Abstract
One of the main peculiarities in protein chromatography is that the adsorbing proteins and the adsorbent pores have comparable sizes. This has the consequence that the pore accessibility depends not only on the solute size but also on the loading conditions of the adsorbent because protein adsorption significantly reduces the size of the pores. A model that accounts for the pore size distribution of the stationary phase and for the pore shrinkage due to protein adsorption has been developed to describe mass transport and adsorption in the porous particles. This model has been shown to be equivalent to the general rate model (GRM) in the case of processes under highly diluted conditions with little adsorption. This implies that the model parameters determination follows the same procedure as for the classical GRM. The new pore model has been applied and compared to the GRM for the simulation of lysozyme breakthrough experiments and for the prediction of 5% dynamic binding capacity values solely based on static capacity measurements.
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