Purification of Immunoglobulin G using different matrices in simulated moving bed chromatography

In the course of the last decade the interest in therapeutic monoclonal antibodies has increased continuously. Consequently an effective purification scheme is of great interest. In most cases protein A affinity chromatography is used. However, due to the high costs of the stationary phases and the potential leakage of ligands there is a trend towards other modes of operation [1]. Simulated moving bed chromatography (SMB) has been considered as an interesting alternative [2]; applications however are still far from common. In this work we present the separation of bovine Immunoglobulin G (IgG) from three model mixtures. Differently functionalised resins for ion-exchange, hydrophobic interaction and size-exclusion chromatography were investigated systematically regarding their adsorption and retention properties for IgG. The obtained parameters were used to calculate appropriate operating conditions for the separation in SMB chromatography