A direct comparison between membrane adsorber and packed column chromatography performance

J Chromatogr A. 2020 Feb 8:1612:460629. doi: 10.1016/j.chroma.2019.460629. Epub 2019 Oct 16.

Abstract

The purpose of this work was to compare side by side the performance of packed bed and membrane chromatography adsorption processes for protein purification. The comparison was performed using anion exchange media with the same ligand immobilized on the adsorbing surface, namely the strong Q quaternary ammonium group, R-CH2-N+-(CH3)3, and bovine serum albumin (BSA) as a model protein. In addition, the stationary phase volume was held constant for each geometry (3 mL) and runs were executed using the same mobile phase superficial velocity. As expected, the packed bed column showed higher equilibrium binding of BSA at 66.9 mg/mL versus 43.04 mg/mL for the membrane adsorber. Dynamic binding capacities were also higher in the packed bed; for example, at 97.5 cm/h, a capacity of 62.8 mg/mL was measured for the packed bed versus 20.7 mg/mL for the membrane adsorber. The higher equilibrium and dynamic capacities of the packed bed are likely due to the higher surface area per unit volume of the resin. However, the maximum productivity for the membrane adsorber was 111 mg/(mL h), a value that was 3.3 times higher than the one of the packed column. The bed utilization - defined as the ratio of the dynamic binding capacity at 10% breakthrough to the saturation binding capacity - was also higher for the packed column at long residence times and lower at short residence times confirming the better performance of membrane chromatography at high flow rates.

Keywords: Binding capacity; Chromatography; Membrane adsorber; Packed column; Productivity.

Publication types

  • Comparative Study

MeSH terms

  • Adsorption
  • Anion Exchange Resins
  • Chromatography, Ion Exchange / methods*
  • Proteins / isolation & purification*
  • Serum Albumin, Bovine / isolation & purification

Substances

  • Anion Exchange Resins
  • Proteins
  • Serum Albumin, Bovine