Development of an enzyme-coated microcantilever-based biosensor for specific detection of short-chain alcohols.
Autor(a) principal: | |
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Data de Publicação: | 2021 |
Outros Autores: | , , , |
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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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) instacron:EMBRAPA |
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Empresa Brasileira de Pesquisa Agropecuária (Embrapa) |
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EMBRAPA |
institution |
EMBRAPA |
reponame_str |
Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice) |
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Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice) |
repository.name.fl_str_mv |
Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice) - Empresa Brasileira de Pesquisa Agropecuária (Embrapa) |
repository.mail.fl_str_mv |
cg-riaa@embrapa.br |
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1794503509739044864 |