Protein adsorption on novel acrylamido-based polymeric ion-exchangers. IV. Effects of protein size on adsorption capacity and rate.

The effects of protein size on the adsorption capacity and rate is determined for an acrylamido-based polymeric anion-exchanger. The proteins lactalbumin, myoglobin, ovalbumin, BSA, conalbumin, IgG, and ferritin with molecular masses ranging from 15,000 to 450,000 were investigated. At high salt concentration (50 mM Tris-HCl containing 500 mM NaCl), only the smaller proteins lactalbumin and myoglobin gained access to a significant portion of the particle volume. The larger proteins were nearly completely excluded, in agreement with the results obtained for neutral macromolecules. By contrast, at low salt concentration (50 mM Tris-HCl), the adsorption capacity was very large (280-400 mg/ml of particle volume) for all the proteins studied except for ferritin, for which the capacity was much lower. This suggests that, provided the solute is not too large, the favorable electrostatic interaction overcomes the size exclusion effect. Adsorption rate measurements showed that mass transfer rates are also quite fast at low salt concentration. Effective diffusivities were determined by matching model and experimental results and were found to decrease substantially as the protein size increased. As previously observed, the homogeneous diffusion model was found to predict the experimentally observed trends with respect to protein concentration and boundary layer mass transfer effects.