Oxidation of persistent environmental pollutants by a white rot fungus

Science ◽  
1985 ◽  
Vol 228 (4706) ◽  
pp. 1434-1436 ◽  
Author(s):  
J. Bumpus ◽  
M Tien ◽  
D Wright ◽  
S. Aust
2021 ◽  
Vol 12 ◽  
Author(s):  
Jing Si ◽  
Hongfei Ma ◽  
Yongjia Cao ◽  
Baokai Cui ◽  
Yucheng Dai

This study introduces a valuable laccase, designated ThLacc-S, purified from white rot fungus Trametes hirsuta. ThLacc-S is a monomeric protein in nature with a molecular weight of 57.0 kDa and can efficiently metabolize endocrine disrupting chemicals. The enzyme was successfully purified to homogeneity via three consecutive steps consisting of salt precipitation and column chromatography, resulting in a 20.76-fold increase in purity and 46.79% yield, with specific activity of 22.111 U/mg protein. ThLacc-S was deciphered as a novel member of the laccase family and is a rare metalloenzyme that contains cysteine, serine, histidine, and tyrosine residues in its catalytic site, and follows Michaelis-Menten kinetic behavior with a Km and a kcat/Km of 87.466 μM and 1.479 s–1μM–1, respectively. ThLacc-S exerted excellent thermo-alkali stability, since it was markedly active after a 2-h incubation at temperatures ranging from 20 to 70°C and retained more than 50% of its activity after incubation for 72 h in a broad pH range of 5.0–10.0. Enzymatic activities of ThLacc-S were enhanced and preserved when exposed to metallic ions, surfactants, and organic solvents, rendering this novel enzyme of interest as a green catalyst for versatile biotechnological and industrial applications that require these singularities of laccases, particularly biodegradation and bioremediation of environmental pollutants.


Toxins ◽  
2020 ◽  
Vol 12 (8) ◽  
pp. 476 ◽  
Author(s):  
Zhimin Zhou ◽  
Renkuan Li ◽  
Tzi Bun Ng ◽  
Yunyun Lai ◽  
Jie Yang ◽  
...  

Aflatoxin B1 (AFB1) is a known toxic human carcinogen and can be detoxified by laccases, which are multicopper oxidases that convert several environmental pollutants and toxins. In this study, a new laccase that could catalyze AFB1 degradation was purified and identified from the white-rot fungus Cerrena unicolor 6884. The laccase was purified using (NH4)2SO4 precipitation and anion exchange chromatography, and then identified as Lac 2 through zymogram and UHPLC-MS/MS based on the Illumina transcriptome analysis of C. unicolor 6884. Six putative laccase protein sequences were obtained via functional annotation. The lac 2 cDNA encoding a full-length protein of 512 amino acids was cloned and sequenced to expand the fungus laccase gene library for AFB1 detoxification. AFB1 degradation by Lac 2 was conducted in vitro at pH 7.0 and 45 °C for 24 h. The half-life of AFB1 degradation catalyzed by Lac 2 was 5.16 h. Acetosyringone (AS), Syrinagaldehyde (SA) and [2,2′ -azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid)] (ABTS) at 1 mM concentration seemed to be similar mediators for strongly enhancing AFB1 degradation by Lac 2. The product of AFB1 degradation catalyzed by Lac 2 was traced and identified to be Aflatoxin Q1 (AFQ1) based on mass spectrometry data. These findings are promising for a possible application of Lac 2 as a new aflatoxin oxidase in degrading AFB1 present in food and feeds.


2014 ◽  
Vol 97 (5) ◽  
pp. 1416-1420 ◽  
Author(s):  
Hatice Ardag Akdogan ◽  
Merve Canpolat

Abstract White rot fungus participates in biological degradation of many organic environmental pollutants. Also, white rot fungus contains a variety of extracellular enzymes, and these enzymes are used for biological degradation of organic matter. We investigated the biological treatment of synthetic dyes, at a low cost and in the shortest possible time, that are used especially in the dye and textile industries and are important polluting agents in the wastewater discharged into the environment by these industries. For this purpose, removal of Remazol Brillant Blue by Pleurotus ostreatus and Coprinus plicatilis was studied. This dye was removed 100% (dye concentration, 10.0 mg/L) by both organisms. Laccase and manganese peroxidase enzyme activities were also monitored. There was an attempt to identify metabolites via GC/MS at the end of the decolorization. No detectable metabolite was found.


2018 ◽  
Vol 4 (3) ◽  
Author(s):  
Donawati Dkk

Indonesia is a tropical country and the richest country in the world for biodiversity, including fl ora and fauna, invertebrates, phytoplankton, bacteria, and huge number of fungus such as mushrooms, molds, mildews and smuts. White rot fungi is one of the ubiquitous creatures in Indonesia. Results indicated that white rot fungus has ability to degrade successfully some organic pollutansin the environment, such as polycyclic aromatic hydrocarbons (PAH), Polychlorinated Biphenyls (PCB’s), Trinitrotoluence (TNT), and DDT. This organism has ability to release intra and extra-cellular enzymes. There are three important rules in these degradation processes, called lignin modifi ed enzymes (LME’s) including Lignin peroxidase, Mn-dependent peroxidase and Laccase. White rot fungi contains all three enzymes and able to breakdown and mineralize several environmental pollutants into non toxic forms. This paper discuss several processes responsible for this degradation.Key words: White rot fungi, bioremediation, lignin modifi ed enzymes, persistent organic pollutants.


2012 ◽  
Vol 3 (1) ◽  
pp. 20-21
Author(s):  
A.Sangeetha A.Sangeetha ◽  
◽  
K.Thanigai K.Thanigai ◽  
Narasimhamurthy Narasimhamurthy ◽  
S.K.Nath S.K.Nath

2020 ◽  
Vol 93 (9) ◽  
pp. 289-292
Author(s):  
Yumi SHIMIZU ◽  
Shuma SATHO ◽  
Taro NAKAJIMA ◽  
Hiroaki KOUZAI ◽  
Kiminori SHIMIZU

2018 ◽  
Vol 69 (1) ◽  
pp. 38-44
Author(s):  
Nicoleta Mirela Marin ◽  
Olga Tiron ◽  
Luoana Florentina Pascu ◽  
Mihaela Costache ◽  
Mihai Nita Lazar ◽  
...  

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.


1991 ◽  
Vol 24 (3-4) ◽  
pp. 189-198 ◽  
Author(s):  
V. P. Lankinen ◽  
M. M. Inkeröinen ◽  
J. Pellinen ◽  
A. I. Hatakka

Decrease of adsorbable organic chlorine (AOX) is becoming the most important criterion for the efficiency of pulp mill effluent treatment in the 1990s. Two methods, designated MYCOR and MYCOPOR which utilize the white-rot fungus Phanerochaete chrysosporium have earlier been developed for the color removal of pulp mill effluents, but the processes have also a capacity to decrease the amount of chlorinated organic compounds. Lignin peroxidases (ligninases) produced by P. chrvsosporium may dechlorinate chlorinated phenols. In this work possibilities to use selected white-rot fungi in the treatment of E1-stage bleach plant effluent were studied. Phlebia radiata. Phanerochaete chrvsosporium and Merulius (Phlebia) tremellosus were compared in shake flasks for their ability to produce laccase, lignin peroxidase(s) and manganese-dependent peroxidase(s) and to remove color from a medium containing effluent. Softwood bleaching effluents were treated by carrier-immobilized P. radiata in 2 1 bioreactors and a 10 1 BiostatR -fermentor. Dechlorination was followed using Cl ion and AOX determinations. All fungi removed the color of the effluent. In P. radiata cultivations AOX decrease was ca. 4 mg l−1 in one day. Apparent lignin peroxidase activities as determined by veratryl alcohol oxidation method were negligible or zero in a medium with AOX content of ca. 60 mg l−1, prepared using about 20 % (v/v) of softwood effluent. However, the purification of extracellular enzymes implied that large amounts of lignin peroxidases were present in the medium and, after the purification, in active form. Enzyme proteins were separated using anion exchange chromatography, and they were further characterized by electrophoresis (SDS-PAGE) to reveal the kind of enzymes that were present during AOX decrease and color removal. The most characteristic lignin peroxidase isoenzymes in effluent media were LiP2 and LiP3.


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