Two-component protein adsorption kinetics in porous ion exchange media.

This work provides a theoretical analysis of multicomponent adsorption kinetics for conditions typical of protein adsorption in porous ion exchangers as well as experimental results for the adsorption of lysozyme/cytochrome c mixtures in the cation exchanger SP-Sepharose-FF. The theory predicts the formation of overshoots in the intraparticle concentration profiles and in the total amount adsorbed for the more weakly adsorbed component. An analytical solution valid for the case where the isotherms are rectangular is developed and found to be in good agreement with the limiting behavior of the general numerical solution of the model equations. The experimental results show that the two proteins are competitively adsorbed and that an overshoot of adsorbed cytochrome c occurs during simultaneous adsorption. Model predictions based on the assumption that the adsorption isotherms are rectangular and that lysozyme completely displaces cytochrome c are in qualitative and quantitative agreement with the experimental kinetics suggesting that the overshoot phenomena observed with multicomponent systems in these resins can be explained with a diffusion model without the need to account for flux coupling or electrophoretic contributions to transport.

[1]  Giorgio Carta,et al.  Binary protein adsorption on gel‐composite ion‐exchange media , 1999 .

[2]  G. Carta,et al.  Particle‐size distribution effects in batch adsorption , 2003 .

[3]  M. Kula,et al.  Dynamics of protein uptake within the adsorbent particle during packed bed chromatography. , 2002, Biotechnology and bioengineering.

[4]  Stuart R. Gallant.  Modeling ion-exchange adsorption of proteins in a spherical particle. , 2004, Journal of chromatography. A.

[5]  G. Carta,et al.  Protein adsorption on novel acrylamido-based polymeric ion exchangers. II. Adsorption rates and column behavior. , 2000, Journal of chromatography. A.

[6]  Douglas M. Ruthven,et al.  Principles of Adsorption and Adsorption Processes , 1984 .

[7]  Magnus Östberg,et al.  Apparent pore size distributions of chromatography media , 1996 .

[8]  Thomas Linden,et al.  Mechanism and kinetics of protein transport in chromatographic media studied by confocal laser scanning microscopy. Part I. The interplay of sorbent structure and fluid phase conditions. , 2003, Journal of chromatography. A.

[9]  M. Kula,et al.  Visualizing patterns of protein uptake to porous media using confocal scanning laser microscopy , 2002 .

[10]  M. Etzel,et al.  Competitive adsorption of α-lactalbumin and bovine serum albumin to a sulfopropyl ion-exchange membrane , 1994 .

[11]  G. Carta,et al.  Protein partitioning and transport in supported cationic acrylamide-based hydrogels , 2003 .

[12]  G. Carta,et al.  Protein diffusion in charged polyacrylamide gels. Visualization and analysis. , 1999, Journal of chromatography. A.

[13]  A. Lenhoff,et al.  Nondiffusive mechanisms enhance protein uptake rates in ion exchange particles , 2003, Proceedings of the National Academy of Sciences of the United States of America.

[14]  A. Ljunglöf,et al.  Confocal microscopy as a tool for studying protein adsorption to chromatographic matrices , 1996 .

[15]  H. Chase,et al.  Two-component protein adsorption to the cation exchanger S Sepharose FF. , 1990, Journal of chromatography.

[16]  Steven M. Cramer,et al.  Steric mass‐action ion exchange: Displacement profiles and induced salt gradients , 1992 .

[17]  C. H. Byers,et al.  Continuous separation of proteins by annular chromatography , 1991 .

[18]  G. Carta,et al.  Protein Transport in Constrained Anionic Hydrogels: Diffusion and Boundary-Layer Mass Transfer , 2001 .