Steric mass-action ion exchange: Displacement profiles and induced salt gradients

Authors

  • Clayton A. Brooks,

    1. Bioseparations Research Center, Howard P. Isermann Dept. of Chemical Engineering, Rensselaer Polytechnic Institute, Troy, NY 12180
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  • Steven M. Cramer

    Corresponding author
    1. Bioseparations Research Center, Howard P. Isermann Dept. of Chemical Engineering, Rensselaer Polytechnic Institute, Troy, NY 12180
    • Bioseparations Research Center, Howard P. Isermann Dept. of Chemical Engineering, Rensselaer Polytechnic Institute, Troy, NY 12180
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Abstract

The study of nonlinear competitive equilibrium is of fundamental importance in understanding the behavior of proteins in preparative ion-exchange chromatographic separations. In this work we present a steric mass-action (SMA) ion-exchange equilibrium formalism, which explicitly accounts for the steric hindrance of salt counterions upon protein binding in multicomponent equilibria. An analytical solution has been derived for the calculation of isotachic effluent profiles of displaced proteins and induced salt gradients under ideal chromatographic conditions. A stability analysis has been employed to establish the order of the feed components in the displacement train. Theoretical predictions are compared to experimental results for the separation of proteins by cation-exchange displacement chromatography. These results demonstrate the efficacy of the SMA formalism in predicting complex behavior present in ion-exchange displacement systems. Furthermore, the analytical solution of ideal isotachic displacement profiles with the SMA formalism enables rapid methods development and optimization of ion-exchange displacement separations.

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