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Influence of calcium chloride on the chymosin-initiated coagulation of casein micelles

Published online by Cambridge University Press:  01 June 2009

Neal A. Bringe  and
John E. Kinsella
Neal A. Bringe
Affiliation:
Institute of Food Science, Cornell University, Ithaca, NY 14853, USA
John E. Kinsella
Affiliation:
Institute of Food Science, Cornell University, Ithaca, NY 14853, USA
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Summary

Coagulation of para-casein micelles was monitored using a Platelet Aggregometer at 37·8 °C and pH 6·7. The macropeptide released by chymosin was determined quantitatively with fluorescamine. The aggregatability of para-casein micelles integrated over the complete hydrolysis of κ-casein was calculated from the amount of κ-casein hydrolysed during the clotting time (Tc). Low concentrations of CaCl2 enhanced the rate of κ-casein hydrolysis but increases in CaCl2 concentration above 8 mM caused marked decreases in this rate. Calcium chloride enhanced the ability of para-casein micelles to aggregate. Little aggregation of para-casein micelles occurred at 0·6 mM-CaCl2 even after all of the κ-casein was hydrolysed. As the concentration of CaCl2 was increased from 3 to 60 mM, aggregation of para-casein micelles took place at progressively lower levels of κ-casein hydrolysis and the percentage hydrolysis at the Tc decreased markedly from 71±7% to 26±8%. The combined influence of CaCl2 on the velocity of the chymosin-catalysed reaction and on para-casein micelle aggregatability accounted for its effect on the average rate of coagulation (calculated by the reciprocal of the Tc). Results are consistent with the hypothesis that electrostatic repulsions and ionic bonding are involved in the interaction between chymosin and κ-casein.

Type
Original Articles
Information
Journal of Dairy Research , Volume 53 , Issue 3 , August 1986 , pp. 371 - 379
Copyright
Copyright © Proprietors of Journal of Dairy Research 1986

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References

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