Journal
CHEMOSPHERE
Volume 263, Issue -, Pages -Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.chemosphere.2020.128280
Keywords
2,3,7,8-Tetrachlorodibenzo-p-dioxin; Laccase; Lignin-modifying enzymes; Ligninolytic fungi; Fungal biodegradation; Laccase-mediators
Categories
Funding
- BE-Basic Foundation grant from the Ministry of Economic Affairs from the Netherlands
- Ministry of Science & Technology Vietnam (MOST) [826/QD-BKHCN, DTDLCN 13/14]
Ask authors/readers for more resources
The ligninolytic fungus Rigidoporus sp. FMD21 produces extracellular enzymes, mainly laccases, that can degrade the highly recalcitrant and toxic pollutant 2,3,7,8-TCDD into 3,4-dichlorophenol. Laccase-mediators such as 1-hydroxybenzotriazole (HBT), syringaldehyde (Syr) and violuric acid (Vio) have an equipotent added effect on the degradation of 2,3,7,8-TCDD by the extracellular enzyme extract.
Ligninolytic fungi secrete extracellular lignin-modifying enzymes (LME) that degrade plant polymers for fungal nutrition but that are, because of their broad substrate specificity, also applicable for the degradation of many hazardous pollutants. Laccase is one of the most well characterized LME and is involved in the removal and degradation of recalcitrant aromatic compounds with or without the assistance of laccase-mediators. The Ligninolytic fungus Rigidoporus sp. FMD21 can degrade 2,3,7,8-tetrachlorodibenzo-p-dioxin (2,3,7,8-TCDD) with a half-life of 6.2 days. Using Rigidoporus sp. FMD21 crude extracellular enzyme extract (ExE) that mainly consisted of laccase, 77.4% of 2,3,7,8-TCDD was degraded within 36 days. The degradation rate did not depend on the 2,3,7,8-TCDD concentration in the tested range between 0.005 and 0.5 pgTEQ/mL. 2,3,7,8-TCDD was analysed by DR-CALUX (R) bioassay and the degradation was confirmed by GC-HRMS. In this study, we found evidence for cleavage of the diaryl ether bond in the 2,3,7,8-TCDD molecule and here we propose a new degradation mechanism in which 3,4-dichlorophenol is the main metabolite of 2,3,7,8-TCDD degradation by FMD21's ExE. Six laccase-mediators were tested. Three of them 1-hydroxybenzotriazole (HBT), syringaldehyde (Syr) and violuric acid (Vio) showed an equipotent added effect on 2,3,7,8-TCDD degradation by ExE, however only in case of Vio a level of significance was reached. The others showed no effect or negatively impacted degradation. In conclusion, we have shown that Rigidoporus sp. FMD21 produces extracellular enzymes, mainly laccases that apparently are able to degrade the highly recalcitrant and most toxic 2,3,7,8-congener of TCDD via diaryl bond cleavage into 3,4-dichlorophenol. (C) 2020 Elsevier Ltd. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available