Oxidation of flame retardant Tetrabromobisphenol A by a biocatalytic nanofiber of chloroperoxidase

Background: Tetrabromobisphenol (TBBPA), a flame retardant compound, is considered a ubiquitous pollutant, with potential impact on the environment and human health. Several technologies have been applied to accelerate its degradation and minimize environmental impacts. Due to its aromaticity charac...

Descripción completa

Detalles Bibliográficos
Autores: García Zamora, José Luis, Santacruz Vázquez, Verónica, Valera Pérez, Miguel Ángel, Moreira Vilar, María Teresa, Cárdenas Chávez, Diana, Tapia Salazar, Mireya, Torres, Eduardo
Tipo de recurso: artículo
Fecha de publicación:2019
País:España
Institución:Universidad de Santiago de Compostela (USC)
Repositorio:Minerva. Repositorio Institucional de la Universidad de Santiago de Compostela
Idioma:inglés
OAI Identifier:oai:minerva.usc.gal:10347/22163
Acceso en línea:http://hdl.handle.net/10347/22163
Access Level:acceso abierto
id ES_9deeffd07c26885926c6bf118800a2d7
oai_identifier_str oai:minerva.usc.gal:10347/22163
network_acronym_str ES
network_name_str España
repository_id_str
spelling Oxidation of flame retardant Tetrabromobisphenol A by a biocatalytic nanofiber of chloroperoxidaseGarcía Zamora, José LuisSantacruz Vázquez, VerónicaValera Pérez, Miguel ÁngelMoreira Vilar, María TeresaCárdenas Chávez, DianaTapia Salazar, MireyaTorres, EduardoBackground: Tetrabromobisphenol (TBBPA), a flame retardant compound, is considered a ubiquitous pollutant, with potential impact on the environment and human health. Several technologies have been applied to accelerate its degradation and minimize environmental impacts. Due to its aromaticity character, peroxidase enzymes may be employed to carry out its transformation in mild conditions. Therefore, the purpose of this work was to determine the capacity of the enzyme chloroperoxidase (CPO) to oxidize TBBPA in several water samples. Methods: The oxidation capacity of CPO was evaluated in catalytic conditions using water samples from surface and groundwater, as well as effluents from wastewater treatment plants. The biocatalytic performance of CPO was improved due to its immobilization on nanofibers composed of polyvinyl alcohol and chitosan (PVA/chitosan). Results: Free and immobilized CPO were able to transform more than 80% in short reaction times (60 min); producing more biodegradable and less toxic products. Particularly, the immobilized enzyme was catalytically active in a wider range of pH than the free enzyme with the possibility of reusing it up to five times. Conclusions: The biocatalytic oxidation of TBBPA under environmental conditions is highly efficient, even in complex media such as treated effluents of wastewater treatment plantsMDPIUniversidade de Santiago de Compostela. Departamento de Enxeñaría QuímicaÁrea de Enxeñaría e Arquitectura20192019-01-0120192019-01-01journal articlehttp://purl.org/coar/resource_type/c_6501VoRhttp://purl.org/coar/version/c_970fb48d4fbd8a85info:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10347/22163reponame:Minerva. Repositorio Institucional de la Universidad de Santiago de Compostelainstname:Universidad de Santiago de Compostela (USC)InglésengMinisterio de Economía y Competitividad http://dx.doi.org/10.13039/501100003329 Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016 CTQ2016-79461-Ropen accesshttp://purl.org/coar/access_right/c_abf2© 2019 by the authors. Open Access. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/)https://creativecommons.org/licenses/by/4.0/info:eu-repo/semantics/openAccessoai:minerva.usc.gal:10347/221632026-06-15T12:47:27Z
dc.title.none.fl_str_mv Oxidation of flame retardant Tetrabromobisphenol A by a biocatalytic nanofiber of chloroperoxidase
title Oxidation of flame retardant Tetrabromobisphenol A by a biocatalytic nanofiber of chloroperoxidase
spellingShingle Oxidation of flame retardant Tetrabromobisphenol A by a biocatalytic nanofiber of chloroperoxidase
García Zamora, José Luis
title_short Oxidation of flame retardant Tetrabromobisphenol A by a biocatalytic nanofiber of chloroperoxidase
title_full Oxidation of flame retardant Tetrabromobisphenol A by a biocatalytic nanofiber of chloroperoxidase
title_fullStr Oxidation of flame retardant Tetrabromobisphenol A by a biocatalytic nanofiber of chloroperoxidase
title_full_unstemmed Oxidation of flame retardant Tetrabromobisphenol A by a biocatalytic nanofiber of chloroperoxidase
title_sort Oxidation of flame retardant Tetrabromobisphenol A by a biocatalytic nanofiber of chloroperoxidase
dc.creator.none.fl_str_mv García Zamora, José Luis
Santacruz Vázquez, Verónica
Valera Pérez, Miguel Ángel
Moreira Vilar, María Teresa
Cárdenas Chávez, Diana
Tapia Salazar, Mireya
Torres, Eduardo
author García Zamora, José Luis
author_facet García Zamora, José Luis
Santacruz Vázquez, Verónica
Valera Pérez, Miguel Ángel
Moreira Vilar, María Teresa
Cárdenas Chávez, Diana
Tapia Salazar, Mireya
Torres, Eduardo
author_role author
author2 Santacruz Vázquez, Verónica
Valera Pérez, Miguel Ángel
Moreira Vilar, María Teresa
Cárdenas Chávez, Diana
Tapia Salazar, Mireya
Torres, Eduardo
author2_role author
author
author
author
author
author
dc.contributor.none.fl_str_mv Universidade de Santiago de Compostela. Departamento de Enxeñaría Química
Área de Enxeñaría e Arquitectura
description Background: Tetrabromobisphenol (TBBPA), a flame retardant compound, is considered a ubiquitous pollutant, with potential impact on the environment and human health. Several technologies have been applied to accelerate its degradation and minimize environmental impacts. Due to its aromaticity character, peroxidase enzymes may be employed to carry out its transformation in mild conditions. Therefore, the purpose of this work was to determine the capacity of the enzyme chloroperoxidase (CPO) to oxidize TBBPA in several water samples. Methods: The oxidation capacity of CPO was evaluated in catalytic conditions using water samples from surface and groundwater, as well as effluents from wastewater treatment plants. The biocatalytic performance of CPO was improved due to its immobilization on nanofibers composed of polyvinyl alcohol and chitosan (PVA/chitosan). Results: Free and immobilized CPO were able to transform more than 80% in short reaction times (60 min); producing more biodegradable and less toxic products. Particularly, the immobilized enzyme was catalytically active in a wider range of pH than the free enzyme with the possibility of reusing it up to five times. Conclusions: The biocatalytic oxidation of TBBPA under environmental conditions is highly efficient, even in complex media such as treated effluents of wastewater treatment plants
publishDate 2019
dc.date.none.fl_str_mv 2019
2019-01-01
2019
2019-01-01
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 http://hdl.handle.net/10347/22163
url http://hdl.handle.net/10347/22163
dc.language.none.fl_str_mv Inglés
eng
language_invalid_str_mv Inglés
language eng
dc.relation.none.fl_str_mv Ministerio de Economía y Competitividad http://dx.doi.org/10.13039/501100003329 Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016 CTQ2016-79461-R
dc.rights.none.fl_str_mv open access
http://purl.org/coar/access_right/c_abf2
https://creativecommons.org/licenses/by/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
https://creativecommons.org/licenses/by/4.0/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv MDPI
publisher.none.fl_str_mv MDPI
dc.source.none.fl_str_mv reponame:Minerva. Repositorio Institucional de la Universidad de Santiago de Compostela
instname:Universidad de Santiago de Compostela (USC)
instname_str Universidad de Santiago de Compostela (USC)
reponame_str Minerva. Repositorio Institucional de la Universidad de Santiago de Compostela
collection Minerva. Repositorio Institucional de la Universidad de Santiago de Compostela
repository.name.fl_str_mv
repository.mail.fl_str_mv
_version_ 1869414783957073920
score 15.812429

Similares en LA Referencia