Kinetic study of the concentration dependence of the mass transfer rate coefficient in anion-exchange chromatography of bovine serum albumin
- Univ. of Tennessee, Knoxville, TN (United States). Dept. of Chemistry
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{sub 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{sub m,L}, the surface diffusivity (D{sub s}) of BSA increases with increasing concentration. The linear concentration dependence of k{sub m,L} seems to originate in a similar dependence of D{sub s}. The use of a heterogeneous-surface model for the anion-exchange resin provides an explanation of the positive concentration dependence of D{sub 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.
- Sponsoring Organization:
- National Science Foundation, Washington, DC (United States); Tennessee Univ., Knoxville, TN (United States); Oak Ridge National Lab., TN (United States)
- OSTI ID:
- 687345
- Journal Information:
- Biotechnology Progress, Vol. 15, Issue 4; Other Information: PBD: Jul-Aug 1999
- Country of Publication:
- United States
- Language:
- English
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