Transformation of Tetracycline by Manganese Peroxidase from <i>Phanerochaete chrysosporium</i>

The negative impacts on the ecosystem of antibiotic residues in the environment have become a global concern. However, little is known about the transformation mechanism of antibiotics by manganese peroxidase (MnP) from microorganisms. This work investigated the transformation characteristics, the a...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Xuemei Sun, Yifei Leng, Duanji Wan, Fengyi Chang, Yu Huang, Zhu Li, Wen Xiong, Jun Wang
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	tetracycline manganese peroxidase antibacterial potency transformation products transformation mechanism Organic chemistry QD241-441
Acceso en línea:	https://doaj.org/article/3872fa00aefc471eb27338d135ca2b52
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:3872fa00aefc471eb27338d135ca2b52
record_format	dspace
spelling	oai:doaj.org-article:3872fa00aefc471eb27338d135ca2b522021-11-25T18:27:22ZTransformation of Tetracycline by Manganese Peroxidase from <i>Phanerochaete chrysosporium</i>10.3390/molecules262268031420-3049https://doaj.org/article/3872fa00aefc471eb27338d135ca2b522021-11-01T00:00:00Zhttps://www.mdpi.com/1420-3049/26/22/6803https://doaj.org/toc/1420-3049The negative impacts on the ecosystem of antibiotic residues in the environment have become a global concern. However, little is known about the transformation mechanism of antibiotics by manganese peroxidase (MnP) from microorganisms. This work investigated the transformation characteristics, the antibacterial activity of byproducts, and the degradation mechanism of tetracycline (TC) by purified MnP from <i>Phanerochaete chrysosporium</i>. The results show that nitrogen-limited and high level of Mn<sup>2+</sup> medium could obtain favorable MnP activity and inhibit the expression of lignin peroxidase by <i>Phanerochaete chrysosporium</i>. The purified MnP could transform 80% tetracycline in 3 h, and the threshold of reaction activator (H<sub>2</sub>O<sub>2</sub>) was about 0.045 mmol L<sup>−1</sup>. After the 3rd cyclic run, the transformation rate was almost identical at the low initial concentration of TC (77.05–88.47%), while it decreased when the initial concentration was higher (49.36–60.00%). The antimicrobial potency of the TC transformation products by MnP decreased throughout reaction time. We identified seven possible degradation products and then proposed a potential TC transformation pathway, which included demethylation, oxidation of the dimethyl amino, decarbonylation, hydroxylation, and oxidative dehydrogenation. These findings provide a novel comprehension of the role of MnP on the fate of antibiotics in nature and may develop a potential technology for tetracycline removal.Xuemei SunYifei LengDuanji WanFengyi ChangYu HuangZhu LiWen XiongJun WangMDPI AGarticletetracyclinemanganese peroxidaseantibacterial potencytransformation productstransformation mechanismOrganic chemistryQD241-441ENMolecules, Vol 26, Iss 6803, p 6803 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	tetracycline manganese peroxidase antibacterial potency transformation products transformation mechanism Organic chemistry QD241-441
spellingShingle	tetracycline manganese peroxidase antibacterial potency transformation products transformation mechanism Organic chemistry QD241-441 Xuemei Sun Yifei Leng Duanji Wan Fengyi Chang Yu Huang Zhu Li Wen Xiong Jun Wang Transformation of Tetracycline by Manganese Peroxidase from <i>Phanerochaete chrysosporium</i>
description	The negative impacts on the ecosystem of antibiotic residues in the environment have become a global concern. However, little is known about the transformation mechanism of antibiotics by manganese peroxidase (MnP) from microorganisms. This work investigated the transformation characteristics, the antibacterial activity of byproducts, and the degradation mechanism of tetracycline (TC) by purified MnP from <i>Phanerochaete chrysosporium</i>. The results show that nitrogen-limited and high level of Mn<sup>2+</sup> medium could obtain favorable MnP activity and inhibit the expression of lignin peroxidase by <i>Phanerochaete chrysosporium</i>. The purified MnP could transform 80% tetracycline in 3 h, and the threshold of reaction activator (H<sub>2</sub>O<sub>2</sub>) was about 0.045 mmol L<sup>−1</sup>. After the 3rd cyclic run, the transformation rate was almost identical at the low initial concentration of TC (77.05–88.47%), while it decreased when the initial concentration was higher (49.36–60.00%). The antimicrobial potency of the TC transformation products by MnP decreased throughout reaction time. We identified seven possible degradation products and then proposed a potential TC transformation pathway, which included demethylation, oxidation of the dimethyl amino, decarbonylation, hydroxylation, and oxidative dehydrogenation. These findings provide a novel comprehension of the role of MnP on the fate of antibiotics in nature and may develop a potential technology for tetracycline removal.
format	article
author	Xuemei Sun Yifei Leng Duanji Wan Fengyi Chang Yu Huang Zhu Li Wen Xiong Jun Wang
author_facet	Xuemei Sun Yifei Leng Duanji Wan Fengyi Chang Yu Huang Zhu Li Wen Xiong Jun Wang
author_sort	Xuemei Sun
title	Transformation of Tetracycline by Manganese Peroxidase from <i>Phanerochaete chrysosporium</i>
title_short	Transformation of Tetracycline by Manganese Peroxidase from <i>Phanerochaete chrysosporium</i>
title_full	Transformation of Tetracycline by Manganese Peroxidase from <i>Phanerochaete chrysosporium</i>
title_fullStr	Transformation of Tetracycline by Manganese Peroxidase from <i>Phanerochaete chrysosporium</i>
title_full_unstemmed	Transformation of Tetracycline by Manganese Peroxidase from <i>Phanerochaete chrysosporium</i>
title_sort	transformation of tetracycline by manganese peroxidase from <i>phanerochaete chrysosporium</i>
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/3872fa00aefc471eb27338d135ca2b52
work_keys_str_mv	AT xuemeisun transformationoftetracyclinebymanganeseperoxidasefromiphanerochaetechrysosporiumi AT yifeileng transformationoftetracyclinebymanganeseperoxidasefromiphanerochaetechrysosporiumi AT duanjiwan transformationoftetracyclinebymanganeseperoxidasefromiphanerochaetechrysosporiumi AT fengyichang transformationoftetracyclinebymanganeseperoxidasefromiphanerochaetechrysosporiumi AT yuhuang transformationoftetracyclinebymanganeseperoxidasefromiphanerochaetechrysosporiumi AT zhuli transformationoftetracyclinebymanganeseperoxidasefromiphanerochaetechrysosporiumi AT wenxiong transformationoftetracyclinebymanganeseperoxidasefromiphanerochaetechrysosporiumi AT junwang transformationoftetracyclinebymanganeseperoxidasefromiphanerochaetechrysosporiumi
_version_	1718411127064363008

Transformation of Tetracycline by Manganese Peroxidase from <i>Phanerochaete chrysosporium</i>

Ejemplares similares