Fractionation of proteins by ultrafiltration is an interesting challen
ge. With a particular membrane, the protein-protein and protein-membra
ne interactions largely decide which protein passes through and which
is retained. System hydrodynamics also affects protein fractionation a
s the transmission behavior of a protein is altered by concentration p
olarization. Therefore, disruption of the concentration polarization l
ayer would help to maintain the native selectivity of the membrane and
hence aid in protein fractionation. An attempt is made to use gas spa
rging, a technique proven effective in controlling concentration polar
ization to enhance the selectivity of separation of BSA (MW 67,000) an
d lysozyme (MW 14,100). The effects of gas flow rate, liquid flow rate
and feed concentration on the selectivity of fractionation are examin
ed. Gas sparging enhances protein fractionation; under suitable soluti
on conditions, nearly complete separation of BSA and lysozyme was achi
eved with gas sparged ultrafiltration. The permeate flux was also incr
eased by gas sparing. The mechanism of enhancement is explained in ter
ms of disruption of the concentration polarization layer and enhanced
mass transfer due to bubble-induced secondary flow.