HIGH-THROUGHPUT PROCESSING OF PROTEINS USING A POROUS AND TENTACLE ANION-EXCHANGE MEMBRANE

The immobilization of polymer chains containing a diethylamino (DEA) g roup on the pore surface of a porous hollow-fibre membrane is reported . This novel membrane can collect proteins at a high rate and high cap acity because of convective transport and multi-layering of proteins. Overlapping of the breakthrough curves for different residence times o f bovine serum albumin (BSA) solution demonstrates that the diffusiona l resistance of BSA to the DEA group anchored to the polymer chain was negligible. Membranes with a higher density of DEA groups exhibited a higher binding capacity for BSA. For example, a membrane with a DEA g roup density of 2.9 mol/kg had a BSA binding capacity of 490 g/kg, whi ch was equivalent to eleven times the adsorption capacity of a monolay er. This vertical layering is due to holding of the BSA molecules in a tentacle-like manner by the graft chains extending from the pore surf ace towards the pore interior.