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Adsorption of proteins and the effect of the chemical nature of membrane surfaces on protein adsorption were investigated
using14C-tagged albumin and several microporous membranes (polyvinilydene fluoride, PVDF; nylon; polypropylene, PP; and polycarbonate,
PC). The membrane surfaces were modified by exposing them to low-temperature plasma of several different monomers (n-butane, oxygen, nitrogen alone or as mixtures) in a radiofrequency plasma reactor. Transients in the permeability of albumin
solutions through the membranes and changes in flux of distilled water through the membranes before and after adsorption of
albumin were used to investigate the role of protein adsorption on membrane fouling. The results show that the extent of adsorption
of albumin on hydrophobic membranes was considerably more than that on hydrophilic membranes. The hydrophilic membranes were
susceptible to electrostatic interactions and less prone to fouling. A pore-blocking model was successfully used to correlate
the loss of water flux through pores of defined geometry 相似文献
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