Development of an enzyme-coated microcantilever-based biosensor for specific detection of short-chain alcohols.

Detalhes bibliográficos
Autor(a) principal: MARGARIDO, A.
Data de Publicação: 2021
Outros Autores: MANZINE, L. R., ARAUJO-MOREIRA, F. M., GONÇALVES, R. V., HERRMANN JUNIOR, P. S. de P.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice)
Texto Completo: http://www.alice.cnptia.embrapa.br/alice/handle/doc/1134534
https://doi.org/10.3390/I3S2021Dresden-10175
Resumo: This paper describes the development of a biosensor designed for the enzymatic detection of short-chain alcohols. The biorecognition element, alcohol dehydrogenase, was immobilized on selfassembled monolayers deposited on top of silicon nitride microcantilevers. The self-assembly process was performed by surface activation using 3-aminopropyltriethoxysilane, followed by glutaraldehyde and biomolecule binding. X-ray photoelectron spectroscopy and atomic force microscopy were used. The biosensor showed a lower response time and sensibility from 0.03 to 1.2 mL/L. Its selectivity was analyzed through exposure to pure and mixed volatile solvents. Sensor sensibility was higher in the presence of short-chain alcohols and practically null involving other polar or nonpolar solvents.
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spelling Development of an enzyme-coated microcantilever-based biosensor for specific detection of short-chain alcohols.BiosensorMicrocantileverBiorecognition elementThis paper describes the development of a biosensor designed for the enzymatic detection of short-chain alcohols. The biorecognition element, alcohol dehydrogenase, was immobilized on selfassembled monolayers deposited on top of silicon nitride microcantilevers. The self-assembly process was performed by surface activation using 3-aminopropyltriethoxysilane, followed by glutaraldehyde and biomolecule binding. X-ray photoelectron spectroscopy and atomic force microscopy were used. The biosensor showed a lower response time and sensibility from 0.03 to 1.2 mL/L. Its selectivity was analyzed through exposure to pure and mixed volatile solvents. Sensor sensibility was higher in the presence of short-chain alcohols and practically null involving other polar or nonpolar solvents.Presented at the 8th International Symposium on Sensor Science.PAULO SERGIO DE P HERRMANN JUNIOR, CNPDIA.MARGARIDO, A.MANZINE, L. R.ARAUJO-MOREIRA, F. M.GONÇALVES, R. V.HERRMANN JUNIOR, P. S. de P.2021-09-18T02:20:27Z2021-09-18T02:20:27Z2021-09-172021info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article1 - 5Engineering Proceedings, v. 6, n. 75 2021.2359-1757http://www.alice.cnptia.embrapa.br/alice/handle/doc/1134534https://doi.org/10.3390/I3S2021Dresden-10175enginfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice)instname:Empresa Brasileira de Pesquisa Agropecuária (Embrapa)instacron:EMBRAPA2021-09-18T02:20:35Zoai:www.alice.cnptia.embrapa.br:doc/1134534Repositório InstitucionalPUBhttps://www.alice.cnptia.embrapa.br/oai/requestopendoar:21542021-09-18T02:20:35falseRepositório InstitucionalPUBhttps://www.alice.cnptia.embrapa.br/oai/requestcg-riaa@embrapa.bropendoar:21542021-09-18T02:20:35Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice) - Empresa Brasileira de Pesquisa Agropecuária (Embrapa)false
dc.title.none.fl_str_mv Development of an enzyme-coated microcantilever-based biosensor for specific detection of short-chain alcohols.
title Development of an enzyme-coated microcantilever-based biosensor for specific detection of short-chain alcohols.
spellingShingle Development of an enzyme-coated microcantilever-based biosensor for specific detection of short-chain alcohols.
MARGARIDO, A.
Biosensor
Microcantilever
Biorecognition element
title_short Development of an enzyme-coated microcantilever-based biosensor for specific detection of short-chain alcohols.
title_full Development of an enzyme-coated microcantilever-based biosensor for specific detection of short-chain alcohols.
title_fullStr Development of an enzyme-coated microcantilever-based biosensor for specific detection of short-chain alcohols.
title_full_unstemmed Development of an enzyme-coated microcantilever-based biosensor for specific detection of short-chain alcohols.
title_sort Development of an enzyme-coated microcantilever-based biosensor for specific detection of short-chain alcohols.
author MARGARIDO, A.
author_facet MARGARIDO, A.
MANZINE, L. R.
ARAUJO-MOREIRA, F. M.
GONÇALVES, R. V.
HERRMANN JUNIOR, P. S. de P.
author_role author
author2 MANZINE, L. R.
ARAUJO-MOREIRA, F. M.
GONÇALVES, R. V.
HERRMANN JUNIOR, P. S. de P.
author2_role author
author
author
author
dc.contributor.none.fl_str_mv PAULO SERGIO DE P HERRMANN JUNIOR, CNPDIA.
dc.contributor.author.fl_str_mv MARGARIDO, A.
MANZINE, L. R.
ARAUJO-MOREIRA, F. M.
GONÇALVES, R. V.
HERRMANN JUNIOR, P. S. de P.
dc.subject.por.fl_str_mv Biosensor
Microcantilever
Biorecognition element
topic Biosensor
Microcantilever
Biorecognition element
description This paper describes the development of a biosensor designed for the enzymatic detection of short-chain alcohols. The biorecognition element, alcohol dehydrogenase, was immobilized on selfassembled monolayers deposited on top of silicon nitride microcantilevers. The self-assembly process was performed by surface activation using 3-aminopropyltriethoxysilane, followed by glutaraldehyde and biomolecule binding. X-ray photoelectron spectroscopy and atomic force microscopy were used. The biosensor showed a lower response time and sensibility from 0.03 to 1.2 mL/L. Its selectivity was analyzed through exposure to pure and mixed volatile solvents. Sensor sensibility was higher in the presence of short-chain alcohols and practically null involving other polar or nonpolar solvents.
publishDate 2021
dc.date.none.fl_str_mv 2021-09-18T02:20:27Z
2021-09-18T02:20:27Z
2021-09-17
2021
dc.type.driver.fl_str_mv info:eu-repo/semantics/publishedVersion
info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv Engineering Proceedings, v. 6, n. 75 2021.
2359-1757
http://www.alice.cnptia.embrapa.br/alice/handle/doc/1134534
https://doi.org/10.3390/I3S2021Dresden-10175
identifier_str_mv Engineering Proceedings, v. 6, n. 75 2021.
2359-1757
url http://www.alice.cnptia.embrapa.br/alice/handle/doc/1134534
https://doi.org/10.3390/I3S2021Dresden-10175
dc.language.iso.fl_str_mv eng
language eng
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 1 - 5
dc.source.none.fl_str_mv reponame:Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice)
instname:Empresa Brasileira de Pesquisa Agropecuária (Embrapa)
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instname_str Empresa Brasileira de Pesquisa Agropecuária (Embrapa)
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institution EMBRAPA
reponame_str Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice)
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repository.mail.fl_str_mv cg-riaa@embrapa.br
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