Kinetic resolution of racemic naproxen methyl ester by magnetic and non-magnetic cross-linked lipase aggregates

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dc.authoridSALGIN, SEMA/0000-0001-6354-3553
dc.contributor.authorSalgin, Sema
dc.contributor.authorCakal, Mustafa
dc.contributor.authorSalgin, Ugur
dc.date.accessioned2024-10-26T18:02:41Z
dc.date.available2024-10-26T18:02:41Z
dc.date.issued2020
dc.departmentSivas Cumhuriyet Üniversitesi
dc.description.abstractIn this study, the non-magnetic and the magnetic cross-linked enzyme aggregates (CLEAs) from Candida rugosa lipase were synthesized to catalyze the kinetic resolution reaction of naproxen methyl ester (NME). Magnetic iron oxide nanoparticles (MIONPs) were produced through co-precipitation method and their surfaces were modified by silanization reaction. The MIONPs were used as a platform to synthesize the magnetic CLEAs (M-CLEAs). The biocatalysts and MIONPs synthesized were characterized by FTIR spectroscopy and SEM analysis. The kinetic resolution of racemic NME was studied in aqueous buffer solution/isooctane biphasic system to compare the performance of M-CLEAs and CLEAs. The effects of reaction parameters such as temperature, pH, stirring rate on the enantiomeric excess of the substrate (ee(s)%) were investigated in a batch reactor system. The activity recovery of CRL enzyme in CLEAs was higher than M-CLEAs. Compared with M-CLEAs, CLEAs biocatalysts had previously reached ee(s)% values. Although both biocatalysts showed similar cavity structure from SEM analysis, the lower performance of M-CLEAs may be due to the different microenvironments of M-CLEAs from CLEAs. However, the reusability performance of M-CLEAs was higher than that of CLEAs. The optimal reaction conditions for M-CLEAs and CLEAs were found to be 37 degrees C, pH 7.5, and 300 rpm.
dc.description.sponsorshipScientific and Technological Research Council of Turkey (TUBITAK) [113Z170]; Cumhuriyet University Scientific Research Projects (CUBAP) [M-591]
dc.description.sponsorshipThis research was supported by the Scientific and Technological Research Council of Turkey (TUBITAK) [Grant No. 113Z170] and Cumhuriyet University Scientific Research Projects (CUBAP) [Grant No. M-591].
dc.identifier.doi10.1080/10826068.2019.1679178
dc.identifier.endpage155
dc.identifier.issn1082-6068
dc.identifier.issn1532-2297
dc.identifier.issue2
dc.identifier.pmid31647366
dc.identifier.scopus2-s2.0-85074462152
dc.identifier.scopusqualityQ3
dc.identifier.startpage148
dc.identifier.urihttps://doi.org/10.1080/10826068.2019.1679178
dc.identifier.urihttps://hdl.handle.net/20.500.12418/28274
dc.identifier.volume50
dc.identifier.wosWOS:000492310300001
dc.identifier.wosqualityQ4
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.indekslendigikaynakPubMed
dc.language.isoen
dc.publisherTaylor & Francis Inc
dc.relation.ispartofPreparative Biochemistry & Biotechnology
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectCLEAs
dc.subjectkinetic resolution
dc.subjectlipase
dc.subjectmagnetic CLEAs
dc.subjectnaproxen methyl ester
dc.titleKinetic resolution of racemic naproxen methyl ester by magnetic and non-magnetic cross-linked lipase aggregates
dc.typeArticle

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