Abstract
The effect of pH and NaCl concentration on the equilibrium adsorptive behavior of β-lactoglobulin at hydrophilic and hydrophobic silicon surfaces was studied using ellipsometry. Experimental conditions studied included pH 3.00, 0.1 M Na +; pH 6.60, 0.1 M Na +; pH 8.90, 0.1 M Na +; and pH 8.90, 0.5 M Na +. Plots of adsorbed mass as a function of protein concentration exhibited attainment of plateau values beyond a protein concentration of 0.25 mg/ml. At a given pH and ionic strength, as expected, plateau values associated with hydrophobic surfaces were observed to be greater than those associated with hydrophilic surfaces. A Langmuir-type adsorption isotherm was chosen as an appropriate model to represent the data and was used to compare results obtained under different experimental conditions. Effects of pH and NaCl concentration on protein adsorption at hydrophilic surfaces indicate that electrostatics play a major role, while pH and NaCl concentration effects on adsorption at hydrophobic surfaces reflect a greater importance of nonelectrostatic interactions.
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