Insights on the role of blocking agent on the properties of the lipase from Thermomyces lanuginosus immobilized on heterofunctional support for hydroesterification reactions

Here, we report a study of the effect of the blocking agent on the properties of the lipase from Thermomyces lanuginosus (TLL) immobilized on a heterofunctional support (Purolite C18-ethylnediamina (EDA)- vinyl sulfone (VS)-TLL-blocking agent) in different reactions. The performance of the biocataly...

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Authors: Miranda, Felipe Cardoso, Oliveira, Kaíque Souza G. C., Tardioli, Paulo W., Fernández-Lafuente, Roberto, Guimarães, José Renato
Format: article
Status:Published version
Publication Date:2024
Country:España
Institution:Consejo Superior de Investigaciones Científicas (CSIC)
Repository:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/389782
Online Access:http://hdl.handle.net/10261/389782
https://api.elsevier.com/content/abstract/scopus_id/85197020427
Access Level:Open access
Keyword:Biolubricant esters
Experimental design
Lipase catalyzed hydrolysis and esterification
Lipase properties tuning
Waste cooking soybean oil
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spelling Insights on the role of blocking agent on the properties of the lipase from Thermomyces lanuginosus immobilized on heterofunctional support for hydroesterification reactionsMiranda, Felipe CardosoOliveira, Kaíque Souza G. C.Tardioli, Paulo W.Fernández-Lafuente, RobertoGuimarães, José RenatoBiolubricant estersExperimental designLipase catalyzed hydrolysis and esterificationLipase properties tuningWaste cooking soybean oilHere, we report a study of the effect of the blocking agent on the properties of the lipase from Thermomyces lanuginosus (TLL) immobilized on a heterofunctional support (Purolite C18-ethylnediamina (EDA)- vinyl sulfone (VS)-TLL-blocking agent) in different reactions. The performance of the biocatalysts was compared to those immobilized on standard hydrophobic support (Purolite C18-TLL) and the commercial one (TLL-IM). The nature of the blocking agent (Cys, Gly and Asp) altered the enzyme features. TLL-IM always gave a comparatively worse performance, with its specificity for the oil being very different to the Purolite biocatalysts. Under optimized conditions, Purolite C18-TLL yielded 97 % of hydrolysis conversion after 4 h using a water/waste cooking soybean oil (WCSO) mass ratio of 4.3, biocatalyst load of 6.5 wt% and a temperature of 44.2 °C (without buffer or emulsification agent). In esterification reactions of the purified free fatty acids (FFAs) obtained from WCSO, the best TLL biocatalysts depended on the utilized alcohol: linear amyl alcohol was preferred by Purolite C18-TLL and Purolite C18-EDA-VS-TLL-Gly, while higher activity was achieved utilizing isoamyl alcohol as nucleophile by Purolite C18-EDA-VS-TLL-Cys, Purolite C18-EDA-VS-TLL-Asp and IM-TLL as catalysts. All the results indicate the influence of the blocking step on the final biocatalyst features.This work was funded by Federal University of Itajubá (Edital 06/2023 - UNIVERSAL UNIFEI), São Paulo Research Foundation (FAPESP, grant number 2016/10636-8), Coordenação de Aperfeiçoamento de Pessoal de Nível Superior–Brasil (CAPES, Finance Code 001), Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq, project numbers 405889/2016-0 and 133204/2023-5), and Ministerio de Ciencia e Innovación and Agencia Estatal de Investigación (Spanish Government), with FEDER cofinancial support (project PID2022-136535OB-I00).Peer reviewedElsevier BVUniversidade Federal de ItajubáFundação de Amparo à Pesquisa do Estado de São PauloCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (Brasil)Conselho Nacional de Desenvolvimento Científico e Tecnológico (Brasil)Ministerio de Ciencia e Innovación (España)Agencia Estatal de Investigación (España)European CommissionConsejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]202520252024info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionapplication/pdfhttp://hdl.handle.net/10261/389782https://api.elsevier.com/content/abstract/scopus_id/85197020427reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Inglés#PLACEHOLDER_PARENT_METADATA_VALUE#info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2021-2023/PID2022-136535OB-I00The underlying dataset has been published as supplementary material of the article in the publisher platform at DOI https://doi.org/10.1016/j.ijbiomac.2024.133555https://doi.org/10.1016/j.ijbiomac.2024.133555Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/3897822026-05-22T06:33:51Z
dc.title.none.fl_str_mv Insights on the role of blocking agent on the properties of the lipase from Thermomyces lanuginosus immobilized on heterofunctional support for hydroesterification reactions
title Insights on the role of blocking agent on the properties of the lipase from Thermomyces lanuginosus immobilized on heterofunctional support for hydroesterification reactions
spellingShingle Insights on the role of blocking agent on the properties of the lipase from Thermomyces lanuginosus immobilized on heterofunctional support for hydroesterification reactions
Miranda, Felipe Cardoso
Biolubricant esters
Experimental design
Lipase catalyzed hydrolysis and esterification
Lipase properties tuning
Waste cooking soybean oil
title_short Insights on the role of blocking agent on the properties of the lipase from Thermomyces lanuginosus immobilized on heterofunctional support for hydroesterification reactions
title_full Insights on the role of blocking agent on the properties of the lipase from Thermomyces lanuginosus immobilized on heterofunctional support for hydroesterification reactions
title_fullStr Insights on the role of blocking agent on the properties of the lipase from Thermomyces lanuginosus immobilized on heterofunctional support for hydroesterification reactions
title_full_unstemmed Insights on the role of blocking agent on the properties of the lipase from Thermomyces lanuginosus immobilized on heterofunctional support for hydroesterification reactions
title_sort Insights on the role of blocking agent on the properties of the lipase from Thermomyces lanuginosus immobilized on heterofunctional support for hydroesterification reactions
dc.creator.none.fl_str_mv Miranda, Felipe Cardoso
Oliveira, Kaíque Souza G. C.
Tardioli, Paulo W.
Fernández-Lafuente, Roberto
Guimarães, José Renato
author Miranda, Felipe Cardoso
author_facet Miranda, Felipe Cardoso
Oliveira, Kaíque Souza G. C.
Tardioli, Paulo W.
Fernández-Lafuente, Roberto
Guimarães, José Renato
author_role author
author2 Oliveira, Kaíque Souza G. C.
Tardioli, Paulo W.
Fernández-Lafuente, Roberto
Guimarães, José Renato
author2_role author
author
author
author
dc.contributor.none.fl_str_mv Universidade Federal de Itajubá
Fundação de Amparo à Pesquisa do Estado de São Paulo
Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (Brasil)
Conselho Nacional de Desenvolvimento Científico e Tecnológico (Brasil)
Ministerio de Ciencia e Innovación (España)
Agencia Estatal de Investigación (España)
European Commission
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Biolubricant esters
Experimental design
Lipase catalyzed hydrolysis and esterification
Lipase properties tuning
Waste cooking soybean oil
topic Biolubricant esters
Experimental design
Lipase catalyzed hydrolysis and esterification
Lipase properties tuning
Waste cooking soybean oil
description Here, we report a study of the effect of the blocking agent on the properties of the lipase from Thermomyces lanuginosus (TLL) immobilized on a heterofunctional support (Purolite C18-ethylnediamina (EDA)- vinyl sulfone (VS)-TLL-blocking agent) in different reactions. The performance of the biocatalysts was compared to those immobilized on standard hydrophobic support (Purolite C18-TLL) and the commercial one (TLL-IM). The nature of the blocking agent (Cys, Gly and Asp) altered the enzyme features. TLL-IM always gave a comparatively worse performance, with its specificity for the oil being very different to the Purolite biocatalysts. Under optimized conditions, Purolite C18-TLL yielded 97 % of hydrolysis conversion after 4 h using a water/waste cooking soybean oil (WCSO) mass ratio of 4.3, biocatalyst load of 6.5 wt% and a temperature of 44.2 °C (without buffer or emulsification agent). In esterification reactions of the purified free fatty acids (FFAs) obtained from WCSO, the best TLL biocatalysts depended on the utilized alcohol: linear amyl alcohol was preferred by Purolite C18-TLL and Purolite C18-EDA-VS-TLL-Gly, while higher activity was achieved utilizing isoamyl alcohol as nucleophile by Purolite C18-EDA-VS-TLL-Cys, Purolite C18-EDA-VS-TLL-Asp and IM-TLL as catalysts. All the results indicate the influence of the blocking step on the final biocatalyst features.
publishDate 2024
dc.date.none.fl_str_mv 2024
2025
2025
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Publisher's version
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/389782
https://api.elsevier.com/content/abstract/scopus_id/85197020427
url http://hdl.handle.net/10261/389782
https://api.elsevier.com/content/abstract/scopus_id/85197020427
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv #PLACEHOLDER_PARENT_METADATA_VALUE#
info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2021-2023/PID2022-136535OB-I00
The underlying dataset has been published as supplementary material of the article in the publisher platform at DOI https://doi.org/10.1016/j.ijbiomac.2024.133555
https://doi.org/10.1016/j.ijbiomac.2024.133555
Sí
dc.rights.none.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 Elsevier BV
publisher.none.fl_str_mv Elsevier BV
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,811543

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