Although a number of previous studies have demonstrated that solution pH can have a dramatic effect on protein transport through ultrafiltration membranes, the exact origin of this behavior has been unclear. Experimental data were obtained for the transport of a broad range of proteins with different surface charge and molecular weight. The effective hydrodynamic size of the proteins was evaluated using size-exclusion chromatography. The membrane charge, both before and after exposure to a given protein, was evaluated using streaming potential measurements. In most cases, the electrostatic interactions were dominated by the distortion of the electrical double layer surrounding the protein, leading to a distinct maximum in protein transmission at the protein isoelectric point. Attractive electrostatic interactions did occur when the protein and membrane had a large opposite charge, causing a second maximum in transmission at a pH between the isoelectric points of the protein and membrane. The sieving data were in good agreement with theoretical calculations based on available models for the partitioning of charged solutes in cylindrical pores.
|Original language||English (US)|
|Number of pages||11|
|Journal||Biotechnology and bioengineering|
|State||Published - Jul 5 1999|
All Science Journal Classification (ASJC) codes
- Applied Microbiology and Biotechnology