Em. Tracey et Rh. Davis, PROTEIN FOULING OF TRACK-ETCHED POLYCARBONATE MICROFILTRATION MEMBRANES, Journal of colloid and interface science, 167(1), 1994, pp. 104-116
Bovine serum albumin (BSA) solutions of 0.1 g/liter and 1.0 g/liter we
re filtered through 0.05 mum and 0.2 mum polycarbonate microfiltration
membranes using a stir cell. Total resistance versus time and permeat
e concentration versus time curves and scanning electron micrographs w
ere generated. From these, together with comparing the results to inte
rnal and external fouling models, several different fouling mechanisms
are hypothesized. For 0.1 g/liter concentration and 0.2 mum pore diam
eter, the fouling occurs at the mouths of the pores, slowly closing of
f pore entrance areas while allowing complete transmission of the prot
ein for a period of time. Eventually, the pores become so constricted
that protein transmission decreases and a layer of rejected protein fo
rms on the external membrane surface. For 0.1 g/liter concentration an
d 0.05 mum pore diameter, fouling immediately closes off pores, and pe
rmeate concentration decreases quickly. For 1.0 g/liter concentration
and 0.2 mum pore diameter, the fouling allows for nearly complete tran
smission of proteins for the entire length of the experiment, unlike t
he more dilute case of 0.1 g/liter. Since the diameters of BSA molecul
es are more than an order of magnitude smaller than the pore radii, it
is believed that the proteins form aggregates which accumulate on or
just below the top surface of the membrane, depending on their size re
lative to the pore openings. (C) 1994 Academic Press, Inc.