The immobilization protocol greatly alters the effects of metal phosphate modification on the activity/stability of immobilized lipases

Mineralization of immobilized enzymes has showed to couple the advantages of both processes. Here, the influence of the immobilization protocol on the effects of mineralization has been investigated. The lipases from Thermomyces lanuginosus and Candida rugosa were immobilized on octyl-, vinyl sulfon...

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Detalles Bibliográficos
Autores: Guimarães, José R., Carballares Navarro, Diego, Rocha Martín, Javier, Tardioli, Paulo W., Fernandez Lafuente, Roberto
Tipo de recurso: artículo
Fecha de publicación:2022
País:España
Institución:Universidad Complutense de Madrid (UCM)
Repositorio:Docta Complutense
Idioma:inglés
OAI Identifier:oai:docta.ucm.es:20.500.14352/124790
Acceso en línea:https://hdl.handle.net/20.500.14352/124790
Access Level:acceso abierto
Palabra clave:577.1
572
577.15
544.478
Solid-phase enzyme mineralization
Enzyme stabilization
Tuning enzyme specificity
Bioquímica (Biología)
Biología molecular (Biología)
2403 Bioquímica
2415 Biología Molecular
2302.09 Enzimología
2210.01 Catálisis
id ES_54e88296d2718b2c5aaa72fce4eec94b
oai_identifier_str oai:docta.ucm.es:20.500.14352/124790
network_acronym_str ES
network_name_str España
repository_id_str
spelling The immobilization protocol greatly alters the effects of metal phosphate modification on the activity/stability of immobilized lipasesGuimarães, José R.Carballares Navarro, DiegoRocha Martín, JavierTardioli, Paulo W.Fernandez Lafuente, Roberto577.1572577.15544.478Solid-phase enzyme mineralizationEnzyme stabilizationTuning enzyme specificityBioquímica (Biología)Biología molecular (Biología)2403 Bioquímica2415 Biología Molecular2302.09 Enzimología2210.01 CatálisisMineralization of immobilized enzymes has showed to couple the advantages of both processes. Here, the influence of the immobilization protocol on the effects of mineralization has been investigated. The lipases from Thermomyces lanuginosus and Candida rugosa were immobilized on octyl-, vinyl sulfone (VS) octyl (blocked with different nucleophiles) and glutaraldehyde- (at different pH values) agarose beads. The stability, activity and specificity of the biocatalysts were very different, both the differently blocked VS-biocatalysts and the glutaraldehyde biocatalysts prepared at different pH. All biocatalysts were submitted to mineralization using different metals. The activity, specificity and stability effects of the mineralization strongly depended on the enzyme and on the immobilization protocol. For the same enzyme, a mineralization protocol could be negative, positive or present no effect depending on the enzyme immobilization procedure and substrate. In the best cases, activity could be increased by a two-fold factor, while stability was significantly improved in many instances. These results highlight the great potential of mineralization of immobilized enzymes to improve their properties, as well as the great interactions that immobilization protocol and mineralization can exhibit. The combination of both methodologies greatly increases the possibilities to find a biocatalyst that can be suitable for a specific process.ElsevierUniversidad Complutense de Madrid20222022-12-0120222022-12-01journal articlehttp://purl.org/coar/resource_type/c_6501VoRhttp://purl.org/coar/version/c_970fb48d4fbd8a85info:eu-repo/semantics/articleapplication/pdfhttps://hdl.handle.net/20.500.14352/124790reponame: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:20.500.14352/1247902026-06-02T12:44:21Z
dc.title.none.fl_str_mv The immobilization protocol greatly alters the effects of metal phosphate modification on the activity/stability of immobilized lipases
title The immobilization protocol greatly alters the effects of metal phosphate modification on the activity/stability of immobilized lipases
spellingShingle The immobilization protocol greatly alters the effects of metal phosphate modification on the activity/stability of immobilized lipases
Guimarães, José R.
577.1
572
577.15
544.478
Solid-phase enzyme mineralization
Enzyme stabilization
Tuning enzyme specificity
Bioquímica (Biología)
Biología molecular (Biología)
2403 Bioquímica
2415 Biología Molecular
2302.09 Enzimología
2210.01 Catálisis
title_short The immobilization protocol greatly alters the effects of metal phosphate modification on the activity/stability of immobilized lipases
title_full The immobilization protocol greatly alters the effects of metal phosphate modification on the activity/stability of immobilized lipases
title_fullStr The immobilization protocol greatly alters the effects of metal phosphate modification on the activity/stability of immobilized lipases
title_full_unstemmed The immobilization protocol greatly alters the effects of metal phosphate modification on the activity/stability of immobilized lipases
title_sort The immobilization protocol greatly alters the effects of metal phosphate modification on the activity/stability of immobilized lipases
dc.creator.none.fl_str_mv Guimarães, José R.
Carballares Navarro, Diego
Rocha Martín, Javier
Tardioli, Paulo W.
Fernandez Lafuente, Roberto
author Guimarães, José R.
author_facet Guimarães, José R.
Carballares Navarro, Diego
Rocha Martín, Javier
Tardioli, Paulo W.
Fernandez Lafuente, Roberto
author_role author
author2 Carballares Navarro, Diego
Rocha Martín, Javier
Tardioli, Paulo W.
Fernandez Lafuente, Roberto
author2_role author
author
author
author
dc.contributor.none.fl_str_mv Universidad Complutense de Madrid
dc.subject.none.fl_str_mv 577.1
572
577.15
544.478
Solid-phase enzyme mineralization
Enzyme stabilization
Tuning enzyme specificity
Bioquímica (Biología)
Biología molecular (Biología)
2403 Bioquímica
2415 Biología Molecular
2302.09 Enzimología
2210.01 Catálisis
topic 577.1
572
577.15
544.478
Solid-phase enzyme mineralization
Enzyme stabilization
Tuning enzyme specificity
Bioquímica (Biología)
Biología molecular (Biología)
2403 Bioquímica
2415 Biología Molecular
2302.09 Enzimología
2210.01 Catálisis
description Mineralization of immobilized enzymes has showed to couple the advantages of both processes. Here, the influence of the immobilization protocol on the effects of mineralization has been investigated. The lipases from Thermomyces lanuginosus and Candida rugosa were immobilized on octyl-, vinyl sulfone (VS) octyl (blocked with different nucleophiles) and glutaraldehyde- (at different pH values) agarose beads. The stability, activity and specificity of the biocatalysts were very different, both the differently blocked VS-biocatalysts and the glutaraldehyde biocatalysts prepared at different pH. All biocatalysts were submitted to mineralization using different metals. The activity, specificity and stability effects of the mineralization strongly depended on the enzyme and on the immobilization protocol. For the same enzyme, a mineralization protocol could be negative, positive or present no effect depending on the enzyme immobilization procedure and substrate. In the best cases, activity could be increased by a two-fold factor, while stability was significantly improved in many instances. These results highlight the great potential of mineralization of immobilized enzymes to improve their properties, as well as the great interactions that immobilization protocol and mineralization can exhibit. The combination of both methodologies greatly increases the possibilities to find a biocatalyst that can be suitable for a specific process.
publishDate 2022
dc.date.none.fl_str_mv 2022
2022-12-01
2022
2022-12-01
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/20.500.14352/124790
url https://hdl.handle.net/20.500.14352/124790
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
_version_ 1869408225394163712
score 15.81155

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