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Proteolysis and aggregation of casein micelles treated with immobilized or soluble chymosin

Published online by Cambridge University Press:  01 June 2009

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

The relationship between extent of κ-casein proteolysis and aggregatability of milk casein micelles has been studied using chymosin either bound to porous glass supports or free in solution. Both enzyme preparations demonstrated that, overall, 86–90 % of the κ-casein had to be destroyed before any aggregation could occur. Based on these results, a mathematical model of chymosin action on casein is described involving (i) the attack on κ-casein by chymosin, via a Michaelis–Menten mechanism (ii) the probability that sufficient κ-casein on any micelle is destroyed to allow aggregation, and (iii) the aggregation of para-casein micelles by a von Smoluchowski mechanism.

Type
Original Articles
Information
Journal of Dairy Research , Volume 46 , Issue 4 , November 1979 , pp. 653 - 661
Copyright
Copyright © Proprietors of Journal of Dairy Research 1979

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References

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