Abstract
To determine further the enhancement and mitigation mechanisms of protein fouling, filtration experiments were carried out with polyvinylidene fluoride (PVDF) ultrafiltration (UF) membranes and bovine serum albumin (BSA) over a range of ionic strengths. The interaction forces, the adsorption behavior of BSA on the membrane surface, and the structure of the BSA adsorbed layers at corresponding ionic strengths were investigated. Results indicate that when the ionic strength increased from 0 to 1 mM, there was a decrease in the PVDF-BSA and BSA-BSA electrostatic repulsion forces, resulting in a higher deposition rate of BSA onto the membrane surface, and the formation of a denser BSA layer; consequently, membrane fouling was enhanced. However, at ionic strengths of 10 and 100 mM, membrane fouling and the BSA removal rate decreased significantly. This was mainly due to the increased hydration repulsion forces, which caused a decrease in the PVDF-BSA and BSA-BSA interaction forces accompanied by a decreased hydrodynamic radius and increased diffusion coefficient of BSA. Consequently, BSA passed more easily through the membrane and into permeate. There was less accumulation of BSA on the membrane surface. A more nonrigid and open structure BSA layer was formed on the membrane surface.
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