SepFastTM Supor Q (DEAE, S, CM) is a strong anion exchange chromatography product in a ready-to-use disposable format. The working medium possesses a combination of small pores (50-100nm) and large pores (micro level). It shows fast accessibility to both small and large molecules (e.g. plasmid and virus). Therefore, it has comparable binding capacity to those of membrane or monolith product in respect of DNA or virus. However, SepFastTM Supor media shows much higher binding capacity to protein molecules than the membrane or monolith type of products.
The base matrix is made of a composite of polysaccharides that have been well cross-linked. The medium is stable to most of the chemical conditions experienced in the bioprocessing industry. It shows excellent binding capacity to both protein and macromolecule e.g. DNAs (Table 1) at high flowrate. Certainly the capacity is further increased at lower flowrates.
Table 1: A comparison of the dynamic binding capacity (DBC at 10% breakthrough) of different products (1 cm bed height).
SepFastTM Supor IEX media can be used in the final polishing step (shallow bed format) or be used for the binding-elution of both small (proteins) and large molecules (e.g. plasmid and virus) at deep bed format. Please contact us for further information.
It can be operated at both high flowrate or low-to-moderate flowrate. The column is compatible to most of the liquid-handling equipment. The operational pressure should not exceed 4 bars.
The medium was stored in 20% denatured ethanol. Before a chromatography run, equilibrate the column with working buffer until the effluent shows stable conductivity and pH value.
We recommend scouting for optimal binding pH and for optimal ionic strength.
SepFastTM Supor media has a protein binding capacity (tested with BSA) virtually independent of the flowrate. We recommend to pay special attention to optimising elution conditions to avoid tailing in the elution step.
Lim, S.L et. al. 2018. Single-step purification of recombinant hepatitis B core antigen Y132A dimer from clarified Escherichia coli feedstock using a packed bed anion exchange chromatography. Process Biochemistry, 69, pp.208-215.
Lim, S.L.et.al. 2015. Direct purification of hepatitis B core antigen Y132A dimer using packed bed anion exchange chromatography. In Asia Pacific Confederation of Chemical Engineering Congress 2015: APCChE 2015, incorporating CHEMECA 2015 (p. 1370). Engineers Australia.
Yap, C.F. et. al. 2013. Purification of long helical capsid of newcastle disease virus from Escherichia coli using anion exchange chromatography. Biotechnology progress, 29(2), pp.564-567.
Monjezi, R. et. al. 2010. Purification of bacteriophage M13 by anion exchange chromatography. Journal of Chromatography B, 878(21), pp.1855-1859.