Adsorption of proteins at the solution/air interface influenced by added nonionic surfactants at very low...

The influence of the addition of the nonionic surfactants dodecyl dimethyl phosphine oxide (C12DMPO), tetradecyl dimethyl phosphine oxide (C14DMPO), decyl alcohol (C10OH), and C10EO5 at concentrations between 10(-5) and 10(-1) mmol/L to solutions of β-casein (BCS) and β-lactoglobulin (BLG) at a fixed concentration of 10(-5) mmol/L on the surface tension is studied. It is shown that a significant decrease of the water/air surface tension occurs for all the surfactants studied at very low concentrations (10(-5)-10(-3) mmol/L). All measurements were performed with the buoyant bubble profile method. The dynamics of the surface tension was simulated using the Fick and Ward-Tordai equations. The calculation results agree well with the experimental data, indicating that the equilibration times in the system studied do not exceed 30 000 s, while the time required to attain the equilibrium on a plane surface is by one order of magnitude higher. To achieve agreement between theory and experiment for the mixtures, a supposition was made about the influence of the concentration of nonionic surfactant on the adsorption activity of the protein. The adsorption isotherm equation of the protein was modified accordingly, and this corrected model agrees well with all experimental data.