Investigation on electrochemical behavior of peroxidase enzyme in the presence of hydrogen peroxide and 5-aminosalicylic acid

Detalhes bibliográficos
Autor(a) principal: Uliana, C. V. [UNESP]
Data de Publicação: 2008
Outros Autores: Riccardi, C. S. [UNESP], Yamanaka, H. [UNESP]
Tipo de documento: Artigo
Idioma: por
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://dx.doi.org/10.26850/1678-4618EQJ.V33.1.2008.P57-62
http://hdl.handle.net/11449/222606
Resumo: The electrochemical behavior of the enzyme peroxidase (HRP) was investigated using the hydrogen peroxide as enzymatic substrate and the 5-aminosalicylic acid (5-ASA) as mediator of electrons on graphite electrodes. Several parameters were optimized, namely, the applied potential to the amperometric technique fixed in -0.125V, the 0.1 mol L-1phosphate-citrate buffer at pH 5.0 as supporting electrolyte and the proportion between the 5-ASA and H2O2in 1:7, among others. It was observed the catalysis of the oxidation reaction of the H2O2in the presence of the enzyme HRP and 5- ASA. The oxidation product was reduced in the electrode surface, evidencing a significant increase in the intensity of the cathodic current.
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spelling Investigation on electrochemical behavior of peroxidase enzyme in the presence of hydrogen peroxide and 5-aminosalicylic acidEstudo do comportamento eletroquímico da enzima peroxidase na presença de peróxido de hidrogênio e ácido 5-aminossalicílico5-aminosalicilic acidGraphite electrodeHydrogen peroxidePeroxidaseThe electrochemical behavior of the enzyme peroxidase (HRP) was investigated using the hydrogen peroxide as enzymatic substrate and the 5-aminosalicylic acid (5-ASA) as mediator of electrons on graphite electrodes. Several parameters were optimized, namely, the applied potential to the amperometric technique fixed in -0.125V, the 0.1 mol L-1phosphate-citrate buffer at pH 5.0 as supporting electrolyte and the proportion between the 5-ASA and H2O2in 1:7, among others. It was observed the catalysis of the oxidation reaction of the H2O2in the presence of the enzyme HRP and 5- ASA. The oxidation product was reduced in the electrode surface, evidencing a significant increase in the intensity of the cathodic current.Universidade Estadual Paulista Instituto de Química Campus de Araraquara, CP 355, SPUniversidade Estadual Paulista Instituto de Química Campus de Araraquara, CP 355, SPUniversidade Estadual Paulista (UNESP)Uliana, C. V. [UNESP]Riccardi, C. S. [UNESP]Yamanaka, H. [UNESP]2022-04-28T19:45:46Z2022-04-28T19:45:46Z2008-01-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article57-62http://dx.doi.org/10.26850/1678-4618EQJ.V33.1.2008.P57-62Ecletica Quimica, v. 33, n. 1, p. 57-62, 2008.1678-46180100-4670http://hdl.handle.net/11449/22260610.26850/1678-4618EQJ.V33.1.2008.P57-622-s2.0-85116795873Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPporEcletica Quimicainfo:eu-repo/semantics/openAccess2022-04-28T19:45:46Zoai:repositorio.unesp.br:11449/222606Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462022-04-28T19:45:46Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Investigation on electrochemical behavior of peroxidase enzyme in the presence of hydrogen peroxide and 5-aminosalicylic acid
Estudo do comportamento eletroquímico da enzima peroxidase na presença de peróxido de hidrogênio e ácido 5-aminossalicílico
title Investigation on electrochemical behavior of peroxidase enzyme in the presence of hydrogen peroxide and 5-aminosalicylic acid
spellingShingle Investigation on electrochemical behavior of peroxidase enzyme in the presence of hydrogen peroxide and 5-aminosalicylic acid
Uliana, C. V. [UNESP]
5-aminosalicilic acid
Graphite electrode
Hydrogen peroxide
Peroxidase
title_short Investigation on electrochemical behavior of peroxidase enzyme in the presence of hydrogen peroxide and 5-aminosalicylic acid
title_full Investigation on electrochemical behavior of peroxidase enzyme in the presence of hydrogen peroxide and 5-aminosalicylic acid
title_fullStr Investigation on electrochemical behavior of peroxidase enzyme in the presence of hydrogen peroxide and 5-aminosalicylic acid
title_full_unstemmed Investigation on electrochemical behavior of peroxidase enzyme in the presence of hydrogen peroxide and 5-aminosalicylic acid
title_sort Investigation on electrochemical behavior of peroxidase enzyme in the presence of hydrogen peroxide and 5-aminosalicylic acid
author Uliana, C. V. [UNESP]
author_facet Uliana, C. V. [UNESP]
Riccardi, C. S. [UNESP]
Yamanaka, H. [UNESP]
author_role author
author2 Riccardi, C. S. [UNESP]
Yamanaka, H. [UNESP]
author2_role author
author
dc.contributor.none.fl_str_mv Universidade Estadual Paulista (UNESP)
dc.contributor.author.fl_str_mv Uliana, C. V. [UNESP]
Riccardi, C. S. [UNESP]
Yamanaka, H. [UNESP]
dc.subject.por.fl_str_mv 5-aminosalicilic acid
Graphite electrode
Hydrogen peroxide
Peroxidase
topic 5-aminosalicilic acid
Graphite electrode
Hydrogen peroxide
Peroxidase
description The electrochemical behavior of the enzyme peroxidase (HRP) was investigated using the hydrogen peroxide as enzymatic substrate and the 5-aminosalicylic acid (5-ASA) as mediator of electrons on graphite electrodes. Several parameters were optimized, namely, the applied potential to the amperometric technique fixed in -0.125V, the 0.1 mol L-1phosphate-citrate buffer at pH 5.0 as supporting electrolyte and the proportion between the 5-ASA and H2O2in 1:7, among others. It was observed the catalysis of the oxidation reaction of the H2O2in the presence of the enzyme HRP and 5- ASA. The oxidation product was reduced in the electrode surface, evidencing a significant increase in the intensity of the cathodic current.
publishDate 2008
dc.date.none.fl_str_mv 2008-01-01
2022-04-28T19:45:46Z
2022-04-28T19:45:46Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://dx.doi.org/10.26850/1678-4618EQJ.V33.1.2008.P57-62
Ecletica Quimica, v. 33, n. 1, p. 57-62, 2008.
1678-4618
0100-4670
http://hdl.handle.net/11449/222606
10.26850/1678-4618EQJ.V33.1.2008.P57-62
2-s2.0-85116795873
url http://dx.doi.org/10.26850/1678-4618EQJ.V33.1.2008.P57-62
http://hdl.handle.net/11449/222606
identifier_str_mv Ecletica Quimica, v. 33, n. 1, p. 57-62, 2008.
1678-4618
0100-4670
10.26850/1678-4618EQJ.V33.1.2008.P57-62
2-s2.0-85116795873
dc.language.iso.fl_str_mv por
language por
dc.relation.none.fl_str_mv Ecletica Quimica
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 57-62
dc.source.none.fl_str_mv Scopus
reponame:Repositório Institucional da UNESP
instname:Universidade Estadual Paulista (UNESP)
instacron:UNESP
instname_str Universidade Estadual Paulista (UNESP)
instacron_str UNESP
institution UNESP
reponame_str Repositório Institucional da UNESP
collection Repositório Institucional da UNESP
repository.name.fl_str_mv Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)
repository.mail.fl_str_mv
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