Yacon (Smallanthus sonchifolius) peel as a promising peroxidase source for the treatment of phenolic wastewater

Bibliographic Details
Main Author: Souza D.H.*
Publication Date: 2022
Other Authors: Fernandes M., de Lourdes Borba Magalhaes M.*, Kempka, Aniela Pinto, Trevisan, Viviane, Skoronski, Everton
Format: Article
Language: eng
Source: Repositório Institucional da Udesc
Download full: https://repositorio.udesc.br/handle/UDESC/3407
Summary: © 2021 Elsevier LtdPeroxidases are versatile enzymes that catalyse the oxidation of many inorganic and organic substrates. There are numerous vegetable sources of peroxidases, including the yacon (Smallanthus sonchifolius), an easy-to-grow plant. This study aimed to extract, purify and characterise the peroxidases obtained from yacon roots. We partially purified the enzyme from yacon pell using an aqueous two-phase system (ATPS) and obtained 4.66 purification-fold and 33.87% activity recovery. The enzyme showed an optimal temperature of catalysis 60 °C and optimal pH 11 using pyrogallol as substrate. Considering the oxidation of 2,4-dichlorophenol, these conditions were 37.5 °C and pH 7. Furthermore, the enzyme presented substrate inhibition at high hydrogen peroxide concentrations. The presence of 5 mM Cu2+ inhibited, while and 5 mM Co2+ activated the enzyme. The enzyme remained stable at 50 °C for 60 min and showed improved thermostability compared to horseradish peroxidase. The kinetic mechanism of yacon peroxidase was investigated, and our studies suggested the enzyme follows a Ping-Pong Bi–Bi mechanism. Finally, 2,4-dichlorophenol was selected as a target pollutant, and we obtained as many as 86.26% of bioconversion using yacon peroxidase. The results presented in this article suggest that yacon is a promising source of peroxidase and can be an alternative for bioprocesses applications.
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spelling Yacon (Smallanthus sonchifolius) peel as a promising peroxidase source for the treatment of phenolic wastewater© 2021 Elsevier LtdPeroxidases are versatile enzymes that catalyse the oxidation of many inorganic and organic substrates. There are numerous vegetable sources of peroxidases, including the yacon (Smallanthus sonchifolius), an easy-to-grow plant. This study aimed to extract, purify and characterise the peroxidases obtained from yacon roots. We partially purified the enzyme from yacon pell using an aqueous two-phase system (ATPS) and obtained 4.66 purification-fold and 33.87% activity recovery. The enzyme showed an optimal temperature of catalysis 60 °C and optimal pH 11 using pyrogallol as substrate. Considering the oxidation of 2,4-dichlorophenol, these conditions were 37.5 °C and pH 7. Furthermore, the enzyme presented substrate inhibition at high hydrogen peroxide concentrations. The presence of 5 mM Cu2+ inhibited, while and 5 mM Co2+ activated the enzyme. The enzyme remained stable at 50 °C for 60 min and showed improved thermostability compared to horseradish peroxidase. The kinetic mechanism of yacon peroxidase was investigated, and our studies suggested the enzyme follows a Ping-Pong Bi–Bi mechanism. Finally, 2,4-dichlorophenol was selected as a target pollutant, and we obtained as many as 86.26% of bioconversion using yacon peroxidase. The results presented in this article suggest that yacon is a promising source of peroxidase and can be an alternative for bioprocesses applications.2024-12-05T23:11:16Z2022info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article1878-818110.1016/j.bcab.2021.102254https://repositorio.udesc.br/handle/UDESC/3407Biocatalysis and Agricultural Biotechnology39Souza D.H.*Fernandes M.de Lourdes Borba Magalhaes M.*Kempka, Aniela PintoTrevisan, VivianeSkoronski, Evertonengreponame:Repositório Institucional da Udescinstname:Universidade do Estado de Santa Catarina (UDESC)instacron:UDESCinfo:eu-repo/semantics/openAccess2024-12-07T20:41:37Zoai:repositorio.udesc.br:UDESC/3407Biblioteca Digital de Teses e Dissertaçõeshttps://pergamumweb.udesc.br/biblioteca/index.phpPRIhttps://repositorio-api.udesc.br/server/oai/requestri@udesc.bropendoar:63912024-12-07T20:41:37Repositório Institucional da Udesc - Universidade do Estado de Santa Catarina (UDESC)false
dc.title.none.fl_str_mv Yacon (Smallanthus sonchifolius) peel as a promising peroxidase source for the treatment of phenolic wastewater
title Yacon (Smallanthus sonchifolius) peel as a promising peroxidase source for the treatment of phenolic wastewater
spellingShingle Yacon (Smallanthus sonchifolius) peel as a promising peroxidase source for the treatment of phenolic wastewater
Souza D.H.*
title_short Yacon (Smallanthus sonchifolius) peel as a promising peroxidase source for the treatment of phenolic wastewater
title_full Yacon (Smallanthus sonchifolius) peel as a promising peroxidase source for the treatment of phenolic wastewater
title_fullStr Yacon (Smallanthus sonchifolius) peel as a promising peroxidase source for the treatment of phenolic wastewater
title_full_unstemmed Yacon (Smallanthus sonchifolius) peel as a promising peroxidase source for the treatment of phenolic wastewater
title_sort Yacon (Smallanthus sonchifolius) peel as a promising peroxidase source for the treatment of phenolic wastewater
author Souza D.H.*
author_facet Souza D.H.*
Fernandes M.
de Lourdes Borba Magalhaes M.*
Kempka, Aniela Pinto
Trevisan, Viviane
Skoronski, Everton
author_role author
author2 Fernandes M.
de Lourdes Borba Magalhaes M.*
Kempka, Aniela Pinto
Trevisan, Viviane
Skoronski, Everton
author2_role author
author
author
author
author
dc.contributor.author.fl_str_mv Souza D.H.*
Fernandes M.
de Lourdes Borba Magalhaes M.*
Kempka, Aniela Pinto
Trevisan, Viviane
Skoronski, Everton
description © 2021 Elsevier LtdPeroxidases are versatile enzymes that catalyse the oxidation of many inorganic and organic substrates. There are numerous vegetable sources of peroxidases, including the yacon (Smallanthus sonchifolius), an easy-to-grow plant. This study aimed to extract, purify and characterise the peroxidases obtained from yacon roots. We partially purified the enzyme from yacon pell using an aqueous two-phase system (ATPS) and obtained 4.66 purification-fold and 33.87% activity recovery. The enzyme showed an optimal temperature of catalysis 60 °C and optimal pH 11 using pyrogallol as substrate. Considering the oxidation of 2,4-dichlorophenol, these conditions were 37.5 °C and pH 7. Furthermore, the enzyme presented substrate inhibition at high hydrogen peroxide concentrations. The presence of 5 mM Cu2+ inhibited, while and 5 mM Co2+ activated the enzyme. The enzyme remained stable at 50 °C for 60 min and showed improved thermostability compared to horseradish peroxidase. The kinetic mechanism of yacon peroxidase was investigated, and our studies suggested the enzyme follows a Ping-Pong Bi–Bi mechanism. Finally, 2,4-dichlorophenol was selected as a target pollutant, and we obtained as many as 86.26% of bioconversion using yacon peroxidase. The results presented in this article suggest that yacon is a promising source of peroxidase and can be an alternative for bioprocesses applications.
publishDate 2022
dc.date.none.fl_str_mv 2022
2024-12-05T23:11:16Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv 1878-8181
10.1016/j.bcab.2021.102254
https://repositorio.udesc.br/handle/UDESC/3407
identifier_str_mv 1878-8181
10.1016/j.bcab.2021.102254
url https://repositorio.udesc.br/handle/UDESC/3407
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Biocatalysis and Agricultural Biotechnology
39
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.source.none.fl_str_mv reponame:Repositório Institucional da Udesc
instname:Universidade do Estado de Santa Catarina (UDESC)
instacron:UDESC
instname_str Universidade do Estado de Santa Catarina (UDESC)
instacron_str UDESC
institution UDESC
reponame_str Repositório Institucional da Udesc
collection Repositório Institucional da Udesc
repository.name.fl_str_mv Repositório Institucional da Udesc - Universidade do Estado de Santa Catarina (UDESC)
repository.mail.fl_str_mv ri@udesc.br
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