Multiple co-interactions of different parameters on the functional properties of immobilized lipases

In order to determine possible co-interactions between enzyme-support effects, and the influence of enzyme-enzyme interactions on their effects on the final enzyme properties, lipase B from Candida antarctica was immobilized on different supports, initially immobilized via interfacial activation, at...

Full description

Bibliographic Details
Authors: Abellanas-Pérez, Pedro, Andrades, Diandra de, Alcántara León, Andrés Rafael, López-Gallego, Fernando, Rocha Martín, Javier, Polizeli, Maria de Lourdes Teixeira de Moraes, Fernández-Lafuente, Roberto
Format: article
Publication Date:2025
Country:España
Institution:Universidad Complutense de Madrid (UCM)
Repository:Docta Complutense
Language:English
OAI Identifier:oai:docta.ucm.es:20.500.14352/124817
Online Access:https://hdl.handle.net/20.500.14352/124817
Access Level:Open access
Keyword:577
663.12
Lipase immobilization
Interfacial activation
Lipase tuning
Support effect
Loading effect
Co-interactions
Bioquímica (Biología)
Biotecnología
Microbiología (Biología)
2403 Bioquímica
2302.09 Enzimología
2302.27 Proteínas
2415 Biología Molecular
3206 Ciencias de la Nutrición
id ES_56ac4de2d0344566f85d84ea11059593
oai_identifier_str oai:docta.ucm.es:20.500.14352/124817
network_acronym_str ES
network_name_str España
repository_id_str
spelling Multiple co-interactions of different parameters on the functional properties of immobilized lipasesAbellanas-Pérez, PedroAndrades, Diandra deAlcántara León, Andrés RafaelLópez-Gallego, FernandoRocha Martín, JavierPolizeli, Maria de Lourdes Teixeira de MoraesFernández-Lafuente, Roberto577663.12Lipase immobilizationInterfacial activationLipase tuningSupport effectLoading effectCo-interactionsBioquímica (Biología)BiotecnologíaMicrobiología (Biología)2403 Bioquímica2302.09 Enzimología2302.27 Proteínas2415 Biología Molecular3206 Ciencias de la NutriciónIn order to determine possible co-interactions between enzyme-support effects, and the influence of enzyme-enzyme interactions on their effects on the final enzyme properties, lipase B from Candida antarctica was immobilized on different supports, initially immobilized via interfacial activation, at low and saturating enzyme loadings. The used supports were octyl, amino-hexyl-, and the heterofunctional ones obtained by modification with divinyl sulfone, (blocking agents used were ethylenediamine or Gly). The different biocatalysts activities were analyzed using p-nitro phenyl butyrate, triacetin and R and S methyl mandelate. The comparison of the biocatalyst as a function of the activity depended on the utilized substrate. In some instances, the effects of the enzyme-enzyme interactions were reflected by the increase in specific enzyme activity (even by a factor over 3). Regarding the stability, the support and the enzyme loading defined this, and all changed when comparing the stabilities of the biocatalysts in phosphate or Tris, where depending on the enzyme loading the most stable biocatalysts could be either one or the other. Fluorescence studies suggested (mainly intensity at the maximal emission wavelength) that the enzymes present different conformations and that the inactivation on Tris and phosphate follows different pathways, and this also depended on enzyme loading.ElsevierUniversidad Complutense de Madrid20252025-08-1320252025-08-13journal articlehttp://purl.org/coar/resource_type/c_6501VoRhttp://purl.org/coar/version/c_970fb48d4fbd8a85info:eu-repo/semantics/articleapplication/pdfhttps://hdl.handle.net/20.500.14352/124817reponame: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:20.500.14352/1248172026-06-02T12:44:21Z
dc.title.none.fl_str_mv Multiple co-interactions of different parameters on the functional properties of immobilized lipases
title Multiple co-interactions of different parameters on the functional properties of immobilized lipases
spellingShingle Multiple co-interactions of different parameters on the functional properties of immobilized lipases
Abellanas-Pérez, Pedro
577
663.12
Lipase immobilization
Interfacial activation
Lipase tuning
Support effect
Loading effect
Co-interactions
Bioquímica (Biología)
Biotecnología
Microbiología (Biología)
2403 Bioquímica
2302.09 Enzimología
2302.27 Proteínas
2415 Biología Molecular
3206 Ciencias de la Nutrición
title_short Multiple co-interactions of different parameters on the functional properties of immobilized lipases
title_full Multiple co-interactions of different parameters on the functional properties of immobilized lipases
title_fullStr Multiple co-interactions of different parameters on the functional properties of immobilized lipases
title_full_unstemmed Multiple co-interactions of different parameters on the functional properties of immobilized lipases
title_sort Multiple co-interactions of different parameters on the functional properties of immobilized lipases
dc.creator.none.fl_str_mv Abellanas-Pérez, Pedro
Andrades, Diandra de
Alcántara León, Andrés Rafael
López-Gallego, Fernando
Rocha Martín, Javier
Polizeli, Maria de Lourdes Teixeira de Moraes
Fernández-Lafuente, Roberto
author Abellanas-Pérez, Pedro
author_facet Abellanas-Pérez, Pedro
Andrades, Diandra de
Alcántara León, Andrés Rafael
López-Gallego, Fernando
Rocha Martín, Javier
Polizeli, Maria de Lourdes Teixeira de Moraes
Fernández-Lafuente, Roberto
author_role author
author2 Andrades, Diandra de
Alcántara León, Andrés Rafael
López-Gallego, Fernando
Rocha Martín, Javier
Polizeli, Maria de Lourdes Teixeira de Moraes
Fernández-Lafuente, Roberto
author2_role author
author
author
author
author
author
dc.contributor.none.fl_str_mv Universidad Complutense de Madrid
dc.subject.none.fl_str_mv 577
663.12
Lipase immobilization
Interfacial activation
Lipase tuning
Support effect
Loading effect
Co-interactions
Bioquímica (Biología)
Biotecnología
Microbiología (Biología)
2403 Bioquímica
2302.09 Enzimología
2302.27 Proteínas
2415 Biología Molecular
3206 Ciencias de la Nutrición
topic 577
663.12
Lipase immobilization
Interfacial activation
Lipase tuning
Support effect
Loading effect
Co-interactions
Bioquímica (Biología)
Biotecnología
Microbiología (Biología)
2403 Bioquímica
2302.09 Enzimología
2302.27 Proteínas
2415 Biología Molecular
3206 Ciencias de la Nutrición
description In order to determine possible co-interactions between enzyme-support effects, and the influence of enzyme-enzyme interactions on their effects on the final enzyme properties, lipase B from Candida antarctica was immobilized on different supports, initially immobilized via interfacial activation, at low and saturating enzyme loadings. The used supports were octyl, amino-hexyl-, and the heterofunctional ones obtained by modification with divinyl sulfone, (blocking agents used were ethylenediamine or Gly). The different biocatalysts activities were analyzed using p-nitro phenyl butyrate, triacetin and R and S methyl mandelate. The comparison of the biocatalyst as a function of the activity depended on the utilized substrate. In some instances, the effects of the enzyme-enzyme interactions were reflected by the increase in specific enzyme activity (even by a factor over 3). Regarding the stability, the support and the enzyme loading defined this, and all changed when comparing the stabilities of the biocatalysts in phosphate or Tris, where depending on the enzyme loading the most stable biocatalysts could be either one or the other. Fluorescence studies suggested (mainly intensity at the maximal emission wavelength) that the enzymes present different conformations and that the inactivation on Tris and phosphate follows different pathways, and this also depended on enzyme loading.
publishDate 2025
dc.date.none.fl_str_mv 2025
2025-08-13
2025
2025-08-13
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/20.500.14352/124817
url https://hdl.handle.net/20.500.14352/124817
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_ 1869408396917080064
score 15,812429

Similar Items