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, Pedro; Carballares Navarro, Diego; Bolívar Bolívar, Juan Manuel; Rodrigues, Rafael C.; Fernandez Lafuente, Roberto

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 Navarro, Diego, Bolívar Bolívar, Juan Manuel, Rodrigues, Rafael C., Fernandez Lafuente, Roberto
Tipo de recurso:	artículo
Fecha de publicación:	2025
País:	España
Institución:	Universidad Complutense de Madrid (UCM)
Repositorio:	Docta Complutense
Idioma:	inglés
OAI Identifier:	oai:docta.ucm.es:20.500.14352/123832
Acceso en línea:	https://hdl.handle.net/20.500.14352/123832
Access Level:	acceso abierto
Palabra clave:	66.0 Lipase immobilization Chemically modified lipases Specificity tuning Activation energy Interfacially activated lipase Bioquímica (Química) Ingeniería química 2302 Bioquímica 3302 Tecnología Bioquímica 3303 Ingeniería y Tecnología Químicas

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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 Navarro, DiegoBolívar Bolívar, Juan ManuelRodrigues, Rafael C.Fernandez Lafuente, Roberto66.0Lipase immobilizationChemically modified lipasesSpecificity tuningActivation energyInterfacially activated lipaseBioquímica (Química)Ingeniería química2302 Bioquímica3302 Tecnología Bioquímica3303 Ingeniería y Tecnología QuímicasLipase 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 behaviorElsevierUniversidad Complutense de Madrid20252025-09-0120252025-09-01journal articlehttp://purl.org/coar/resource_type/c_6501VoRhttp://purl.org/coar/version/c_970fb48d4fbd8a85info:eu-repo/semantics/articleapplication/pdfhttps://hdl.handle.net/20.500.14352/123832reponame:Docta Complutenseinstname:Universidad Complutense de Madrid (UCM)Inglésengopen accesshttp://purl.org/coar/access_right/c_abf2Attribution-NonCommercial-NoDerivatives 4.0 Internationalhttp://creativecommons.org/licenses/by-nc-nd/4.0/info:eu-repo/semantics/openAccessoai:docta.ucm.es:20.500.14352/1238322026-06-02T12:44:21Z
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. 66.0 Lipase immobilization Chemically modified lipases Specificity tuning Activation energy Interfacially activated lipase Bioquímica (Química) Ingeniería química 2302 Bioquímica 3302 Tecnología Bioquímica 3303 Ingeniería y Tecnología Químicas
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 Navarro, Diego Bolívar Bolívar, Juan Manuel Rodrigues, Rafael C. Fernandez Lafuente, Roberto
author	Hackenhaar, Camila R.
author_facet	Hackenhaar, Camila R. Abellanas Perez, Pedro Carballares Navarro, Diego Bolívar Bolívar, Juan Manuel Rodrigues, Rafael C. Fernandez Lafuente, Roberto
author_role	author
author2	Abellanas Perez, Pedro Carballares Navarro, Diego Bolívar Bolívar, Juan Manuel Rodrigues, Rafael C. Fernandez Lafuente, Roberto
author2_role	author author author author author
dc.contributor.none.fl_str_mv	Universidad Complutense de Madrid
dc.subject.none.fl_str_mv	66.0 Lipase immobilization Chemically modified lipases Specificity tuning Activation energy Interfacially activated lipase Bioquímica (Química) Ingeniería química 2302 Bioquímica 3302 Tecnología Bioquímica 3303 Ingeniería y Tecnología Químicas
topic	66.0 Lipase immobilization Chemically modified lipases Specificity tuning Activation energy Interfacially activated lipase Bioquímica (Química) Ingeniería química 2302 Bioquímica 3302 Tecnología Bioquímica 3303 Ingeniería y Tecnología Químicas
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 2025-09-01 2025 2025-09-01
dc.type.none.fl_str_mv	journal article http://purl.org/coar/resource_type/c_6501 VoR http://purl.org/coar/version/c_970fb48d4fbd8a85
dc.type.openaire.fl_str_mv	info:eu-repo/semantics/article
format	article
dc.identifier.none.fl_str_mv	https://hdl.handle.net/20.500.14352/123832
url	https://hdl.handle.net/20.500.14352/123832
dc.language.none.fl_str_mv	Inglés eng
language_invalid_str_mv	Inglés
language	eng
dc.rights.none.fl_str_mv	open access http://purl.org/coar/access_right/c_abf2 Attribution-NonCommercial-NoDerivatives 4.0 International http://creativecommons.org/licenses/by-nc-nd/4.0/
dc.rights.openaire.fl_str_mv	info:eu-repo/semantics/openAccess
rights_invalid_str_mv	open access http://purl.org/coar/access_right/c_abf2 Attribution-NonCommercial-NoDerivatives 4.0 International http://creativecommons.org/licenses/by-nc-nd/4.0/
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:Docta Complutense instname:Universidad Complutense de Madrid (UCM)
instname_str	Universidad Complutense de Madrid (UCM)
reponame_str	Docta Complutense
collection	Docta Complutense
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score	15,811543

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?

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