Transcriptome analysis reveals self-redox mineralization mechanism of azo dyes and novel decolorizing hydrolases in Aspergillus tabacinus LZ-M. (15th May 2023)
- Record Type:
- Journal Article
- Title:
- Transcriptome analysis reveals self-redox mineralization mechanism of azo dyes and novel decolorizing hydrolases in Aspergillus tabacinus LZ-M. (15th May 2023)
- Main Title:
- Transcriptome analysis reveals self-redox mineralization mechanism of azo dyes and novel decolorizing hydrolases in Aspergillus tabacinus LZ-M
- Authors:
- Yu, Xuan
Mao, Chunlan
Zong, Simin
Khan, Aman
Wang, Wenxue
Yun, Hui
Zhang, Peng
Shigaki, Toshiro
Fang, Yitian
Han, Huawen
Li, Xiangkai - Abstract:
- Abstract: Bio-degradation is the most affordable method of azo dye decontamination, while its drawbacks such as aromatic amines accumulation and low degradation efficiency must be overcome. In this study, a novel mechanism of azo dye degradation by a fungus was discovered. At a concentration of 400 mg/L, the decolorization efficiency of Acid Red 73 (AR73) by Aspergillus tabacinus LZ-M was 90.28%. Metabolite analysis and transcriptome sequencing analysis revealed a self-redox process of AR73 degradation, where the electrons generated in carbon oxidation were transferred to the reduction of -C-N = and –NN. The metabolites, 2-hydroxynaphthalene and N-phenylnitrous amide were mineralized into CO2 through catechol pathway and a glycolytic process. Furthermore, the mineralization ratio of dye was computed to be 31.8% by the carbon balance and electron balance. By using comparative transcriptome, a novel decoloring enzyme Ord95 was discovered in unknown genes through gene cloning. It hydrolyzed AR73 into 2-hydroxynaphthalene and N-phenylnitrous amide, containing a glutathione S-transferase domain with three arginines as key active sites. Here the new mechanism of azo dye degradation was discovered with identification of a novel enzyme in Aspergillus tabacinus LZ-M. Graphical abstract: Image 1 Highlights: AcId red 73 (AR73) was mineralized by A. tabacinus LZ-M under anaerobic condition. The self-redox mechanism of AR73 degradation was revealed firstly. New hydrolase Ord95 was foundAbstract: Bio-degradation is the most affordable method of azo dye decontamination, while its drawbacks such as aromatic amines accumulation and low degradation efficiency must be overcome. In this study, a novel mechanism of azo dye degradation by a fungus was discovered. At a concentration of 400 mg/L, the decolorization efficiency of Acid Red 73 (AR73) by Aspergillus tabacinus LZ-M was 90.28%. Metabolite analysis and transcriptome sequencing analysis revealed a self-redox process of AR73 degradation, where the electrons generated in carbon oxidation were transferred to the reduction of -C-N = and –NN. The metabolites, 2-hydroxynaphthalene and N-phenylnitrous amide were mineralized into CO2 through catechol pathway and a glycolytic process. Furthermore, the mineralization ratio of dye was computed to be 31.8% by the carbon balance and electron balance. By using comparative transcriptome, a novel decoloring enzyme Ord95 was discovered in unknown genes through gene cloning. It hydrolyzed AR73 into 2-hydroxynaphthalene and N-phenylnitrous amide, containing a glutathione S-transferase domain with three arginines as key active sites. Here the new mechanism of azo dye degradation was discovered with identification of a novel enzyme in Aspergillus tabacinus LZ-M. Graphical abstract: Image 1 Highlights: AcId red 73 (AR73) was mineralized by A. tabacinus LZ-M under anaerobic condition. The self-redox mechanism of AR73 degradation was revealed firstly. New hydrolase Ord95 was found for cleaving -C-N = in AR73 at initial step. Intermediate metabolites were degraded via catechol pathway and glycolysis process. … (more)
- Is Part Of:
- Environmental pollution. Volume 325(2023)
- Journal:
- Environmental pollution
- Issue:
- Volume 325(2023)
- Issue Display:
- Volume 325, Issue 2023 (2023)
- Year:
- 2023
- Volume:
- 325
- Issue:
- 2023
- Issue Sort Value:
- 2023-0325-2023-0000
- Page Start:
- Page End:
- Publication Date:
- 2023-05-15
- Subjects:
- Azo dyes -- Aspergillus -- Mechanism -- Decolorizing enzyme
Pollution -- Periodicals
Pollution -- Environmental aspects -- Periodicals
Environmental Pollution -- Periodicals
Pollution -- Périodiques
Pollution -- Aspect de l'environnement -- Périodiques
Pollution -- Effets physiologiques -- Périodiques
Pollution
Pollution -- Environmental aspects
Periodicals
Electronic journals
363.73 - Journal URLs:
- http://www.sciencedirect.com/science/journal/02697491 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.envpol.2023.121459 ↗
- Languages:
- English
- ISSNs:
- 0269-7491
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3791.539000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 26890.xml