scholarly journals Self-Sustaining Bioelectrochemical Cell from Fungal Degradation of Lignin-Rich Agrowaste

Energies ◽  
2021 ◽  
Vol 14 (8) ◽  
pp. 2098
Author(s):  
Asiah Sukri ◽  
Raihan Othman ◽  
Firdaus Abd-Wahab ◽  
Noraini M. Noor
Keyword(s):  
Ligninolytic Enzymes ◽  
Linear Sweep Voltammetry ◽  
White Rot ◽  
White Rot Fungus ◽  
Air Electrode ◽  
Prolonged Duration ◽  
Specific Affinity ◽  
Metabolic Activities ◽  
Laccase Enzyme

The present work describes a self-sustaining bioelectrochemical system that adopts simple cell configurations and operates in uncontrolled ambient surroundings. The microbial fuel cell (MFC) was comprised of white-rot fungus of Phanaerochaete chrysosporium fed with oil palm empty fruit bunch (EFB) as the substrate. This fungal strain degrades lignin by producing ligninolytic enzymes such as laccase, which demonstrates a specific affinity for oxygen as its electron acceptor. By simply pairing zinc and the air electrode in a membraneless, single-chamber, 250-mL enclosure, electricity could be harvested. The microbial zinc/air cell is capable of sustaining a 1 mA discharge current continuously for 44 days (i.e., discharge capacity of 1056 mAh). The role of the metabolic activities of P. chrysosporium on EFB towards the MFC’s performance is supported by linear sweep voltammetry measurement and scanning electron microscopy observations. The ability of the MFC to sustain its discharge for a prolonged duration despite the fungal microbes not being attached to the air electrode is attributed to the formation of a network of filamentous hyphae under the submerged culture. Further, gradual lignin decomposition by fungal inocula ensures a continuous supply of laccase enzyme and radical oxidants to the MFC. These factors promote a self-sustaining MFC devoid of any control features.

scholarly journals Degradation of Diuron byPhanerochaete chrysosporium: Role of Ligninolytic Enzymes and Cytochrome P450

2013 ◽  
Vol 2013 ◽  
pp. 1-9 ◽  
Author(s):  
Jaqueline da Silva Coelho-Moreira ◽  
Adelar Bracht ◽  
Aline Cristine da Silva de Souza ◽  
Roselene Ferreira Oliveira ◽  
Anacharis Babeto de Sá-Nakanishi ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Manganese Peroxidase ◽  
Culture Medium ◽  
Ligninolytic Enzymes ◽  
White Rot ◽  
White Rot Fungus ◽  
Metabolites Production ◽  
Herbicide Diuron

The white-rot fungusPhanerochaete chrysosporiumwas investigated for its capacity to degrade the herbicide diuron in liquid stationary cultures. The presence of diuron increased the production of lignin peroxidase in relation to control cultures but only barely affected the production of manganese peroxidase. The herbicide at the concentration of 7 μg/mL did not cause any reduction in the biomass production and it was almost completely removed after 10 days. Concomitantly with the removal of diuron, two metabolites, DCPMU [1-(3,4-dichlorophenyl)-3-methylurea] and DCPU [(3,4-dichlorophenyl)urea], were detected in the culture medium at the concentrations of 0.74 μg/mL and 0.06 μg/mL, respectively. Crude extracellular ligninolytic enzymes were not efficient in thein vitrodegradation of diuron. In addition, 1-aminobenzotriazole (ABT), a cytochrome P450 inhibitor, significantly inhibited both diuron degradation and metabolites production. Significant reduction in the toxicity evaluated by theLactuca sativaL. bioassay was observed in the cultures after 10 days of cultivation. In conclusion,P. chrysosporiumcan efficiently metabolize diuron without the accumulation of toxic products.

Synergistic Methodology Based on Ion Exchange and Biodegradation Mechanisms Applied for Metal Complex Dye Removal from Waste Waters

2018 ◽  
Vol 69 (1) ◽  
pp. 38-44
Author(s):  
Nicoleta Mirela Marin ◽  
Olga Tiron ◽  
Luoana Florentina Pascu ◽  
Mihaela Costache ◽  
Mihai Nita Lazar ◽  
...  
Keyword(s):  
Ion Exchange ◽  
Synergistic Effects ◽  
Freundlich Isotherm ◽  
White Rot ◽  
White Rot Fungus ◽  
Basic Anion Exchange Resin ◽  
Km Value ◽  
Points Of View ◽  
Basic Anion

This study investigates the synergistic effects of ion exchange and biodegradation methods to remove the Acid Blue 193 also called Gryfalan Navy Blue RL (GNB) dye from wastewater. Ion exchange studies were performed using a strongly basic anion exchange resin Amberlite IRA 400. The equilibrium was characterized by a kinetic and thermodynamic points of view, establishing that the sorption of the GNB dye was subject to the Freundlich isotherm model with R2 = 0.8710. Experimental results showed that the activated resin can removed up to 93.4% when the concentration of dye solution is 5.62�10-2 mM. The biodegradation of the GNB was induced by laccase, an enzyme isolated from white-rot fungus. It was also analyzed the role of pH and dye concentration on GNB biodegradation, so 5�10-2 mM dye had a maximum discoloration efficiency of 82.9% at pH of 4. The laccase showed a very fast and robust activity reaching in a few minutes a Km value of 2.2�10-1mM. In addition, increasing the GNB concentration up to 8�10-1 mM did not triggered a substrat inhibition effect on the laccase activity. Overall, in this study we proposed a mixt physicochemical and biological approach to enhance the GNB removal and biodegradability from the wastewaters and subsequently the environment.

scholarly journals Role of ligninolytic enzymes of white rot fungi (Pleurotus spp.) grown with azo dyes

SpringerPlus ◽  
2016 ◽  
Vol 5 (1) ◽  
Author(s):  
Prashant D. Kunjadia ◽  
Gaurav V. Sanghvi ◽  
Anju P. Kunjadia ◽  
Pratap N. Mukhopadhyay ◽  
Gaurav S. Dave
Keyword(s):  
Azo Dyes ◽  
White Rot Fungi ◽  
Ligninolytic Enzymes ◽  
White Rot

scholarly journals Transcriptomics analysis reveals the high biodegradation efficiency of white-rot fungus Phanerochaete sordida YK-624 on native lignin

2020 ◽  
Author(s):  
Jianqiao Wang ◽  
Tomohiro Suzuki ◽  
Hideo Dohra ◽  
Toshio Mori ◽  
Hirokazu Kawagishi ◽  
...  
Keyword(s):  
Gene Expression ◽  
Lignin Degradation ◽  
Ligninolytic Enzymes ◽  
Organic Matrix ◽  
Tca Cycle ◽  
Underlying Mechanism ◽  
White Rot ◽  
White Rot Fungus ◽  
Lignin Biodegradation ◽  
Phanerochaete Sordida

Abstract Background Lignocellulosic biomass is an organic matrix composed of cellulose, hemicellulose, and lignin. In nature, lignin degradation by basidiomycetes is the key step in lignocellulose decay. The white-rot fungus Phanerochaete sordida YK-624 (YK-624) has been extensively studied due to its high lignin degradation ability. In our previous study, it was demonstrated that YK-624 can secrete lignin peroxidase and manganese peroxidase for lignin degradation. However, the underlying mechanism for lignin degradation by YK-624 remains unknown.Results Here, we analyzed YK-624 gene expression following growth under ligninolytic and nonligninolytic conditions and compared the differentially expressed genes in YK-624 to those in the model white-rot fungus P. chrysosporium by next-generation sequencing. More ligninolytic enzymes and lignin-degrading auxiliary enzymes were upregulated in YK-624. This might explain the high degradation efficiency of YK-624. In addition, the genes involved in energy metabolism pathways, such as the TCA cycle, oxidative phosphorylation, lipid metabolism, carbon metabolism and glycolysis, were upregulated under ligninolytic conditions in YK-624.Conclusions In the present study, the first differential gene expression analysis of YK-624 under ligninolytic and nonligninolytic conditions was reported. The results obtained in this study indicated that YK-624 produces more energy- and lignin-degrading enzymes for more efficient lignin biodegradation.

scholarly journals The Mechanism of Degradation of Alizarin Red by a White-Rot Fungus (Lenzites Gibbosa)

2021 ◽  
Author(s):  
Jian Zhang ◽  
YuJie Chi ◽  
Lianrong Feng
Keyword(s):  
Metabolic Pathway ◽  
Intermediate Product ◽  
Degradation Process ◽  
White Rot ◽  
White Rot Fungus ◽  
Alizarin Red ◽  
Anthraquinone Dye ◽  
Key Enzymes ◽  
Important Intermediate ◽  
Laccase Enzyme

Abstract Background Alizarin red (AR) is a typical anthraquinone dye, and the resulting wastewater is toxic and difficult to remove. A study showed that the white rot fungus Lenzites gibbosa (L. gibbosa) can degrade dye wastewater by decolorization and has evolved its own enzyme-producing traits. Methods In this study, transcriptome sequencing was performed after alizarin red treatment for 0, 3, 7, 10, and 14 h. The key pathways and key enzymes involved in alizarin red degradation were found to be though the analysis of KEGG, GO and COG. The GST, MnP and Laccase enzyme activities of L. gibbosa treated with alizarin red for 0–14 h were detected. LC-MS and GC-MS analyses of alizarin red decomposition products after 7 h and 14 h were performed. Results The glutathione metabolic pathway ko00480, and the key enzymes GST, MnP, Laccase and CYP450 were selected. Most of the genes encoding these enzymes were upregulated under alizarin red conditions. The GST activity increased 1.8 times from 117.55 U/mg prot at 0 h to 217.03 U/mg prot at 14 h. The MnP activity increased 2.9 times from 6.45 U/L to 18.55U/L. The Laccase activity increased 3.7 times from 7.22 U/L to 27.28 U/L. Analysis of the alizarin red decolourization rate showed that the decolourization rate at 14 h reached 20.21%. The main degradation intermediates were found to be 1,4-butene diacid, phthalic acid, 1,1-diphenylethylene, 9,10-dihydroanthracene, 1,2-naphthalene dicarboxylic acid, bisphenol, benzophenol-5,2-butene, acrylaldehyde, and 1-butylene, and the degradation process of AR was inferred. Overall, 1,4-butene diacid is the most important intermediate product produced by AR degradation. Conclusions The glutathione metabolic pathway was the key pathway for AR degradation. GST, MnP, Laccase and CYP450 were the key enzymes for AR degradation. 1,4-butene diacid is the most important intermediate product. This study explored the process of AR biodegradation at the molecular and biochemical levels and provided a theoretical basis for its application in practical production.

scholarly journals Secretion of Ligninolytic Enzymes by the White Rot Fungus Stereum Ostrea Immobilized on Polyurethane Cubes Under the Influence of Chlorpyrifos

2017 ◽  
pp. 265-275
Author(s):  
B. S. Shanthi Kumari ◽  
Kanderi Dileep Kumar ◽  
K. Y. Usha ◽  
A. Ramya ◽  
B. Rajasekhar Reddy
Keyword(s):  
Ligninolytic Enzymes ◽  
White Rot ◽  
White Rot Fungus

Investigation of the role of 3-hydroxyanthranilic acid in the degradation of lignin by white-rot fungus Pycnoporus cinnabarinus

2001 ◽  
Vol 28 (4-5) ◽  
pp. 301-307 ◽  
Author(s):  
Kaichang Li ◽  
Peter S Horanyi ◽  
Robert Collins ◽  
Robert S Phillips ◽  
Karl-Erik L Eriksson
Keyword(s):  
White Rot ◽  
White Rot Fungus ◽  
Pycnoporus Cinnabarinus ◽  
Hydroxyanthranilic Acid

scholarly journals Optimization of Laccase from Ganoderma lucidum Decolorizing Remazol Brilliant Blue R and Glac1 as Main Laccase-Contributing Gene

Molecules ◽  
2019 ◽  
Vol 24 (21) ◽  
pp. 3914 ◽  
Author(s):  
Peng Qin ◽  
Yuetong Wu ◽  
Bilal Adil ◽  
Jie Wang ◽  
Yunfu Gu ◽  
...  
Keyword(s):  
Ganoderma Lucidum ◽  
Reactive Dye ◽  
White Rot ◽  
Brilliant Blue ◽  
White Rot Fungus ◽  
Protein Mass ◽  
Remazol Brilliant Blue R ◽  
Protein Mass Spectrometry ◽  
Laccase Enzyme

Many dyes and pigments are used in textile and printing industries, and their wastewater has been classed as a top source of pollution. Biodegradation of dyes by fungal laccase has great potential. In this work, the influence of reaction time, pH, temperature, dye concentration, metal ions, and mediators on laccase-catalyzed Remazol Brilliant Blue R dye (RBBR) decolorization were investigated in vitro using crude laccase from the white-rot fungus Ganoderma lucidum. The optimal decolorization percentage (50.3%) was achieved at 35 °C, pH 4.0, and 200 ppm RBBR in 30 min. The mediator effects from syringaldehyde, 1-hydroxybenzotriazole, and vanillin were compared, and 0.1 mM vanillin was found to obviously increase the decolorization percentage of RBBR to 98.7%. Laccase-mediated decolorization percentages significantly increased in the presence of 5 mM Na+ and Cu2+, and decolorization percentages reached 62.4% and 62.2%, respectively. Real-time fluorescence-quantitative PCR (RT-PCR) and protein mass spectrometry results showed that among the 15 laccase isoenzyme genes, Glac1 was the main laccase-contributing gene, contributing the most to the laccase enzyme activity and decolorization process. These results also indicate that under optimal conditions, G. lucidum laccases, especially Glac1, have a strong potential to remove RBBR from reactive dye effluent.

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