Preparation and characterization of different immobilized and chemically modified preparations of lipase B from Candida antarctica: is it the activation energy a good indicator of the biocatalyst expressed activity?

Lipase B from Candida antarctica immobilized on octyl (via interfacial activation) and octyl-vinyl sulfone (covalently attached) agarose beads via different immobilization protocols was submitted to amination and/or glutaraldehyde modifications. The catalytic performance of the resulting biocatalyst...

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Autores: Hackenhaar, Camila R., Abellanas-Perez, Pedro, Carballares, Diego, Bolivar, Juan M, Rodrigues, Rafael C, Fernandez-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:10261/414949
Acceso en línea:http://hdl.handle.net/10261/414949
https://api.elsevier.com/content/abstract/scopus_id/105014736148
Access Level:acceso abierto
Palabra clave:Activation energy
Chemically modified lipases
Interfacially activated lipase
Lipase immobilization
Specificity tuning
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spelling Preparation and characterization of different immobilized and chemically modified preparations of lipase B from Candida antarctica: is it the activation energy a good indicator of the biocatalyst expressed activity?Hackenhaar, Camila R.Abellanas-Perez, PedroCarballares, DiegoBolivar, Juan MRodrigues, Rafael CFernandez-Lafuente, RobertoActivation energyChemically modified lipasesInterfacially activated lipaseLipase immobilizationSpecificity tuningLipase B from Candida antarctica immobilized on octyl (via interfacial activation) and octyl-vinyl sulfone (covalently attached) agarose beads via different immobilization protocols was submitted to amination and/or glutaraldehyde modifications. The catalytic performance of the resulting biocatalysts significantly varied across different substrates: using octyl-CALB with the double modification, activity increased 3.5 fold versus triacetin and decreased by 5 % using R-methyl mandelate, while using the covalent biocatalyst, activity increase by 2.2 or 20 %, respectively. Similarly, the stability of the biocatalysts -both in absolute and relative terms- was strongly influenced by the inactivation pH and the substrate used for residual activity determination. Under the tested conditions, activity versus substrate concentration followed first-order kinetics up to the substrate solubility limit, preventing the determination of kinetic parameters such as Kcat or Km. Activation energy (Eₐ) for triacetin hydrolysis was also measured for each biocatalyst under different inactivation states. Interestingly, no consistent correlation was found between Eₐ and enzyme activity. Generally, partial inactivation of the biocatalysts increased Eₐ, although some exceptions were observed. These findings suggest that Eₐ alone does not directly correlate with enzymatic activity, highlighting the complex interplay between structural enzyme modifications, substrate used to determine the enzyme activity, and the enzyme catalytic behavior.JMB acknowledges funding from project CNS2022-135541 financed by MICIU/AEI /10.13039/501100011033 and by European Union NextGeneration EU/PRTR. DCN and JMB acknowledges funding from Pathfinder Open 2022, a European Innovation Council (EIC) work program that is part of Horizon Europe (grant agreement no. 101099528) and UK Innovation Funding Agency (UKRI) (reference no. 10062709). RFL acknowledges the support from MINECO and AEI via project PID2022-136535OB-I00. RCR acknowledges the support from CNPq (Process: 403151/2023-6) and FAPERGS (Process: 22/2551-0000397-4). CRH acknowledges the support by the Coordenação de Aperfeiçoamento de Pessoal de Nível Superior – Brazil (CAPES) – Finance Code 001.Peer reviewedElsevier BVAgencia Estatal de Investigación (España)European Innovation CouncilNational capability funding (UK)Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (Brasil)#NODATA##NODATA##NODATA##NODATA##NODATA##NODATA#Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]202620262025info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionhttp://hdl.handle.net/10261/414949https://api.elsevier.com/content/abstract/scopus_id/105014736148reponame: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//info:eu-repo/grantAgreement/EC/HE/101099528info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2021-2023/PID2022-136535OB-I00International journal of biological macromoleculeshttps://doi.org/10.1016/j.ijbiomac.2025.147310Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/4149492026-05-22T06:33:51Z
dc.title.none.fl_str_mv Preparation and characterization of different immobilized and chemically modified preparations of lipase B from Candida antarctica: is it the activation energy a good indicator of the biocatalyst expressed activity?
title Preparation and characterization of different immobilized and chemically modified preparations of lipase B from Candida antarctica: is it the activation energy a good indicator of the biocatalyst expressed activity?
spellingShingle Preparation and characterization of different immobilized and chemically modified preparations of lipase B from Candida antarctica: is it the activation energy a good indicator of the biocatalyst expressed activity?
Hackenhaar, Camila R.
Activation energy
Chemically modified lipases
Interfacially activated lipase
Lipase immobilization
Specificity tuning
title_short Preparation and characterization of different immobilized and chemically modified preparations of lipase B from Candida antarctica: is it the activation energy a good indicator of the biocatalyst expressed activity?
title_full Preparation and characterization of different immobilized and chemically modified preparations of lipase B from Candida antarctica: is it the activation energy a good indicator of the biocatalyst expressed activity?
title_fullStr Preparation and characterization of different immobilized and chemically modified preparations of lipase B from Candida antarctica: is it the activation energy a good indicator of the biocatalyst expressed activity?
title_full_unstemmed Preparation and characterization of different immobilized and chemically modified preparations of lipase B from Candida antarctica: is it the activation energy a good indicator of the biocatalyst expressed activity?
title_sort Preparation and characterization of different immobilized and chemically modified preparations of lipase B from Candida antarctica: is it the activation energy a good indicator of the biocatalyst expressed activity?
dc.creator.none.fl_str_mv Hackenhaar, Camila R.
Abellanas-Perez, Pedro
Carballares, Diego
Bolivar, Juan M
Rodrigues, Rafael C
Fernandez-Lafuente, Roberto
author Hackenhaar, Camila R.
author_facet Hackenhaar, Camila R.
Abellanas-Perez, Pedro
Carballares, Diego
Bolivar, Juan M
Rodrigues, Rafael C
Fernandez-Lafuente, Roberto
author_role author
author2 Abellanas-Perez, Pedro
Carballares, Diego
Bolivar, Juan M
Rodrigues, Rafael C
Fernandez-Lafuente, Roberto
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv Agencia Estatal de Investigación (España)
European Innovation Council
National capability funding (UK)
Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (Brasil)
#NODATA#
#NODATA#
#NODATA#
#NODATA#
#NODATA#
#NODATA#
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Activation energy
Chemically modified lipases
Interfacially activated lipase
Lipase immobilization
Specificity tuning
topic Activation energy
Chemically modified lipases
Interfacially activated lipase
Lipase immobilization
Specificity tuning
description Lipase B from Candida antarctica immobilized on octyl (via interfacial activation) and octyl-vinyl sulfone (covalently attached) agarose beads via different immobilization protocols was submitted to amination and/or glutaraldehyde modifications. The catalytic performance of the resulting biocatalysts significantly varied across different substrates: using octyl-CALB with the double modification, activity increased 3.5 fold versus triacetin and decreased by 5 % using R-methyl mandelate, while using the covalent biocatalyst, activity increase by 2.2 or 20 %, respectively. Similarly, the stability of the biocatalysts -both in absolute and relative terms- was strongly influenced by the inactivation pH and the substrate used for residual activity determination. Under the tested conditions, activity versus substrate concentration followed first-order kinetics up to the substrate solubility limit, preventing the determination of kinetic parameters such as Kcat or Km. Activation energy (Eₐ) for triacetin hydrolysis was also measured for each biocatalyst under different inactivation states. Interestingly, no consistent correlation was found between Eₐ and enzyme activity. Generally, partial inactivation of the biocatalysts increased Eₐ, although some exceptions were observed. These findings suggest that Eₐ alone does not directly correlate with enzymatic activity, highlighting the complex interplay between structural enzyme modifications, substrate used to determine the enzyme activity, and the enzyme catalytic behavior.
publishDate 2025
dc.date.none.fl_str_mv 2025
2026
2026
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/10261/414949
https://api.elsevier.com/content/abstract/scopus_id/105014736148
url http://hdl.handle.net/10261/414949
https://api.elsevier.com/content/abstract/scopus_id/105014736148
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//
info:eu-repo/grantAgreement/EC/HE/101099528
info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2021-2023/PID2022-136535OB-I00
International journal of biological macromolecules
https://doi.org/10.1016/j.ijbiomac.2025.147310
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
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repository.mail.fl_str_mv
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