Immobilization of lipases via interfacial activation on hydrophobic supports: Production of biocatalysts libraries by altering the immobilization conditions

Lipases A and B from Candida antarctica (CALA, CALB), and those from Candida rugosa (CRL) and Rhizomucor miehei (RML) have been immobilized on octyl agarose beads under 16 different conditions. The activities of the biocatalysts versus different substrates were analyzed, as well as their thermal sta...

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Detalles Bibliográficos
Autores: Arana-Peña, Sara, Rios, Nathalia S., Carballares, Diego, Gonçalves, Luciana R. B., Fernández-Lafuente, Roberto
Tipo de recurso: artículo
Estado:Versión aceptada para publicación
Fecha de publicación:2020
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/373216
Acceso en línea:http://hdl.handle.net/10261/373216
https://www.scopus.com/inward/record.uri?eid=2-s2.0-85083529115&doi=10.1016%2fj.cattod.2020.03.059&partnerID=40&md5=47dd1bfa1a69aa5470bfa69e9af2615a
Access Level:acceso abierto
Palabra clave:Interfacial activation
Lipase immobilization
Lipase modulation
Lipase specificity
Lipase stability
Biocatalysts
Candida
Enzyme activity
Isomers
Yeast
Candida antarctica
Different substrates
Hydrophobic supports
Immobilization conditions
Immobilization method
Rhizomucor miehei
Strong interaction
Enzyme immobilization
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spelling Immobilization of lipases via interfacial activation on hydrophobic supports: Production of biocatalysts libraries by altering the immobilization conditionsArana-Peña, SaraRios, Nathalia S.Carballares, DiegoGonçalves, Luciana R. B.Fernández-Lafuente, RobertoInterfacial activationLipase immobilizationLipase modulationLipase specificityLipase stabilityBiocatalystsCandidaEnzyme activityIsomersYeastCandida antarcticaDifferent substratesHydrophobic supportsImmobilization conditionsImmobilization methodRhizomucor mieheiStrong interactionEnzyme immobilizationLipases A and B from Candida antarctica (CALA, CALB), and those from Candida rugosa (CRL) and Rhizomucor miehei (RML) have been immobilized on octyl agarose beads under 16 different conditions. The activities of the biocatalysts versus different substrates were analyzed, as well as their thermal stabilities at pH 7.0. All CALB and CRL preparations showed very similar properties, except the CRL biocatalysts prepared at pH 9. Under these conditions the free enzyme was partially inactivated. Immobilized CALA showed some significant differences in activity depending on the immobilization conditions when using esters of mandelic acid as substrates (the activities of the different preparations differed by more than a 2-fold factor), while when using the other substrates the differences were minimal. However, immobilized RML enzyme greatly alters its activity depending on the immobilization conditions, reaching differences up to 4–5 fold in both activity and stability. It is remarkable that the effect of one immobilization variable depends on the substrates, and that there are strong interactions between the different immobilization variables. Thus, this immobilization method was very robust (producing almost identical functional biocatalysts independently from the immobilization conditions) using CRL or CALB, while the immobilization conditions must be carefully controlled using RML to have reproducible results. © 2020 Elsevier B.V.We gratefully recognize the support from the MICINN from Spanish Government, (project number CTQ2017-86170-R). NSR thanks to CNPq for a predoctoral fellowship (CNPq scholarship– Brazil) and to Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (PNPD/ CAPES) for a postdoctoral fellowship. DC gratefully thanks for a pre doctotal FPI fellowship to MICINN, Spain. Mr Martinez (Novozymes Spain) is gratefully recognized by the donation of the enzymes.Peer reviewedElsevier BVAgencia Estatal de Investigación (España)Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (Brasil)Ministerio de Ciencia e Innovación (España)Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]202420242020info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Postprintinfo:eu-repo/semantics/acceptedVersionhttp://hdl.handle.net/10261/373216https://www.scopus.com/inward/record.uri?eid=2-s2.0-85083529115&doi=10.1016%2fj.cattod.2020.03.059&partnerID=40&md5=47dd1bfa1a69aa5470bfa69e9af2615areponame: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 2013-2016/CTQ2017-86170-RCatalysis Todayhttps://doi.org/10.1016/j.cattod.2020.03.059Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/3732162026-05-22T06:33:51Z
dc.title.none.fl_str_mv Immobilization of lipases via interfacial activation on hydrophobic supports: Production of biocatalysts libraries by altering the immobilization conditions
title Immobilization of lipases via interfacial activation on hydrophobic supports: Production of biocatalysts libraries by altering the immobilization conditions
spellingShingle Immobilization of lipases via interfacial activation on hydrophobic supports: Production of biocatalysts libraries by altering the immobilization conditions
Arana-Peña, Sara
Interfacial activation
Lipase immobilization
Lipase modulation
Lipase specificity
Lipase stability
Biocatalysts
Candida
Enzyme activity
Isomers
Yeast
Candida antarctica
Different substrates
Hydrophobic supports
Immobilization conditions
Immobilization method
Rhizomucor miehei
Strong interaction
Enzyme immobilization
title_short Immobilization of lipases via interfacial activation on hydrophobic supports: Production of biocatalysts libraries by altering the immobilization conditions
title_full Immobilization of lipases via interfacial activation on hydrophobic supports: Production of biocatalysts libraries by altering the immobilization conditions
title_fullStr Immobilization of lipases via interfacial activation on hydrophobic supports: Production of biocatalysts libraries by altering the immobilization conditions
title_full_unstemmed Immobilization of lipases via interfacial activation on hydrophobic supports: Production of biocatalysts libraries by altering the immobilization conditions
title_sort Immobilization of lipases via interfacial activation on hydrophobic supports: Production of biocatalysts libraries by altering the immobilization conditions
dc.creator.none.fl_str_mv Arana-Peña, Sara
Rios, Nathalia S.
Carballares, Diego
Gonçalves, Luciana R. B.
Fernández-Lafuente, Roberto
author Arana-Peña, Sara
author_facet Arana-Peña, Sara
Rios, Nathalia S.
Carballares, Diego
Gonçalves, Luciana R. B.
Fernández-Lafuente, Roberto
author_role author
author2 Rios, Nathalia S.
Carballares, Diego
Gonçalves, Luciana R. B.
Fernández-Lafuente, Roberto
author2_role author
author
author
author
dc.contributor.none.fl_str_mv Agencia Estatal de Investigación (España)
Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (Brasil)
Ministerio de Ciencia e Innovación (España)
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Interfacial activation
Lipase immobilization
Lipase modulation
Lipase specificity
Lipase stability
Biocatalysts
Candida
Enzyme activity
Isomers
Yeast
Candida antarctica
Different substrates
Hydrophobic supports
Immobilization conditions
Immobilization method
Rhizomucor miehei
Strong interaction
Enzyme immobilization
topic Interfacial activation
Lipase immobilization
Lipase modulation
Lipase specificity
Lipase stability
Biocatalysts
Candida
Enzyme activity
Isomers
Yeast
Candida antarctica
Different substrates
Hydrophobic supports
Immobilization conditions
Immobilization method
Rhizomucor miehei
Strong interaction
Enzyme immobilization
description Lipases A and B from Candida antarctica (CALA, CALB), and those from Candida rugosa (CRL) and Rhizomucor miehei (RML) have been immobilized on octyl agarose beads under 16 different conditions. The activities of the biocatalysts versus different substrates were analyzed, as well as their thermal stabilities at pH 7.0. All CALB and CRL preparations showed very similar properties, except the CRL biocatalysts prepared at pH 9. Under these conditions the free enzyme was partially inactivated. Immobilized CALA showed some significant differences in activity depending on the immobilization conditions when using esters of mandelic acid as substrates (the activities of the different preparations differed by more than a 2-fold factor), while when using the other substrates the differences were minimal. However, immobilized RML enzyme greatly alters its activity depending on the immobilization conditions, reaching differences up to 4–5 fold in both activity and stability. It is remarkable that the effect of one immobilization variable depends on the substrates, and that there are strong interactions between the different immobilization variables. Thus, this immobilization method was very robust (producing almost identical functional biocatalysts independently from the immobilization conditions) using CRL or CALB, while the immobilization conditions must be carefully controlled using RML to have reproducible results. © 2020 Elsevier B.V.
publishDate 2020
dc.date.none.fl_str_mv 2020
2024
2024
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Postprint
info:eu-repo/semantics/acceptedVersion
format article
status_str acceptedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/373216
https://www.scopus.com/inward/record.uri?eid=2-s2.0-85083529115&doi=10.1016%2fj.cattod.2020.03.059&partnerID=40&md5=47dd1bfa1a69aa5470bfa69e9af2615a
url http://hdl.handle.net/10261/373216
https://www.scopus.com/inward/record.uri?eid=2-s2.0-85083529115&doi=10.1016%2fj.cattod.2020.03.059&partnerID=40&md5=47dd1bfa1a69aa5470bfa69e9af2615a
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 2013-2016/CTQ2017-86170-R
Catalysis Today
https://doi.org/10.1016/j.cattod.2020.03.059
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
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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