Insights on the laccase extraction and activity in ionic-liquid-based aqueous biphasic systems

Detalhes bibliográficos
Autor(a) principal: Capela, Emanuel V.
Data de Publicação: 2020
Outros Autores: Valente, Ana I., Nunes, João C.F., Magalhães, Flávia F., Rodriguez, Oscar, Soto, Ana, Freire, Mara G., 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/10773/28499
Resumo: Due to their catalytic properties, selectivity, and efficiency, enzymes are excellent biocatalysts. In particular, laccases are versatile multi-copper oxidases with great interest for a wide plethora of biotechnological and environmental applications. Even though several laccase-catalysed processes have been reported at an industrial level, the high costs of their downstream processing required to provide biocatalysts with high purity levels, stability and activity remains one of the main drawbacks when economically evaluating the overall processes. Aqueous biphasic systems based on ionic liquids (ILs) can be foreseen as a promising alternative approach for the extraction and activity maintenance/improvement of enzymes, essentially due to the designer solvents ability of ionic liquids. However, to take advantage of this feature and to use the full potential of IL-based aqueous biphasic systems, it is necessary to understand the effect of ILs as phase-forming constituents and how they affect the enzymes extraction and activity. In order to overcome the lack of information on this topic in the literature, in this work, IL-based aqueous biphasic systems were investigated to extract and enhance the laccase activity, in order to gather evidences that could be used to improve the enzymes downstream processing. To this end, a wide screening of imidazolium-, pyridinium-, pyrrolidinium-, piperidinium-, tetraalkylphosphonium-, and tetraalkylammonium-based ILs as phase-forming components of ABS was carried out. Furthermore, these ILs were used to create ABS combined with salts, polymers and used as adjuvants in polymer-based ABS. Most ABS comprising ILs revealed to be highly efficient extraction platforms, allowing the complete extraction of laccase for all the conditions tested, and with an enzyme activity enhancement by more than 50%. Overall, the obtained results demonstrate that laccase preferentially partitions to the most hydrophilic phase in ABS comprising ILs, both used as adjuvants or as phase-forming components, corresponding to the phase in which the IL is enriched. Furthermore, the IL chemical structure of the IL plays a significant role in the enzyme activity, where ILs with a higher number of hydroxyl groups seem to be relevant to improve the laccase activity.
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spelling Insights on the laccase extraction and activity in ionic-liquid-based aqueous biphasic systemsLaccaseOxidative EnzymesExtractionActivityAqueous Biphasic SystemsIonic liquidsDue to their catalytic properties, selectivity, and efficiency, enzymes are excellent biocatalysts. In particular, laccases are versatile multi-copper oxidases with great interest for a wide plethora of biotechnological and environmental applications. Even though several laccase-catalysed processes have been reported at an industrial level, the high costs of their downstream processing required to provide biocatalysts with high purity levels, stability and activity remains one of the main drawbacks when economically evaluating the overall processes. Aqueous biphasic systems based on ionic liquids (ILs) can be foreseen as a promising alternative approach for the extraction and activity maintenance/improvement of enzymes, essentially due to the designer solvents ability of ionic liquids. However, to take advantage of this feature and to use the full potential of IL-based aqueous biphasic systems, it is necessary to understand the effect of ILs as phase-forming constituents and how they affect the enzymes extraction and activity. In order to overcome the lack of information on this topic in the literature, in this work, IL-based aqueous biphasic systems were investigated to extract and enhance the laccase activity, in order to gather evidences that could be used to improve the enzymes downstream processing. To this end, a wide screening of imidazolium-, pyridinium-, pyrrolidinium-, piperidinium-, tetraalkylphosphonium-, and tetraalkylammonium-based ILs as phase-forming components of ABS was carried out. Furthermore, these ILs were used to create ABS combined with salts, polymers and used as adjuvants in polymer-based ABS. Most ABS comprising ILs revealed to be highly efficient extraction platforms, allowing the complete extraction of laccase for all the conditions tested, and with an enzyme activity enhancement by more than 50%. Overall, the obtained results demonstrate that laccase preferentially partitions to the most hydrophilic phase in ABS comprising ILs, both used as adjuvants or as phase-forming components, corresponding to the phase in which the IL is enriched. Furthermore, the IL chemical structure of the IL plays a significant role in the enzyme activity, where ILs with a higher number of hydroxyl groups seem to be relevant to improve the laccase activity.Elsevier2021-05-09T00:00:00Z2020-05-07T00:00:00Z2020-05-07info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10773/28499eng1383-586610.1016/j.seppur.2020.117052Capela, Emanuel V.Valente, Ana I.Nunes, João C.F.Magalhães, Flávia F.Rodriguez, OscarSoto, AnaFreire, Mara G.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:RCAAP2024-02-22T11:55:05Zoai:ria.ua.pt:10773/28499Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:01:00.874197Repositório 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 Insights on the laccase extraction and activity in ionic-liquid-based aqueous biphasic systems
title Insights on the laccase extraction and activity in ionic-liquid-based aqueous biphasic systems
spellingShingle Insights on the laccase extraction and activity in ionic-liquid-based aqueous biphasic systems
Capela, Emanuel V.
Laccase
Oxidative Enzymes
Extraction
Activity
Aqueous Biphasic Systems
Ionic liquids
title_short Insights on the laccase extraction and activity in ionic-liquid-based aqueous biphasic systems
title_full Insights on the laccase extraction and activity in ionic-liquid-based aqueous biphasic systems
title_fullStr Insights on the laccase extraction and activity in ionic-liquid-based aqueous biphasic systems
title_full_unstemmed Insights on the laccase extraction and activity in ionic-liquid-based aqueous biphasic systems
title_sort Insights on the laccase extraction and activity in ionic-liquid-based aqueous biphasic systems
author Capela, Emanuel V.
author_facet Capela, Emanuel V.
Valente, Ana I.
Nunes, João C.F.
Magalhães, Flávia F.
Rodriguez, Oscar
Soto, Ana
Freire, Mara G.
Tavares, Ana P.M.
author_role author
author2 Valente, Ana I.
Nunes, João C.F.
Magalhães, Flávia F.
Rodriguez, Oscar
Soto, Ana
Freire, Mara G.
Tavares, Ana P.M.
author2_role author
author
author
author
author
author
author
dc.contributor.author.fl_str_mv Capela, Emanuel V.
Valente, Ana I.
Nunes, João C.F.
Magalhães, Flávia F.
Rodriguez, Oscar
Soto, Ana
Freire, Mara G.
Tavares, Ana P.M.
dc.subject.por.fl_str_mv Laccase
Oxidative Enzymes
Extraction
Activity
Aqueous Biphasic Systems
Ionic liquids
topic Laccase
Oxidative Enzymes
Extraction
Activity
Aqueous Biphasic Systems
Ionic liquids
description Due to their catalytic properties, selectivity, and efficiency, enzymes are excellent biocatalysts. In particular, laccases are versatile multi-copper oxidases with great interest for a wide plethora of biotechnological and environmental applications. Even though several laccase-catalysed processes have been reported at an industrial level, the high costs of their downstream processing required to provide biocatalysts with high purity levels, stability and activity remains one of the main drawbacks when economically evaluating the overall processes. Aqueous biphasic systems based on ionic liquids (ILs) can be foreseen as a promising alternative approach for the extraction and activity maintenance/improvement of enzymes, essentially due to the designer solvents ability of ionic liquids. However, to take advantage of this feature and to use the full potential of IL-based aqueous biphasic systems, it is necessary to understand the effect of ILs as phase-forming constituents and how they affect the enzymes extraction and activity. In order to overcome the lack of information on this topic in the literature, in this work, IL-based aqueous biphasic systems were investigated to extract and enhance the laccase activity, in order to gather evidences that could be used to improve the enzymes downstream processing. To this end, a wide screening of imidazolium-, pyridinium-, pyrrolidinium-, piperidinium-, tetraalkylphosphonium-, and tetraalkylammonium-based ILs as phase-forming components of ABS was carried out. Furthermore, these ILs were used to create ABS combined with salts, polymers and used as adjuvants in polymer-based ABS. Most ABS comprising ILs revealed to be highly efficient extraction platforms, allowing the complete extraction of laccase for all the conditions tested, and with an enzyme activity enhancement by more than 50%. Overall, the obtained results demonstrate that laccase preferentially partitions to the most hydrophilic phase in ABS comprising ILs, both used as adjuvants or as phase-forming components, corresponding to the phase in which the IL is enriched. Furthermore, the IL chemical structure of the IL plays a significant role in the enzyme activity, where ILs with a higher number of hydroxyl groups seem to be relevant to improve the laccase activity.
publishDate 2020
dc.date.none.fl_str_mv 2020-05-07T00:00:00Z
2020-05-07
2021-05-09T00:00:00Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
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status_str publishedVersion
dc.identifier.uri.fl_str_mv http://hdl.handle.net/10773/28499
url http://hdl.handle.net/10773/28499
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 1383-5866
10.1016/j.seppur.2020.117052
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
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dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
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