RESUMO
The classic application of ultrafiltration (UF) is for the complete retention of proteins, and in that situation, the transport behavior is well established. More open membranes with fractional retention are used when separating different proteins. However, protein transport has not been well documented yet in the literature. The bovine serum albumin (â¼69 kDa) observed rejection ranges from 0.65 to 1 using a 300 kDa molecular weight cut-off membrane at different pH, ionic strength, and pressure. We demonstrated that, especially with open UF, the transport of proteins through the membrane is dominated by advection, with insignificant diffusion effects (p value > 0.05). We showed that with open UF, retention is not only caused by size exclusion but also to a large extent by electrostatic interactions and oligomerization of the proteins. Mass transfer in the polarization layer was relatively independent of the pH and ionic strength. It was underestimated by common Sherwood relations due to a relatively large contribution of the reduction in the flow turbulence near the membrane by the removal of fluid through the membrane. We propose a model that allows relatively quick characterization of the rejection of proteins without prior knowledge of the pore sizes and charges based on just a limited set of experiments. Therefore, protein rejection with the open UF system can be targeted by tuning the processing conditions, which might be useful for designing protein fractionation processes.
