Vinyl sulfone-amino-alkyl supports: heterofunctional matrixes to prevent enzyme release and stabilize lipases via covalent immobilization

New trifunctional supports were prepared (amino-octyl-vinyl sulfone (VS)- and amino-hexyl-VS-agarose) and compared to octyl-VS-agarose. They were utilized to immobilize the lipases A and B from Candida antarctica (CALA and CALB). After incubation to generate some enzyme-support bonds and blocking wi...

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Autores: Abellanas Pérez, Pedro, de Andrades, Diandra, Alcántara León, Andrés Rafael, Rocha Martín, Javier, Polizeli, Maria de Lourdes Teixeira de Moraes, 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:20.500.14352/121053
Acceso en línea:https://hdl.handle.net/20.500.14352/121053
Access Level:acceso abierto
Palabra clave:577.15
66.081
661.12
Heterofunctional supports
Support surface tailoring
Enzyme properties tuning
Bioquímica (Química)
Ingeniería química
Biotecnología
2302.26 Bioquímica Física
2302.27 Proteínas
2306 Química Orgánica
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oai_identifier_str oai:docta.ucm.es:20.500.14352/121053
network_acronym_str ES
network_name_str España
repository_id_str
spelling Vinyl sulfone-amino-alkyl supports: heterofunctional matrixes to prevent enzyme release and stabilize lipases via covalent immobilizationAbellanas Pérez, Pedrode Andrades, DiandraAlcántara León, Andrés RafaelRocha Martín, JavierPolizeli, Maria de Lourdes Teixeira de MoraesFernandez Lafuente, Roberto577.1566.081661.12Heterofunctional supportsSupport surface tailoringEnzyme properties tuningBioquímica (Química)Ingeniería químicaBiotecnología2302.26 Bioquímica Física2302.27 Proteínas2306 Química OrgánicaNew trifunctional supports were prepared (amino-octyl-vinyl sulfone (VS)- and amino-hexyl-VS-agarose) and compared to octyl-VS-agarose. They were utilized to immobilize the lipases A and B from Candida antarctica (CALA and CALB). After incubation to generate some enzyme-support bonds and blocking with different nucleophiles, SDS-PAGE analyses showed that all enzyme molecules become covalently immobilized on the support. In all VS biocatalysts, the blocking reagent presented a great effect in the properties of enzymes. The best blocking agents promoted a significant enzyme stabilization compared to the enzyme stability using the amino-alkyl-agarose supports, higher than that using octyl-VS-agarose supports, although these remained the most stable ones in most cases, as the octyl-biocatalysts were significantly more stable than the enzyme immobilized on amino-alkyl-support. Enzyme activities and specificities could be also greatly tuned by the immobilization in the new trifunctional supports, with enzyme activities in many instances enhancing that of the best non-covalently immobilized enzyme. That way, the results on this paper show that the properties of the enzymes when immobilized on these new trifunctional supports may be significantly tuned by the nature of the acyl chain in the support and the nature of the reagent used to block the reactivity of the remaining VS groups.ElsevierUniversidad Complutense de Madrid20252025-04-0120252025-04-01journal articlehttp://purl.org/coar/resource_type/c_6501VoRhttp://purl.org/coar/version/c_970fb48d4fbd8a85info:eu-repo/semantics/articleapplication/pdfhttps://hdl.handle.net/20.500.14352/121053reponame:Docta Complutenseinstname:Universidad Complutense de Madrid (UCM)InglésengMinisterio de Ciencia e Innovación http://dx.doi.org/10.13039/501100004837 Not available PID2022-136535OB-I00MICIU Not available PID2022-139209OB-C22MICIU Not available CNS2022-135135open 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:20.500.14352/1210532026-06-02T12:44:21Z
dc.title.none.fl_str_mv Vinyl sulfone-amino-alkyl supports: heterofunctional matrixes to prevent enzyme release and stabilize lipases via covalent immobilization
title Vinyl sulfone-amino-alkyl supports: heterofunctional matrixes to prevent enzyme release and stabilize lipases via covalent immobilization
spellingShingle Vinyl sulfone-amino-alkyl supports: heterofunctional matrixes to prevent enzyme release and stabilize lipases via covalent immobilization
Abellanas Pérez, Pedro
577.15
66.081
661.12
Heterofunctional supports
Support surface tailoring
Enzyme properties tuning
Bioquímica (Química)
Ingeniería química
Biotecnología
2302.26 Bioquímica Física
2302.27 Proteínas
2306 Química Orgánica
title_short Vinyl sulfone-amino-alkyl supports: heterofunctional matrixes to prevent enzyme release and stabilize lipases via covalent immobilization
title_full Vinyl sulfone-amino-alkyl supports: heterofunctional matrixes to prevent enzyme release and stabilize lipases via covalent immobilization
title_fullStr Vinyl sulfone-amino-alkyl supports: heterofunctional matrixes to prevent enzyme release and stabilize lipases via covalent immobilization
title_full_unstemmed Vinyl sulfone-amino-alkyl supports: heterofunctional matrixes to prevent enzyme release and stabilize lipases via covalent immobilization
title_sort Vinyl sulfone-amino-alkyl supports: heterofunctional matrixes to prevent enzyme release and stabilize lipases via covalent immobilization
dc.creator.none.fl_str_mv Abellanas Pérez, Pedro
de Andrades, Diandra
Alcántara León, Andrés Rafael
Rocha Martín, Javier
Polizeli, Maria de Lourdes Teixeira de Moraes
Fernandez Lafuente, Roberto
author Abellanas Pérez, Pedro
author_facet Abellanas Pérez, Pedro
de Andrades, Diandra
Alcántara León, Andrés Rafael
Rocha Martín, Javier
Polizeli, Maria de Lourdes Teixeira de Moraes
Fernandez Lafuente, Roberto
author_role author
author2 de Andrades, Diandra
Alcántara León, Andrés Rafael
Rocha Martín, Javier
Polizeli, Maria de Lourdes Teixeira de Moraes
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 577.15
66.081
661.12
Heterofunctional supports
Support surface tailoring
Enzyme properties tuning
Bioquímica (Química)
Ingeniería química
Biotecnología
2302.26 Bioquímica Física
2302.27 Proteínas
2306 Química Orgánica
topic 577.15
66.081
661.12
Heterofunctional supports
Support surface tailoring
Enzyme properties tuning
Bioquímica (Química)
Ingeniería química
Biotecnología
2302.26 Bioquímica Física
2302.27 Proteínas
2306 Química Orgánica
description New trifunctional supports were prepared (amino-octyl-vinyl sulfone (VS)- and amino-hexyl-VS-agarose) and compared to octyl-VS-agarose. They were utilized to immobilize the lipases A and B from Candida antarctica (CALA and CALB). After incubation to generate some enzyme-support bonds and blocking with different nucleophiles, SDS-PAGE analyses showed that all enzyme molecules become covalently immobilized on the support. In all VS biocatalysts, the blocking reagent presented a great effect in the properties of enzymes. The best blocking agents promoted a significant enzyme stabilization compared to the enzyme stability using the amino-alkyl-agarose supports, higher than that using octyl-VS-agarose supports, although these remained the most stable ones in most cases, as the octyl-biocatalysts were significantly more stable than the enzyme immobilized on amino-alkyl-support. Enzyme activities and specificities could be also greatly tuned by the immobilization in the new trifunctional supports, with enzyme activities in many instances enhancing that of the best non-covalently immobilized enzyme. That way, the results on this paper show that the properties of the enzymes when immobilized on these new trifunctional supports may be significantly tuned by the nature of the acyl chain in the support and the nature of the reagent used to block the reactivity of the remaining VS groups.
publishDate 2025
dc.date.none.fl_str_mv 2025
2025-04-01
2025
2025-04-01
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/20.500.14352/121053
url https://hdl.handle.net/20.500.14352/121053
dc.language.none.fl_str_mv Inglés
eng
language_invalid_str_mv Inglés
language eng
dc.relation.none.fl_str_mv Ministerio de Ciencia e Innovación http://dx.doi.org/10.13039/501100004837 Not available PID2022-136535OB-I00
MICIU Not available PID2022-139209OB-C22
MICIU Not available CNS2022-135135
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
_version_ 1869413599012716544
score 15.811543

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