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Spectrometric and voltammetric analysis of urease - nickel nanoelectrode as an electrochemical sensor

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dc.title Spectrometric and voltammetric analysis of urease - nickel nanoelectrode as an electrochemical sensor en
dc.contributor.author Hubálek, Jaromír
dc.contributor.author Hradecký, Jan
dc.contributor.author Adam, Vojtěch
dc.contributor.author Kryštofová, Olga
dc.contributor.author Húska, Dalibor
dc.contributor.author Masařík, Michal
dc.contributor.author Trnková, Libuše
dc.contributor.author Horna, Aleš
dc.contributor.author Klosová, Kateřina
dc.contributor.author Adámek, Martin
dc.contributor.author Zehnálek, Josef
dc.contributor.author Kizek, René
dc.relation.ispartof Sensors
dc.identifier.issn 1424-8220 Scopus Sources, Sherpa/RoMEO, JCR
dc.date.issued 2007-07
utb.relation.volume 7
utb.relation.issue 7
dc.citation.spage 1238
dc.citation.epage 1255
dc.type article
dc.language.iso en
dc.publisher MDPI AG en
dc.identifier.doi 10.3390/s7071238
dc.relation.uri http://www.mdpi.com/1424-8220/7/7/1238/
dc.subject urease en
dc.subject electrochemical methods en
dc.subject nanotechnology en
dc.subject nanotube en
dc.subject nickel electrode en
dc.subject hanging mercury drop electrode en
dc.subject spectrometry en
dc.description.abstract Urease is the enzyme catalyzing the hydrolysis of urea into carbon dioxide and ammonia. This enzyme is substrate- specific, which means that the enzyme catalyzes the hydrolysis of urea only. This feature is a basic diagnostic criterion used in the determination of many bacteria species. Most of the methods utilized for detection of urease are based on analysis of its enzyme activity - the hydrolysis of urea. The aim of this work was to detect urease indirectly by spectrometric method and directly by voltammetric methods. As spectrometric method we used is called indophenol assay. The sensitivity of detection itself is not sufficient to analyse the samples without pre- concentration steps. Therefore we utilized adsorptive transfer stripping technique coupled with differential pulse voltammetry to detect urease. The influence of accumulation time, pH of supporting electrolyte and concentration of urease on the enzyme peak height was investigated. Under the optimized experimental conditions ( 0.2 M acetate buffer pH 4.6 and accumulation time of 120 s) the detection limit of urease evaluated as 3 S/ N was 200 ng/ ml. The activity of urease enzyme depends on the presence of nickel. Thus the influence of nickel( II) ions on electrochemical response of the enzyme was studied. Based on the results obtained the interaction of nickel( II) ions and urease can be determined using electrochemical methods. Therefore we prepared Ni nanoelectrodes to measure urease. The Ni nanoelectrodes was analysed after the template dissolution by scanning electron microscopy. The results shown vertically aligned Ni nanopillars almost covered the electrode surface, whereas the defect places are minor and insignificant in comparison with total electrode surface. We were able to not only detect urease itself but also to distinguish its native and denatured form. en
utb.faculty Faculty of Technology
dc.identifier.uri http://hdl.handle.net/10563/1002106
utb.identifier.obdid 43865402
utb.identifier.scopus 2-s2.0-34547645009
utb.identifier.wok 000248319500013
utb.source j-wok
dc.date.accessioned 2011-08-16T15:06:29Z
dc.date.available 2011-08-16T15:06:29Z
dc.rights Attribution 3.0 International
dc.rights.uri http://creativecommons.org/licenses/by/3.0/
dc.rights.access openAccess
utb.contributor.internalauthor Horna, Aleš
utb.fulltext.affiliation Jaromir Hubalek 1, Jan Hradecky 2, Vojtech Adam 2,3, Olga Krystofova 2, Dalibor Huska 2, Michal Masarik 4, Libuse Trnkova 5, Ales Horna 6, Katerina Klosova 1, Martin Adamek 1, Josef Zehnalek 2 and Rene Kizek 1,* 1 Department of Microelectronics, Faculty of Electrical Engineering and Communication, Brno University of Technology, Udolni 53, CZ-602 00 Brno, Czech Republic 2 Department of Chemistry and Biochemistry, and 3 Department of Animal Nutrition and Forage Production, Faculty of Agronomy, Mendel University of Agriculture and Forestry, Zemedelska 1, CZ613 00 Brno, Czech Republic 4 Department of Pathological Physiology, Faculty of Medicine, Masaryk University, Komenskeho namesti 2, CZ-662 43 Brno, Czech Republic 5 Department of Chemistry, Faculty of Science, Masaryk University, Kotlarska 2, CZ-611 37 Brno, Czech Republic 6 Department of Food Engineering, Faculty of Technology, Tomas Bata University, T.G. Masaryka 275, CZ-762 72 Zlin, Czech Republic * Author to whom correspondence should be addressed; E-mail: kizek@sci.muni.cz
utb.fulltext.dates Received: 3 July 2007 / Accepted: 13 July 2007 / Published: 16 July 2007
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utb.fulltext.sponsorship This work was supported from the grant of the Grant Agency of Academy of Sciences of the Czech Republic No. GAAV IAA401990701, and GAAV 1QS201710508, and from the Czech Ministry of Education within the framework of Research Plan MSM 0021630503 and IGA MZLU 5/2007.
utb.fulltext.projects GAAV IAA401990701
utb.fulltext.projects GAAV 1QS201710508
utb.fulltext.projects MSM 0021630503
utb.fulltext.projects IGA MZLU 5/2007
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