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Disruption and reassociation of casein micelles during high pressure treatment: influence of whey proteins

Published online by Cambridge University Press:  12 February 2007

Thom Huppertz
Affiliation:
Department of Food and Nutritional Sciences, University College Cork, Cork, Ireland Current address: School of Land and Food Sciences, University of Queensland, Brisbane, QLD 4072, Australia
Cornelis G de Kruif
Affiliation:
NIZO food research, PO Box 20, 6710 BA, Ede, The Netherlands Van ‘t Hoff laboratory for Physical and Colloid Chemistry, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands

Abstract

In the study presented in this article, the influence of added α-lactalbumin and β-lactoglobulin on the changes that occur in casein micelles at 250 and 300 MPa were investigated by in-situ measurement of light transmission. Light transmission of a serum protein-free casein micelle suspension initially increased with increasing treatment time, indicating disruption of micelles, but prolonged holding of micelles at high pressure partially reversed HP-induced increases in light transmission, suggesting reformation of micellar particles of colloidal dimensions. The presence of α-la and/or β-lg did not influence the rate and extent of micellar disruption and the rate and extent of reformation of casein particles. These data indicate that reformation of casein particles during prolonged HP treatment occurs as a result of a solvent-mediated association of the micellar fragments. During the final stages of reformation, κ-casein, with or without denatured whey proteins attached, associates on the surface of the reformed particle to provide steric stabilisation.

Type
Research Article
Copyright
Proprietors of Journal of Dairy Research 2007

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