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The action of calf rennet and other proteolytic enzymes on κ-casein

Published online by Cambridge University Press:  01 June 2009

R. C. Lawrence  and
L. K. Creamer
R. C. Lawrence
Affiliation:
New Zealand Dairy Research Institute, Palmerston North, New Zealand
L. K. Creamer
Affiliation:
New Zealand Dairy Research Institute, Palmerston North, New Zealand
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Summary

The hydrolysis of κ-casein by a number of rennets and other proteolytic enzymes has been followed by measuring the increase in opacity due to the formation of insoluble aggregates of para-κ-caseins. The stability of these precipitates varied markedly, some being solubilized rapidly by the further action of the enzyme. The turbidity obtained with certain enzymes was dependent upon the calcium ion concentration, indicating that the para-κ-caseins produced were not identical for all enzymes.

For high concentrations of calf rennet, the rate of aggregation was linear with respect to time. With low concentrations of enzyme, increase in turbidity was preceded by a lag period which was lengthened by decreasing the enzyme concentration or increasing the κ-casein concentration. This increase in lag is favoured by a high κ-casein/para-κ-casein ratio, suggesting that the aggregation of newly formed para-κ-casein is prevented by the unchanged κ-casein. In addition, small amounts of αs1- or β-caseins present in the κ-casein also markedly affected the aggregation of para-κ-casein, indicating that all 3 major casein components can inhibit the aggregation of para-κ-casein in the absence of calcium ions. In the light of these observations the possible role of protein-protein interactions in casein coagulation by calf rennet is discussed.

Type
Original Articles
Information
Journal of Dairy Research , Volume 36 , Issue 1 , February 1969 , pp. 11 - 20
Copyright
Copyright © Proprietors of Journal of Dairy Research 1969

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