Please use this identifier to cite or link to this item: https://hdl.handle.net/11147/13578
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dc.contributor.authorBalcı, Esintr
dc.contributor.authorRosales, Emilio-
dc.contributor.authorPazos, Marta-
dc.contributor.authorSofuoğlu, Aysuntr
dc.contributor.authorSanroman, Maria Angeles-
dc.date.accessioned2023-07-27T19:49:54Z-
dc.date.available2023-07-27T19:49:54Z-
dc.date.issued2023-05-
dc.identifier.issn2352-1864-
dc.identifier.urihttps://doi.org/10.1016/j.eti.2023.103113-
dc.identifier.urihttps://hdl.handle.net/11147/13578-
dc.description.abstractDibutyl phthalate (DBP) is one of the listed phthalic acid esters (PAEs) known as the priority toxicants which exhibit carcinogenic and teratogenic properties and is responsible for endocrine disruption. Therefore, its removal has become a matter to tackle with. In this work, the feasibility of DBP degradation by esterase and lipase enzymes obtained from various microorganisms and the immobilization of the most effective in a clayey material were investigated. Esterase from Bacillus subtilis exhibited the highest degradation efficiency reaching a complete degradation. Its immobilization onto halloysite nanotubes (HNTs) by adsorption method was studied by response surface methodology using a central composite design face-centered. The four selected factors that affect the HNT-enzyme composite generation were: pH, adsorption time, enzyme/HNT (E/H) ratio, and adsorption temperature, and the optimal conditions were determined (pH 7, time 360 min, E/H ratio 0.2, temperature 30oC). Consequently, the activity did not significantly decrease by immobilization, and the adsorption efficiency and relative activity were determined to be 73.15% and 82.7%, respectively. Besides, the immobilization enhanced thermal and storage stability. As for enzyme reusability, after 7 continuous cycles, the composite maintained almost 75% of its initial activity. Both the free enzyme (1 mg/mL) and the composite degraded 100 mg/L DBP with 100% efficiency and several byproducts were detected. Moreover, the composite could be reused for 7 cycles keeping a remarkable catalytic activity. Overall, this study indicated that the HNT-enzyme composite may be used as an effective candidate for remediation of the environmental media contaminated with DBP and other PAEs.(c) 2023 The Author(s). Published by Elsevier B.V. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).en_US
dc.description.sponsorshipThis research was funded through the 2019-2020 Biodiversa & Water JPI joint call for research proposals, under the BiodivRestore ERA-Net COFUND programme. Project PCI2022-132941 was funded by MCIN/AEI/10.13039/501100011033 and European UnionNextGeneration EU/PRTR and Xunta de Galicia and ERDF (ED431C 2021-43). Additionally, the research has been provided with financial support by the Scientific and Technological Research Council of Turkey (TUBITAK) under the 2214-A Doctoral Research Fellowship Program. Funding for open access charge: Universidade de Vigo/CISUG.en_US
dc.language.isoenen_US
dc.publisherElsevieren_US
dc.relation.ispartofEnvironmental Technology & Innovationen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectEsteraseen_US
dc.subjectDibutyl phthalateen_US
dc.subjectHalloysiteen_US
dc.subjectEnzyme immobilizationen_US
dc.subjectEnzymatic degradationen_US
dc.titleImmobilization of esterase from Bacillus subtilis on Halloysite nanotubes and applications on dibutyl phthalate degradationen_US
dc.typeArticleen_US
dc.authorid0000-0001-8076-6476-
dc.institutionauthorBalcı, Esintr
dc.institutionauthorSofuoğlu, Aysuntr
dc.departmentİzmir Institute of Technology. Chemical Engineeringen_US
dc.departmentİzmir Institute of Technology. Environmental Engineeringen_US
dc.identifier.volume30en_US
dc.identifier.wosWOS:000966131200001en_US
dc.identifier.scopus2-s2.0-85150861349en_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıtr
dc.identifier.doi10.1016/j.eti.2023.103113-
dc.authorscopusid57208907582-
dc.authorscopusid6602563555-
dc.authorscopusid56659233000-
dc.authorscopusid6602341360-
dc.authorscopusid56586197300-
dc.identifier.scopusqualityQ1-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.cerifentitytypePublications-
item.fulltextWith Fulltext-
item.languageiso639-1en-
item.grantfulltextopen-
item.openairetypeArticle-
crisitem.author.dept03.02. Department of Chemical Engineering-
Appears in Collections:Chemical Engineering / Kimya Mühendisliği
Environmental Engineering / Çevre Mühendisliği
Scopus İndeksli Yayınlar Koleksiyonu / Scopus Indexed Publications Collection
WoS İndeksli Yayınlar Koleksiyonu / WoS Indexed Publications Collection
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