Abstract
The effect of in-place regeneration on equilibrium and kinetic characteristics of the adsorption of bovine serum albumin to a DEAE-cellulose anion exchanger has been determined. Regeneration with sodium hydroxide and time of exposure showed no effect on equilibrium behavior. Breakthrough curves were measured for protein adsorption on fixed-bed columns and analyzed by a simple model to determine the relevant rate constants for the adsorption process. It was found that forward adsorption rate constant decreased exponentially with the chemical treatment exposure time. The implications of the results on the design and optimization of ion-exchange chromatographic processes are discussed.
Original language | English (US) |
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Pages (from-to) | 99-107 |
Number of pages | 9 |
Journal | Journal of Chromatography A |
Volume | 791 |
Issue number | 1-2 |
DOIs | |
State | Published - Dec 12 1997 |
Keywords
- Adsorption isotherms
- Albumin
- Column regeneration
- Computer simulation
- Ion-exchange chromatography
- Kinetic studies
- Proteins
ASJC Scopus subject areas
- Analytical Chemistry
- Biochemistry
- Organic Chemistry