Abstract
A method was conceived for the purification of biomolecules on a continuous-flow basis using affinity adsorption. The affinity ligand was bound to a nylon belt which was passed sequentially through four chambers to which flows of feedstock, wash medium, eluent and regeneration medium were applied. The target compound was thus removed from the feedstock stream and desorbed into a continuous flow of eluent. Prototype laboratory-scale apparatus was designed and constructed and the technical feasibility of this method was demonstrated using soybean trypsin inhibitor as a ligand for the adsorption of trypsin. The effects of various operational parameters on apparatus function were investigated using this model system. In addition, continuous removal of trypsin from a bovine pancreatic extract was carried out during an 8 h experiment.
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