Fabrication of a novel enzymatic electrochemical biosensor for determination of tyrosine in some food samples
- Autores
- Varmira, Kambiz; Mohammadi, Ghobad; Mahmoudi, Majid; Khodarahmi, Reza; Rashidi, Khodabakhsh; Hedayati, Mehdi; Goicoechea, Hector Casimiro; Jalalvand, Ali R.
- Año de publicación
- 2018
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- In this work, fabrication of a novel and ultrasensitive electrochemical biosensor based on immobilization oftyrosine hydroxylase onto palladium-platinum bimetallic alloy nanoparticles/chitosan-1-ethyl-3-methylimidazolium bis(trifluoromethylsulfonyl) imide/graphene-multiwalled carbon nanotubes-IL/glassycarbon electrode for determination of L-tyrosine in some high tyrosine foods including cheese, egg and yogurtwas reported. Immobilization of tyrosine hydroxylase onto the surface of the biosensor was performed bycross-linking tyrosine hydroxylase and chitosan through the addition of glutaraldehyde. Enzymatic biosensorsemploy the affinity and selectivity of catalytically active proteins towards their target molecules and here, thetyrosine hydroxylase selectively catalyzes the conversion of tyrosine to levodopa which can be oxidized atlower potentials than tyrosine. The modifications were characterized by electrochemical impedancespectroscopy, cyclic voltammetry, energy dispersive X-ray spectroscopic and scanning electron microscopy.Under optimal conditions, the biosensor detected tyrosine in concentration ranges of 0.01×10-9 to 8.0×10-9 molL-1 and 8.0×10-9 to 160.0×10-9 mol L-1 with a limit of detection of 0.009×10-9 mol L-1. The biosensor was ableto selective determination of tyrosine even in the presence of common interferents therefore, the biosensor washighly selective. The biosensor also showed good operational stability, antifouling properties, sensitivity,repeatability and reproducibility.
Fil: Varmira, Kambiz. Kermanshah University Of Medical Sciences; Irán
Fil: Mohammadi, Ghobad. Kermanshah University Of Medical Sciences; Irán
Fil: Mahmoudi, Majid. Kermanshah University Of Medical Sciences; Irán
Fil: Khodarahmi, Reza. Kermanshah University Of Medical Sciences; Irán
Fil: Rashidi, Khodabakhsh. Kermanshah University Of Medical Sciences; Irán
Fil: Hedayati, Mehdi. The Cellular And Molecular Endocrine Research Center; Irán
Fil: Goicoechea, Hector Casimiro. Universidad Nacional del Litoral; Argentina
Fil: Jalalvand, Ali R.. Kermanshah University Of Medical Sciences; Irán - Materia
-
Tyrosine
High tyrosine foods
Levodopa
Biosensor - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/89243
Ver los metadatos del registro completo
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Fabrication of a novel enzymatic electrochemical biosensor for determination of tyrosine in some food samplesVarmira, KambizMohammadi, GhobadMahmoudi, MajidKhodarahmi, RezaRashidi, KhodabakhshHedayati, MehdiGoicoechea, Hector CasimiroJalalvand, Ali R.TyrosineHigh tyrosine foodsLevodopaBiosensorhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1In this work, fabrication of a novel and ultrasensitive electrochemical biosensor based on immobilization oftyrosine hydroxylase onto palladium-platinum bimetallic alloy nanoparticles/chitosan-1-ethyl-3-methylimidazolium bis(trifluoromethylsulfonyl) imide/graphene-multiwalled carbon nanotubes-IL/glassycarbon electrode for determination of L-tyrosine in some high tyrosine foods including cheese, egg and yogurtwas reported. Immobilization of tyrosine hydroxylase onto the surface of the biosensor was performed bycross-linking tyrosine hydroxylase and chitosan through the addition of glutaraldehyde. Enzymatic biosensorsemploy the affinity and selectivity of catalytically active proteins towards their target molecules and here, thetyrosine hydroxylase selectively catalyzes the conversion of tyrosine to levodopa which can be oxidized atlower potentials than tyrosine. The modifications were characterized by electrochemical impedancespectroscopy, cyclic voltammetry, energy dispersive X-ray spectroscopic and scanning electron microscopy.Under optimal conditions, the biosensor detected tyrosine in concentration ranges of 0.01×10-9 to 8.0×10-9 molL-1 and 8.0×10-9 to 160.0×10-9 mol L-1 with a limit of detection of 0.009×10-9 mol L-1. The biosensor was ableto selective determination of tyrosine even in the presence of common interferents therefore, the biosensor washighly selective. The biosensor also showed good operational stability, antifouling properties, sensitivity,repeatability and reproducibility.Fil: Varmira, Kambiz. Kermanshah University Of Medical Sciences; IránFil: Mohammadi, Ghobad. Kermanshah University Of Medical Sciences; IránFil: Mahmoudi, Majid. Kermanshah University Of Medical Sciences; IránFil: Khodarahmi, Reza. Kermanshah University Of Medical Sciences; IránFil: Rashidi, Khodabakhsh. Kermanshah University Of Medical Sciences; IránFil: Hedayati, Mehdi. The Cellular And Molecular Endocrine Research Center; IránFil: Goicoechea, Hector Casimiro. Universidad Nacional del Litoral; ArgentinaFil: Jalalvand, Ali R.. Kermanshah University Of Medical Sciences; IránElsevier Science2018-06info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/89243Varmira, Kambiz; Mohammadi, Ghobad; Mahmoudi, Majid; Khodarahmi, Reza; Rashidi, Khodabakhsh; et al.; Fabrication of a novel enzymatic electrochemical biosensor for determination of tyrosine in some food samples; Elsevier Science; Talanta; 183; 6-2018; 1-100039-9140CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://linkinghub.elsevier.com/retrieve/pii/S0039914018301619info:eu-repo/semantics/altIdentifier/doi/10.1016/j.talanta.2018.02.053info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T14:22:19Zoai:ri.conicet.gov.ar:11336/89243instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-15 14:22:20.001CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Fabrication of a novel enzymatic electrochemical biosensor for determination of tyrosine in some food samples |
title |
Fabrication of a novel enzymatic electrochemical biosensor for determination of tyrosine in some food samples |
spellingShingle |
Fabrication of a novel enzymatic electrochemical biosensor for determination of tyrosine in some food samples Varmira, Kambiz Tyrosine High tyrosine foods Levodopa Biosensor |
title_short |
Fabrication of a novel enzymatic electrochemical biosensor for determination of tyrosine in some food samples |
title_full |
Fabrication of a novel enzymatic electrochemical biosensor for determination of tyrosine in some food samples |
title_fullStr |
Fabrication of a novel enzymatic electrochemical biosensor for determination of tyrosine in some food samples |
title_full_unstemmed |
Fabrication of a novel enzymatic electrochemical biosensor for determination of tyrosine in some food samples |
title_sort |
Fabrication of a novel enzymatic electrochemical biosensor for determination of tyrosine in some food samples |
dc.creator.none.fl_str_mv |
Varmira, Kambiz Mohammadi, Ghobad Mahmoudi, Majid Khodarahmi, Reza Rashidi, Khodabakhsh Hedayati, Mehdi Goicoechea, Hector Casimiro Jalalvand, Ali R. |
author |
Varmira, Kambiz |
author_facet |
Varmira, Kambiz Mohammadi, Ghobad Mahmoudi, Majid Khodarahmi, Reza Rashidi, Khodabakhsh Hedayati, Mehdi Goicoechea, Hector Casimiro Jalalvand, Ali R. |
author_role |
author |
author2 |
Mohammadi, Ghobad Mahmoudi, Majid Khodarahmi, Reza Rashidi, Khodabakhsh Hedayati, Mehdi Goicoechea, Hector Casimiro Jalalvand, Ali R. |
author2_role |
author author author author author author author |
dc.subject.none.fl_str_mv |
Tyrosine High tyrosine foods Levodopa Biosensor |
topic |
Tyrosine High tyrosine foods Levodopa Biosensor |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.4 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
In this work, fabrication of a novel and ultrasensitive electrochemical biosensor based on immobilization oftyrosine hydroxylase onto palladium-platinum bimetallic alloy nanoparticles/chitosan-1-ethyl-3-methylimidazolium bis(trifluoromethylsulfonyl) imide/graphene-multiwalled carbon nanotubes-IL/glassycarbon electrode for determination of L-tyrosine in some high tyrosine foods including cheese, egg and yogurtwas reported. Immobilization of tyrosine hydroxylase onto the surface of the biosensor was performed bycross-linking tyrosine hydroxylase and chitosan through the addition of glutaraldehyde. Enzymatic biosensorsemploy the affinity and selectivity of catalytically active proteins towards their target molecules and here, thetyrosine hydroxylase selectively catalyzes the conversion of tyrosine to levodopa which can be oxidized atlower potentials than tyrosine. The modifications were characterized by electrochemical impedancespectroscopy, cyclic voltammetry, energy dispersive X-ray spectroscopic and scanning electron microscopy.Under optimal conditions, the biosensor detected tyrosine in concentration ranges of 0.01×10-9 to 8.0×10-9 molL-1 and 8.0×10-9 to 160.0×10-9 mol L-1 with a limit of detection of 0.009×10-9 mol L-1. The biosensor was ableto selective determination of tyrosine even in the presence of common interferents therefore, the biosensor washighly selective. The biosensor also showed good operational stability, antifouling properties, sensitivity,repeatability and reproducibility. Fil: Varmira, Kambiz. Kermanshah University Of Medical Sciences; Irán Fil: Mohammadi, Ghobad. Kermanshah University Of Medical Sciences; Irán Fil: Mahmoudi, Majid. Kermanshah University Of Medical Sciences; Irán Fil: Khodarahmi, Reza. Kermanshah University Of Medical Sciences; Irán Fil: Rashidi, Khodabakhsh. Kermanshah University Of Medical Sciences; Irán Fil: Hedayati, Mehdi. The Cellular And Molecular Endocrine Research Center; Irán Fil: Goicoechea, Hector Casimiro. Universidad Nacional del Litoral; Argentina Fil: Jalalvand, Ali R.. Kermanshah University Of Medical Sciences; Irán |
description |
In this work, fabrication of a novel and ultrasensitive electrochemical biosensor based on immobilization oftyrosine hydroxylase onto palladium-platinum bimetallic alloy nanoparticles/chitosan-1-ethyl-3-methylimidazolium bis(trifluoromethylsulfonyl) imide/graphene-multiwalled carbon nanotubes-IL/glassycarbon electrode for determination of L-tyrosine in some high tyrosine foods including cheese, egg and yogurtwas reported. Immobilization of tyrosine hydroxylase onto the surface of the biosensor was performed bycross-linking tyrosine hydroxylase and chitosan through the addition of glutaraldehyde. Enzymatic biosensorsemploy the affinity and selectivity of catalytically active proteins towards their target molecules and here, thetyrosine hydroxylase selectively catalyzes the conversion of tyrosine to levodopa which can be oxidized atlower potentials than tyrosine. The modifications were characterized by electrochemical impedancespectroscopy, cyclic voltammetry, energy dispersive X-ray spectroscopic and scanning electron microscopy.Under optimal conditions, the biosensor detected tyrosine in concentration ranges of 0.01×10-9 to 8.0×10-9 molL-1 and 8.0×10-9 to 160.0×10-9 mol L-1 with a limit of detection of 0.009×10-9 mol L-1. The biosensor was ableto selective determination of tyrosine even in the presence of common interferents therefore, the biosensor washighly selective. The biosensor also showed good operational stability, antifouling properties, sensitivity,repeatability and reproducibility. |
publishDate |
2018 |
dc.date.none.fl_str_mv |
2018-06 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
format |
article |
status_str |
publishedVersion |
dc.identifier.none.fl_str_mv |
http://hdl.handle.net/11336/89243 Varmira, Kambiz; Mohammadi, Ghobad; Mahmoudi, Majid; Khodarahmi, Reza; Rashidi, Khodabakhsh; et al.; Fabrication of a novel enzymatic electrochemical biosensor for determination of tyrosine in some food samples; Elsevier Science; Talanta; 183; 6-2018; 1-10 0039-9140 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/89243 |
identifier_str_mv |
Varmira, Kambiz; Mohammadi, Ghobad; Mahmoudi, Majid; Khodarahmi, Reza; Rashidi, Khodabakhsh; et al.; Fabrication of a novel enzymatic electrochemical biosensor for determination of tyrosine in some food samples; Elsevier Science; Talanta; 183; 6-2018; 1-10 0039-9140 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/url/http://linkinghub.elsevier.com/retrieve/pii/S0039914018301619 info:eu-repo/semantics/altIdentifier/doi/10.1016/j.talanta.2018.02.053 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
dc.format.none.fl_str_mv |
application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
Elsevier Science |
publisher.none.fl_str_mv |
Elsevier Science |
dc.source.none.fl_str_mv |
reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
reponame_str |
CONICET Digital (CONICET) |
collection |
CONICET Digital (CONICET) |
instname_str |
Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.name.fl_str_mv |
CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.mail.fl_str_mv |
dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
_version_ |
1846082621711319040 |
score |
13.22299 |