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

Journal Article · · Biotechnology Progress
DOI:https://doi.org/10.1021/bp990062x· OSTI ID:687345
;  [1]
  1. 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, Journal Name: Biotechnology Progress Journal Issue: 4 Vol. 15; ISSN 8756-7938; ISSN BIPRET
Country of Publication:
United States
Language:
English

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