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

1997; Royal Society of Chemistry; Volume: 93; Issue: 3 Linguagem: Inglês

10.1039/a604864a

1364-5455

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

Enzyme Production and Characterization

The theoretical adsorption behaviour of the milk proteins, α s1 - 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 α s1 -casein. We find a lower adsorbed amount for α s1 -casein, and a more complex adsorbed conformation because of its more heterogeneous primary structure. The predominant conformation appears to involve a substantial loop for α s1 -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.