2006 AIChE Annual Meeting
(113e) Protein Transport in Nanoporous Membranes
Author
The fluxes of bovine serum albumin and bovine hemoglobin through charged nanopores inside polymeric membranes are measured and analysed as a function of the pore size, the applied voltage to the nanopore surface, the solution ionic strength and pH. The pore surface has been modified by a self-assembled monolayer. The electrostatic interaction of the protein with the nanopore surface gives low transport rates except at the protein's isoelectric point and the minimum of the effective, voltage-induced nanopore charge. The electrostatic sieving effect allows for the separation of proteins with similar molecular weights.