Investigation on electrochemical behavior of peroxidase enzyme in the presence of hydrogen peroxide and 5-aminosalicylic acid
Autor(a) principal: | |
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Data de Publicação: | 2008 |
Outros Autores: | , |
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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Repositório Institucional da UNESP |
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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 |
|
_version_ |
1792962012034105344 |