Casein structure, self-assembly and gelation

Current Opinion in Colloid and Interface Science

Volumn 7, Issue 5-6, 2002, Pages 456-461

  Horne, David S ^a  

^a Charis Food Research   (United Kingdom)

Author keywords

S1 , S2 , and casein; Block copolymers; Casein micelle models; Casein micelles; Caseins; Secondary structure; Self association

Indexed keywords

ALPHAS1 CASEIN; ALPHAS2 CASEIN; BETA CASEIN; CASEIN; COPOLYMER; KAPPA CASEIN; PROTEIN; UNCLASSIFIED DRUG;

ADSORPTION; GELATION; MICELLE; MODEL; PROTEIN ASSEMBLY; PROTEIN FUNCTION; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; REVIEW; SCIENTIFIC LITERATURE; STRUCTURE ANALYSIS;

EID: 0036866003     PISSN: 13590294     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1359-0294(02)00082-1     Document Type: Review

References (36)

1. Wright PE, Dyson HJ. Intrinsically unstructured proteins: Re-assessing the protein structure-function paradigm. J Mol Biol 1999;293:321-31. A thoughtful review on the issue of structure and folding and the importance of unstructured proteins to regulatory functions in the cell.
2. Swaisgood HE. Chemistry of the caseins. In: Fox PF, editor. Advanced Dairy Chemistry 1. Proteins. New York: Elsevier, 1992. p. 63-110.
3. Schmidt DG. Association of caseins and casein micelle structure. In: Fox PF, editor. Developments in Dairy Chemistry 1. Proteins. London: Applied Science Publishers, 1982. p. 61-85.
4. Rollema HS. Casein association and micelle formation. In: Fox PF, editor. Advanced Dairy Chemistry 1. Proteins. New York: Elsevier, 1992. p. 111-40. An excellent summary of the status of casein micelle models in the early 1990s.
5. Walstra P, Jenness R. Dairy Chemistry and Physics. New York: Wiley, 1984.
6. Holt C. Casein structure and casein-calcium phosphate interactions. In: Proceedings of 25th International Dairy Congress, Aarhus, Denmark. Copenhagen: Danish National Committee of International Dairy Federation, 1998:200-208. Distinguished for its treatment of the calcium phosphate nanocluster.
7. Holt C. The relation of secondary structure to function in caseins. Proceedings of 8th Egyptian Conference on Dairy Science and Technology. 2001. p. 187-200.
8. Holt C, Sawyer L. Caseins as rheomorphic proteins. J Chem Soc Faraday Trans 1993;89:2683-90. The definitive paper on the rheomorphic hypothesis.
9. S1- and β-caseins in solution. Arch Biochem Biophys 1981;211:689-96.
10. Paulsson M, Dejmek P. Thermal denaturation of whey proteins in mixtures with caseins studied by calorimetry. J Dairy Sci 1990;73:590-600.
11. Andrews AL, Atkinson D, Evans MTA, et al. Biopolymers 1979;18:1105.
12. S1-casein (136-196). Biochim Biophys Acta 1999;1431:410-20.
13. Curley DM, Kumosinski TF, Unruh JJ, Farrell HM Jr. Changes in the secondary structure of bovine casein studied by Fourier transform infrared spectroscopy: Effects of calcium and temperature. J Dairy Sci 1998;81:3154-62.
14. S1-casein (59-79). Biochim Biophys Acta 1995;1247:201-8.
15. Wahlgren NM, Leonil J, Dejmek P, Drakenberg T. Two dimensional nmr study of the β-casein peptide 1-25. Biochim Biophys Acta 1993;1202:121-8.
16. Farrell Jr HM, Wickham ED, Unruh JJ, Qi PX, Hoagland PD. Secondary structural studies of bovine caseins: Temperature dependence of casein structure as analyzed by circular dichroism and FTIR spectroscopy and correlation with micellization. Food Hydrocolloids 2001;15:341-54. A clearly presented experimental study of the behaviour of the CD spectra of β-casein as a function of temperature. By comparing the changes in molar ellipticity with temperature with measured changes in molecular weight, the authors demonstrate the structural changes to occur in the monomer and not as a result of self-association.
17. Syme CD, Blanch EW, Holt C, Jakes R, Goedert M, Hecht L, Barron LD. A Raman optical activity study of rheomorphism in caseins, synucleins and tau. Eur J Biochem 2002;269:148-56. A new technique of promise but presently dogged by low signal-to-noise and needing many more proteins to be studied before definitive results can be assured. Also noteworthy for its redefinition of the rheomorphic hypothesis.
18. Farrell Jr HM, Qi PX, Brown EM, Cooke PH, Tunick MH, Wickham ED, Unruh JJ. Molten globule structures in milk proteins: Implications for potential new structure-function relationships. J Dairy Sci 2002;85:459-71. Notable for the suggestion that native casein molecules in solution should be regarded as molten globules and also for the proposition that the notions of tensegrity, borrowed from architecture, be applied to casein behaviour.
19. Arai M, Kuwajima K. Role of molten globule state in protein folding. Adv Protein Chem 2000;53:209-82.
20. Tiffany ML, Krimm S. New chain conformations of poly (glutamic acid) and polylysine. Biopolymers 1968;6:1379-82.
21. Horne DS. Casein interaction: Casting light on the Black Boxes, the structure in dairy products. Int Dairy J 1998;8:171-7. The paper which introduced the notion that caseins be treated as block copolymers and applied this to casein self-association and micelle formation.
22. Horne DS. Protein-stabilized emulsions. Current Opin Coll Interface Sci 1996;1:752-8.
23. Kegeles G. A shell model for size distribution in micelles. J Phys Chem 1979;83:1728-82.
24. S1-casein at pH 6.6. Biochim Biophys Acta 1970;207:130-8.
25. S1-casein: Effect of inclusion of citrate or phosphate. J Dairy Res 1982;49:107-18.
26. Horne DS. Caseins - Molecular properties, casein micelle formation and structure. In: Roginski H, Fuquay JW, Fox PF, editors. Encyclopaedia of Dairy Sciences. New York: Elsevier, 2002; in press.
27. DeKruif CG. Casein micelle interactions. Int Dairy J 1999;9:183-8. A definitive summary of the adhesive sphere model of casein micelle stability.
28. Holt C. Structure and stability of the bovine casein micelle. In: Anfinsen CB, Edsall JD, Richards FR, Eisenberg DS, editors. Advances in Protein Chemistry 43. San Diego: Academic Press, 1992. p. 63-151.
29. Bhatia SR, Mourchid A, Joanicot M. Block copolymer assembly to control fluid rheology. Curr Opinion Coll Interface Sci 2001;6:471-8. Is this the way forward for casein self-assembly?
30. Farrell Jr HM, Brown EM, Hoagland PD, Malin EL. Higher order structures of caseins: A paradox. In: Fox PF, McSweeney P, editors. Advanced Dairy Chemistry, 3rd Edition. New York: Kluwer Academic, 2002. In press.
31. 1. Int J Biol Macromol 1984;6:155-61.
32. Byler DM, Farrell HM Jr., Susi H. Raman spectroscopic study of casein structure. J Dairy Sci 1988;71:2622-9.
33. Caessens PWJR, DeJongh HHJ, Norde W, Gruppen H. The adsorption-induced secondary structure of β-casein and of distinct parts of its sequence. Biochim Biophys Acta 1999;1430:73-83.
34. Farrell HM Jr., Kumosinski TF, Cooke PH, et al. Particle sizes of purified κ-casein: Metal effects. J Protein Chem 1996;15:435-45.
35. S2-group-casein. Agric Biol Chem 1983;47:1467-71.
36. S2-casein: Theoretical and experimental approaches. J Dairy Sci 2001;84:1944-9.