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

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 be...

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Bibliographic Details
Published in:Process biochemistry (1991) 2006, Vol.41 (1), p.142-151
Main Authors: Gutiérrez, R., Del Valle, E.M.M., Galán, M.A.
Format: Article
Language:English
Subjects:
Affinity chromatography
Catalase
Diffusion
Dynamic methods
Mass transfer
Purification
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Summary: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.
ISSN:1359-5113
1873-3298
DOI:10.1016/j.procbio.2005.06.014