Comparative performance study of polyethersulfone and polysulfone membranes for trypsin isolation from goat pancreas using affinity ultrafiltration

The comparative performance of polysulfone and polyethersulfone membranes (of 30 kDa MWCO) in isolation of trypsin from goat pancreas by affinity ultrafiltration is examined using cross-linked soybean trypsin inhibitor (STI) as affinity ligand, 0.1 M Tris–HCl as wash buffer and 0.5 M KCl–HCl as elution buffer in an unstirred, dead-ended module at 392.28 kPa (4 kg/cm2) transmembrane pressure and room temperature (ca. 30 °C) with 1:1 (v/v) ratio of pancreatic extract and wash buffer. No active trypsin was found to be detectably present in the washing phase permeate in any of the experiments, indicating good binding efficiency of the target enzyme with the ligand employed. The total protein recovery obtained with the polyethersulfone membrane (70%) is 1.5 times higher than that with the polysulfone (46%). Yields of active trypsin for the two membranes are, however, similar (74% for polyethersulfone and 70% for polysulfone) although comparable with earlier reported trypsin yield (from porcine pancreas). In both the washing and elution phases of affinity ultrafiltration, the polyethersulfone membrane facilitates consistently and substantially higher volumetric flux as well as permeated protein throughput than the polysulfone.