ABSTRACTThe adsorption of proteins onto polymeric surfaces is encountered in many natural and industrial processes and is a prerequisite to their efficient identification, separation, and purification by methods such as chromatography, and filtration. Nevertheless, the exact nature of the adsorption mechanisms and interfacial interactions is not easy to identify for a given protein–polymer system. Here, we aim to document the adsorption mechanism of a protein–polymer system by investigating the adsorption as well as desorption phenomenon of a protein [bovine serum albumin (BSA)] from the polymeric surface [polyethersulfone (PES)]. The analyses performed to document the adsorption mechanism of the BSA–PES system include scanning electron microscope (SEM), attenuated total reflection‐Fourier transform infrared (FTIR), contact angle, zeta potential, surface charge density measurement, and Derjaguin–Landau–Verwey–Overbeek (DLVO). Here, SEM and FTIR identified the physical and chemical properties of pure PES and PES–BSA membranes. The low water contact angle of the PES–BSA membrane confirms its applicability for tissue engineering applications. Further, the zeta potential, surface charge density measurement, and DLVO analyses were performed to document the adsorption mechanism. The adsorption of BSA particles on the PES surface was carried out for pH values that ranged from 4 to 10 for contact times that ranged from 1 to 3 days. A monotonic increase in the zeta potential of the PES–BSA system indicated considerable adsorption of BSA particles on the PES surface. Further, BSA adsorption was very strong for pH values greater than 4.7 which confirms to strong electrostatic interactions between BSA and PES. The strong electrostatic interaction is also collaborated by low desorption rate, which was only ∼22% for pH 10 after 3 days of contact. © 2019 Wiley Periodicals, Inc. J. Appl. Polym. Sci. 2019, 136, 47931.