Covalent Immobilization of Candida rugosa Lipase on Epichlorohydrin-Coated Magnetite Nanoparticles: Enantioselective Hydrolysis Studies of Some Racemic Esters and HPLC Analysis

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dc.contributor.authorCakmak, Resit
dc.contributor.authorTopal, Giray
dc.contributor.authorCinar, Ercan
dc.date.accessioned2024-04-24T16:02:36Z
dc.date.available2024-04-24T16:02:36Z
dc.date.issued2020
dc.departmentDicle Üniversitesien_US
dc.description.abstractIn this study, a new biocatalyst was prepared by immobilizing Candida rugosa lipase epichlorohydrin-functionalized onto the surface of the nanoparticles. Magnetite nanoparticles were obtained by chemical co-precipitation method of Fe2+ and Fe3+, and then the prepared uncoated and coated nanoparticles were characterized by XRD, FT-IR and TGA. Lipase was covalently attached to activated nanoparticles. The catalytic properties of free and immobilized lipases were determined. It was found that the optimum temperature for free and immobilized lipases was 30 degrees C and 35 degrees C, respectively. The optimum pH values were found to be 7.0 and 8 for free and immobilized lipases, respectively. Immobilized lipase was found to retain significant activity even after the seventh use. In the final section of the study, optically pure compounds were obtained by carrying out the enantioselective hydrolysis studies of racemic esters by using immobilized lipase. Enantiomeric excesses of the products in the enantioselective hydrolysis of racemic ibuprofen and naproxen methyl ester and racemic butyl mandelate were determined to be 94.93, 77.30 and 68.15, respectively.en_US
dc.description.sponsorshipTUBITAK [:113Z773]; Dicle University [:14-ZEF-16]en_US
dc.description.sponsorshipThis research was supported by TUBITAK (grant number:113Z773) and Dicle University (grant number:14-ZEF-16).en_US
dc.identifier.doi10.1007/s12010-020-03274-1
dc.identifier.endpage1431en_US
dc.identifier.issn0273-2289
dc.identifier.issn1559-0291
dc.identifier.issue4en_US
dc.identifier.pmid32103473
dc.identifier.scopus2-s2.0-85081023575
dc.identifier.scopusqualityQ2
dc.identifier.startpage1411en_US
dc.identifier.urihttps://doi.org/10.1007/s12010-020-03274-1
dc.identifier.urihttps://hdl.handle.net/11468/14854
dc.identifier.volume191en_US
dc.identifier.wosWOS:000516817800004
dc.identifier.wosqualityQ3
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.indekslendigikaynakPubMed
dc.language.isoenen_US
dc.publisherSpringeren_US
dc.relation.ispartofApplied Biochemistry and Biotechnology
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectFe3o4en_US
dc.subjectLipaseen_US
dc.subjectImmobilizationen_US
dc.subjectBiocatalysisen_US
dc.subjectRacemic Estersen_US
dc.subjectHydrolysisen_US
dc.subjectHplcen_US
dc.titleCovalent Immobilization of Candida rugosa Lipase on Epichlorohydrin-Coated Magnetite Nanoparticles: Enantioselective Hydrolysis Studies of Some Racemic Esters and HPLC Analysisen_US
dc.titleCovalent Immobilization of Candida rugosa Lipase on Epichlorohydrin-Coated Magnetite Nanoparticles: Enantioselective Hydrolysis Studies of Some Racemic Esters and HPLC Analysis
dc.typeArticleen_US

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