Monitoring and control of the release of soluble O2 from H2O2 inside porous enzyme carrier for O2 supply to an immobilized d-amino acid oxidase

While O2 substrate for bio-transformations in bulk liquid is routinely provided from entrained air or O2 gas, tailored solutions of O2 supply are required when the bio-catalysis happens spatially confined to the microstructure of a solid support. Release of soluble O2 from H2O2 by catalase is promis...

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Detalles Bibliográficos
Autores: Schelch, S., Bolívar Bolívar, Juan Manuel, Nidetzky, B.
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:20.500.14352/102213
Acceso en línea:https://hdl.handle.net/20.500.14352/102213
Access Level:acceso abierto
Palabra clave:66.0
620
Bioquímica (Química)
Ingeniería química
23 Química
3302 Tecnología Bioquímica
3303 Ingeniería y Tecnología Químicas
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spelling Monitoring and control of the release of soluble O2 from H2O2 inside porous enzyme carrier for O2 supply to an immobilized d-amino acid oxidaseSchelch, S.Bolívar Bolívar, Juan ManuelNidetzky, B.66.0620Bioquímica (Química)Ingeniería química23 Química3302 Tecnología Bioquímica3303 Ingeniería y Tecnología QuímicasWhile O2 substrate for bio-transformations in bulk liquid is routinely provided from entrained air or O2 gas, tailored solutions of O2 supply are required when the bio-catalysis happens spatially confined to the microstructure of a solid support. Release of soluble O2 from H2O2 by catalase is promising, but spatiotemporal control of the process is challenging to achieve. Here, we show monitoring and control by optical sensing within a porous carrier of the soluble O2 formed by an immobilized catalase upon feeding of H2O2. The internally released O2 is used to drive the reaction of d-amino acid oxidase (oxidation of d-methionine) that is co-immobilized with the catalase in the same carrier. The H2O2 is supplied in portions at properly timed intervals, or continuously at controlled flow rate, to balance the O2 production and consumption inside the carrier so as to maintain the internal O2 concentration in the range of 100–500 µM. Thus, enzyme inactivation by excess H2O2 is prevented and gas formation from the released O2 is avoided at the same time. The reaction rate of the co-immobilized enzyme preparation is shown to depend linearly on the internal O2 concentration up to the air-saturated level. Conversions at a 200 ml scale using varied H2O2 feed rate (0.04–0.18 mmol/min) give the equivalent production rate from d-methionine (200 mM) and achieve rate enhancement by ∼1.55-fold compared to the same oxidase reaction under bubble aeration. Collectively, these results show an integrated strategy of biomolecular engineering for tightly controlled supply of O2 substrate from H2O2 into carrier-immobilized enzymes. By addressing limitations of O2 supply via gas-liquid transfer, especially at the microscale, this can be generally useful to develop specialized process strategies for O2-dependent biocatalytic reactions.Universidad Complutense de Madrid20222022-01-0120222022-01-01journal articlehttp://purl.org/coar/resource_type/c_6501VoRhttp://purl.org/coar/version/c_970fb48d4fbd8a85info:eu-repo/semantics/articleapplication/pdfhttps://hdl.handle.net/20.500.14352/102213reponame: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:20.500.14352/1022132026-06-02T12:44:21Z
dc.title.none.fl_str_mv Monitoring and control of the release of soluble O2 from H2O2 inside porous enzyme carrier for O2 supply to an immobilized d-amino acid oxidase
title Monitoring and control of the release of soluble O2 from H2O2 inside porous enzyme carrier for O2 supply to an immobilized d-amino acid oxidase
spellingShingle Monitoring and control of the release of soluble O2 from H2O2 inside porous enzyme carrier for O2 supply to an immobilized d-amino acid oxidase
Schelch, S.
66.0
620
Bioquímica (Química)
Ingeniería química
23 Química
3302 Tecnología Bioquímica
3303 Ingeniería y Tecnología Químicas
title_short Monitoring and control of the release of soluble O2 from H2O2 inside porous enzyme carrier for O2 supply to an immobilized d-amino acid oxidase
title_full Monitoring and control of the release of soluble O2 from H2O2 inside porous enzyme carrier for O2 supply to an immobilized d-amino acid oxidase
title_fullStr Monitoring and control of the release of soluble O2 from H2O2 inside porous enzyme carrier for O2 supply to an immobilized d-amino acid oxidase
title_full_unstemmed Monitoring and control of the release of soluble O2 from H2O2 inside porous enzyme carrier for O2 supply to an immobilized d-amino acid oxidase
title_sort Monitoring and control of the release of soluble O2 from H2O2 inside porous enzyme carrier for O2 supply to an immobilized d-amino acid oxidase
dc.creator.none.fl_str_mv Schelch, S.
Bolívar Bolívar, Juan Manuel
Nidetzky, B.
author Schelch, S.
author_facet Schelch, S.
Bolívar Bolívar, Juan Manuel
Nidetzky, B.
author_role author
author2 Bolívar Bolívar, Juan Manuel
Nidetzky, B.
author2_role author
author
dc.contributor.none.fl_str_mv Universidad Complutense de Madrid
dc.subject.none.fl_str_mv 66.0
620
Bioquímica (Química)
Ingeniería química
23 Química
3302 Tecnología Bioquímica
3303 Ingeniería y Tecnología Químicas
topic 66.0
620
Bioquímica (Química)
Ingeniería química
23 Química
3302 Tecnología Bioquímica
3303 Ingeniería y Tecnología Químicas
description While O2 substrate for bio-transformations in bulk liquid is routinely provided from entrained air or O2 gas, tailored solutions of O2 supply are required when the bio-catalysis happens spatially confined to the microstructure of a solid support. Release of soluble O2 from H2O2 by catalase is promising, but spatiotemporal control of the process is challenging to achieve. Here, we show monitoring and control by optical sensing within a porous carrier of the soluble O2 formed by an immobilized catalase upon feeding of H2O2. The internally released O2 is used to drive the reaction of d-amino acid oxidase (oxidation of d-methionine) that is co-immobilized with the catalase in the same carrier. The H2O2 is supplied in portions at properly timed intervals, or continuously at controlled flow rate, to balance the O2 production and consumption inside the carrier so as to maintain the internal O2 concentration in the range of 100–500 µM. Thus, enzyme inactivation by excess H2O2 is prevented and gas formation from the released O2 is avoided at the same time. The reaction rate of the co-immobilized enzyme preparation is shown to depend linearly on the internal O2 concentration up to the air-saturated level. Conversions at a 200 ml scale using varied H2O2 feed rate (0.04–0.18 mmol/min) give the equivalent production rate from d-methionine (200 mM) and achieve rate enhancement by ∼1.55-fold compared to the same oxidase reaction under bubble aeration. Collectively, these results show an integrated strategy of biomolecular engineering for tightly controlled supply of O2 substrate from H2O2 into carrier-immobilized enzymes. By addressing limitations of O2 supply via gas-liquid transfer, especially at the microscale, this can be generally useful to develop specialized process strategies for O2-dependent biocatalytic reactions.
publishDate 2022
dc.date.none.fl_str_mv 2022
2022-01-01
2022
2022-01-01
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/20.500.14352/102213
url https://hdl.handle.net/20.500.14352/102213
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.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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