Effect of the support alkyl chain nature in the functional properties of the immobilized lipases

No data was used for the research described in the article.

Detalles Bibliográficos
Autores: Andrades, Diandra de, Abellanas-Pérez, Pedro, Rocha-Martín, Javier, López-Gallego, Fernando, Alcántara, Andrés R., Polizeli, Maria de Lourdes T. M., Fernández-Lafuente, Roberto
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2025
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/402683
Acceso en línea:http://hdl.handle.net/10261/402683
https://api.elsevier.com/content/abstract/scopus_id/85214801207
Access Level:acceso abierto
Palabra clave:Enzyme specificity
Enzyme stability
Lipase interfacial activation
Tailor made supports
id ES_960e0d754d60ec5af87a2f6744c4e010
oai_identifier_str oai:digital.csic.es:10261/402683
network_acronym_str ES
network_name_str España
repository_id_str
spelling Effect of the support alkyl chain nature in the functional properties of the immobilized lipasesAndrades, Diandra deAbellanas-Pérez, PedroRocha-Martín, JavierLópez-Gallego, FernandoAlcántara, Andrés R.Polizeli, Maria de Lourdes T. M.Fernández-Lafuente, RobertoEnzyme specificityEnzyme stabilityLipase interfacial activationTailor made supportsNo data was used for the research described in the article.Supports coated with amino-hexyl and amino octyl have been prepared from glyoxyl agarose beads and compared in their performance with octyl-agarose to immobilize lipases A and B from Candida antarctica (CALA and CALB). Immobilization courses were similar using all supports, but enzyme release was more difficult using the amino-alkyl supports suggesting a mixed interfacial activation/ionic exchange immobilization. The enzyme activity and specificity (using p-nitrophenyl propionate, triacetin and both isomers of methyl mandelate) greatly depended on the support. In many instances the enzymes immobilized on the new supports offered higher activities and enantiospecificity in the hydrolysis of both enantiomers of methyl mandelate (mainly using CALB). This was coupled to a lower enzyme stability using the new supports, even in the presence of high ionic strength, suggesting that the amphipathic could be responsible of the enzyme lower stability. Using CALB, it was possible to detect a higher exposition of the enzyme Trp groups to the medium by florescence spectra after its immobilization on the amino-alkyl-supports, correlating to the higher activity and lower stability results.We gratefully recognize the financial support from Ministerio de Ciencia e Innovación and Agencia Estatal de Investigación (Spanish Government) (PID2022–136535OB-I00). JR-M recognizes the support from Grant CNS2022–135135 funded by MICIU/AEI/10.13039/501100011033 and European Union NextGenerationEU/PRTR and Grant PID2022–139209OB-C22 funded by MICIU/AEI/10.13039/501100011033 and ERDF/EU. The authors gratefully acknowledge FAPESP (São Paulo Research Foundation) by research scholarship to DA (Grant No: 2020/15510–8 and 2023/01338–7). The help and suggestions from Dr. Ángel Berenguer (Departamento de Química Inorgánica, Universidad de Alicante) are gratefully recognized.Peer reviewedElsevierMinisterio de Ciencia e Innovación (España)Agencia Estatal de Investigación (España)Ministerio de Ciencia, Innovación y Universidades (España)European CommissionFundação de Amparo à Pesquisa do Estado de São PauloFernández-Lafuente, Roberto [0000-0003-4976-7096]Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]202520252025info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionapplication/pdfhttp://hdl.handle.net/10261/402683https://api.elsevier.com/content/abstract/scopus_id/85214801207reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Inglés#PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE#info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2021-2023/info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2021-2023/PID2022-139209OB-C22info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2021-2023/CNS2022–135135https://doi.org/10.1016/j.enzmictec.2025.110583Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/4026832026-05-22T06:33:51Z
dc.title.none.fl_str_mv Effect of the support alkyl chain nature in the functional properties of the immobilized lipases
title Effect of the support alkyl chain nature in the functional properties of the immobilized lipases
spellingShingle Effect of the support alkyl chain nature in the functional properties of the immobilized lipases
Andrades, Diandra de
Enzyme specificity
Enzyme stability
Lipase interfacial activation
Tailor made supports
title_short Effect of the support alkyl chain nature in the functional properties of the immobilized lipases
title_full Effect of the support alkyl chain nature in the functional properties of the immobilized lipases
title_fullStr Effect of the support alkyl chain nature in the functional properties of the immobilized lipases
title_full_unstemmed Effect of the support alkyl chain nature in the functional properties of the immobilized lipases
title_sort Effect of the support alkyl chain nature in the functional properties of the immobilized lipases
dc.creator.none.fl_str_mv Andrades, Diandra de
Abellanas-Pérez, Pedro
Rocha-Martín, Javier
López-Gallego, Fernando
Alcántara, Andrés R.
Polizeli, Maria de Lourdes T. M.
Fernández-Lafuente, Roberto
author Andrades, Diandra de
author_facet Andrades, Diandra de
Abellanas-Pérez, Pedro
Rocha-Martín, Javier
López-Gallego, Fernando
Alcántara, Andrés R.
Polizeli, Maria de Lourdes T. M.
Fernández-Lafuente, Roberto
author_role author
author2 Abellanas-Pérez, Pedro
Rocha-Martín, Javier
López-Gallego, Fernando
Alcántara, Andrés R.
Polizeli, Maria de Lourdes T. M.
Fernández-Lafuente, Roberto
author2_role author
author
author
author
author
author
dc.contributor.none.fl_str_mv Ministerio de Ciencia e Innovación (España)
Agencia Estatal de Investigación (España)
Ministerio de Ciencia, Innovación y Universidades (España)
European Commission
Fundação de Amparo à Pesquisa do Estado de São Paulo
Fernández-Lafuente, Roberto [0000-0003-4976-7096]
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Enzyme specificity
Enzyme stability
Lipase interfacial activation
Tailor made supports
topic Enzyme specificity
Enzyme stability
Lipase interfacial activation
Tailor made supports
description No data was used for the research described in the article.
publishDate 2025
dc.date.none.fl_str_mv 2025
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/10261/402683
https://api.elsevier.com/content/abstract/scopus_id/85214801207
url http://hdl.handle.net/10261/402683
https://api.elsevier.com/content/abstract/scopus_id/85214801207
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv #PLACEHOLDER_PARENT_METADATA_VALUE#
#PLACEHOLDER_PARENT_METADATA_VALUE#
#PLACEHOLDER_PARENT_METADATA_VALUE#
info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2021-2023/
info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2021-2023/PID2022-139209OB-C22
info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2021-2023/CNS2022–135135
https://doi.org/10.1016/j.enzmictec.2025.110583
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
publisher.none.fl_str_mv Elsevier
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
_version_ 1869413903950151680
score 15,812429

Similares en LA Referencia