scholarly journals Enzyme degradation mechanism of white rot fungi and its research progress on Refractory Wastewater

2021 ◽  
Vol 237 ◽  
pp. 01002
Author(s):  
ShiYuan Huang ◽  
Sheng Li ◽  
ZhenYu Wang ◽  
SenHuan Lin ◽  
Jian Deng
Keyword(s):  
Phenolic Compounds ◽  
Enzymatic Degradation ◽  
Enzyme System ◽  
Degradation Mechanism ◽  
White Rot Fungi ◽  
White Rot ◽  
Research Progress ◽  
Degrading Enzyme ◽  
Research Status ◽  
Enzyme Degradation

The lignin-degrading enzyme system of white rot fungi is highly efficient and non-specific, and can degrade a variety of pollutants, including dyes, phenolic compounds and pesticides.The article presents an overview of the mechanism of enzymatic degradation of white rot fungi and its research status in several refractory wastewater were described.

Resistance of graft-compatible and graft-incompatible Pseudotsugamenziesii rooted cuttings to Phellinusweirii

1994 ◽  
Vol 24 (5) ◽  
pp. 878-881 ◽  
Author(s):  
James A. Entry ◽  
Nan C. Vance ◽  
Donald L. Copes
Keyword(s):  
Energy Source ◽  
Phenolic Compounds ◽  
White Rot Fungi ◽  
White Rot ◽  
Infection Frequency ◽  
Rooted Cuttings ◽  
Defense Compounds ◽  
Positive Linear Correlation ◽  
Pathogen Response ◽  
Cellulose Concentration

One-year-old rooted cuttings taken from 23- and 26-year-old graft-compatible and graft-incompatible Pseudotsugamenziesii (Mirb.) Franco were inoculated with one of three isolates of Phellinusweirii. After 20 months in a greenhouse, infection frequency and severity were significantly greater in the graft-incompatible cuttings. Cellulose concentration in the root tissue was higher in graft-incompatible than graft-compatible cuttings. Concentrations of lignin, phenolic compounds, and tannins were higher in graft-compatible than graft-incompatible cuttings. Cellulose concentration had a positive linear correlation (r2 = 0.84) with the P. weirii infection rating. The concentration of phenolic compounds and lignin in secondary root tissues was negatively correlated with the infection rating (r = 0.73 and 0.84, respectively). The lignin/cellulose and phenolic/cellulose ratios were negatively correlated with the infection rating of P. weirii infection in a linear relationship (r2 = 0.82 and 0.77, respectively). White-rot fungi cannot use tree defense compounds, such as lignin and phenolics, as the sole energy source; an alternate energy source is necessary to degrade these compounds. The lignin/cellulose and phenolic/cellulose ratios in the roots may be important measurements to explain the host–pathogen response of P. weirii infection.

scholarly journals Cellobiose:Quinone Oxidoreductase, a New Wood-degrading Enzyme from White-rot Fungi.

1974 ◽  
Vol 28b ◽  
pp. 209-214 ◽  
Author(s):  
Ulla Westermark ◽  
Karl-Erik Eriksson ◽  
Kari Daasvatn ◽  
Synnøve Liaaen-Jensen ◽  
Curt R. Enzell ◽  
...  
Keyword(s):  
White Rot Fungi ◽  
White Rot ◽  
Degrading Enzyme

scholarly journals Biodegradation of Olive Mill Effluent by White-Rot Fungi

2021 ◽  
Vol 11 (21) ◽  
pp. 9930
Author(s):  
Ana Isabel Díaz ◽  
Marta Ibañez ◽  
Adriana Laca ◽  
Mario Díaz
Keyword(s):  
Phenolic Compounds ◽  
Phanerochaete Chrysosporium ◽  
Liquid Fraction ◽  
Liquid Waste ◽  
White Rot Fungi ◽  
Extraction Process ◽  
White Rot ◽  
Total Phenolic ◽  
Total Phenolic Compounds ◽  
Two Phase

The liquid fraction from the two-phase extraction process in the olive industry (alperujo), is a waste that contains lignocellulosic organic matter and phenolic compounds, difficult to treat by conventional biological methods. Lignocellulosic enzymes from white-rot fungi can be an interesting solution to break down these recalcitrant compounds and advance the treatment of that waste. In the present work the ability of Phanerochaete chrysosporium to degrade the abovementioned liquid waste (AL) was studied. Experiments were carried out at 26 °C within the optimal pH range 4–6 for 10 days and with and without the addition of glucose, measuring the evolution of COD, BOD5, biodegradability index, reducing sugars, total phenolic compounds, and colour. The results obtained in this study revealed the interest of Phanerochaete chrysosporium for an economical and eco-friendly treatment of alperujo, achieving COD and colour removals around 60%, and 32% of total phenolic compounds degradation, regardless of glucose addition.

scholarly journals Enzyme Activities of Two Recombinant Heme-Containing Peroxidases, Tv DyP1 and Tv VP2, Identified from the Secretome of Trametes versicolor

2018 ◽  
Vol 84 (8) ◽  
Author(s):  
Sawsan Amara ◽  
Thomas Perrot ◽  
David Navarro ◽  
Aurélie Deroy ◽  
Amine Benkhelfallah ◽  
...  
Keyword(s):  
Phenolic Compounds ◽  
White Rot Fungi ◽  
White Rot ◽  
Versatile Peroxidase ◽  
Enzymatic System ◽  
High Tolerance ◽  
Content Type ◽  
Oak Wood ◽  
Ph Range ◽  
Oxidative System

ABSTRACT Trametes versicolor is a wood-inhabiting agaricomycete known for its ability to cause strong white-rot decay on hardwood and for its high tolerance of phenolic compounds. The goal of the present work was to gain insights into the molecular biology and biochemistry of the heme-including class II and dye-decolorizing peroxidases secreted by this fungus. Proteomic analysis of the secretome of T. versicolor BRFM 1218 grown on oak wood revealed a set of 200 secreted proteins, among which were the dye-decolorizing peroxidase Tv DyP1 and the versatile peroxidase Tv VP2. Both peroxidases were heterologously produced in Escherichia coli , biochemically characterized, and tested for the ability to oxidize complex substrates. Both peroxidases were found to be active against several substrates under acidic conditions, and Tv DyP1 was very stable over a relatively large pH range of 2.0 to 6.0, while Tv VP2 was more stable at pH 5.0 to 6.0 only. The thermostability of both enzymes was also tested, and Tv DyP1 was globally found to be more stable than Tv VP2. After 180 min of incubation at temperatures ranging from 30 to 50°C, the activity of Tv VP2 drastically decreased, with 10 to 30% of the initial activity retained. Under the same conditions, Tv DyP1 retained 20 to 80% of its enzyme activity. The two proteins were catalytically characterized, and Tv VP2 was shown to accept a wider range of reducing substrates than Tv DyP1. Furthermore, both enzymes were found to be active against two flavonoids, quercetin and catechin, found in oak wood, with Tv VP2 displaying more rapid oxidation of the two compounds. They were tested for the ability to decolorize five industrial dyes, and Tv VP2 presented a greater ability to oxidize and decolorize the dye substrates than Tv DyP1. IMPORTANCE Trametes versicolor is a wood-inhabiting agaricomycete known for its ability to cause strong white-rot decay on hardwood and for its high tolerance of phenolic compounds. Among white-rot fungi, the basidiomycete T. versicolor has been extensively studied for its ability to degrade wood, specifically lignin, thanks to an extracellular oxidative enzymatic system. The corresponding oxidative system was previously studied in several works for classical lignin and manganese peroxidases, and in this study, two new components of the oxidative system of T. versicolor , one dye-decolorizing peroxidase and one versatile peroxidase, were biochemically characterized in depth and compared to other fungal peroxidases.

scholarly journals Lignin degradation potential and draft genome sequence of Trametes trogii S0301

2019 ◽  
Vol 12 (1) ◽  
Author(s):  
Yuan Liu ◽  
Yuanyuan Wu ◽  
Yu Zhang ◽  
Xulei Yang ◽  
En Yang ◽  
...  
Keyword(s):  
Genome Sequence ◽  
Lignin Degradation ◽  
Draft Genome ◽  
White Rot Fungi ◽  
Small Subunit ◽  
White Rot ◽  
Phylogenetic Position ◽  
Degrading Enzyme ◽  
Wide Range ◽  
Trametes Trogii

Abstract Background Trametes trogii is a member of the white-rot fungi family, which has a unique ability to break down recalcitrant lignin polymers to CO2 and water, and they have enormous potential to biodegrade a wide range of toxic environmental pollutants. Because of its industrial potential, the identification of lignin-degrading enzyme systems in Trametes is an important area of research. Development and utilization of industrial value genes are suffering due to deficiency knowledge of genome available for their manipulation. Results In the present study, Homokaryotic strains of T. trogii S0301 were screened and sequencing by PacBio Sequel II platform. The final draft genome is ~ 39.88 Mb, with a contig N50 size of 2.4 Mb, this was the first genome sequencing and assembly of T. trogii species. Further analyses predicted 14,508 protein-coding genes. Results showed that T. trogii S0301 contains 602 genes encoding CAZymes, include 211 glycoside hydrolase and 117 lignin-degrading family genes, nine laccases related genes. Small subunit ribosomal RNA gene (18S rRNA) sequencing confirms its phylogenetic position. Moreover, T. trogii S0301 has the largest number of cytochromes P450 (CYPs) superfamily genes compare to other fungi. All these results are consistent with enzymatic assays and transcriptome analysis results. We also analyzed other genome characteristics in the T. trogii S0301genome. Conclusion Here, we present a nearly complete genome for T. trogii S0301, which will help elucidate the biosynthetic pathways of the lignin-degrading enzyme, advancing the discovery, characterization, and modification of novel enzymes from this genus. This genome sequence will provide a valuable reference for the investigation of lignin degradation in the Trametes genus.

scholarly journals Dynamics of ligninolytic enzyme production in Ganoderma applanatum depending on cultivation type

2011 ◽  
pp. 327-331
Author(s):  
Jasmina Cilerdzic ◽  
Jelena Vukojevic ◽  
Mirjana Stajic
Keyword(s):  
Raw Materials ◽  
Enzyme System ◽  
White Rot Fungi ◽  
Maximum Level ◽  
Ligninolytic Enzyme ◽  
White Rot ◽  
Versatile Peroxidase ◽  
Submerged Cultivation ◽  
Enzymatic System ◽  
Ganoderma Applanatum

Ganoderma applanatum belongs to the group of white-rot fungi, due to a well-developed ligninolytic enzyme system. White-rot fungi have attracted great scientific attention in recent years, especially with respect to their enzymatic potential for the bioremediation of persistent pollutants. Contrary to G. lucidum, which medicinal properties, as well as ligninolytic enzyme system have been extensively studied, enzymatic system of G. applanatum has not been studied yet. Thus, the aim of this study was to analyze the dynamics of laccase, Mn-dependent peroxidase, and versatile peroxidase activity during submerged and solid state cultivation on two selected plant raw materials. Enzyme activity was determined spectrophotometrically after 7, 10 and 14 days of cultivation. The peak of laccase activity (220.14 Ul-1) was noted after 14 days of submerged wheat straw fermentation. Maximum level of Mn-dependent peroxidase (110.91 Ul-1) and versatile peroxidase (116.20 Ul-1) activity was obtained in the medium with oak sawdust after 14 days of submerged cultivation.

scholarly journals Purification and Characterization of a Nylon-Degrading Enzyme

1998 ◽  
Vol 64 (4) ◽  
pp. 1366-1371 ◽  
Author(s):  
Tetsuya Deguchi ◽  
Yoshihisa Kitaoka ◽  
Masaaki Kakezawa ◽  
Tomoaki Nishida
Keyword(s):  
Reaction Mechanism ◽  
Manganese Peroxidase ◽  
Gel Filtration ◽  
White Rot Fungi ◽  
Exchange Chromatography ◽  
White Rot ◽  
White Rot Fungus ◽  
Extracellular Medium ◽  
Degrading Enzyme ◽  
Key Enzyme

ABSTRACT A nylon-degrading enzyme found in the extracellular medium of a ligninolytic culture of the white rot fungus strain IZU-154 was purified by ion-exchange chromatography, gel filtration chromatography, and hydrophobic chromatography. The characteristics of the purified protein (i.e., molecular weight, absorption spectrum, and requirements for 2,6-dimethoxyphenol oxidation) were identical to those of manganese peroxidase, which was previously characterized as a key enzyme in the ligninolytic systems of many white rot fungi, and this result led us to conclude that nylon degradation is catalyzed by manganese peroxidase. However, the reaction mechanism for nylon degradation differed significantly from the reaction mechanism reported for manganese peroxidase. The nylon-degrading activity did not depend on exogenous H2O2 but nevertheless was inhibited by catalase, and superoxide dismutase inhibited the nylon-degrading activity strongly. These features are identical to those of the peroxidase-oxidase reaction catalyzed by horseradish peroxidase. In addition, α-hydroxy acids which are known to accelerate the manganese peroxidase reaction inhibited the nylon-degrading activity strongly. Degradation of nylon-6 fiber was also investigated. Drastic and regular erosion in the nylon surface was observed, suggesting that nylon is degraded to soluble oligomers and that nylon is degraded selectively.

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