To determine the fouling behavior of bovine serum albumin (BSA) on differet hydropniic PVDF ultrafiltration membrane over a range of pH, atomic force microscopy (AFM) and self-made colloidal probes were used to detect the microscopic adhesion forces of membrane-BSA and BSA-BSA, respectively. The results showed a positive correlation between the flux decline extent and the membrane-foulant adhesion force in the initial filtration stage, whereas the foulant-foulant interaction force was closely related to the membrane fouling in the later filtration stage. Moreover, the membrane-BSA adhesion interaction was stronger than the BSA-BSA adhesion interaction, which indicated that the fouling was mainly caused by the adhesion interaction between membrane and foulant. At the same pH, the adhesion force between PA membrane-BSA was smaller than that of PP membrane-BSA, illustrating the more hydrophilic the membrane was, the better the antifouling ability it had. The adhesion force between BSA-BSA fouled PA membrane was similar to that between BSA-BSA fouled PP membrane. These results confirmed that elimination of the membrane-BSA adhesion force is important to control the protein fouling of membranes.

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