Polydopamine-assisted one-step immobilization of lipase on α-alumina membrane for fouling control in the treatment of oily wastewater

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dc.citation.articleNumber141516
dc.citation.journalTitleChemical Engineering Journal
dc.citation.volumeNumber459
dc.contributor.authorMulinari, Jéssica
dc.contributor.authorAmbrosi, Alan
dc.contributor.authorFeng, Yuren
dc.contributor.authorHe, Ze
dc.contributor.authorHuang, Xiaochuan
dc.contributor.authorLi, Qilin
dc.contributor.authorDi Luccio, Marco
dc.contributor.authorHotza, Dachamir
dc.contributor.authorOliveira, J. Vladimir
dc.contributor.orgNanotechnology-Enabled Water Treatment Center (NEWT)
dc.date.accessioned2023-02-20T17:17:47Z
dc.date.available2023-02-20T17:17:47Z
dc.date.issued2023
dc.description.abstractCovalent 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.
dc.identifier.citationMulinari, 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.
dc.identifier.doihttps://doi.org/10.1016/j.cej.2023.141516
dc.identifier.urihttps://hdl.handle.net/1911/114462
dc.language.isoeng
dc.publisherElsevier
dc.rightsThis is an author's peer-reviewed final manuscript, as accepted by the publisher. The published article is copyrighted by Elsevier.
dc.subject.keywordEversa transform 2.0
dc.subject.keywordEnzyme immobilization
dc.subject.keywordCeramic membrane
dc.subject.keywordReactive membrane
dc.subject.keywordPolydopamine
dc.subject.keywordOne-pot immobilization
dc.titlePolydopamine-assisted one-step immobilization of lipase on α-alumina membrane for fouling control in the treatment of oily wastewater
dc.typeJournal article
dc.type.dcmiText
dc.type.publicationpost-print
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