Yacon (Smallanthus sonchifolius) peel as a promising peroxidase source for the treatment of phenolic wastewater
| Main Author: | |
|---|---|
| Publication Date: | 2022 |
| Other Authors: | , , , , |
| 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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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 |
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info:eu-repo/semantics/publishedVersion |
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info:eu-repo/semantics/article |
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article |
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publishedVersion |
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1878-8181 10.1016/j.bcab.2021.102254 https://repositorio.udesc.br/handle/UDESC/3407 |
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1878-8181 10.1016/j.bcab.2021.102254 |
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https://repositorio.udesc.br/handle/UDESC/3407 |
| dc.language.iso.fl_str_mv |
eng |
| language |
eng |
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Biocatalysis and Agricultural Biotechnology 39 |
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info:eu-repo/semantics/openAccess |
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openAccess |
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