Membrane modification to avoid wettability changes due to protein adsorption in an emulsion/membrane bioreactor

This study addresses problems encountered with an emulsion/membrane bioreactor. In this reactor, enzyme- (lipase) catalyzed hydrolysis in an emulsion was combined with two in-line separation steps. One is carried out with a hydrophilic membrane, to separate the water phase, the other with a hydrophobic membrane, to separate the oil phase. In the absence of enzyme, sunflower oil/water emulsions with an oil fraction between 0.3 and 0.7 could be separated with both membranes operating simultaneously. However, two problems arose with emulsions containing lipase. First, the flux through both the hydrophilic and the hydrophobic membranes decreased with exposure to the enzyme. Second, the hydrophobic membrane showed a loss of selectivity demonstrated by permeation of both the oil phase and the water phase through the hydrophobic membrane at low transmembrane pressure. These phenomena can be explained by protein (i.e. lipase) adsorption to the polymer surface within the pores of the membrane. It was proven that lipase was present at the hydrophilic membrane and that this, in part, explains the flux decrease of the hydrophilic membrane. To prevent the observed loss of selectivity with exposure to protein, the hydrophobic polypropylene membrane (Enka) was modified with block copolymers of propylene oxide (PO) and ethylene oxide (EO). These block copolymers act as a steric hindrance for proteins that come near the surface. The modification was successful: After 10 days of continuous operation the minimum transmembrane pressure at which water could permeate through an F 108-modified membrane was 0.5 bar, the same value as that observed in the beginning of the experiment. This indicates that loss of selectivity due to protein adsorption is prevented by the modification of the membrane.