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Equilibrium and kinetics of protein binding on ion-exchange cellulose membranes with grafted polymer layer

Ivana Tatárová, Peter Dreveňák, Anna Kosior, and Milan Polakovič

Department of Chemical and Biochemical Engineering, Institute of Chemical and Environmental Engineering, Faculty of Chemical and Food Technology, Slovak University of Technology, Radlinského 9, 812 37, Bratislava, Slovakia

 

E-mail: milan.polakovic@stuba.sk

Abstract: The performance of weak and strong anion- and cation-exchange membrane adsorbents with a grafted gel layer (Sartobind Q, D, S, and C) was investigated using six proteins: bovine serum albumin, human serum albumin, α-lactalbumin, β-lactoglobulin, lysozyme, and myoglobin. Static binding experiments were used to assess the effect of pH and buffer concentration and to determine the adsorption isotherms for selected membrane/protein combinations. The equilibrium data were duly described either by the Langmuir or Freundlich isotherms. Dynamic binding experiments were carried out for the same membrane/protein combinations in a broad range of linear flow velocity. Both the dynamic binding capacity at 10 % breakthrough and the final binding capacity at complete breakthrough were independent of the flow velocity despite strong dispersion of the adsorption zone. A good match between the equilibrium data from static and dynamic experiments was obtained for the anion exchangers. The correlation between the dynamic binding capacity and protein molecule size was observed for the strong cation exchanger. This was due to the different accessibility of the gel layer for the protein molecules.

Keywords: membrane chromatography – ion-exchange chromatography – protein – adsorption isotherm – static binding capacity – dynamic binding capacity

Full paper is available at www.springerlink.com.

DOI: 10.2478/s11696-012-0269-5

 

Chemical Papers 67 (12) 1527–1536 (2013)

Thursday, July 18, 2024

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