Destabilization and removal of immobilized enzymes adsorbed onto polyethersulfone ultrafiltration membranes by salt solutions

• A PESH 30 kDa UF membrane was fouled with enzymatic solutions at 2, 7.5 and 15 g/L.
• Protein aggregation was analyzed by DLS, AFM and ATR-FTIR techniques.
• Complete blocking/adsorption and cake formation dominated membrane fouling.
• Both NaCl effect and temperature cooperated in protein aggregates destabilization.

In this work the effectiveness of two saline solutions (NaCl and Na2SO4) to clean a permanently hydrophilic polyethersulfone (PESH) ultrafiltration (UF) membrane with a molecular weight cut-off (MWCO) of 30 kDa previously fouled with enzymatic solutions was investigated. The influence of protein concentration in the enzymatic solution during the fouling step and the effect of salt type during the cleaning procedure were studied.The protein aggregation was analyzed in solution and onto the membrane surface by using several techniques including Dynamic Light Scattering (DLS), Atomic Force Microscopy (AFM) and Infrared Spectroscopy with Attenuated Total Reflectance (ATR-FTIR). In addition, mechanisms that dominate membrane fouling were studied by fitting some mathematical models (Hermia׳s models adapted to crossflow filtration, a combined model based on the complete blocking and cake formation equations and a resistance-in-series model) to the experimental data.Fouling results showed that the complete blocking/adsorption on membrane surface was the predominant fouling mechanism. Regarding the cleaning results, higher cleaning efficiency and low residual protein concentration was obtained with NaCl solutions for all the feed solutions tested due to the favorable interaction between Cl− and proteins.