Surfactant cleaning of ultrafiltration membranes fouled by whey

A polyethersulphone ultrafiltration membrane was prepared for concentration of whey. The membrane was fouled by whey and the effect of different cleaning agents on flux recovery of the fouled membrane was studied. The optimum cleaning procedure for membrane regeneration was elucidated. The results showed that a combination of surfactants (anionic, cationic and nonionic) may be employed as the optimum cleaning agent for maximum flux recovery. The fluorescence studies revealed that the cationic surfactant interact with proteins by breaking the intra-chain hydrophobic bonding and providing electrostatic repulsion. Changing the alkyl chain from dodecyl to hexadecyl increases the interaction of surfactant-protein. Dodecyltrimethylammonium bromide (DTAB) provided a weak interaction with whey proteins than to tetradecyltrimethylammonium bromide (TTAB) and cetyltrimethylammonium bromide (CTAB). All data obtained in this study support a surfactant-protein interaction in which hydrophobic forces play a dominant role. The nonionic surfactants poly(oxyethylene) isooctyl phenyl ether (TX-100) and anionic surfactants SDS interact with amino acids in the inner protein structure thus denaturate tertiary protein structure and reduce hydrophobic interaction of proteins by membrane surface.