Multienzyme coimmobilization on triheterofunctional supports

IImmobilized multienzyme systems are gaining momentum in applied biocatalysis; however, the coimmobilization of several enzymes on one carrier is still challenging. In this work, we exploited a heterofunctional support activated with three different chemical functionalities to immobilize a wide vari...

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Autores: Santiago-Arcos, J., Velasco-Lozano, S., López-Gallego, F.
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2023
País:España
Institución:Universidad de Zaragoza
Repositorio:Zaguán. Repositorio Digital de la Universidad de Zaragoza
OAI Identifier:oai:zaguan.unizar.es:127004
Acceso en línea:http://zaguan.unizar.es/record/127004
Access Level:acceso abierto
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spelling Multienzyme coimmobilization on triheterofunctional supportsSantiago-Arcos, J.Velasco-Lozano, S.López-Gallego, F.IImmobilized multienzyme systems are gaining momentum in applied biocatalysis; however, the coimmobilization of several enzymes on one carrier is still challenging. In this work, we exploited a heterofunctional support activated with three different chemical functionalities to immobilize a wide variety of different enzymes. This support is based on agarose microbeads activated with aldehyde, amino, and cobalt chelate moieties that allow a fast and irreversible immobilization of enzymes, enhancing the thermostability of most of the heterogeneous biocatalysts (up to 21-fold higher than the soluble one). Furthermore, this trifunctional support serves to efficiently coimmobilize a multienzyme system composed of an alcohol dehydrogenase, a reduced nicotinamide adenine dinucleotide (NADH) oxidase, and a catalase. The confined multienzymatic system demonstrates higher performance than its free counterpart, achieving a total turnover number (TTN) of 1 × 105 during five batch consecutive cycles. We envision this solid material as a platform for coimmobilizing multienzyme systems with enhanced properties to catalyze stepwise biotransformations.2023info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfhttp://zaguan.unizar.es/record/127004reponame:Zaguán. Repositorio Digital de la Universidad de Zaragozainstname:Universidad de ZaragozaInglésinfo:eu-repo/grantAgreement/ES/AEI/MDM-2017-0720info:eu-repo/grantAgreement/EC/H2020/818089This project has received funding from the European Union’s Horizon 2020 research and innovation program under grant agreement No H2020 818089-METACELLinfo:eu-repo/grantAgreement/ES/MCIU/RTI2018-094398-B-I00info:eu-repo/grantAgreement/ES/MINECO/PCI2018-092984info:eu-repo/semantics/openAccessoai:zaguan.unizar.es:1270042026-05-29T13:59:51Z
dc.title.none.fl_str_mv Multienzyme coimmobilization on triheterofunctional supports
title Multienzyme coimmobilization on triheterofunctional supports
spellingShingle Multienzyme coimmobilization on triheterofunctional supports
Santiago-Arcos, J.
title_short Multienzyme coimmobilization on triheterofunctional supports
title_full Multienzyme coimmobilization on triheterofunctional supports
title_fullStr Multienzyme coimmobilization on triheterofunctional supports
title_full_unstemmed Multienzyme coimmobilization on triheterofunctional supports
title_sort Multienzyme coimmobilization on triheterofunctional supports
dc.creator.none.fl_str_mv Santiago-Arcos, J.
Velasco-Lozano, S.
López-Gallego, F.
author Santiago-Arcos, J.
author_facet Santiago-Arcos, J.
Velasco-Lozano, S.
López-Gallego, F.
author_role author
author2 Velasco-Lozano, S.
López-Gallego, F.
author2_role author
author
description IImmobilized multienzyme systems are gaining momentum in applied biocatalysis; however, the coimmobilization of several enzymes on one carrier is still challenging. In this work, we exploited a heterofunctional support activated with three different chemical functionalities to immobilize a wide variety of different enzymes. This support is based on agarose microbeads activated with aldehyde, amino, and cobalt chelate moieties that allow a fast and irreversible immobilization of enzymes, enhancing the thermostability of most of the heterogeneous biocatalysts (up to 21-fold higher than the soluble one). Furthermore, this trifunctional support serves to efficiently coimmobilize a multienzyme system composed of an alcohol dehydrogenase, a reduced nicotinamide adenine dinucleotide (NADH) oxidase, and a catalase. The confined multienzymatic system demonstrates higher performance than its free counterpart, achieving a total turnover number (TTN) of 1 × 105 during five batch consecutive cycles. We envision this solid material as a platform for coimmobilizing multienzyme systems with enhanced properties to catalyze stepwise biotransformations.
publishDate 2023
dc.date.none.fl_str_mv 2023
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
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status_str publishedVersion
dc.identifier.none.fl_str_mv http://zaguan.unizar.es/record/127004
url http://zaguan.unizar.es/record/127004
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv info:eu-repo/grantAgreement/ES/AEI/MDM-2017-0720
info:eu-repo/grantAgreement/EC/H2020/818089
This project has received funding from the European Union’s Horizon 2020 research and innovation program under grant agreement No H2020 818089-METACELL
info:eu-repo/grantAgreement/ES/MCIU/RTI2018-094398-B-I00
info:eu-repo/grantAgreement/ES/MINECO/PCI2018-092984
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
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dc.source.none.fl_str_mv reponame:Zaguán. Repositorio Digital de la Universidad de Zaragoza
instname:Universidad de Zaragoza
instname_str Universidad de Zaragoza
reponame_str Zaguán. Repositorio Digital de la Universidad de Zaragoza
collection Zaguán. Repositorio Digital de la Universidad de Zaragoza
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