Hostname: page-component-78c5997874-4rdpn Total loading time: 0 Render date: 2024-11-10T11:31:18.786Z Has data issue: false hasContentIssue false

Pressurisation of raw skim milk and of a dispersion of phosphocaseinate at 9 °C or 20 °C: effects on the distribution of minerals and proteins between colloidal and soluble phases

Published online by Cambridge University Press:  24 January 2006

Stéphanie Regnault
Affiliation:
Equipe de Biochimie et Technologie Alimentaires, UMR 1208 – Département Agro-ressources et Procédés Biologiques, Université Montpellier II (Sciences et Techniques), 34095 Montpellier Cedex 05, France
Eliane Dumay
Affiliation:
Equipe de Biochimie et Technologie Alimentaires, UMR 1208 – Département Agro-ressources et Procédés Biologiques, Université Montpellier II (Sciences et Techniques), 34095 Montpellier Cedex 05, France
Jean Claude Cheftel
Affiliation:
Equipe de Biochimie et Technologie Alimentaires, UMR 1208 – Département Agro-ressources et Procédés Biologiques, Université Montpellier II (Sciences et Techniques), 34095 Montpellier Cedex 05, France

Abstract

The effects of high pressure treatments (100–300 MPa; 15 min; 9 °C or 20 °C) on the distribution of minerals and proteins of raw skim milk (RSM) and of a dispersion of industrial phosphocaseinate (PC) were studied after separation of the micellar and soluble phases by ultracentrifugation (UCF). Whatever the temperature of high pressure treatments, the pressure-induced dissociation of the casein micelles was accompanied by calcium (Ca), phosphorus (P) and casein release from the micelles. The released Ca and P were or became bound to soluble proteins since progressive increases in Ca and P concentrations were observed in the UCF supernatants of RSM and of the PC dispersion but not in the ultrafiltrates from these UCF supernatants (free of soluble proteins). Simultaneously, αS1-, αS2-, β- and κ-caseins were progressively released from the micelles, as seen by electrophoretic analysis. The pressure-induced solubilisation of αS1- and αS2-caseins, essentially located in the core of the micelles, suggests that high pressure destabilised micelles including their internal structure.

Type
Research Article
Copyright
Proprietors of Journal of Dairy Research 2006

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)