Protein adsorption and hydrodynamic stability of a dense, pellicular adsorbent in high-biomass expanded bed chromatography

A dense, pellicular UpFront adsorbent (rho = 1.5 g/cm(3), UpFront Chromatography, Cophenhagen, Denmark) was characterized in terms of hydrodynamic properties and protein adsorption performance in expanded bed chromatography. Cibacron Blue 3GA was immobilised into the adsorbent and protein adsorption of bovine serum albumin (BSA) was selected to test the setup. The Bodenstein number and axial dispersion coefficient estimated for this dense pellicular adsorbent was 54 and 1.63 X 10(-5) m(2)/s, respectively, indicating a stable expanded bed. It could be shown that the BSA protein was captured by the adsorbent in the presence of 30% (w/v) of whole-yeast cells with an estimated dynamic binding capacity (C/C-o = 0.01) of approximately 6.5 mg/mL adsorbent.