Immobilization of Candida rugosa lipase on magnetic sol-gel composite supports for enzymatic resolution of (R,S)-Naproxen methyl ester

Basit Öğe Kaydı
dc.contributor.authorYılmaz, Elif
dc.contributor.authorSezgin, Mehmet
dc.contributor.authorYılmaz, Mustafa
dc.date.accessioned2020-03-26T18:14:51Z
dc.date.available2020-03-26T18:14:51Z
dc.date.issued2011
dc.departmentSelçuk Üniversitesien_US
dc.description.abstractIn the present study, the Candida rugosa lipase (CRL) was encapsulated within a chemically inert sol-gel support prepared by polycondensation with tetraethoxysilane (TEOS) and octyltriethoxysilane (OTES) in the presence and absence of magnetic Fe3O4 nanoparticles or sporopollenin with Fe3O4 as additive. The catalytic properties of the immobilized lipases were evaluated through model reactions, i.e. the hydrolysis of p-nitrophenylpalmitate (p-NPP), and the enantioselective hydrolysis of racemic Naproxen methyl ester that was studied in aqueous buffer solution/isooctane reaction system. The results indicate that the sporopollenin based encapsulated lipase (Fe3O4-Spo-E) particularly has higher conversion and enantioselectivity compared to the encapsulated lipase without supports (lipase-enc). It has also been noticed that the sporopollenin based encapsulated lipase has excellent enantioselectivity (E = > 400) as compared to the free enzyme (E = 166) with an ee value of similar to 98% for S-Naproxen. (C) 2010 Elsevier B.V. All rights reserved.en_US
dc.description.sponsorshipScientific Research Foundation of Selcuk University, Konya, TurkeySelcuk University [08101024]en_US
dc.description.sponsorshipWe thank the Scientific Research Foundation of Selcuk University, Konya, Turkey (BAP-grant number: 08101024) for financial support of this work. We also would like to thank Dr. Shahabuddin Memon for his assistance in editing this paper.en_US
dc.identifier.doi10.1016/j.molcatb.2010.12.007en_US
dc.identifier.endpage41en_US
dc.identifier.issn1381-1177en_US
dc.identifier.issn1873-3158en_US
dc.identifier.issue01.02.2020en_US
dc.identifier.scopusqualityN/Aen_US
dc.identifier.startpage35en_US
dc.identifier.urihttps://dx.doi.org/10.1016/j.molcatb.2010.12.007
dc.identifier.urihttps://hdl.handle.net/20.500.12395/26544
dc.identifier.volume69en_US
dc.identifier.wosWOS:000287981500006en_US
dc.identifier.wosqualityQ2en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.language.isoenen_US
dc.publisherELSEVIERen_US
dc.relation.ispartofJOURNAL OF MOLECULAR CATALYSIS B-ENZYMATICen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.selcuk20240510_oaigen_US
dc.subjectCandida rugosa lipaseen_US
dc.subjectMagnetic nanoparticlesen_US
dc.subjectImmobilizationen_US
dc.subjectEnantioselective hydrolysisen_US
dc.subjectSol-gelen_US
dc.subjectS-Naproxenen_US
dc.titleImmobilization of Candida rugosa lipase on magnetic sol-gel composite supports for enzymatic resolution of (R,S)-Naproxen methyl esteren_US
dc.typeArticleen_US

Dosyalar

Koleksiyon

WoS İndeksli Yayınlar Koleksiyonu
Scopus İndeksli Yayınlar Koleksiyonu