Mulinari, JéssicaAmbrosi, AlanFeng, YurenHe, ZeHuang, XiaochuanLi, QilinDi Luccio, MarcoHotza, DachamirOliveira, J. Vladimir2023-02-202023-02-202023Mulinari, Jéssica, Ambrosi, Alan, Feng, Yuren, et al.. "Polydopamine-assisted one-step immobilization of lipase on α-alumina membrane for fouling control in the treatment of oily wastewater." <i>Chemical Engineering Journal,</i> 459, (2023) Elsevier: https://doi.org/10.1016/j.cej.2023.141516.https://hdl.handle.net/1911/114462Covalent enzyme immobilization is generally a time-consuming and multistep procedure that uses toxic solvents and requires more than one chemical, making industrial upscaling unattractive. Using an aqueous polydopamine (PDA) solution for enzyme immobilization is a greener alternative. Usually, enzyme immobilization using PDA is performed in two steps: dopamine polymerization on the material surface followed by enzyme immobilization. A few recent studies applied a one-step strategy by mixing dopamine and enzyme in the coating solution, reducing the immobilization time, chemical consumption, and wastewater generation. This study compares the two-step and one-step approaches to immobilizing the lipase Eversa Transform 2.0 (ET2) on an α-alumina membrane. The one-step immobilization method achieved similar enzyme loading, membrane hydrolytic activity, and enzyme-specific activity to those of the two-step method. The ET2 immobilized using both strategies showed excellent fouling resistance and self-cleaning performance in oily wastewater filtration. The membrane modified by the one-step approach exhibited a lower reduction in pure water permeance after oil fouling (35%) and a higher permeance recovery (90%) than the one modified by the two-step method (40% and 74%, respectively). This better performance can be due to the higher hydrophilicity of the modified membrane and higher stability over reaction time shown by the enzyme immobilized by the one-step strategy. The higher stability can be attributed to more attachment points between the enzyme and PDA, increasing the enzyme rigidity and preventing conformational changes.engThis is an author's peer-reviewed final manuscript, as accepted by the publisher. The published article is copyrighted by Elsevier.Journal articleEversa transform 2.0Enzyme immobilizationCeramic membraneReactive membranePolydopamineOne-pot immobilizationhttps://doi.org/10.1016/j.cej.2023.141516