Abstract
A mathematical model for the linear gradient elution chromatography of a binary protein system was established based on the axial dispersion theory and pore diffusion model. Bovine serum albumin (BSA) and hemoglobin (Hb) were used as model proteins and Cibacron blue 3GA (CB) modified Sepharose CL-6B (CB-Sepharose) was used as adsorbent. The binary adsorption isotherms of the proteins were expressed by the steric mass-action (SMA) formulism, and its parameters were determined by batch adsorption equilibrium experiments of each protein. With all the model parameters determined by independent experiments or calculated from available correlations, model simulations were performed and compared with the chromatograms of the single-component and binary protein systems. It was found that the model predictions agreed reasonably well with the experimental data obtained under various conditions. The results indicate that the binary SMA formulism with its parameters determined by single-component equilibrium experiments was useful for simulation of nonlinear chromatography.
Published Version
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