Purifying protein is often a complicated task. This is due to protein’s heterogeneity, complexity and instability when not in their native environment. It is the goal of this book to assemble the most generic approach for protein purification. The use of an expanded bed adsorption (EBA) chromatography as an integrative product capture and concentration technique allows single step purification of biomolecules from complex feedstock a possible alternative. There are a number of different approaches that can be taken in the choice and design of an appropriate adsorbent for use in EBA procedure. In this book, experimental investigation was focused on the choice of the ligand to be used on the solid phase adsorbent to ensure selective isolation of the target protein from a complex feedstock. True biospecific affinity, immobilized metal affinity chelating and ion exchange strategies were investigated for EBA purification. Recombinant glutathione-S-transferase (GST) expressed intracellularly in E.coli was chosen as a model protein. The book is aimed at researchers working in the area of protein purification.

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