A cluster of genes encoding major isozymes of lignin peroxidase and manganese peroxidase from the white-rot fungus Trametes versicolor

Gene ◽  
1996 ◽  
Vol 170 (1) ◽  
pp. 31-38 ◽  
Author(s):  
Tomas Johansson ◽  
Per Olof Nyman
Keyword(s):  
Lignin Peroxidase ◽  
Manganese Peroxidase ◽  
Trametes Versicolor ◽  
White Rot ◽  
White Rot Fungus ◽  
Genes Encoding

Decoloration of Amaranth by the white-rot fungusTrametes versicolor. Part I. Statistical analysis

2007 ◽  
Vol 53 (2) ◽  
pp. 313-326 ◽  
Author(s):  
Mihaela Gavril ◽  
Peter V. Hodson ◽  
Jim McLellan
Keyword(s):  
Regression Analysis ◽  
Lignin Peroxidase ◽  
Manganese Peroxidase ◽  
Trametes Versicolor ◽  
Stepwise Regression ◽  
White Rot ◽  
White Rot Fungus ◽  
Percent Concentration ◽  
The Relationship ◽  
Decoloration Rate

The white-rot fungus Trametes versicolor decolorized the mono-azo-substituted naphthalenic dye Amaranth. The relationship between the amount of enzymes present in the system and the efficiency of the decoloration process was investigated. The two responses used to quantify the process of decoloration (i.e., initial decoloration rate, v0, and the percent concentration of dye decolorized in 1 h, %c) were correlated with the amount of three enzymes considered for the study (lignin peroxidase, manganese peroxidase, and laccase) and analyzed through stepwise regression analysis (forward, backward, and mixed). The results of the correlation analysis and those of the regression analysis indicated that lignin peroxidase is the enzyme having the greatest influence on the two responses.

scholarly journals Ligninolytic activity of Phlebiopsis gigantea strains in cultivation on Norway spruce wood

2019 ◽  
Vol 25 (1) ◽  
pp. 15-24
Author(s):  
Anna Zolciak
Keyword(s):  
Norway Spruce ◽  
Lignin Peroxidase ◽  
Manganese Peroxidase ◽  
Protocatechuic Acid ◽  
Extracellular Enzymes ◽  
White Rot ◽  
Versatile Peroxidase ◽  
White Rot Fungus ◽  
Spruce Wood ◽  
Phlebiopsis Gigantea

Abstract   As a white-rot basidiomycetous and wood-decaying fungus, Phlebiopsis gigantea (Fr.: Fr.) Jülich is able to degrade lignin, cellulose and hemicellulose with a complex set of extracellular enzymes. Enzyme activity of this fungus has not been sufficiently explored. The aim of this study was to assess the activity of laccase and peroxidases as well as the level of micromolecular compounds in P. gigantea strains, grown on pieces of Norway spruce wood (sapwood and heartwood) over 50 days of incubation under laboratory conditions. Enzymatic activity was determined using spectrophotometry. Phlebiopsis gigantea strains showed laccase (Lacc), manganese peroxidase (MnP), lignin peroxidase (LiP) and versatile peroxidase (VP) activity.  Hydroxy– and methoxyphenols were released during this process also. High levels of MnP activity (from 5.5 to 107.847 mU/μg of protein in cultures on sapwood and from 7.585 to 229.055 mU/μg of protein in cultures on heartwood) were observed in P. gigantea strains, as well as high activity of VP with manganese-oxidizing properties (from 3.36 to 61.708 mU/μg of protein on sapwood and from 1.7 to 254.479 mU/μg of protein on heartwood) compared with the other examined extracellular enzymes. The activity of Lacc ranged from 0 to 0.731 mU/μg of protein on sapwood and from 0 to 0.216 of protein on heartwood. LiP activity was also low and ranged from 0.025 to 0.593 mU/μg of protein on sapwood, and from 0.060 to 1.566 mU/μg of protein on heartwood. The activity of VP in terms of guaiacol-oxidizing properties ranged from 0.016 to 1.432 mU/μg of protein in cultures on sapwood, and from 0.042 to 1.238 mU/μg of protein on heartwood. Released hydroxyphenols for P. gigantea strains ranged from 39.204-129.157 μg of protocatechuic acid/ml in cultures on sapwood, and from 23.098-83.630 μg of protocatechuic acid/ml on heartwood. Methoxyphenols produced by P. gigantea strains ranged from 7.5 to 22.987 μg of vanillin acid/ml on sapwood, and from 10.187 to 36.885 μg of vanillin acid/ml on heartwood. Keywords: white-rot fungus, Phlebiopsis gigantea, laccase, manganese peroxidase, lignin peroxidase, versatile peroxidase, hydroxy–, methoxyphenols.  

The Onset of Lignin-Modifying Enzymes, Decrease of AOX and Color Removal by White-Rot Fungi Grown on Bleach Plant Effluents

1991 ◽  
Vol 24 (3-4) ◽  
pp. 189-198 ◽  
Author(s):  
V. P. Lankinen ◽  
M. M. Inkeröinen ◽  
J. Pellinen ◽  
A. I. Hatakka
Keyword(s):  
Lignin Peroxidase ◽  
Active Form ◽  
White Rot Fungi ◽  
Pulp Mill ◽  
Color Removal ◽  
Effluent Treatment ◽  
White Rot ◽  
White Rot Fungus ◽  
Lignin Peroxidases ◽  
Pulp Mill Effluents

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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