Comparative modeling of breakthrough curves of bovine serum albumin in anion-exchange chromatography.

The experimental results of a previous study of the mass transfer kinetics of bovine serum albumin (BSA) in ion-exchange chromatography, under nonlinear conditions, were reevaluated using the general rate model of chromatography. Solutions of this model were obtained numerically. The influences of axial dispersion, the resistance to mass transfer from the bulk mobile phase to the surface of the packing particles, and the intraparticle mass transfer resistances on the profiles of the breakthrough curves of BSA were investigated. The results obtained are compared to those of a previous investigation of the same data, using the simple transport-dispersive model and the lumped pore diffusion model. The results obtained show that the use of an oversimplified model for the analysis of chromatographic data can lead to erroneous interpretations of the experimental data and to misunderstandings of the fundamentals of the processes involved. Finally, a theoretical comparison between the properties and the range of application of the three models is provided.