Laccase activation in deep eutectic solvents

Detalhes bibliográficos
Autor(a) principal: Toledo, Mariah L.
Data de Publicação: 2019
Outros Autores: Pereira, Matheus M., Freire, Mara G., Silva, João P. A., Coutinho, João A. P., Tavares, Ana P. M.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10773/26344
Resumo: The research on alternative solvents and co-solvents is a relevant aspect when envisioning the improvement of biocatalytic reactions. Among these solvents and co-solvents, deep eutectic solvents (DES) may be considered as customizable new reaction media for biocatalysis. Accordingly, in this work, sixteen DES aqueous solutions, as well as of the individual DES components at the same conditions have been investigated in laccase-catalyzed reactions. Cholinium- and betaine-based DES formed with polyols at different molar ratio and concentrations were evaluated. The results reported show that in presence of most DES the laccase activity is preserved and, with a particular DES, enhanced up to 200%. Molecular docking studies demonstrated that while most DES components establish hydrogen-bonds with the enzyme amino acids, those that establish stronger interactions with the enzyme (expressed by absolute values of docking affinity energies) lead to an enhanced laccase activity. Finally, the laccase stability was evaluated in additional tests under extreme storage temperatures (60 ºC and -80 ºC). Although no significant protection to high temperatures was afforded by DES, an enhanced laccase activity when stored at low temperatures was found, at least up to 20 days. Combining experimental results and molecular docking this work shows that DES can be designed as co-solvents to improve biocatalytic reactions.
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spelling Laccase activation in deep eutectic solventsDeep eutectic solventsEnzyme activityGreen solventsLaccaseMolecular dockingThe research on alternative solvents and co-solvents is a relevant aspect when envisioning the improvement of biocatalytic reactions. Among these solvents and co-solvents, deep eutectic solvents (DES) may be considered as customizable new reaction media for biocatalysis. Accordingly, in this work, sixteen DES aqueous solutions, as well as of the individual DES components at the same conditions have been investigated in laccase-catalyzed reactions. Cholinium- and betaine-based DES formed with polyols at different molar ratio and concentrations were evaluated. The results reported show that in presence of most DES the laccase activity is preserved and, with a particular DES, enhanced up to 200%. Molecular docking studies demonstrated that while most DES components establish hydrogen-bonds with the enzyme amino acids, those that establish stronger interactions with the enzyme (expressed by absolute values of docking affinity energies) lead to an enhanced laccase activity. Finally, the laccase stability was evaluated in additional tests under extreme storage temperatures (60 ºC and -80 ºC). Although no significant protection to high temperatures was afforded by DES, an enhanced laccase activity when stored at low temperatures was found, at least up to 20 days. Combining experimental results and molecular docking this work shows that DES can be designed as co-solvents to improve biocatalytic reactions.ACS Sustainable Chemistry & Engineering2020-04-01T00:00:00Z2019-05-31T00:00:00Z2019-05-31info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10773/26344eng10.1021/acssuschemeng.9b02179Toledo, Mariah L.Pereira, Matheus M.Freire, Mara G.Silva, João P. A.Coutinho, João A. P.Tavares, Ana P. M.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:RCAAP2024-02-22T11:51:02Zoai:ria.ua.pt:10773/26344Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T02:59:22.200500Repositório 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 Laccase activation in deep eutectic solvents
title Laccase activation in deep eutectic solvents
spellingShingle Laccase activation in deep eutectic solvents
Toledo, Mariah L.
Deep eutectic solvents
Enzyme activity
Green solvents
Laccase
Molecular docking
title_short Laccase activation in deep eutectic solvents
title_full Laccase activation in deep eutectic solvents
title_fullStr Laccase activation in deep eutectic solvents
title_full_unstemmed Laccase activation in deep eutectic solvents
title_sort Laccase activation in deep eutectic solvents
author Toledo, Mariah L.
author_facet Toledo, Mariah L.
Pereira, Matheus M.
Freire, Mara G.
Silva, João P. A.
Coutinho, João A. P.
Tavares, Ana P. M.
author_role author
author2 Pereira, Matheus M.
Freire, Mara G.
Silva, João P. A.
Coutinho, João A. P.
Tavares, Ana P. M.
author2_role author
author
author
author
author
dc.contributor.author.fl_str_mv Toledo, Mariah L.
Pereira, Matheus M.
Freire, Mara G.
Silva, João P. A.
Coutinho, João A. P.
Tavares, Ana P. M.
dc.subject.por.fl_str_mv Deep eutectic solvents
Enzyme activity
Green solvents
Laccase
Molecular docking
topic Deep eutectic solvents
Enzyme activity
Green solvents
Laccase
Molecular docking
description The research on alternative solvents and co-solvents is a relevant aspect when envisioning the improvement of biocatalytic reactions. Among these solvents and co-solvents, deep eutectic solvents (DES) may be considered as customizable new reaction media for biocatalysis. Accordingly, in this work, sixteen DES aqueous solutions, as well as of the individual DES components at the same conditions have been investigated in laccase-catalyzed reactions. Cholinium- and betaine-based DES formed with polyols at different molar ratio and concentrations were evaluated. The results reported show that in presence of most DES the laccase activity is preserved and, with a particular DES, enhanced up to 200%. Molecular docking studies demonstrated that while most DES components establish hydrogen-bonds with the enzyme amino acids, those that establish stronger interactions with the enzyme (expressed by absolute values of docking affinity energies) lead to an enhanced laccase activity. Finally, the laccase stability was evaluated in additional tests under extreme storage temperatures (60 ºC and -80 ºC). Although no significant protection to high temperatures was afforded by DES, an enhanced laccase activity when stored at low temperatures was found, at least up to 20 days. Combining experimental results and molecular docking this work shows that DES can be designed as co-solvents to improve biocatalytic reactions.
publishDate 2019
dc.date.none.fl_str_mv 2019-05-31T00:00:00Z
2019-05-31
2020-04-01T00:00:00Z
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dc.identifier.uri.fl_str_mv http://hdl.handle.net/10773/26344
url http://hdl.handle.net/10773/26344
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1021/acssuschemeng.9b02179
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dc.publisher.none.fl_str_mv ACS Sustainable Chemistry & Engineering
publisher.none.fl_str_mv ACS Sustainable Chemistry & Engineering
dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
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