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

Abstract

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.

Authors:
;  [1]
  1. Univ. of Tennessee, Knoxville, TN (United States). Dept. of Chemistry
Publication Date:
Sponsoring Org.:
National Science Foundation, Washington, DC (United States); Tennessee Univ., Knoxville, TN (United States); Oak Ridge National Lab., TN (United States)
OSTI Identifier:
687345
Resource Type:
Journal Article
Journal Name:
Biotechnology Progress
Additional Journal Information:
Journal Volume: 15; Journal Issue: 4; Other Information: PBD: Jul-Aug 1999
Country of Publication:
United States
Language:
English
Subject:
55 BIOLOGY AND MEDICINE, BASIC STUDIES; ALBUMINS; CATTLE; ION EXCHANGE CHROMATOGRAPHY; BIOCHEMICAL REACTION KINETICS; MASS TRANSFER

Citation Formats

Miyabe, Kanji, Guiochon, G, and Oak Ridge National Lab., TN. Kinetic study of the concentration dependence of the mass transfer rate coefficient in anion-exchange chromatography of bovine serum albumin. United States: N. p., 1999. Web. doi:10.1021/bp990062x.
Miyabe, Kanji, Guiochon, G, & Oak Ridge National Lab., TN. Kinetic study of the concentration dependence of the mass transfer rate coefficient in anion-exchange chromatography of bovine serum albumin. United States. https://doi.org/10.1021/bp990062x
Miyabe, Kanji, Guiochon, G, and Oak Ridge National Lab., TN. 1999. "Kinetic study of the concentration dependence of the mass transfer rate coefficient in anion-exchange chromatography of bovine serum albumin". United States. https://doi.org/10.1021/bp990062x.
@article{osti_687345,
title = {Kinetic study of the concentration dependence of the mass transfer rate coefficient in anion-exchange chromatography of bovine serum albumin},
author = {Miyabe, Kanji and Guiochon, G and Oak Ridge National Lab., TN},
abstractNote = {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.},
doi = {10.1021/bp990062x},
url = {https://www.osti.gov/biblio/687345}, journal = {Biotechnology Progress},
number = 4,
volume = 15,
place = {United States},
year = {Thu Jul 01 00:00:00 EDT 1999},
month = {Thu Jul 01 00:00:00 EDT 1999}
}