Ellipsometry as a tool to study the adsorption behavior of synthetic and biopolymers at the air–water interface

Abstract The application of ellipsometry of the study of the adsorption behavior of proteins and synthetic macromolecules at the air‐water interface has been investigated. It is shown that for macromolecules the amount adsorbed per unit area, Γ, as determined by ellipsometry, only has a well‐defined physical meaning if the refractive‐index increment remains constant up to high concentrations present in the adsorbed layer. It has been found experimentally that this conditioned is fulfilled for proteins. The ellipsometric Γ values of some protein agree satisfactorily with those obtained by two independent techniques has been used to investigate the adsorption from solution of κ‐casein, bovine serum albumin, and polyvinyl alcohol. For bovine serum albumin, Γ reaches a plateau value of 2.9 mg/m 2 for concentrations ≥ 0.05 wt%. The thickness of the adsorbed molecules. For κ‐casein, Γ steadily increases with increasing centration and multilayers are formed. The technique provides interesting information on conformational changes in adsorbed macromolecules, on the rate of the process, and on the conditions under which these occur.