Kinetic study of the concentration dependence of the mass transfer rate coefficient in anion-exchange chromatography of bovine serum albumin.

The experimental results of a previous study of the mass transfer kinetics of bovine serum albumin (BSA) in ion-exchange chromatography under nonlinear conditions are reevaluated. The analysis of the concentration dependence of the lumped mass-transfer rate coefficient (k(m,L)) provides information on the kinetics of axial dispersion, fluid-to-particle mass transfer, intraparticle mass transfer, and adsorption/desorption. The new analysis shows that the contribution of intraparticle mass transfer is the dominant one. Similar to k(m,L), the surface diffusivity (D(s)) of BSA increases with increasing concentration. The linear concentration dependence of k(m,L) seems to originate in a similar dependence of D(s). The use of an heterogeneous-surface model for the anion-exchange resin provides an explanation of the positive concentration dependence of D(s). This work illustrates how frontal analysis data can be used for a detailed investigation of the kinetics of mass transfer between the phases of a chromatographic column, in addition to its conventional use in the determination of the thermodynamic characteristics of the phase equilibrium.