Abstract
The equilibrium and kinetic characteristics of the adsorption of bovine serum albumin (BSA) and lysozyme to the strong cation exchanger S Sepharose FF have been determined. The rates of protein adsorption have been compared to two different models, the first being based on a single lumped kinetic parameter, whilst the second model considers the individual transport processes occurring prior to the adsorption reaction, that is taking into account diffusion across the liquid film surrounding individual particles and also the diffusion within the ion-exchanger particle itself. It was found that the adsorption of lysozyme to S Sepharose FF, in both batch, agitated tanks and in packed beds was consistent with both models. In the case of BSA however, the agitated tank adsorption profile was consistent only with the pore diffusion model and neither model correctly predicted the latter part of the breakthrough profile observed in packed-bed experiments.
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