RESUMEN
The properties of adsorbed layers of protein fibrils differ significantly from the properties of fibril spread layers on an aqueous subphase. If the dependencies of the dynamic surface elasticity on surface pressure of Lysozyme (LYS) and ß-lactoglobulin (BLG) aqueous dispersions proved to be close to the results for native protein solutions, LYS and BLG spread layers on the surface of 0.1 M NaCl solution exhibited the surface elasticity more than two times higher than the values for protein solutions with the same NaCl concentatration, presumably due to lower surface concentrations of hydrolysed peptides in the latter case. The properties of fibril spread and adsorbed layers and also their morphology, unlike the surface properties of protein solutions, depend noticeably on the ionic strength of the aqueous bulk phase. This dependence is stronger in case of LYS layers, which are also more prone to the formation of macroscopic and mesoscopic surface aggregates as compared with BLG layers.
Asunto(s)
Cloruro de Sodio , Agua , Agua/química , Adsorción , Lactoglobulinas/química , Propiedades de SuperficieRESUMEN
Urea and guanidine hydrochloride (GuHCl) have different influence on surface properties of lysozyme solutions. The increase of GuHCl concentration leads to noticeable changes of kinetic dependencies of the dynamic surface elasticity and ellipsometric angles while the main effect of urea reduces to a strong drop of the static surface tension. The difference between the effects of these two denaturants on the surface properties of other investigated globular proteins is significantly weaker and is mainly a consequence of a different extent of the globule unfolding in the surface layer at equal concentrations of the denaturants. The obtained results for lysozyme solutions are connected with the strongly different denaturation mechanisms under the influence of urea and GuHCl. In the former case the protein preserves its globular structure in the adsorption layer at high urea concentrations (up to 9M) but without tightly packed interior of the globule and with a dynamic tertiary structure (molten globule state). On the contrary, the increase of GuHCl concentration leads to partial destruction of the protein tertiary structure in the surface layer, although this effect is not as strong as in the case of previously studied bovine serum albumin and ß-lactoglobulin.