Effect of H20-co2 Organization on Ovalbumin Adsorption at the Supercritical Co2-water Interface

We have previously investigated the formation of water-CO2 interface by means of a drop tensiometer [1]. In presence of CO2 , the interaction between the two adjacent phases leads to an organization of interfacial cluster network which controls the tension and the mechanical properties of the interface. The formation of those clusters at CO2 pressure lower than 80 bar inhibits the adsorption of protein (ovalbumin (OVA)) dissolved in water at low concentration (0.002 g/L) whereas higher concentration (0.047 g/L) led to a protein film. We noticed a peculiar behavior at 90 bar where penetration of protein into the interface modified the kinetics and elasticity of the interface whatever the protein concentration.