scholarly journals Description of a Versatile Peroxidase Involved in the Natural Degradation of Lignin That Has Both Manganese Peroxidase and Lignin Peroxidase Substrate Interaction Sites

1999 ◽  
Vol 274 (15) ◽  
pp. 10324-10330 ◽  
Author(s):  
Susana Camarero ◽  
Sovan Sarkar ◽  
Francisco Javier Ruiz-Dueñas ◽  
Marı́a Jesús Martı́nez ◽  
Ángel T. Martı́nez
Keyword(s):  
Lignin Peroxidase ◽  
Manganese Peroxidase ◽  
Versatile Peroxidase ◽  
Interaction Sites ◽  
Substrate Interaction ◽  
Natural Degradation

scholarly journals Linking Enzymatic Oxidative Degradation of Lignin to Organics Detoxification

2018 ◽  
Vol 19 (11) ◽  
pp. 3373 ◽  
Author(s):  
Xiaolu Wang ◽  
Bin Yao ◽  
Xiaoyun Su
Keyword(s):  
Redox Potential ◽  
Lignin Peroxidase ◽  
Manganese Peroxidase ◽  
Lignin Degradation ◽  
Oxidative Degradation ◽  
Class Ii ◽  
Substrate Preference ◽  
Versatile Peroxidase

The major enzymes involved in lignin degradation are laccase, class II peroxidases (lignin peroxidase, manganese peroxidase, and versatile peroxidase) and dye peroxidase, which use an oxidative or peroxidative mechanism to deconstruct the complex and recalcitrant lignin. Laccase and manganese peroxidase directly oxidize phenolic lignin components, while lignin peroxidase and versatile peroxidase can act on the more recalcitrant non-phenolic lignin compounds. Mediators or co-oxidants not only increase the catalytic ability of these enzymes, but also largely expand their substrate scope to those with higher redox potential or more complicated structures. Neither laccase nor the peroxidases are stringently selective of substrates. The promiscuous nature in substrate preference can be employed in detoxification of a range of organics.

Two Substrate Interaction Sites in Lignin Peroxidase Revealed by Site-Directed Mutagenesis†

Biochemistry ◽  
1998 ◽  
Vol 37 (43) ◽  
pp. 15097-15105 ◽  
Author(s):  
Wendy A. Doyle ◽  
Wolfgang Blodig ◽  
Nigel C. Veitch ◽  
Klaus Piontek ◽  
Andrew T. Smith
Keyword(s):  
Lignin Peroxidase ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Interaction Sites ◽  
Substrate Interaction

High-yield production of manganese peroxidase, lignin peroxidase, and versatile peroxidase in Phanerochaete chrysosporium

2014 ◽  
Vol 98 (22) ◽  
pp. 9283-9294 ◽  
Author(s):  
Nancy Coconi-Linares ◽  
Denis Magaña-Ortíz ◽  
Doralinda A. Guzmán-Ortiz ◽  
Francisco Fernández ◽  
Achim M. Loske ◽  
...  
Keyword(s):  
Phanerochaete Chrysosporium ◽  
Lignin Peroxidase ◽  
Manganese Peroxidase ◽  
Versatile Peroxidase ◽  
High Yield ◽  
Yield Production ◽  
High Yield Production

scholarly journals Erratum to: High-yield production of manganese peroxidase, lignin peroxidase, and versatile peroxidase in Phanerochaete chrysosporium

2014 ◽  
Vol 98 (22) ◽  
pp. 9519-9519
Author(s):  
Nancy Coconi-Linares ◽  
Denis Magaña-Ortíz ◽  
Doralinda A. Guzmán-Ortiz ◽  
Francisco Fernández ◽  
Achim M. Loske ◽  
...  
Keyword(s):  
Phanerochaete Chrysosporium ◽  
Lignin Peroxidase ◽  
Manganese Peroxidase ◽  
Versatile Peroxidase ◽  
High Yield ◽  
Yield Production ◽  
High Yield Production

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.  

scholarly journals Congo Red Decolorization and Detoxification by Aspergillus niger: Removal Mechanisms and Dye Degradation Pathway

2018 ◽  
Vol 2018 ◽  
pp. 1-9 ◽  
Author(s):  
Nedra Asses ◽  
Lamia Ayed ◽  
Neila Hkiri ◽  
Moktar Hamdi
Keyword(s):  
Molecular Structure ◽  
Aspergillus Niger ◽  
Azo Dyes ◽  
Lignin Peroxidase ◽  
Congo Red ◽  
Manganese Peroxidase ◽  
Dye Degradation ◽  
Degradation Pathway ◽  
Effects Of Ph ◽  
Maximum Decolorization

Congo red is one of the best known and used azo dyes which has two azo bonds (-N=N-) chromophore in its molecular structure. Its structural stability makes it highly toxic and resistant to biodegradation. The objective of this study was to assess the congo red biodegradation and detoxification by Aspergillus niger. The effects of pH, initial dye concentration, temperature, and shaking speed on the decolorization rate and enzymes production were studied. The maximum decolorization was correlated with lignin peroxidase and manganese peroxidase production. Above 97% were obtained when 2 g mycelia were incubated at pH 5, in presence of 200 mg/L of dye during 6 days at 28°C and under 120 to 150 rpm shaking speed. The degraded metabolites were characterized by using LC-MS/MS analyses and the biodegradation mechanism was also studied. Congo red bioconversion formed degradation metabolites mainly by peroxidases activities, i.e., the sodium naphthalene sulfonate (m/z = 227) and the cycloheptadienylium (m/z = 91). Phytotoxicity and microtoxicity tests confirmed that degradation metabolites were less toxic than original dye.

scholarly journals Functional Characterization of Melanin Decolorizing Extracellular Peroxidase of Bjerkandera adusta

2021 ◽  
Vol 7 (9) ◽  
pp. 762
Author(s):  
Jina Baik ◽  
Anwesha Purkayastha ◽  
Kyung Hye Park ◽  
Taek Jin Kang
Keyword(s):  
Lignin Peroxidase ◽  
Functional Characterization ◽  
Veratryl Alcohol ◽  
Storage Conditions ◽  
Versatile Peroxidase ◽  
Bjerkandera Adusta ◽  
Cellular Mechanisms ◽  
Melanin Pigmentation ◽  
Crude Enzyme Preparation

Melanin pigmentation in the human skin results from complicated cellular mechanisms that remain to be entirely understood. Uneven melanin pigmentation has been counteracted by inhibiting synthesis or transfer of melanin in the skin. Recently, an enzymatic approach has been proposed, wherein the melanin in the skin is decolorized using lignin peroxidase. However, not many enzymes are available for decolorizing melanin; the most studied one is lignin peroxidase derived from a lignin degrading fungus, Phanerochaete chrysosporium. Our current study reveals that versatile peroxidase from Bjerkandera adusta can decolorize synthetic melanin. Melanin decolorization was found to be dependent on veratryl alcohol and hydrogen peroxide, but not on Mn2+. The degree of decolorization reached over 40% in 10 min at 37 °C and a pH of 4.5. Optimized storage conditions were slightly different from those for the reaction; crude enzyme preparation was the most stable at 25 °C at pH 5.5. Since the enzyme rapidly lost its activity at 50 °C, stabilizers were screened. As a result, glycerol, a major component in several cosmetic formulations, was found to be a promising excipient. Our results suggest that B. adusta versatile peroxidase can be considered for future cosmetic applications aimed at melanin decolorization.

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