Enhanced thermostability of the immobilized thermoalkalophilic esterase onto magnetic-cornstarch nanoparticle

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dc.authorwosidSURMELI, YUSUF/AAR-3671-2020
dc.contributor.authorÖz, Yasin
dc.contributor.authorSürmeli, Yusuf
dc.contributor.authorŞanlı Mohamed, Gülşah
dc.date.accessioned2022-05-11T14:07:12Z
dc.date.available2022-05-11T14:07:12Z
dc.date.issued2021
dc.departmentFakülteler, Ziraat Fakültesi, Tarımsal Biyoteknoloji Bölümü
dc.description.abstractThe immobilization of the biocatalysts onto magnetic nanoparticles has been extensively applied as the external magnetic field facilitates the enzyme recovery from the reaction mixture. In the present study, glutaraldehyde-modified magnetite-cornstarch nanoparticles (MCNs) were successfully synthesized, elaborately characterized by ZetaSizer and surface-enhanced Raman spectroscopy, and used for the immobilization of a thermoalkalophilic esterase from Geobacillus sp. The optimal immobilization conditions were obtained at 65 degrees C, 2:3 molar ratios of Fe2+:Fe3+, and 1 g cornstarch resulted in approximately 90 nm magnetic particles in size. Also, immobilization yield and immobilization efficiency of the esterase were found as 74% and 82%, respectively. Scanning electron microscopy micrographs showed that MCNs were uniform, spherical in shape, and well dispersed and esterase immobilized MCNs displayed similar morphology as free MCNs. The maximum activity of free and immobilized esterase was obtained at 65 degrees C and pH 9. Immobilization onto glutaraldehyde-modified MCNs significantly enhanced the esterase thermostability. Additionally, the immobilized esterase kept its residual activity of 75% after three sequential cycles, suggesting that it has favorable operational stability.
dc.identifier.doi10.1002/bab.2213
dc.identifier.issn0885-4513
dc.identifier.issn1470-8744
dc.identifier.pmid34151468
dc.identifier.scopus2-s2.0-85136513398
dc.identifier.scopusqualityQ3
dc.identifier.urihttps://doi.org/10.1002/bab.2213
dc.identifier.urihttps://hdl.handle.net/20.500.11776/5010
dc.identifier.wosWOS:000667267800001
dc.identifier.wosqualityQ3
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.indekslendigikaynakPubMed
dc.institutionauthorSürmeli, Yusuf
dc.language.isoen
dc.publisherWiley
dc.relation.ispartofBiotechnology And Applied Biochemistry
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectGeobacillus sp
dc.subjectimmobilization
dc.subjectmagnetic nanoparticles
dc.subjectthermoalkalophilic esterase
dc.subjectCandida-Rugosa
dc.subjectCarboxyl Esterases
dc.subjectLipase
dc.subjectEnzymes
dc.subjectMicrospheres
dc.subjectStability
dc.subjectBiodiesel
dc.subjectAlcohol
dc.subjectOxidase
dc.subjectLaccase
dc.titleEnhanced thermostability of the immobilized thermoalkalophilic esterase onto magnetic-cornstarch nanoparticle
dc.typeArticle

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