Horseradish Peroxidase Immobilized onto Mesoporous Magnetic Hybrid Nanoflowers for Enzymatic Decolorization of Textile Dyes: A Highly Robust Bioreactor and Boosted Enzyme Stability

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dc.authoridÖZDEMİR, NALAN/0000-0002-8930-5198
dc.authoridAtes, Burhan/0000-0001-6080-229X
dc.authorwosidÖZDEMİR, NALAN/AAL-7083-2021
dc.contributor.authorBakar, Busra
dc.contributor.authorAkbulut, Mustafa
dc.contributor.authorUlusal, Fatma
dc.contributor.authorUlu, Ahmet
dc.contributor.authorOzdemir, Nalan
dc.contributor.authorAtes, Burhan
dc.date.accessioned2024-08-04T20:56:04Z
dc.date.available2024-08-04T20:56:04Z
dc.date.issued2024
dc.departmentİnönü Üniversitesien_US
dc.description.abstractRecently, hybrid nanoflowers (hNFs), which are accepted as popular carrier supports in the development of enzyme immobilization strategies, have attracted much attention. In this study, the horseradish peroxidase (HRP) was immobilized to mesoporous magnetic Fe3O4-NH2 by forming Schiff base compounds and the HRP@Fe3O4-NH2/hNFs were then synthesized. Under optimal conditions, 95.0% of the available HRP was immobilized on the Fe3O4-NH2/hNFs. Structural morphology and characterization of synthesized HRP@Fe3O4-NH2/hNFs were investigated. The results demonstrated that the average size of HRP@Fe3O4-NH2/hNFs was determined to be around 220 nm. The zeta-potential and magnetic saturation values of HRP@Fe3O4-NH2/hNFs were -33.58 mV and similar to 30 emu/g, respectively. Additionally, the optimum pH, optimum temperature, thermal stability, kinetic parameters, reusability, and storage stability were examined. It was observed that the optimum pH value shifted from 5.0 to pH 8.0 after immobilization, while the optimum temperature shifted from 30 to 80 degrees C. K-m values were calculated to be 15.5502 and 7.6707 mM for free HRP and the HRP@Fe3O4-NH2/hNFs, respectively, and V-max values were calculated to be 0.0701 and 0.0038 mM min(-1). The low K-m value observed after immobilization indicated that the affinity of HRP for its substrate increased. The HRP@Fe3O4-NH2/hNFs showed higher thermal stability than free HRP, and its residual activity after six usage cycles was approximately 45%. While free HRP lost all of its activity within 120 min at 65 degrees C, the HRP@Fe3O4-NH2/hNFs retained almost all of its activity during the 6 h incubation period at 80 degrees C. Most importantly, the HRP@Fe3O4-NH2/hNFs demonstrated good potential efficiency for the biodegradation of methyl orange, phenol red, and methylene blue dyes. The HRP@Fe3O4-NH2/hNFs were used for a total of 8 cycles to degrade methyl orange, phenol red, and methylene blue, and degradation of around 81, 96, and 56% was obtained in 8 h, respectively. Overall, we believe that the HRP@Fe3O4-NH2/hNFs reported in this work can be potentially used in various industrial and environmental applications, particularly for the biodegradation of recalcitrant compounds, such as textile dyes.en_US
dc.description.sponsorshipErciyes ?niversitesi [100/2000]; Inonu University and Erciyes University; Council of Higher Education PhD Scholar Biomaterial and Tissue Engineering subdivisionen_US
dc.description.sponsorshipThe research work was supported by Inonu University and Erciyes University. Busra Bakar is a 100/2000 the Council of Higher Education PhD Scholar Biomaterial and Tissue Engineering subdivision.en_US
dc.identifier.doi10.1021/acsomega.4c00703
dc.identifier.endpage24573en_US
dc.identifier.issn2470-1343
dc.identifier.issue23en_US
dc.identifier.pmid38882139en_US
dc.identifier.scopus2-s2.0-85195097441en_US
dc.identifier.scopusqualityQ1en_US
dc.identifier.startpage24558en_US
dc.identifier.urihttps://doi.org/10.1021/acsomega.4c00703
dc.identifier.urihttps://hdl.handle.net/11616/102035
dc.identifier.volume9en_US
dc.identifier.wosWOS:001235242200001en_US
dc.identifier.wosqualityN/Aen_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.indekslendigikaynakPubMeden_US
dc.language.isoenen_US
dc.publisherAmer Chemical Socen_US
dc.relation.ispartofAcs Omegaen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectSilver Nanoparticlesen_US
dc.subjectDegradationen_US
dc.subjectTitaniumen_US
dc.subjectChitosanen_US
dc.titleHorseradish Peroxidase Immobilized onto Mesoporous Magnetic Hybrid Nanoflowers for Enzymatic Decolorization of Textile Dyes: A Highly Robust Bioreactor and Boosted Enzyme Stabilityen_US
dc.typeArticleen_US

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