E. Dickinson et al., SELF-CONSISTENT-FIELD MODELING OF CASEIN ADSORPTION - COMPARISON OF RESULTS FOR ALPHA(S1)-CASEIN AND BETA-CASEIN, Journal of the Chemical Society. Faraday transactions, 93(3), 1997, pp. 425-432
Citations number
11
Categorie Soggetti
Chemistry Physical","Physics, Atomic, Molecular & Chemical
The theoretical adsorption behaviour of the milk proteins, alpha(s1)-
and beta-casein, has been studied using a self-consistent-field (SCF)
model. Previously published results for beta-casein on the effects of
ionic strength and pH on protein conformation are compared with those
for alpha(s1)-casein. We find a lower adsorbed amount for alpha(s1)-ca
sein, and a more complex adsorbed conformation because of its more het
erogeneous primary structure. The predominant conformation appears to
involve a substantial loop for alpha(s1)-casein, producing a thinner a
dsorbed layer than is predicted for beta-casein, which has, predominan
tly, a long tail extending away from the surface into the aqueous regi
on. The overall layer structure for both proteins is shown to consist
of a combination of many coexisting protein conformations. The relativ
e proportion of the different conformations controls the overall layer
properties and their variation with pH and ionic strength.