The vortex flow reactor (VFR) can be used in many chemical engineering applications. This paper assesses its novel use in the purification of monoclonal antibodies from cell broth. To this end, the IgG2a antibody was purified from the unclarified fermentation broth of transgenic mouse 55/6 hybridoma cells. Visual experiments showed that the VFR worked in the laminar vortices flow regime and the vortices displaced slightly faster than the axial flow. The VFR has the advantage of creating two sorts of flows: axial flow to produce the expanded bed and an extra vortex flow to avoid channeling and stabilize the expanded bed, the hydrodynamic behavior of which is plug flow with an experimental Pèclet number higher than 20. The pH was adjusted in the untreated fermentation broth, which was directly introduced into the reactor thus reducing the number of stages. The IgG2a purification was carried out in a single device via two steps: antibody adsorption in the expanded bed and antibody elution in the settled bed using Streamline rProtein A. A thirty-fold increase in the high-purity antibody concentration was achieved at the top of the pH5 elution peak with a total recovery of 93.1% (w/w) between elution peaks pH 5 and 3.
Keywords: Adsorption; Antibody; Expanded bed; Purification; Péclet number; Vortex flow reactor.
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