employed to visualise the casein micelle but are its pictures artefactual?
    • (2004) Int Dairy J , vol.14 , pp. 1025-1031
    • Dalgleish, D.G.1    Spagnulo, P.A.2    Goff, H.D.3
  • 39
    • 0032520111 scopus 로고    scopus 로고
    • A core-shell model of calcium phosphate nanoclusters derived from sedimentation equilibrium and small angle X-ray and neutron scattering measurements
    • Holt C., Timmins P.A., Errington N., and Leaver J. 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 (1998) 73-78
    • (1998) Eur J Biochem , vol.252 , pp. 73-78
    • Holt, C.1    Timmins, P.A.2    Errington, N.3    Leaver, J.4
  • 40
    • 0031602189 scopus 로고    scopus 로고
    • Casein phosphopeptides from casein micelles by successive digestion with pepsin and trypsin
    • Ono T., Tagaki Y., and Kunishi I. Casein phosphopeptides from casein micelles by successive digestion with pepsin and trypsin. Biosci Biotechnol Biochem 62 (1998) 16-21
    • (1998) Biosci Biotechnol Biochem , vol.62 , pp. 16-21
    • Ono, T.1    Tagaki, Y.2    Kunishi, I.3
  • 41
    • 0000009417 scopus 로고    scopus 로고
    • The milk salts and their interaction with casein
    • Advanced dairy chemistry. Fox P.F. (Ed), Chapman and Hall, London
    • Holt C. The milk salts and their interaction with casein. In: Fox P.F. (Ed). Advanced dairy chemistry. Lactose, water, salts and vitamins vol. 3 (1997), Chapman and Hall, London 233-244
    • (1997) Lactose, water, salts and vitamins , vol.3 , pp. 233-244
    • Holt, C.1
  • 43
    • 0026847631 scopus 로고
    • The least number of phosphate groups for cross-linking of casein by colloidal calcium phosphate
    • Aoki T., Umeda T., and Kako Y. The least number of phosphate groups for cross-linking of casein by colloidal calcium phosphate. J Dairy Sci 75 (1992) 971-975
    • (1992) J Dairy Sci , vol.75 , pp. 971-975
    • Aoki, T.1    Umeda, T.2    Kako, Y.3
  • 44
    • 33744976096 scopus 로고    scopus 로고
    • Caseins, micellar structure
    • Roginski R., Fox P.F., and Fuquay J.W. (Eds), Academic Press, New York. The dual-binding model of the casein micelle, in detail.
    • Horne D.S. Caseins, micellar structure. In: Roginski R., Fox P.F., and Fuquay J.W. (Eds). Encyclopaedia of dairy sciences (2002), Academic Press, New York 1902-1909. The dual-binding model of the casein micelle, in detail.
    • (2002) Encyclopaedia of dairy sciences , pp. 1902-1909
    • Horne, D.S.1


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