Achieving Enzyme Stability Using a Simple Fabrication Procedure: The Alcohol Dehydrogenase Example

Detalhes bibliográficos
Autor(a) principal: Ribau, I.
Data de Publicação: 2018
Outros Autores: Fortunato, E.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: https://doi.org/10.17265/2328-2150/2018.02
Resumo: The use of screen-printing biosensors has been updated in this article as a tool to analyze the electron transfer process involving redox proteins or enzymes. The aim of this research was to fabricate a simple apparatus which allowed the use of the enzymes (in the solid state) to maintain their stability. To prove this concept an enzyme in the solid state was mixed with the carbon ink and this mixture was used to print the working electrode. We choose as proving the alcohol dehydrogenase. The first reason is because it metabolizes the alcohol, which can be present in biological samples of blood, saliva and urine and also in the beverage; the second is that this enzyme is still a challenge to electrochemistry due to having lower stability in sensors. The results show that in this device the enzyme was active and stable during all the experiments and in the experimental conditions that could catalyze the ethanol to acetaldehyde. These devices have the advantage of being disposable, cheap and are easy to fabricate. And also, they do not need expensive tools to be fabricated, they only need 2 μL of electrolyte or sample, and they need lower amounts of enzyme to permit electrochemical studies.
id RCAP_63597a1ad71d0ba90b2a31a2219558c2
oai_identifier_str oai:run.unl.pt:10362/68441
network_acronym_str RCAP
network_name_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository_id_str 7160
spelling Achieving Enzyme Stability Using a Simple Fabrication Procedure: The Alcohol Dehydrogenase ExamplePaper biosensorDisposableAlcohol dehydrogenaseMultiple useThe use of screen-printing biosensors has been updated in this article as a tool to analyze the electron transfer process involving redox proteins or enzymes. The aim of this research was to fabricate a simple apparatus which allowed the use of the enzymes (in the solid state) to maintain their stability. To prove this concept an enzyme in the solid state was mixed with the carbon ink and this mixture was used to print the working electrode. We choose as proving the alcohol dehydrogenase. The first reason is because it metabolizes the alcohol, which can be present in biological samples of blood, saliva and urine and also in the beverage; the second is that this enzyme is still a challenge to electrochemistry due to having lower stability in sensors. The results show that in this device the enzyme was active and stable during all the experiments and in the experimental conditions that could catalyze the ethanol to acetaldehyde. These devices have the advantage of being disposable, cheap and are easy to fabricate. And also, they do not need expensive tools to be fabricated, they only need 2 μL of electrolyte or sample, and they need lower amounts of enzyme to permit electrochemical studies.DCM - Departamento de Ciência dos MateriaisRUNRibau, I.Fortunato, E.2019-05-02T22:19:00Z2018-02-282018-02-28T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttps://doi.org/10.17265/2328-2150/2018.02eng2328-2150PURE: 12744409http://www.davidpublisher.org/index.php/Home/Article/index?id=34499.htmlhttps://doi.org/10.17265/2328-2150/2018.02info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2024-03-11T04:32:20Zoai:run.unl.pt:10362/68441Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:34:46.395316Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv Achieving Enzyme Stability Using a Simple Fabrication Procedure: The Alcohol Dehydrogenase Example
title Achieving Enzyme Stability Using a Simple Fabrication Procedure: The Alcohol Dehydrogenase Example
spellingShingle Achieving Enzyme Stability Using a Simple Fabrication Procedure: The Alcohol Dehydrogenase Example
Ribau, I.
Paper biosensor
Disposable
Alcohol dehydrogenase
Multiple use
title_short Achieving Enzyme Stability Using a Simple Fabrication Procedure: The Alcohol Dehydrogenase Example
title_full Achieving Enzyme Stability Using a Simple Fabrication Procedure: The Alcohol Dehydrogenase Example
title_fullStr Achieving Enzyme Stability Using a Simple Fabrication Procedure: The Alcohol Dehydrogenase Example
title_full_unstemmed Achieving Enzyme Stability Using a Simple Fabrication Procedure: The Alcohol Dehydrogenase Example
title_sort Achieving Enzyme Stability Using a Simple Fabrication Procedure: The Alcohol Dehydrogenase Example
author Ribau, I.
author_facet Ribau, I.
Fortunato, E.
author_role author
author2 Fortunato, E.
author2_role author
dc.contributor.none.fl_str_mv DCM - Departamento de Ciência dos Materiais
RUN
dc.contributor.author.fl_str_mv Ribau, I.
Fortunato, E.
dc.subject.por.fl_str_mv Paper biosensor
Disposable
Alcohol dehydrogenase
Multiple use
topic Paper biosensor
Disposable
Alcohol dehydrogenase
Multiple use
description The use of screen-printing biosensors has been updated in this article as a tool to analyze the electron transfer process involving redox proteins or enzymes. The aim of this research was to fabricate a simple apparatus which allowed the use of the enzymes (in the solid state) to maintain their stability. To prove this concept an enzyme in the solid state was mixed with the carbon ink and this mixture was used to print the working electrode. We choose as proving the alcohol dehydrogenase. The first reason is because it metabolizes the alcohol, which can be present in biological samples of blood, saliva and urine and also in the beverage; the second is that this enzyme is still a challenge to electrochemistry due to having lower stability in sensors. The results show that in this device the enzyme was active and stable during all the experiments and in the experimental conditions that could catalyze the ethanol to acetaldehyde. These devices have the advantage of being disposable, cheap and are easy to fabricate. And also, they do not need expensive tools to be fabricated, they only need 2 μL of electrolyte or sample, and they need lower amounts of enzyme to permit electrochemical studies.
publishDate 2018
dc.date.none.fl_str_mv 2018-02-28
2018-02-28T00:00:00Z
2019-05-02T22:19:00Z
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 https://doi.org/10.17265/2328-2150/2018.02
url https://doi.org/10.17265/2328-2150/2018.02
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 2328-2150
PURE: 12744409
http://www.davidpublisher.org/index.php/Home/Article/index?id=34499.html
https://doi.org/10.17265/2328-2150/2018.02
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron:RCAAP
instname_str Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron_str RCAAP
institution RCAAP
reponame_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
collection Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository.name.fl_str_mv Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
repository.mail.fl_str_mv
_version_ 1799137969847664640