Competitive adsorption of lysozyme and C12E5 at the air/liquid interface

We have studied the adsorption of lysozyme and pentaethylene glycol monodod ecyl ether (C12E5) at the air/water interface using neutron reflection and surface tension measurements. The effect of C12E5 concentration was examine d at three fixed lysozyme concentrations of 0.01, 1 and 4 g dm(-3). The sur face tension showed little variation with the addition of C12E5 over the lo w surfactant concentration region, but with the increase of C12E5 concentra tion, the surface tension gradually became identical to that corresponding to pure C12E5. These results suggest a progressive replacement of lysozyme by C12E5 and that the observed surface event is dominated by competitive ad sorption. The parallel neutron measurements showed that, at low surfactant concentration, the surface was predominantly occupied by lysozyme. At inter mediate C12E5 concentrations, the surface layer consisted of both lysozyme and C12E5, with the C12E5 eventually completely replacing the adsorbed lyso zyme as the surfactant concentration was further increased. While the neutr on results confirm the inference from surface tension measurement, structur al analysis clearly showed the partial breakdown of the globular structure of lysozyme induced by the nonionic surfactant. Furthermore, neutron data s howed that the adsorbed C12E5 molecules are present at the top surface laye r only, suggesting no preferential association or binding between the surfa ctant and any immersed protein fragments at the interface.