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A new calculation of the kinetics of the renneting reaction

Published online by Cambridge University Press:  01 June 2009

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

A detailed calculation of the growth of molecular weight during the renneting of milk is given, based on a first-order breakdown of κ-casein followed by development of instability caused either by a decrease in the intermicellar repulsive potential or by the formation of holes in the stabilizing surface layer of the micelles. Unlike most of the models which have been described, this model allows a complete analytical solution. The solution is, however, complex and difficult to use simply, although it is shown that the calculations are in accord with experimental observations of the dependence of the coagulation process upon the enzyme concentration and the concentration of the milk. The calculations are also compared with those from other models of the reaction.

Type
Original articles
Information
Journal of Dairy Research , Volume 55 , Issue 4 , November 1988 , pp. 521 - 528
Copyright
Copyright © Proprietors of Journal of Dairy Research 1988

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References

REFERENCES

Brinkhuis, J. & Payens, T. A. 1984 The influence of temperature on the flocculation rate of renneted casein micelles. Biophysical Chemistry 19 75–81CrossRefGoogle ScholarPubMed
Brinkhuis, J. & Payens, T. A. J. 1985 The rennet-induced clotting of para-κ-casein revisited: inhibition experiments with pepstatin A. Biochimica et Biophysica Acta 832 331–336CrossRefGoogle ScholarPubMed
Carlson, A., Hill, C. G., & Olson, N. F. 1987 a Kinetics of milk coagulation. I. The kinetics of kappa casein hydrolysis in the presence of enzyme deactivation. Biotechnology and Bioengintering 29 582–589CrossRefGoogle ScholarPubMed
Carlson, A., Hill, C. G. & Olson, N. F. 1987 b Kinetics of milk coagulation. II. Kinetics of the secondary phase: micelle flocculation. Biotechnology and Bioengineering 29 590–600CrossRefGoogle ScholarPubMed
Carlson, A., Hill, C. G. & Olson, N. F. 1987 c Kinetics of milk coagulation. III. Mathematical modeling of the kinetics of curd formation following enzymatic hydrolysis of κ-casein — parameter estimation. Biotechnology and Bioengineering 29 601–611CrossRefGoogle ScholarPubMed
Chaplin, B. & Green, M. L. 1980 Determination of the proportion of κ-casein hydrolysed by rennet on coagulation of skim-milk. Journal of Dairy Research 47 351–358CrossRefGoogle 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 A mechanism for the chymosin-induced flocculation of casein micelles. Biophysical Chemistry 11 147–155CrossRefGoogle ScholarPubMed
Dalgleish, D. G. 1980 b Effect of milk concentration on the rennet clotting time. Journal of Dairy Research 47 231–235CrossRefGoogle Scholar
Dalgleish, D. G. 1983 Coagulation of renneted bovine casein micelles: dependence on temperature, calcium ion concentration and ionic strength. Journal of Dairy Research 50 331–340CrossRefGoogle Scholar
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. & Holt, C. 1988 A geometrical model to describe the initial aggregation of partly renneted casein micelles. Journal of Colloid and Interface Science 123 80–84CrossRefGoogle Scholar
Darling, D. F. & Dickson, J. 1979 Electrophoretic mobility of casein micelles. Journal of Dairy Research 46 441–451CrossRefGoogle Scholar
Darling, D. F. & Van Hooydonk, A. C. M. 1981 Derivation of a mathematical model for the mechanism of casein micelle coagulation by rennet. Journal of Dairy Research 48 189–200CrossRefGoogle Scholar
Foltmann, B. 1959 On the enzymatic and the coagulation stages of the rennetting process. 15th International Dairy Congress, London 2 655–661Google 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
Holt, C. 1975 The stability of bovine casein micelles. In Proceedings of the International Conference on Colloid and Surface Science, Budapest pp. 641–644 (Ed. Wolfram, E.). Budapest: Akademiai KiadoGoogle Scholar
Holt, C. & Dalgleish, D. G. 1986 Electrophoretic and hydrodynamic properties of bovine casein micelles interpreted in terms of particles with an outer hairy layer. Journal of Colloid and Interface Science 114 513–524CrossRefGoogle Scholar
Holter, H. 1932 [On the activity of rennet.] Biochemische Zeitschrift 255 160–188Google Scholar
McMahon, D. J. & Brown, R. J. 1983 Milk coagulation time: linear relationship with inverse of rennet activity. Journal of Dairy Science 66, 341–344CrossRefGoogle Scholar
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. 1978 On enzymatic clotting processes. III Flocculation rate constants of paracasein and fibrin. Faraday Discussions of the Chemical Society No. 65 164–174CrossRefGoogle Scholar
Payens, T. A. 1984 The relationship between milk concentration and rennet coagulation time. Journal of Applied Biochemistry 6 232–239Google Scholar
Payens, T. A. 1987 Concerning consistent and inconsistent theories of milk clotting; a comment. Netherlands Milk and Dairy Journal 41 289–291Google Scholar
Payens, T. A. & Brinkhuis, J. 1986 Mean field kinetics of the enzyme-triggered gelation of casein micelles. Colloids and Surfaces 20 37–50CrossRefGoogle Scholar
Payens, T. A. J. & Wiersma, A. K. 1980 On enzymic clotting processes. V. Rate equations for the case of arbitrary rate of production of the clotting species. Biophysical Chemistry 11 137–146CrossRefGoogle ScholarPubMed
Payens, T. A. J., Wiersma, A. K. & Brinkhuis, J. 1977 On enzymatic clotting processes. I. Kinetics of enzyme-triggered coagulation reactions. Biophysical Chemistry 6 253–261.CrossRefGoogle ScholarPubMed
Van Hooydonk, A. C. M. 1987 The Renneting of Milk. Thesis, Agricultural University of Wageningen, pp. 109–126Google Scholar
Van Hooydonk, A. C. M., Olieman, C. & Hagedoorn, H. G. 1984 Kinetics of the chymosin-catalysed proteolysis of κ-casein in milk. Netherlands Milk and Dairy Journal 38 207–222Google Scholar
Van Hooydonk, A. C. M. & Walstra, P. 1987 Interpretation of the kinetics of the renneting reaction in milk. Netherlands Milk and Dairy Journal 41 19–47Google Scholar
Von Smoluchowski, M. 1917 [Research on a mathematical theory of the kinetics of coagulation of colloidal suspensions.] Zeitschrift für Physikalische Chemie 92 129–168Google 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