Abstract
A method has been developed for the study of the adsorption of protein by colloidal particles immobilized at an inert solid/liquid interface. The isotherm for BSA adsorption by β-ferric oxyhydroxide was found to be parallel to the concentration axis over the concentration range from 3.5 to 500 g m −3 and yielded saturation coverages consistent with a monolayer of closely packed molecules. A rotating disk experiment was developed to determine the kinetics of adsorption. At low concentrations and low angular velocities, adsorption was diffusion-controlled, with a diffusion coefficient of 6.0 × 10 −11 m 2s −1, in good agreement with literature values for the conditions of the experiment. At higher angular velocities, diffusion was no longer rate limiting and the kinetics of the experiment reflected the rate of adsorption at particle surfaces.
Published Version
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