Improving the activity of horseradish peroxidase in betaine-based natural deep eutectic systems

Detalhes bibliográficos
Autor(a) principal: Meneses, Liane
Data de Publicação: 2023
Outros Autores: Gajardo-Parra, Nicolás F., Cea-Klapp, Esteban, Garrido, José Matías, Held, Christoph, Duarte, Ana Rita, Paiva, Alexandre
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10362/162706
Resumo: The authors thank the funding from the Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) under Germany's Excellence Strategy - EXC 2033 - 390677874 - RESOLV. Nicolás Gajardo's work was supported by the German Academic Exchange Service (DAAD) under the Graduate School Scholarship Programme, 2020 (57516591). E. C.-K. acknowledges the scholarship from ANID, Chile. This research was partially supported by the supercomputing infrastructure of the Southern GPU Cluster - Fondequip EQM150134. Publisher Copyright: © 2023 RSC.
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spelling Improving the activity of horseradish peroxidase in betaine-based natural deep eutectic systemsChemistry (miscellaneous)Analytical ChemistryElectrochemistryOrganic ChemistryThe authors thank the funding from the Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) under Germany's Excellence Strategy - EXC 2033 - 390677874 - RESOLV. Nicolás Gajardo's work was supported by the German Academic Exchange Service (DAAD) under the Graduate School Scholarship Programme, 2020 (57516591). E. C.-K. acknowledges the scholarship from ANID, Chile. This research was partially supported by the supercomputing infrastructure of the Southern GPU Cluster - Fondequip EQM150134. Publisher Copyright: © 2023 RSC.In this work, the activity of horseradish peroxidase (HRP) in betaine-based natural deep eutectic systems (NADESs) was measured and studied by molecular simulations. Focus was laid on enzymatic activity in the NADESs under thermal stress as well as under the influence of water. Furthermore, the structure of HRP under these different conditions was measured by circular dichroism (CD). As a result, HRP remains enzymatically active in all NADESs upon incubation for 24 h at 37 °C and 60 °C and after 4 h at 80 °C, especially when incubated in a NADES composed of betaine, trehalose, glycerol, and water, in a molar ratio of 2 : 1 : 3 : 5. The CD studies have shown that high activity is obtained in the systems that promoted higher α-helix contents. The molecular simulations showed that using a NADES instead of buffer solvent reduces HRP flexibility, and we found that enzymatic activity correlates with Gibbs energy of solvation of HRP. Finally, hydrophobic hydration interactions govern the stabilization mechanism of the HRP folded state as shown by a drastic enzymatic activity drop upon 5 wt% water addition using a betaine: glycerol NADES as solvent.DQ - Departamento de QuímicaLAQV@REQUIMTERUNMeneses, LianeGajardo-Parra, Nicolás F.Cea-Klapp, EstebanGarrido, José MatíasHeld, ChristophDuarte, Ana RitaPaiva, Alexandre2024-01-24T16:59:50Z2023-04-112023-04-11T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article12application/pdfhttp://hdl.handle.net/10362/162706engPURE: 81993740https://doi.org/10.1039/d2su00127finfo: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:RCAAP2024-03-18T01:43:49Zoai:run.unl.pt:10362/162706Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:59:01.968031Repositório 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 Improving the activity of horseradish peroxidase in betaine-based natural deep eutectic systems
title Improving the activity of horseradish peroxidase in betaine-based natural deep eutectic systems
spellingShingle Improving the activity of horseradish peroxidase in betaine-based natural deep eutectic systems
Meneses, Liane
Chemistry (miscellaneous)
Analytical Chemistry
Electrochemistry
Organic Chemistry
title_short Improving the activity of horseradish peroxidase in betaine-based natural deep eutectic systems
title_full Improving the activity of horseradish peroxidase in betaine-based natural deep eutectic systems
title_fullStr Improving the activity of horseradish peroxidase in betaine-based natural deep eutectic systems
title_full_unstemmed Improving the activity of horseradish peroxidase in betaine-based natural deep eutectic systems
title_sort Improving the activity of horseradish peroxidase in betaine-based natural deep eutectic systems
author Meneses, Liane
author_facet Meneses, Liane
Gajardo-Parra, Nicolás F.
Cea-Klapp, Esteban
Garrido, José Matías
Held, Christoph
Duarte, Ana Rita
Paiva, Alexandre
author_role author
author2 Gajardo-Parra, Nicolás F.
Cea-Klapp, Esteban
Garrido, José Matías
Held, Christoph
Duarte, Ana Rita
Paiva, Alexandre
author2_role author
author
author
author
author
author
dc.contributor.none.fl_str_mv DQ - Departamento de Química
LAQV@REQUIMTE
RUN
dc.contributor.author.fl_str_mv Meneses, Liane
Gajardo-Parra, Nicolás F.
Cea-Klapp, Esteban
Garrido, José Matías
Held, Christoph
Duarte, Ana Rita
Paiva, Alexandre
dc.subject.por.fl_str_mv Chemistry (miscellaneous)
Analytical Chemistry
Electrochemistry
Organic Chemistry
topic Chemistry (miscellaneous)
Analytical Chemistry
Electrochemistry
Organic Chemistry
description The authors thank the funding from the Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) under Germany's Excellence Strategy - EXC 2033 - 390677874 - RESOLV. Nicolás Gajardo's work was supported by the German Academic Exchange Service (DAAD) under the Graduate School Scholarship Programme, 2020 (57516591). E. C.-K. acknowledges the scholarship from ANID, Chile. This research was partially supported by the supercomputing infrastructure of the Southern GPU Cluster - Fondequip EQM150134. Publisher Copyright: © 2023 RSC.
publishDate 2023
dc.date.none.fl_str_mv 2023-04-11
2023-04-11T00:00:00Z
2024-01-24T16:59:50Z
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/10362/162706
url http://hdl.handle.net/10362/162706
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv PURE: 81993740
https://doi.org/10.1039/d2su00127f
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 12
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
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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
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