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Coagulation of renneted bovine casein micelles: dependence on temperature, calcium ion concentration and ionic strength

Published online by Cambridge University Press:  01 June 2009

Douglas G. Dalgleish
Douglas G. Dalgleish
Affiliation:
Hannah Research Institute, Ayr, Scotland, KA6 5HL
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Summary

The rates of coagulation of completely renneted casein micelles have been measured as functions of ionic strength, temperature, and concentration of Ca2+. At 25 °C and below, the rate constants for the coagulation were found to be low, but increased with temperature so that at 60 °C the particles were coagulating at almost maximum rate permitted by diffusion. This maximal rate at 60 °C was achieved at nearly all of the ionic strengths and concentrations of Ca2+ used. At lower temperatures the rate constant decreased with increasing ionic strength, the dependence being more marked at lower temperatures. Increasing concentration of Ca2+ also increased the rate at low and moderate temperatures. The implications of these results are discussed in terms of specific and non-specific ionic interactions and of hydrophobic bond formation.

Type
Original Articles
Information
Journal of Dairy Research , Volume 50 , Issue 3 , August 1983 , pp. 331 - 340
Copyright
Copyright © Proprietors of Journal of Dairy Research 1983

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References

REFERENCES

Berridge, N. J. 1942 The second phase of rennet coagulation. Nature 149 194–195CrossRefGoogle Scholar
Bloomfield, V. A., Benbasat, J. A. & Dwyer, J. D. 1982 Laser light scattering of viruses and vesicles. In Biomedical Applications of Laser Light Scattering pp. 95–109. (Eds. Sattelle, D. B., Lee, W. I., & Ware, B.), London: ElsevierGoogle Scholar
Dalgleish, D. G. 1979 Proteolysis and aggregation of casein micelles treated with immobilized or soluble chymosin. Journal of Dairy Research 46 653–661CrossRefGoogle Scholar
Dalgleish, D. G. 1980 A mechanism for the chymosin-induced flocculation of casein micelles. Biophysical Chemistry 11 147–155CrossRefGoogle ScholarPubMed
Dalgleish, D. G., Brinkhuis, J. & Payens, T. A. J. 1981 The coagulation of differently-sized casein micelles by rennet. European Journal of Biochemistry 119 257–261CrossRefGoogle ScholarPubMed
Dalgleish, D. G. & Parker, T. G. 1980 Binding of calcium ions to bovine αs1-casein and precipitability of the protein-calcium ion complexes. Journal of Dairy Research 47 113–122CrossRefGoogle Scholar
Darling, D. F. & Dickson, J. 1979 Electrophoretic mobility of casein micelles. Journal of Dairy Research 46 441–451CrossRefGoogle Scholar
Green, M. L. & Crutchfield, G. 1971 Density-gradient electrophoresis of native and of rennet-treated casein micelles. Journal of Dairy Research 38 151–164CrossRefGoogle Scholar
Green, M. L., Hobbs, D. G., Morant, S. V. & Hill, V. A. 1978 Intermicellar relationships in rennet-treated separated milk. II. Process of gel assembly. Journal of Dairy Research 45 413–422CrossRefGoogle 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 44 521–531CrossRefGoogle Scholar
Knoop, A. -M. & Peters, K. -H. 1976 [The nature of the forces involved in the production of coagula by rennet or acid, and the role of calcium, phosphate and citrate]. Milchwissenschafl 31 338–345Google 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 47 359–369CrossRefGoogle Scholar
Nemethy, G. & Scheraga, H. A. 1962 The structure of water and hydrophobic bonding in proteins. III. The thermodynamic properties of hydrophobic bonds in proteins. Journal of Physical Chemistry 66 1773–1789CrossRefGoogle Scholar
Overbeek, J. Th. G. 1949 Kinetics of flocculation. In Colloid Science, vol. 1 pp. 278–301 (Ed. Kruyt, H. R.) London: ElsevierGoogle Scholar
Parker, T. G. & Dalgleish, D. G. 1981 Binding of calcium ions to bovine β-casein. Journal of Dairy Research 48 71–76CrossRefGoogle ScholarPubMed
Payens, T. A. J. 1977 On enzymatic clotting processes II. The colloidal instability of chymosin-treated casein micelles. Biophysical Chemistry 6 263–270CrossRefGoogle ScholarPubMed
Payens, T. A. J. & Both, P. 1980 On enzymatic clotting processes. IV. The chymosin-triggered clotting of para-κ-casein. In Bioelectrochemistry: ions, surfaces, membranes, pp. 129–141 (Ed. Blank, M.) Washington, D.C.: American Chemical Society (Advances in Chemistry Series no. 188)CrossRefGoogle Scholar
Payens, T. A. J., Wiersma, A. K., & Brinkhuis, J. 1977 On enzymatic clotting processes I. Kinetics of enzyme-triggered coagulation reactions. Biophysical Chemistry 6 253–261CrossRefGoogle ScholarPubMed
Pearce, K. N. 1976 Moving boundary electrophoresis of native and rennet-treated casein micelles. Journal of Dairy Research 43 27–36CrossRefGoogle Scholar
Tanford, C. 1961 Physical chemistry of macromolecules p. 288. New York: John Wiley Inc.Google Scholar
Walstra, P. 1979 The voluminosity of bovine casein micelles and some of its implications. Journal of Dairy Research 46 317–323CrossRefGoogle ScholarPubMed
Walstra, P., Bloomfield, V. A., Wei, G.J. & Jenness, R. 1981 Effect of chymosin action on the hydrodynamic diameter of casein micelles. Biochimica et Biophysica Acta 669 258–259CrossRefGoogle ScholarPubMed
Waugh, D. F., Slattery, C. W. & Creamer, L. K. 1971 Binding of cations to caseins. Site binding, Donnan binding and system characteristics. Biochemistry 10 817–823CrossRefGoogle ScholarPubMed