Enantioselective Hydrolysis of Rasemic Naproxen Methyl Ester with Sol-Gel Encapsulated Lipase in the Presence of Sporopollenin

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dc.contributor.authorYılmaz, Elif
dc.contributor.authorSezgin, Mehmet
dc.contributor.authorYılmaz, Mustafa
dc.date.accessioned2020-03-26T17:48:26Z
dc.date.available2020-03-26T17:48:26Z
dc.date.issued2010
dc.departmentSelçuk Üniversitesien_US
dc.description.abstractSporopollenin is a natural polymer obtained from Lycopodium clavatum, which is highly stable with constant chemical structure and has high resistant capacity to chemical attack. In this 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 sporopollenin and activated sporopollenin as additive. The catalytic properties of the immobilized lipases were evaluated into model reactions, i.e. the hydrolysis of p-nitrophenylpalmitate (p-NPP), and the enantioselective hydrolysis of rasemic Naproxen methyl ester that was studied in aqueous buffer solution/isooctane reaction system. The results indicated that the sporopollenin based encapsulated lipase particularly had higher conversion and enantioselectivity compared to the sol-gel free lipase. In this study, excellent enantioselectivity (E > 400) has been noticed for most lipase preparations (E = 166 for the free enzyme) with an ee value similar to 98% for S-Naproxen. Moreover, (S)-Naproxen was recovered from the reaction mixture with 98% optical purity.en_US
dc.description.sponsorshipResearch 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.en_US
dc.identifier.citationYılmaz, E., Sezgin, M., Yılmaz, M., (2010). Enantioselective Hydrolysis of Rasemic Naproxen Methyl Ester with Sol-Gel Encapsulated Lipase in the Presence of Sporopollenin. Journal of Molecular Catalysis B-Enzymatic, (62), 162-168. Doi: 10.1016/j.molcatb.2009.10.003
dc.identifier.doi10.1016/j.molcatb.2009.10.003en_US
dc.identifier.endpage168en_US
dc.identifier.issn1381-1177en_US
dc.identifier.issn1873-3158en_US
dc.identifier.scopusqualityN/Aen_US
dc.identifier.startpage162en_US
dc.identifier.urihttps://dx.doi.org/10.1016/j.molcatb.2009.10.003
dc.identifier.urihttps://hdl.handle.net/20.500.12395/24884
dc.identifier.volume62en_US
dc.identifier.wosWOS:000273913400006en_US
dc.identifier.wosqualityQ2en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.institutionauthorYılmaz, Elif
dc.institutionauthorSezgin, Mehmet
dc.institutionauthorYılmaz, Mustafa
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/openAccessen_US
dc.selcuk20240510_oaigen_US
dc.subjectCandida rugosa lipaseen_US
dc.subjectSporopolleninen_US
dc.subjectEncapsulationen_US
dc.subjectEnantioselective hydrolysisen_US
dc.subjectS-naproxenen_US
dc.titleEnantioselective Hydrolysis of Rasemic Naproxen Methyl Ester with Sol-Gel Encapsulated Lipase in the Presence of Sporopolleninen_US
dc.typeArticleen_US

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