Magnetically responsive PA6 microparticles with immobilized laccase show high catalytic efficiency in the enzymatic treatment of catechol

Detalhes bibliográficos
Autor(a) principal: Dencheva, Nadya Vasileva
Data de Publicação: 2021
Outros Autores: Oliveira, Sandra Cristina Gomes, Braz, Joana Filipa Barros, Getya, Dariya, Malfois, Marc, Denchev, Z., Gitsov, Ivan
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/1822/72508
Resumo: Herewith we report the first attempt towards non-covalent immobilization of <i>Trametes versicolor</i> laccase on neat and magnetically responsive highly porous polyamide 6 (PA6) microparticles and their application for catechol oxidation. Four polyamide supports, namely neat PA6 and such carrying Fe, phosphate-coated Fe and Fe<sub>3</sub>O<sub>4</sub> cores were synthesized in suspension by activated anionic ring-opening polymerization (AAROP) of ε-caprolactam (ECL). Enzyme adsorption efficiency up to 92% was achieved in the immobilization process. All empty supports and PA6 laccase complexes were characterized by spectral and synchrotron WAXS/SAXS analyses. The activity of the immobilized laccase was evaluated using 2,2’-Azino-bis-(3- ethylbenzothiazoline-6-sulfonic acid (ABTS) and compared to the native enzyme. The PA6 laccase conjugates displayed up to 105% relative activity at room temperature, pH 4, 40 °C and 20 mM ionic strength (citrate buffer). The kinetic parameters of the ABTS oxidation were also determined. The reusability of the immobilized laccase-conjugates was proven for five consecutive oxidation cycles of catechol.
id RCAP_7d5ae077e86958527f1681d76642b082
oai_identifier_str oai:repositorium.sdum.uminho.pt:1822/72508
network_acronym_str RCAP
network_name_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository_id_str 7160
spelling Magnetically responsive PA6 microparticles with immobilized laccase show high catalytic efficiency in the enzymatic treatment of catecholLaccasePolyamide 6Enzyme immobilizationMagnetic enzyme supportsCatechol oxidationScience & TechnologyHerewith we report the first attempt towards non-covalent immobilization of <i>Trametes versicolor</i> laccase on neat and magnetically responsive highly porous polyamide 6 (PA6) microparticles and their application for catechol oxidation. Four polyamide supports, namely neat PA6 and such carrying Fe, phosphate-coated Fe and Fe<sub>3</sub>O<sub>4</sub> cores were synthesized in suspension by activated anionic ring-opening polymerization (AAROP) of ε-caprolactam (ECL). Enzyme adsorption efficiency up to 92% was achieved in the immobilization process. All empty supports and PA6 laccase complexes were characterized by spectral and synchrotron WAXS/SAXS analyses. The activity of the immobilized laccase was evaluated using 2,2’-Azino-bis-(3- ethylbenzothiazoline-6-sulfonic acid (ABTS) and compared to the native enzyme. The PA6 laccase conjugates displayed up to 105% relative activity at room temperature, pH 4, 40 °C and 20 mM ionic strength (citrate buffer). The kinetic parameters of the ABTS oxidation were also determined. The reusability of the immobilized laccase-conjugates was proven for five consecutive oxidation cycles of catechol.The authors gratefully acknowledge the financial support of the project TSSiPRO NORTE01-0145-FEDER-000015, supported by the regional operation program NORTE2020, under the Portugal 2020 Partnership Agreement, through the European Regional Development Fund, as well as the support by National Funds through Fundação para a Ciência e Tecnologia (FCT), project UID/CTM/50025/2019. D.G. and I.G. wish to thank the Research Foundation of the State of New York—Networks of Excellence and the McIntyre-Stennis program of the US Department of Agriculture for partial funding. N.D. is also grateful for the personal program-contract CTTI-51/18-IPC.Multidisciplinary Digital Publishing Institute (MDPI)Universidade do MinhoDencheva, Nadya VasilevaOliveira, Sandra Cristina GomesBraz, Joana Filipa BarrosGetya, DariyaMalfois, MarcDenchev, Z.Gitsov, Ivan2021-02-112021-02-11T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/1822/72508engDencheva, N.; Oliveira, S.; Braz, J.; Getya, D.; Malfois, M.; Denchev, Z.; Gitsov, I. Magnetically Responsive PA6 Microparticles with Immobilized Laccase Show High Catalytic Efficiency in the Enzymatic Treatment of Catechol. Catalysts 2021, 11, 239. https://doi.org/10.3390/catal110202392073-434410.3390/catal11020239https://www.mdpi.com/2073-4344/11/2/239info: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:RCAAP2023-07-21T11:58:37Zoai:repositorium.sdum.uminho.pt:1822/72508Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T18:48:21.807953Repositório 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 Magnetically responsive PA6 microparticles with immobilized laccase show high catalytic efficiency in the enzymatic treatment of catechol
title Magnetically responsive PA6 microparticles with immobilized laccase show high catalytic efficiency in the enzymatic treatment of catechol
spellingShingle Magnetically responsive PA6 microparticles with immobilized laccase show high catalytic efficiency in the enzymatic treatment of catechol
Dencheva, Nadya Vasileva
Laccase
Polyamide 6
Enzyme immobilization
Magnetic enzyme supports
Catechol oxidation
Science & Technology
title_short Magnetically responsive PA6 microparticles with immobilized laccase show high catalytic efficiency in the enzymatic treatment of catechol
title_full Magnetically responsive PA6 microparticles with immobilized laccase show high catalytic efficiency in the enzymatic treatment of catechol
title_fullStr Magnetically responsive PA6 microparticles with immobilized laccase show high catalytic efficiency in the enzymatic treatment of catechol
title_full_unstemmed Magnetically responsive PA6 microparticles with immobilized laccase show high catalytic efficiency in the enzymatic treatment of catechol
title_sort Magnetically responsive PA6 microparticles with immobilized laccase show high catalytic efficiency in the enzymatic treatment of catechol
author Dencheva, Nadya Vasileva
author_facet Dencheva, Nadya Vasileva
Oliveira, Sandra Cristina Gomes
Braz, Joana Filipa Barros
Getya, Dariya
Malfois, Marc
Denchev, Z.
Gitsov, Ivan
author_role author
author2 Oliveira, Sandra Cristina Gomes
Braz, Joana Filipa Barros
Getya, Dariya
Malfois, Marc
Denchev, Z.
Gitsov, Ivan
author2_role author
author
author
author
author
author
dc.contributor.none.fl_str_mv Universidade do Minho
dc.contributor.author.fl_str_mv Dencheva, Nadya Vasileva
Oliveira, Sandra Cristina Gomes
Braz, Joana Filipa Barros
Getya, Dariya
Malfois, Marc
Denchev, Z.
Gitsov, Ivan
dc.subject.por.fl_str_mv Laccase
Polyamide 6
Enzyme immobilization
Magnetic enzyme supports
Catechol oxidation
Science & Technology
topic Laccase
Polyamide 6
Enzyme immobilization
Magnetic enzyme supports
Catechol oxidation
Science & Technology
description Herewith we report the first attempt towards non-covalent immobilization of <i>Trametes versicolor</i> laccase on neat and magnetically responsive highly porous polyamide 6 (PA6) microparticles and their application for catechol oxidation. Four polyamide supports, namely neat PA6 and such carrying Fe, phosphate-coated Fe and Fe<sub>3</sub>O<sub>4</sub> cores were synthesized in suspension by activated anionic ring-opening polymerization (AAROP) of ε-caprolactam (ECL). Enzyme adsorption efficiency up to 92% was achieved in the immobilization process. All empty supports and PA6 laccase complexes were characterized by spectral and synchrotron WAXS/SAXS analyses. The activity of the immobilized laccase was evaluated using 2,2’-Azino-bis-(3- ethylbenzothiazoline-6-sulfonic acid (ABTS) and compared to the native enzyme. The PA6 laccase conjugates displayed up to 105% relative activity at room temperature, pH 4, 40 °C and 20 mM ionic strength (citrate buffer). The kinetic parameters of the ABTS oxidation were also determined. The reusability of the immobilized laccase-conjugates was proven for five consecutive oxidation cycles of catechol.
publishDate 2021
dc.date.none.fl_str_mv 2021-02-11
2021-02-11T00:00:00Z
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/1822/72508
url http://hdl.handle.net/1822/72508
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Dencheva, N.; Oliveira, S.; Braz, J.; Getya, D.; Malfois, M.; Denchev, Z.; Gitsov, I. Magnetically Responsive PA6 Microparticles with Immobilized Laccase Show High Catalytic Efficiency in the Enzymatic Treatment of Catechol. Catalysts 2021, 11, 239. https://doi.org/10.3390/catal11020239
2073-4344
10.3390/catal11020239
https://www.mdpi.com/2073-4344/11/2/239
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 Multidisciplinary Digital Publishing Institute (MDPI)
publisher.none.fl_str_mv Multidisciplinary Digital Publishing Institute (MDPI)
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
_version_ 1799132244253605888

Registros relacionados