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Enzyme-induced coagulation of casein micelles: a number of different kinetic models

Published online by Cambridge University Press:  01 June 2009

Douglas B. Hyslop
Affiliation:
Department of Food Science, University of Wisconsin, Madison, WI 53706, USA

Summary

Several mathematical models are presented in an attempt to describe the kinetics of the enzyme-induced coagulation of casein micelles. In each model the primary phase of the clotting reaction is assumed to follow first order kinetics. The only differences amongst the various models centre on the definition of the flocculation rate constant, which is defined in seven different ways. The rate constants are defined and discussed in terms of activation energy and functionality theory. The first model is such that the number of functional sites is two. The second is such that the number is much larger. The third and fourth are such that there is an exponential energy barrier, one which has a magnitude proportional to the extent of proteolysis caused by the clotting enzyme. These two definitions differ only in the pre-exponent. In one case the pre-exponent is a constant, whereas in the other it is dependent on the size of clotting particles. The fifth and sixth definitions are also energy barrier rate constants, but the energy barrier changes in an arbitrary fashion with respect to time during proteolysis. The seventh definition assumes a large number of functional sites, but such that the number increases with extent of proteolysis. In the Payens nomenclature (Payens, 1989), all models could be considered to be ‘source’ models, and all are derived using the Drake moment equation (Drake, 1972). Only the first model has a truly constant flocculation rate parameter, and only this model has a relatively simple analytical solution. All other models yield analytical solutions only by way of infinite series expansions. Thus, all models are presented in terms of power series expansions, and only through the first five time-dependent coefficients. This confines all models to the early stages of coagulation. In all cases the first three coefficients are virtually the same. The first two coefficients involve only proteolysis, and the third includes initial flocculation information. Time-dependent changes in the flocculation rate constant begin to take effect in the fourth coefficient. When the fourth coefficients of the third and seventh models are compared, a simple relationship is suggested between free energy barrier removal and functional site generation, but only assuming that the number of functionalities is large.

Type
Original Articles
Copyright
Copyright © Proprietors of Journal of Dairy Research 1993

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References

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