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DOI: 10.1039/A604864A (Paper) Reference Section for: J. Chem. Soc., Faraday Trans., 1997, 93, 425-432

Self-consistent-field modelling of casein adsorption Comparison of results for αs1-casein and β-casein

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Eric Dickinson, David S. Horne, Valerie J. Pinfield and Frans A. M. Leermakers

Abstract

The theoretical adsorption behaviour of the milk proteins, αs1- and β-casein, has been studied using a self-consistent-field (SCF) model. Previously published results for β-casein on the effects of ionic strength and pH on protein conformation are compared with those for αs1-casein. We find a lower adsorbed amount for αs1-casein, and a more complex adsorbed conformation because of its more heterogeneous primary structure. The predominant conformation appears to involve a substantial loop for αs1-casein, producing a thinner adsorbed layer than is predicted for β-casein, which has, predominantly, a long tail extending away from the surface into the aqueous region. The overall layer structure for both proteins is shown to consist of a combination of many coexisting protein conformations. The relative proportion of the different conformations controls the overall layer properties and their variation with pH and ionic strength.

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