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Adsorption and mass transfer studies of Catalase in IMAC chromatography by dynamics methods

Paper ID Volume ID Publish Year Pages File Format Full-Text
36290 45127 2006 10 PDF Available
Title
Adsorption and mass transfer studies of Catalase in IMAC chromatography by dynamics methods
Abstract

The adsorption equilibrium constant and kinetic properties for Catalase on Cu–IDA–agarose matrix have been measured by an impulse chromatography technique.The experiments were performed at pHs of 7.00, 7.40 and 7.80 and flow rates of 1.56–2.66 ml min−1. The impulse chromatographic technique has been applied to determine the equilibrium and kinetic parameters for Catalase in the Cu(II)–IDA–agarose system. It was found that the enzyme adsorption decreases with increasing pH from 7.00 to 7.80 at 298 K, and the optimum adsorption on the pH range studied was found at 7.00. In addition effective axial dispersion and internal, external and global mass transfer resistances decrease with decreasing pH. Molecular and effective intraparticle diffusion coefficients of Catalase in this study decrease with increasing pH. Both, the external and the internal diffusion, are adsorption-controlling steps for the Catalase adsorption on Cu(II)–IDA–agarose packed columns. It was also found that global mass transfer resistance in the system is constant for the different flow rates studied.

Keywords
Affinity chromatography; Purification; Mass transfer; Diffusion; Dynamic methods; Catalase
First Page Preview
Adsorption and mass transfer studies of Catalase in IMAC chromatography by dynamics methods
Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 41, Issue 1, January 2006, Pages 142–151
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering