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Heat stability of milk: pH-dependent dissociation of micellar κ-casein on heating milk at ultra high temperatures

Published online by Cambridge University Press:  01 June 2009

Harjinder Singh  and
Partick F. Fox
Harjinder Singh
Affiliation:
Department of Dairy and Food Chemistry, University College, Cork, Irish Republic,
Partick F. Fox
Affiliation:
Department of Dairy and Food Chemistry, University College, Cork, Irish Republic,
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Summary

Preheating milk at 140 °C for 1 min at pH 6·6, 6·8, 7·0 or 7·2 shifted the heat coagulation time (HCT)/pH profile to acidic values without significantly affecting the maximum stability. Whey proteins (both β-lactoglobulin and α-lactalbumin) co-sedimented with the casein micelles after heating milk at pH < 6·9 and the whey protein-coated micelles, dispersed in milk ultrafiltrate, showed characteristic maxima–minima in their HCT/pH profile. Heating milk at higher pH values (> 6·9) resulted in the dissociation of whey proteins and κ-casein-rich protein from the micelles and the residual micelles were unstable, without a maximum–minimum in the HCT/pH profile. Preformed whey protein–casein micelle complexes formed by preheating (140 °C for 1 min) milk at pH 6·7 dissociated from the micelles on reheating (140 °C for 1 min) at pH > 6·9. The dissociation of micellar-κ-casein, perhaps complexed with whey proteins, may reduce the micellar zeta potential at pH ≃ 6·9 sufficiently to cause a minimum in the HCT/pH profile of milk.

Type
Original Articles
Information
Journal of Dairy Research , Volume 52 , Issue 4 , November 1985 , pp. 529 - 538
Copyright
Copyright © Proprietors of Journal of Dairy Research 1985

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