Lipid-matrix effects on tyrosinase immobilization in Langmuir and Langmuir-Blodgett films
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 UNESP |
Texto Completo: | http://dx.doi.org/10.1590/0001-3765202120200019 http://hdl.handle.net/11449/207496 |
Resumo: | The immobilization of the enzyme tyrosinase (Tyr) in lipid matrices can be explored to produce biosensors for detecting polyphenols, which is relevant for the food industry. Herein, we shall demonstrate the importance of the lipid composition to immobilize the enzyme tyrosinase in Langmuir-Blodgett (LB) films. Tyr could be incorporated into Langmuir monolayers of arachidic acid (AA), 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) and 1,2-dipalmitoyl-sn-glycero-3-phospho-(1’-rac-glycerol) (sodium salt) (DPPG), having as the main effect an expansion in the monolayers. Results from polarization-modulated infrared reflection-absorption spectroscopy (PM-IRRAS) pointed to electrostatic interactions between the charged residues of Try and the lipid headgroups, in addition to changes in the order of lipid chains. The interaction between Tyr and DPPC in Langmuir monolayers can be correlated with the superior performance of DPPC/Tyr LB films used as biosensors to detect catechol by cyclic voltammetry. The molecular-level interactions assessed via PM-IRRAS are therefore believed to drive an immobilization process for Tyr in the lipid LB matrix and may serve as a general criterion to identify matrices that preserve enzyme activity. |
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Lipid-matrix effects on tyrosinase immobilization in Langmuir and Langmuir-Blodgett filmsCyclic voltammetryLangmuir-BlodgettLipid-matrixPM-IRRASTyrosinaseThe immobilization of the enzyme tyrosinase (Tyr) in lipid matrices can be explored to produce biosensors for detecting polyphenols, which is relevant for the food industry. Herein, we shall demonstrate the importance of the lipid composition to immobilize the enzyme tyrosinase in Langmuir-Blodgett (LB) films. Tyr could be incorporated into Langmuir monolayers of arachidic acid (AA), 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) and 1,2-dipalmitoyl-sn-glycero-3-phospho-(1’-rac-glycerol) (sodium salt) (DPPG), having as the main effect an expansion in the monolayers. Results from polarization-modulated infrared reflection-absorption spectroscopy (PM-IRRAS) pointed to electrostatic interactions between the charged residues of Try and the lipid headgroups, in addition to changes in the order of lipid chains. The interaction between Tyr and DPPC in Langmuir monolayers can be correlated with the superior performance of DPPC/Tyr LB films used as biosensors to detect catechol by cyclic voltammetry. The molecular-level interactions assessed via PM-IRRAS are therefore believed to drive an immobilization process for Tyr in the lipid LB matrix and may serve as a general criterion to identify matrices that preserve enzyme activity.Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Instituto Nacional de Ciência e Tecnologia em Eletrônica OrgânicaFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Universidade Estadual Paulista/UNESP Faculdade de Ciências e Tecnologia Departamento de Física, Rua Roberto Símonsen, 305, Centro Educacional, Caixa Postal 467Universidade Estadual Paulista/UNESP Faculdade de Ciências e Letras Departamento de Biotecnologia, Av. Dom Antônio, 2100, Parque Universitário, Caixa Postal 65Universidade de São Paulo/USP Instituto de Física de São Carlos, Av. Trabalhador São Carlense, 400, Parque Arnold Schimidt, Caixa Postal 369Universidade Estadual Paulista/UNESP Faculdade de Ciências e Tecnologia Departamento de Física, Rua Roberto Símonsen, 305, Centro Educacional, Caixa Postal 467Universidade Estadual Paulista/UNESP Faculdade de Ciências e Letras Departamento de Biotecnologia, Av. Dom Antônio, 2100, Parque Universitário, Caixa Postal 65FAPESP: 2013/14262-7FAPESP: 2017/15019-0Universidade Estadual Paulista (Unesp)Universidade de São Paulo (USP)Pereira, Matheus S. [UNESP]Maximino, Mateus D. [UNESP]Martin, Cibely S. [UNESP]Aoki, Pedro H. B. [UNESP]Oliveira, Osvaldo N.Alessio, Priscila [UNESP]2021-06-25T10:56:13Z2021-06-25T10:56:13Z2021-01-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://dx.doi.org/10.1590/0001-3765202120200019Anais da Academia Brasileira de Ciencias, v. 93, n. 1, 2021.1678-26900001-3765http://hdl.handle.net/11449/20749610.1590/0001-3765202120200019S0001-376520210001012212-s2.0-85103003443S0001-37652021000101221.pdfScopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengAnais da Academia Brasileira de Cienciasinfo:eu-repo/semantics/openAccess2023-11-27T06:14:55Zoai:repositorio.unesp.br:11449/207496Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462023-11-27T06:14:55Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Lipid-matrix effects on tyrosinase immobilization in Langmuir and Langmuir-Blodgett films |
title |
Lipid-matrix effects on tyrosinase immobilization in Langmuir and Langmuir-Blodgett films |
spellingShingle |
Lipid-matrix effects on tyrosinase immobilization in Langmuir and Langmuir-Blodgett films Pereira, Matheus S. [UNESP] Cyclic voltammetry Langmuir-Blodgett Lipid-matrix PM-IRRAS Tyrosinase |
title_short |
Lipid-matrix effects on tyrosinase immobilization in Langmuir and Langmuir-Blodgett films |
title_full |
Lipid-matrix effects on tyrosinase immobilization in Langmuir and Langmuir-Blodgett films |
title_fullStr |
Lipid-matrix effects on tyrosinase immobilization in Langmuir and Langmuir-Blodgett films |
title_full_unstemmed |
Lipid-matrix effects on tyrosinase immobilization in Langmuir and Langmuir-Blodgett films |
title_sort |
Lipid-matrix effects on tyrosinase immobilization in Langmuir and Langmuir-Blodgett films |
author |
Pereira, Matheus S. [UNESP] |
author_facet |
Pereira, Matheus S. [UNESP] Maximino, Mateus D. [UNESP] Martin, Cibely S. [UNESP] Aoki, Pedro H. B. [UNESP] Oliveira, Osvaldo N. Alessio, Priscila [UNESP] |
author_role |
author |
author2 |
Maximino, Mateus D. [UNESP] Martin, Cibely S. [UNESP] Aoki, Pedro H. B. [UNESP] Oliveira, Osvaldo N. Alessio, Priscila [UNESP] |
author2_role |
author author author author author |
dc.contributor.none.fl_str_mv |
Universidade Estadual Paulista (Unesp) Universidade de São Paulo (USP) |
dc.contributor.author.fl_str_mv |
Pereira, Matheus S. [UNESP] Maximino, Mateus D. [UNESP] Martin, Cibely S. [UNESP] Aoki, Pedro H. B. [UNESP] Oliveira, Osvaldo N. Alessio, Priscila [UNESP] |
dc.subject.por.fl_str_mv |
Cyclic voltammetry Langmuir-Blodgett Lipid-matrix PM-IRRAS Tyrosinase |
topic |
Cyclic voltammetry Langmuir-Blodgett Lipid-matrix PM-IRRAS Tyrosinase |
description |
The immobilization of the enzyme tyrosinase (Tyr) in lipid matrices can be explored to produce biosensors for detecting polyphenols, which is relevant for the food industry. Herein, we shall demonstrate the importance of the lipid composition to immobilize the enzyme tyrosinase in Langmuir-Blodgett (LB) films. Tyr could be incorporated into Langmuir monolayers of arachidic acid (AA), 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) and 1,2-dipalmitoyl-sn-glycero-3-phospho-(1’-rac-glycerol) (sodium salt) (DPPG), having as the main effect an expansion in the monolayers. Results from polarization-modulated infrared reflection-absorption spectroscopy (PM-IRRAS) pointed to electrostatic interactions between the charged residues of Try and the lipid headgroups, in addition to changes in the order of lipid chains. The interaction between Tyr and DPPC in Langmuir monolayers can be correlated with the superior performance of DPPC/Tyr LB films used as biosensors to detect catechol by cyclic voltammetry. The molecular-level interactions assessed via PM-IRRAS are therefore believed to drive an immobilization process for Tyr in the lipid LB matrix and may serve as a general criterion to identify matrices that preserve enzyme activity. |
publishDate |
2021 |
dc.date.none.fl_str_mv |
2021-06-25T10:56:13Z 2021-06-25T10:56:13Z 2021-01-01 |
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/10.1590/0001-3765202120200019 Anais da Academia Brasileira de Ciencias, v. 93, n. 1, 2021. 1678-2690 0001-3765 http://hdl.handle.net/11449/207496 10.1590/0001-3765202120200019 S0001-37652021000101221 2-s2.0-85103003443 S0001-37652021000101221.pdf |
url |
http://dx.doi.org/10.1590/0001-3765202120200019 http://hdl.handle.net/11449/207496 |
identifier_str_mv |
Anais da Academia Brasileira de Ciencias, v. 93, n. 1, 2021. 1678-2690 0001-3765 10.1590/0001-3765202120200019 S0001-37652021000101221 2-s2.0-85103003443 S0001-37652021000101221.pdf |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Anais da Academia Brasileira de Ciencias |
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 |
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 |
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1797789834042933248 |