Characterization of protein adsorption on membrane surface by enzyme linked immunoassay

A new method for determining the amount of adsorbed protein on membrane surface is developed on the basis of immunoassay using alkaline phosphotase as enzyme label and 4-nitrophenyl phosphate as substrate. Adsorption of human serum albumin (HSA) on HT Tuffryn, a kind of polysulfone microfiltration membrane, in the absence and presence of an electric field is investigated experimentally. It is shown that the adsorption of HSA on HT membrane surface is finished within 5 min and the amount of the adsorbed HSA decreases with the increase in pH but is not sensitive to salt concentration. Desorption of the adsorbed HSA from HT membrane surface can only be achieved with NaOH. Adding surfactants in HSA solution to prevent the adsorption is attempted and Tween 20 shows the best shielding function compared to polyethylene glycol 6000 and pluronic-F108. A critical concentration exists for Tween 20, below which the increase in the concentration of Tween 20 results in a corresponding reduction of adsorbed HSA. Introducing electric field into the adsorption leads to an enhanced adsorption of HSA, which appears to be a function of pH and the electric field strength.