scholarly journals Introducing a Thermo-Alkali-Stable, Metallic Ion-Tolerant Laccase Purified From White Rot Fungus Trametes hirsuta

2021 ◽  
Vol 12 ◽  
Author(s):  
Jing Si ◽  
Hongfei Ma ◽  
Yongjia Cao ◽  
Baokai Cui ◽  
Yucheng Dai
Keyword(s):  
Specific Activity ◽  
Endocrine Disrupting Chemicals ◽  
Environmental Pollutants ◽  
Fold Increase ◽  
Industrial Applications ◽  
White Rot ◽  
White Rot Fungus ◽  
Metallic Ions ◽  
Trametes Hirsuta ◽  
Ph Range

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.

scholarly journals Cerrena unicolor Laccases, Genes Expression and Regulation of Activity

Biomolecules ◽  
2021 ◽  
Vol 11 (3) ◽  
pp. 468
Author(s):  
Anna Pawlik ◽  
Beata Ciołek ◽  
Justyna Sulej ◽  
Andrzej Mazur ◽  
Przemysław Grela ◽  
...  
Keyword(s):  
Laccase Activity ◽  
Environmental Changes ◽  
Specific Activity ◽  
Electrochemical Analysis ◽  
White Rot ◽  
White Rot Fungus ◽  
Cerrena Unicolor ◽  
Genes Expression ◽  
Regulation Of Activity ◽  
Laccase Genes

A white rot fungus Cerrena unicolor has been identified as an important source of laccase, unfortunately regulation of this enzyme genes expression is poorly understood. Using 1D and 2D PAGE and LC-MS/MS, laccase isoenzymes were investigated in the liquid filtrate of C. unicolor culture. The level of expression of laccase genes was measured using qPCR. The elevated concentrations of copper and manganese in the medium caused greatest change in genes expression and three laccase transcripts were significantly affected after culture temperature was decreased from 28 to 4 °C or increased to 40 °C. The small differences in the PAGE band intensities of individual laccase proteins were also observed, indicating that given compound affect particular laccase’s transcript. Analyses of laccase-specific activity, at all tested conditions, showed the increased activities as compared to the control, suggesting that enzyme is regulated at the post-translational stage. We observed that the aspartic protease purified from C. unicolor, significantly stimulate laccase activity. Moreover, electrochemical analysis of protease-treated laccase sample had 5 times higher redox peaks. The obtained results indicate that laccases released by C. unicolor are regulated at transcriptional, translational, and at the post-translational steps of gene expression helping fungus adapt to the environmental changes.

scholarly journals Biomechanical Pulping of Corn Stalk Rind with a White Rot Fungus – Trametes hirsuta – and the Use of Delignified Corn Stalk Pith as a Pulp Additive

BioResources ◽  
2015 ◽  
Vol 10 (4) ◽  
Author(s):  
Fangfang Wang ◽  
Honglei Chen ◽  
Mingqiang Ai ◽  
Yuzhong Zhang ◽  
Peiji Gao ◽  
...  
Keyword(s):  
White Rot ◽  
White Rot Fungus ◽  
Corn Stalk ◽  
Trametes Hirsuta

scholarly journals Genome Sequencing and Carbohydrate-Active Enzyme (CAZyme) Repertoire of the White Rot Fungus Flammulina elastica

2018 ◽  
Vol 19 (8) ◽  
pp. 2379 ◽  
Author(s):  
Young-Jin Park ◽  
Yong-Un Jeong ◽  
Won-Sik Kong
Keyword(s):  
Gene Prediction ◽  
Gc Content ◽  
Industrial Applications ◽  
Fungal Species ◽  
Amino Acid Sequences ◽  
Glycoside Hydrolases ◽  
White Rot ◽  
White Rot Fungus ◽  
Carbohydrate Binding ◽  
Carbohydrate Binding Modules

Next-generation sequencing (NGS) of the Flammulina elastica (wood-rotting basidiomycete) genome was performed to identify carbohydrate-active enzymes (CAZymes). The resulting assembly (31 kmer) revealed a total length of 35,045,521 bp (49.7% GC content). Using the AUGUSTUS tool, 12,536 total gene structures were predicted by ab initio gene prediction. An analysis of orthologs revealed that 6806 groups contained at least one F. elastica protein. Among the 12,536 predicted genes, F. elastica contained 24 species-specific genes, of which 17 genes were paralogous. CAZymes are divided into five classes: glycoside hydrolases (GHs), carbohydrate esterases (CEs), polysaccharide lyases (PLs), glycosyltransferases (GTs), and auxiliary activities (AA). In the present study, annotation of the predicted amino acid sequences from F. elastica genes using the dbCAN CAZyme database revealed 508 CAZymes, including 82 AAs, 218 GHs, 89 GTs, 18 PLs, 59 CEs, and 42 carbohydrate binding modules in the F. elastica genome. Although the CAZyme repertoire of F. elastica was similar to those of other fungal species, the total number of GTs in F. elastica was larger than those of other basidiomycetes. This genome information elucidates newly identified wood-degrading machinery in F. elastica, offers opportunities to better understand this fungus, and presents possibilities for more detailed studies on lignocellulosic biomass degradation that may lead to future biotechnological and industrial applications.

Degradation of endosulfan and endosulfan sulfate by white-rot fungus Trametes hirsuta

2011 ◽  
Vol 57 (4) ◽  
pp. 317-322 ◽  
Author(s):  
Ichiro Kamei ◽  
Kazuhiro Takagi ◽  
Ryuichiro Kondo
Keyword(s):  
White Rot ◽  
White Rot Fungus ◽  
Endosulfan Sulfate ◽  
Trametes Hirsuta

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
Keyword(s):  
Environmental Pollutants ◽  
White Rot ◽  
White Rot Fungus ◽  
Persistent Environmental Pollutants

scholarly journals A New Laccase of Lac 2 from the White Rot Fungus Cerrena unicolor 6884 and Lac 2-Mediated Degradation of Aflatoxin B1

Toxins ◽  
2020 ◽  
Vol 12 (8) ◽  
pp. 476 ◽  
Author(s):  
Zhimin Zhou ◽  
Renkuan Li ◽  
Tzi Bun Ng ◽  
Yunyun Lai ◽  
Jie Yang ◽  
...  
Keyword(s):  
Aflatoxin B1 ◽  
Environmental Pollutants ◽  
Anion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Mass Spectrometry Data ◽  
White Rot ◽  
White Rot Fungus ◽  
Multicopper Oxidases ◽  
Cerrena Unicolor

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.

Comparison of Remazol Brillant Blue Removal from Wastewater by Two Different Organisms and Analysis of Metabolites by GC/MS

2014 ◽  
Vol 97 (5) ◽  
pp. 1416-1420 ◽  
Author(s):  
Hatice Ardag Akdogan ◽  
Merve Canpolat
Keyword(s):  
Biological Treatment ◽  
Extracellular Enzymes ◽  
Low Cost ◽  
Environmental Pollutants ◽  
White Rot ◽  
White Rot Fungus ◽  
Synthetic Dyes ◽  
Biological Degradation ◽  
Peroxidase Enzyme ◽  
Textile Industries

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.

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