Exploring PEGylated and immobilized laccases for catechol polymerization

Detalhes bibliográficos
Autor(a) principal: Jing Su
Data de Publicação: 2018
Outros Autores: Noro, Jennifer Martins, Fu, Jiajia, Wang, Qiang, Silva, Carla, Cavaco-Paulo, Artur
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/1822/55732
Resumo: Laccases have been reported for their ability to eliminate hazardous phenolic compounds by oxidative polymerization. The exploitation of the oxidative behavior of different laccase forms, namely free/native, free/PEGylated, immobilized/native and immobilized/PEGylated, was assessed in this study. We found that PEGylated and immobilized laccase forms have differentiated catalytic behavior revealing distinct conversion rates and differentiated poly(catechol) chains, as confirmed by UV--Visible spectroscopy, by the total content of OH groups and by MALDI-TOF spectroscopy. The synergy underlying on the immobilized/PEGylated enzyme forms reveal to be responsible for the highest conversion rates and for the longer polymers produced.
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spelling Exploring PEGylated and immobilized laccases for catechol polymerizationLaccasePolyethylene glycolImmobilizationPEGylationPolymerizationScience & TechnologyLaccases have been reported for their ability to eliminate hazardous phenolic compounds by oxidative polymerization. The exploitation of the oxidative behavior of different laccase forms, namely free/native, free/PEGylated, immobilized/native and immobilized/PEGylated, was assessed in this study. We found that PEGylated and immobilized laccase forms have differentiated catalytic behavior revealing distinct conversion rates and differentiated poly(catechol) chains, as confirmed by UV--Visible spectroscopy, by the total content of OH groups and by MALDI-TOF spectroscopy. The synergy underlying on the immobilized/PEGylated enzyme forms reveal to be responsible for the highest conversion rates and for the longer polymers produced.This study was supported by Chinese Government Scholarship under China Scholarship Council (No. 201606790036) and Chinese Foundation Key projects of governmental cooperation in international scientific and technological innovation (No. 2016 YFE0115700) and by the Portuguese Foundation for Science and Technology (FCT) under the scope of the strategic funding of UID/BIO/04469/2013 unit and COMPETE 2020 (POCI‑01‑0145‑FEDER‑006684) and BioTecNorte operation (NORTE‑01‑0145‑FEDER‑000004) funded by European Regional Development Fund under the scope of Norte2020—Programa Oper‑ acional Regional do Norte. Jennifer Noro also thanks to FCT‑ Fundação para a Ciência e a Tecnologia for funding her scholarship (SFRH/BD/121673/2016). Carla Silva is an investigator FCT (SFRH/IF/00186/2015).info:eu-repo/semantics/publishedVersionSpringerUniversidade do MinhoJing SuNoro, Jennifer MartinsFu, JiajiaWang, QiangSilva, CarlaCavaco-Paulo, Artur2018-122018-12-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/1822/55732engJing Su; Jennifer Noro; Fu, Jiajia; Wang, Qiang; Silva, Carla; Cavaco-Paulo, Artur, Exploring PEGylated and immobilized laccases for catechol polymerization. AMB Express, 8(1), 134, 2018. doi: 10.1186/s13568-018-0665-52191-08552191-085510.1186/s13568-018-0665-5http://amb-express.springeropen.com/info: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:RCAAP2024-05-11T04:22:32Zoai:repositorium.sdum.uminho.pt:1822/55732Portal AgregadorONGhttps://www.rcaap.pt/oai/openairemluisa.alvim@gmail.comopendoar:71602024-05-11T04:22:32Repositório 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 Exploring PEGylated and immobilized laccases for catechol polymerization
title Exploring PEGylated and immobilized laccases for catechol polymerization
spellingShingle Exploring PEGylated and immobilized laccases for catechol polymerization
Jing Su
Laccase
Polyethylene glycol
Immobilization
PEGylation
Polymerization
Science & Technology
title_short Exploring PEGylated and immobilized laccases for catechol polymerization
title_full Exploring PEGylated and immobilized laccases for catechol polymerization
title_fullStr Exploring PEGylated and immobilized laccases for catechol polymerization
title_full_unstemmed Exploring PEGylated and immobilized laccases for catechol polymerization
title_sort Exploring PEGylated and immobilized laccases for catechol polymerization
author Jing Su
author_facet Jing Su
Noro, Jennifer Martins
Fu, Jiajia
Wang, Qiang
Silva, Carla
Cavaco-Paulo, Artur
author_role author
author2 Noro, Jennifer Martins
Fu, Jiajia
Wang, Qiang
Silva, Carla
Cavaco-Paulo, Artur
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv Universidade do Minho
dc.contributor.author.fl_str_mv Jing Su
Noro, Jennifer Martins
Fu, Jiajia
Wang, Qiang
Silva, Carla
Cavaco-Paulo, Artur
dc.subject.por.fl_str_mv Laccase
Polyethylene glycol
Immobilization
PEGylation
Polymerization
Science & Technology
topic Laccase
Polyethylene glycol
Immobilization
PEGylation
Polymerization
Science & Technology
description Laccases have been reported for their ability to eliminate hazardous phenolic compounds by oxidative polymerization. The exploitation of the oxidative behavior of different laccase forms, namely free/native, free/PEGylated, immobilized/native and immobilized/PEGylated, was assessed in this study. We found that PEGylated and immobilized laccase forms have differentiated catalytic behavior revealing distinct conversion rates and differentiated poly(catechol) chains, as confirmed by UV--Visible spectroscopy, by the total content of OH groups and by MALDI-TOF spectroscopy. The synergy underlying on the immobilized/PEGylated enzyme forms reveal to be responsible for the highest conversion rates and for the longer polymers produced.
publishDate 2018
dc.date.none.fl_str_mv 2018-12
2018-12-01T00:00:00Z
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 http://hdl.handle.net/1822/55732
url http://hdl.handle.net/1822/55732
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Jing Su; Jennifer Noro; Fu, Jiajia; Wang, Qiang; Silva, Carla; Cavaco-Paulo, Artur, Exploring PEGylated and immobilized laccases for catechol polymerization. AMB Express, 8(1), 134, 2018. doi: 10.1186/s13568-018-0665-5
2191-0855
2191-0855
10.1186/s13568-018-0665-5
http://amb-express.springeropen.com/
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.publisher.none.fl_str_mv Springer
publisher.none.fl_str_mv Springer
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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