Mitigation of protein fouling by magnesium ions and the related mechanisms in ultrafiltration process

Although protein is an important membrane foulant in the water body that may be significantly affected by the coexisting common cation magnesium (Mg2+), the effect of Mg2+ on protein fouling is rarely reported. In this context, this study selected bovine serum albumin (BSA) as the model foulant, and investigated its fouling characteristics at different Mg2+ concentrations (0–100 mM). Filtration tests showed that the protein fouling can be significantly mitigated by adding Mg2+, and the specific filtration resistance (SFR) of pure BSA (3.56 × 1014 m kg−1) was at least 5 times that of BSA-Mg2+ solutions (0.5–100 mM). In addition, an optimal Mg2+ concentration exists, which can achieve the lowest BSA SFR. A series of characterizations indicated that the main contributors to the differences in BSA SFR were the changes in BSA adhesion capacity and the thickness and structure of the foulant layer. Basically, the above results were attributed to the hydration repulsion effect of Mg2+, which prevented tight adhesion of foulants to the membrane. Moreover, the lowest BSR SFR at 1 mM Mg2+ was achieved not only by the hydration repulsion effect but also by the particle size compression due to the conformational change of BSA molecules. This combined effect led to the lowest foulant retention on the membrane surface and delivered to the lowest SFR. This study conducts a thorough inspection into the specific effect of Mg2+ on protein fouling and provides a fresh insight into protein fouling control in the UF process.