High enzymatic activity preservation of malate dehydrogenase immobilized in a Langmuir-Blodgett film and its electrochemical biosensor application for malic acid detection

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dc.authorid0000-0003-3667-6902en_US
dc.contributor.authorGur, Bahri
dc.contributor.authorIsik, Mesut
dc.contributor.authorKiransan, Kader Dagci
dc.contributor.authorAlanyalioglu, Murat
dc.contributor.authorBeydemir, Şükrü
dc.contributor.authorMeral, Kadem
dc.date.accessioned2021-03-20T20:14:57Z
dc.date.available2021-03-20T20:14:57Z
dc.date.issued2016
dc.departmentBTÜ, Mühendislik ve Doğa Bilimleri Fakültesi, Kimya Bölümüen_US
dc.description.abstractIn this study, malate dehydrogenase (MDH) enzyme was immobilized on a cation octadecylamine (ODA(+)) monolayer at the air-water interface. Pressure-area (pi-A) isotherm studies confirmed that the ODA-MDH system formed a stable monolayer at the air-water interface. The as-prepared MDH-ODA monolayer was transferred onto an indium tin oxide coated glass substrate (ITO) by the Langmuir-Blodgett (LB) method as an MDH-ODA/ITO LB film and characterized using FT-IR, SEM and UV-Vis absorption spectroscopy. The catalytic activity of the enzyme immobilized electrode (MDH-ODA/ITO) was assayed by sensing malic acid (MA) in the range of 10.0-50.0 mM. The high and preserved enzymatic activity of MDH in in vitro media was explored by following the absorbance (A(340 nm)) of nicotinamide adenine dinucleotide (NADH). Moreover, the highly sensitive electrochemical biosensor behavior of the MDA-ODA/ITO electrode for MA detection was displayed by cyclic voltammetry studies. The electrochemical studies revealed that a voltammetric current from the MDA-ODA/ITO electrode was obtained, while the ODA/ITO electrode did not show this current response. The MDA-ODA/ITO demonstrated sensitive electrochemical sensor ability for quantification of MA in both standard solutions and real samples.en_US
dc.description.sponsorshipAtaturk University Scientific Research Project CouncilAtaturk University [2015/23]en_US
dc.description.sponsorshipThe financial support by "Ataturk University Scientific Research Project Council (Project No. 2015/23)" is gratefully acknowledged.en_US
dc.identifier.doi10.1039/c6ra17465een_US
dc.identifier.endpage79797en_US
dc.identifier.issn2046-2069
dc.identifier.issue83en_US
dc.identifier.scopusqualityQ2en_US
dc.identifier.startpage79792en_US
dc.identifier.urihttp://doi.org/10.1039/c6ra17465e
dc.identifier.urihttps://hdl.handle.net/20.500.12885/1129
dc.identifier.volume6en_US
dc.identifier.wosWOS:000382539600057en_US
dc.identifier.wosqualityQ2en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.institutionauthorBeydemir, Şükrü
dc.language.isoenen_US
dc.publisherRoyal Soc Chemistryen_US
dc.relation.ispartofRsc Advancesen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subject[No Keywords]en_US
dc.titleHigh enzymatic activity preservation of malate dehydrogenase immobilized in a Langmuir-Blodgett film and its electrochemical biosensor application for malic acid detectionen_US
dc.typeArticleen_US

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