Bionanoconjugates of tyrosinase and peptide-derivatised gold nanoparticles for biosensing of phenolic compounds

Detalhes bibliográficos
Autor(a) principal: Cortez, J
Data de Publicação: 2011
Outros Autores: Vorobieva, E, Gralheira, D, Osorio, I, Soares, L, Vale, N, Pereira, E, Gomes, P, Franco, R
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: https://repositorio-aberto.up.pt/handle/10216/82098
Resumo: Bionanoconjugates of the enzyme tyrosinase (TYR) and gold nanoparticles (AuNPs) functionalised with a peptide (CALNN) were produced in solution and characterised. The formation of stable TYR-AuNP:CALNN bionanoconjugates (BNCs) was supported by a decrease of the surface charge of the BNCs as determined by zeta-potential and an increase in hydrodynamic diameter as determined by Dynamic Light Scattering (DLS). UV/Vis studies of pH-induced aggregation revealed distinct protonation patterns for the BNCs when compared with AuNP:CALNN alone, further substantiating BNC formation. Activity studies of the BNCs for the reduction of di-phenols in solution indicated that TYR not only remains active after conjugation, but interestingly its activity in the BNCs is higher than for the free enzyme. In conclusion, AuNP:CALNN can provide a suitable platform for the immobilisation of TYR, leading to BNCs with increased enzyme activity and a wider pH working range, with promising uses in electrochemical biosensors for the detection of mono- and di-phenolic compounds.
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spelling Bionanoconjugates of tyrosinase and peptide-derivatised gold nanoparticles for biosensing of phenolic compoundsEngenharia dos materiaisMaterials engineeringBionanoconjugates of the enzyme tyrosinase (TYR) and gold nanoparticles (AuNPs) functionalised with a peptide (CALNN) were produced in solution and characterised. The formation of stable TYR-AuNP:CALNN bionanoconjugates (BNCs) was supported by a decrease of the surface charge of the BNCs as determined by zeta-potential and an increase in hydrodynamic diameter as determined by Dynamic Light Scattering (DLS). UV/Vis studies of pH-induced aggregation revealed distinct protonation patterns for the BNCs when compared with AuNP:CALNN alone, further substantiating BNC formation. Activity studies of the BNCs for the reduction of di-phenols in solution indicated that TYR not only remains active after conjugation, but interestingly its activity in the BNCs is higher than for the free enzyme. In conclusion, AuNP:CALNN can provide a suitable platform for the immobilisation of TYR, leading to BNCs with increased enzyme activity and a wider pH working range, with promising uses in electrochemical biosensors for the detection of mono- and di-phenolic compounds.20112011-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttps://repositorio-aberto.up.pt/handle/10216/82098eng1388-076410.1007/s11051-010-0099-8Cortez, JVorobieva, EGralheira, DOsorio, ISoares, LVale, NPereira, EGomes, PFranco, Rinfo: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:RCAAP2024-09-27T08:23:25Zoai:repositorio-aberto.up.pt:10216/82098Portal AgregadorONGhttps://www.rcaap.pt/oai/openairemluisa.alvim@gmail.comopendoar:71602024-09-27T08:23:25Repositório 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 Bionanoconjugates of tyrosinase and peptide-derivatised gold nanoparticles for biosensing of phenolic compounds
title Bionanoconjugates of tyrosinase and peptide-derivatised gold nanoparticles for biosensing of phenolic compounds
spellingShingle Bionanoconjugates of tyrosinase and peptide-derivatised gold nanoparticles for biosensing of phenolic compounds
Cortez, J
Engenharia dos materiais
Materials engineering
title_short Bionanoconjugates of tyrosinase and peptide-derivatised gold nanoparticles for biosensing of phenolic compounds
title_full Bionanoconjugates of tyrosinase and peptide-derivatised gold nanoparticles for biosensing of phenolic compounds
title_fullStr Bionanoconjugates of tyrosinase and peptide-derivatised gold nanoparticles for biosensing of phenolic compounds
title_full_unstemmed Bionanoconjugates of tyrosinase and peptide-derivatised gold nanoparticles for biosensing of phenolic compounds
title_sort Bionanoconjugates of tyrosinase and peptide-derivatised gold nanoparticles for biosensing of phenolic compounds
author Cortez, J
author_facet Cortez, J
Vorobieva, E
Gralheira, D
Osorio, I
Soares, L
Vale, N
Pereira, E
Gomes, P
Franco, R
author_role author
author2 Vorobieva, E
Gralheira, D
Osorio, I
Soares, L
Vale, N
Pereira, E
Gomes, P
Franco, R
author2_role author
author
author
author
author
author
author
author
dc.contributor.author.fl_str_mv Cortez, J
Vorobieva, E
Gralheira, D
Osorio, I
Soares, L
Vale, N
Pereira, E
Gomes, P
Franco, R
dc.subject.por.fl_str_mv Engenharia dos materiais
Materials engineering
topic Engenharia dos materiais
Materials engineering
description Bionanoconjugates of the enzyme tyrosinase (TYR) and gold nanoparticles (AuNPs) functionalised with a peptide (CALNN) were produced in solution and characterised. The formation of stable TYR-AuNP:CALNN bionanoconjugates (BNCs) was supported by a decrease of the surface charge of the BNCs as determined by zeta-potential and an increase in hydrodynamic diameter as determined by Dynamic Light Scattering (DLS). UV/Vis studies of pH-induced aggregation revealed distinct protonation patterns for the BNCs when compared with AuNP:CALNN alone, further substantiating BNC formation. Activity studies of the BNCs for the reduction of di-phenols in solution indicated that TYR not only remains active after conjugation, but interestingly its activity in the BNCs is higher than for the free enzyme. In conclusion, AuNP:CALNN can provide a suitable platform for the immobilisation of TYR, leading to BNCs with increased enzyme activity and a wider pH working range, with promising uses in electrochemical biosensors for the detection of mono- and di-phenolic compounds.
publishDate 2011
dc.date.none.fl_str_mv 2011
2011-01-01T00:00:00Z
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://repositorio-aberto.up.pt/handle/10216/82098
url https://repositorio-aberto.up.pt/handle/10216/82098
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 1388-0764
10.1007/s11051-010-0099-8
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 mluisa.alvim@gmail.com
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