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Reactive Black 5 + H2O2
?
lignin peroxidase can only oxidize Reactive Black 5 in the presence of redox mediators such as veratryl alcohol
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?
veratryl alcohol + H2O2 + H+
veratraldehyde + H2O
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?
1,2-bis(3,4-dimethoxyphenyl)propane-1,3-diol + H2O2
3,4-dimethoxybenzaldehyde + 1-(3,4-dimethyl-phenyl)ethane-1,2-diol + H2O
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?
1-(3,4-diethoxyphenyl)-1,3-dihydroxy-2-(4-methoxy-phenyl)propane + O2 + H2O2
1-(4'-methoxyphenyl)-1,2-dihydroxyethane + 3,4-diethoxybenzaldehyde
1-(3,4-diethoxyphenyl)-1,3-dihydroxy-2-(4-methoxyphenyl)-propane + O2 + H2O2
?
1-(4-ethoxy-3-methoxyphenyl)-1,2-propene + O2 + H2O2
1-(4-ethoxy-3-methoxyphenyl)-1,2-dihydroxypropane
1-(4-ethoxy-3-methoxyphenyl)propane + O2 + H2O2
1-(4-ethoxy-3-methoxyphenyl)1-hydroxypropane
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?
2 veratryl alcohol + H2O2
2 veratryl aldehyde + 2 H2O
2,4-dichlorophenol + H2O2
?
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?
3,4-dimethoxybenzyl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
4,5-dichlorocatechol + H2O2
?
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50 mM sodium tartrate buffer, pH 3.5 at 25°C, hydrogen peroxide concentration is 1 mM, addition of gelatin to the reaction mixtures protected lignin peroxidase from precipitation
formation of water-insoluble oxidation products
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?
4-chlorocatechol + H2O2
?
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50 mM sodium tartrate buffer, pH 3.5 at 25°C, hydrogen peroxide concentration is 1 mM, addition of gelatin to the reaction mixtures protected lignin peroxidase from precipitation
formation of water-insoluble oxidation products
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?
4-methoxymandelic acid + veratryl alcohol
?
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?
4-methylcatechol + H2O2
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50 mM sodium tartrate buffer, pH 3.5 at 25°C, hydrogen peroxide concentration is 3 mM, addition of gelatin to the reaction mixtures protected lignin peroxidase from precipitation
formation of water-insoluble oxidation products
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?
4-methylthio-2-oxobutanoate + H2O2
?
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only in presence of veratryl alcohol, it possibly reacts with a veratryl alcohol radical to produce ethylene
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?
catechol + H2O2
?
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50 mM sodium tartrate buffer, pH 3.5 at 25°C, hydrogen peroxide concentration is 2 mM, addition of gelatin to the reaction mixtures protected lignin peroxidase from precipitation
formation of water-insoluble oxidation products
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?
catechol + H2O2
? + 2 H2O
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dimethoxyphenol + H2O2
? + 2 H2O
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?
fuchsine + H2O2
?
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?
guaiacol + H2O2
? + 2 H2O
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?
melanin + H2O2
?
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pH 3, 40 °C, 15 IU/ml, and 10 h incubation are the optimal conditions for the degradation of the melanin. The use of the mediator veratryl alcohol is effective to enhance the efficacy of the melanin degradation, with up to 92% decolorization, method evaluation and optimization, overview
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mitoxantrone + H2O2
hexahydronaphtho-[2,3-f]-quinoxaline-7,12-dione + H2O
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low efficiency
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?
non-phenolic substrates + H2O2
?
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e.g. 1,2,4-trimethoxybenzene, 4,4'-dimethoxybiphenyl, isoeugenol methylether, 1-(3,4-dimethoxyphenyl)-2-(2, 4-dichlorophenoxyl)-ethanol, guaiacyl glycerolether
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?
oxytetracycline + H2O2
?
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LiP shows strong degrading ability
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pyrogallol red + H2O2
?
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rhodamine B + H2O2
?
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?
syringaldehyde + H2O2
? + 2 H2O
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?
tetracycline + H2O2
?
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LiP shows strong degrading ability
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veratryl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
veratryl alcohol + H2O2
?
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veratryl alcohol + H2O2
veratraldehyde + H2O
veratryl alcohol + H2O2 + H+
veratraldehyde + H2O
xylene cyanol + H2O2
?
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?
additional information
?
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1-(3,4-diethoxyphenyl)-1,3-dihydroxy-2-(4-methoxy-phenyl)propane + O2 + H2O2
1-(4'-methoxyphenyl)-1,2-dihydroxyethane + 3,4-diethoxybenzaldehyde
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?
1-(3,4-diethoxyphenyl)-1,3-dihydroxy-2-(4-methoxy-phenyl)propane + O2 + H2O2
1-(4'-methoxyphenyl)-1,2-dihydroxyethane + 3,4-diethoxybenzaldehyde
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i.e. diarylpropane, lignin-model compound, alpha,beta-cleavage with insertion of a single atom of oxygen from O2 into the alpha-position of the product 1-(4'-methoxyphenyl)-1,2-dihydroxyethane
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?
1-(3,4-diethoxyphenyl)-1,3-dihydroxy-2-(4-methoxyphenyl)-propane + O2 + H2O2
?
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?
1-(3,4-diethoxyphenyl)-1,3-dihydroxy-2-(4-methoxyphenyl)-propane + O2 + H2O2
?
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i.e. diarylpropane, involved in the oxidative breakdown of lignin in white rot basidiomycetes, induced by veratryl alcohol
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?
1-(4-ethoxy-3-methoxyphenyl)-1,2-propene + O2 + H2O2
1-(4-ethoxy-3-methoxyphenyl)-1,2-dihydroxypropane
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olefinic hydroxylation
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?
1-(4-ethoxy-3-methoxyphenyl)-1,2-propene + O2 + H2O2
1-(4-ethoxy-3-methoxyphenyl)-1,2-dihydroxypropane
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olefinic hydroxylation
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?
2 veratryl alcohol + H2O2
2 veratryl aldehyde + 2 H2O
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?
2 veratryl alcohol + H2O2
2 veratryl aldehyde + 2 H2O
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?
2 veratryl alcohol + H2O2
2 veratryl aldehyde + 2 H2O
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?
3,4-dimethoxybenzyl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
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veratryl alcohol
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?
3,4-dimethoxybenzyl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
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veratryl alcohol
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?
3,4-dimethoxybenzyl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
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veratryl alcohol
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?
3,4-dimethoxybenzyl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
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veratryl alcohol
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?
3,4-dimethoxybenzyl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
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veratryl alcohol
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?
veratryl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
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?
veratryl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
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ping pong mechanism
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?
veratryl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
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catalytic activity of lignin peroxidase and partition of veratryl alcohol in sodium bis(2-ethylhexyl)sulfosuccinate /isooctane/toluene/water reverse micelles. Activity depends to a great extent, on the composition of the reverse micelles. Optimum activity occurs at a molar ratio of water to sodium bis(2-ethylhexyl)sulfosuccinate of 11, pH 3.6, and a volume ratio of isooctane to toluene of 79. Under optimum conditions, the half-life of LiP is circa 12 h
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?
veratryl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
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optimum culture conditions
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veratryl alcohol + H2O2
veratraldehyde + H2O
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veratryl alcohol + H2O2
veratraldehyde + H2O
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veratryl alcohol + H2O2 + H+
veratraldehyde + H2O
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?
veratryl alcohol + H2O2 + H+
veratraldehyde + H2O
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synthesis of veratraldehyde from veratryl alcohol by Phanerochaete chrysosporium lignin peroxidase with in situ electrogeneration of hydrogen peroxide in an electroenzymatic reactor
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?
additional information
?
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lignin peroxidase is not able to oxidize phenolic compounds efficiently because of inactivation in the absence of veratryl alcohol or related substrates
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?
additional information
?
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catalyzes non-specifically several oxidations in the alkyl-side-chains of lignin-related compounds, Calpha-Cbeta cleavage in lignin model-compounds
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?
additional information
?
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oxidation of various phenolic and non-phenolic lignin model-compounds
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?
additional information
?
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oxidation of various phenolic and non-phenolic lignin model-compounds
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?
additional information
?
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oxidation of various phenolic and non-phenolic lignin model-compounds
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?
additional information
?
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oxidation of various phenolic and non-phenolic lignin model-compounds
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?
additional information
?
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oxidation of various phenolic and non-phenolic lignin model-compounds
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?
additional information
?
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of the aryl-CalphaHOH-CbetaHR-CgammaH2OH-type (R being aryl or O-aryl)
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?
additional information
?
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intradiol cleavage in phenylglycol structures, hydroxylation of benzylic methylene groups, oxidative coupling of phenols, all reactions require H2O2, Calpha-Cbeta cleavage and methylene hydroxylation involve substrate oxygenation, the oxygen atom originates from O2 not H2O2: thus the enzyme acts as oxygenase which requires H2O2
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?
additional information
?
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intradiol cleavage in phenylglycol structures, hydroxylation of benzylic methylene groups, oxidative coupling of phenols, all reactions require H2O2, Calpha-Cbeta cleavage and methylene hydroxylation involve substrate oxygenation, the oxygen atom originates from O2 not H2O2: thus the enzyme acts as oxygenase which requires H2O2
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?
additional information
?
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with concomitant insertion of 1 atom of molecular oxygen
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?
additional information
?
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with concomitant insertion of 1 atom of molecular oxygen
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?
additional information
?
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oxidation of benzyl alcohols to aldehydes or ketones
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?
additional information
?
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oxidation of benzyl alcohols to aldehydes or ketones
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?
additional information
?
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bioelectric oxidation of organic substrates by LiP immobilized on graphite electrodes: the enzyme can establish direct (i.e. mediatorless) electronic contact with graphite electrodes. In the case of the so called direct electron transfer reaction, the oxidized enzyme is directly reduced by the electrode to the initial ferriperoxidase state. In the presence of an electron donor other than electrode, the two-electron reduction of enzyme form E1 (containing an oxyferryl iron and a porphyrin pi cation radical) to the initial ferriperoxidase occurs through the intermediate formation of enzyme form II by a sequential one-electron transfer from the electron donor. The formed oxidized electron donor is then electrochemically reduced by the electrode. Different mechanisms for the bioelectrocatalysis of the enzyme depend on the chemical nature of the mediators and are of a special interest both for fundamental science and for application of the enzyme as solid-phase bio(electro)catalyst for decomposition/detection of of recalcitrant aromatic compounds
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?
additional information
?
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decolourization of two waterless-soluble aromatic dyes (pyrogallol red and bromopyrogallol red) using lignin peroxidase coupled with glucose oxidase in the medium demonstrates that a higher decolourization percentage is obtained if H2O2 is supplied enzymatically
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?
additional information
?
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the removal mechanism of catechol derivatives seems to be different for each catecholic substrate in terms of substrate consumption and transformation, and of enzyme activity
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?
additional information
?
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selective and efficient lignin peroxidase isozyme H8 catalyzed depolymerization of the phenolic lignin dimer
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additional information
?
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selective and efficient lignin peroxidase isozyme H8 catalyzed depolymerization of the phenolic lignin dimer
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additional information
?
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catalysis of degradation of the dimer to products by an acid-stabilized variant of lignin peroxidase isozyme H8 increases from 38.4% at pH 5.0 to 92.5% at pH 2.6. At pH 2.6, the observed product distribution results from 65.5% beta-O-4' ether bond cleavage, 27.0% Calpha-C1 carbon bond cleavage, and 3.6% Calpha-oxidation as by-product. Enzyme LiPH8 catalyzes the oxidative cleavage of both beta-O-4' ether and C-C bonds in aryl ether dimers and catalyzes breaking of beta-O-4' ether, C-C, and C-H bonds in trimeric lignin model compounds. The distribution of products is pH-dependent. Study catalysis of bond cleavage events in a phenolic lignin dimer by quantitative analysis of product formation during LiPH8-catalyzed degradation of a GGE model compound (GGE-NIMS compound) using nanostructure-initiator mass spectrometry. Low pH conditions drive reaction equilibrium toward the favorable formation of the active cationic radical intermediate. The cationic radical intermediate formed from LiPH8/H2O2-catalyzed 1-electron oxidation of GGE dimer is capable of undergoing a variety of reactions such as side-chain oxidation, C-C bond, and beta-O-4' ether bond cleavage. The intermediates are predicted from a heterolytic bond cleavage reaction mechanism when the first step 1-electron oxidation takes place at lower redox potential-Ring A. The deprotonation of the short-lived cationic radical results in the formation of the phenoxy radical which sequentially cleaved into fragments. Protonation of hydroxyl group under acidic conditions is a key step in bond-cleavage pathways
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additional information
?
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catalysis of degradation of the dimer to products by an acid-stabilized variant of lignin peroxidase isozyme H8 increases from 38.4% at pH 5.0 to 92.5% at pH 2.6. At pH 2.6, the observed product distribution results from 65.5% beta-O-4' ether bond cleavage, 27.0% Calpha-C1 carbon bond cleavage, and 3.6% Calpha-oxidation as by-product. Enzyme LiPH8 catalyzes the oxidative cleavage of both beta-O-4' ether and C-C bonds in aryl ether dimers and catalyzes breaking of beta-O-4' ether, C-C, and C-H bonds in trimeric lignin model compounds. The distribution of products is pH-dependent. Study catalysis of bond cleavage events in a phenolic lignin dimer by quantitative analysis of product formation during LiPH8-catalyzed degradation of a GGE model compound (GGE-NIMS compound) using nanostructure-initiator mass spectrometry. Low pH conditions drive reaction equilibrium toward the favorable formation of the active cationic radical intermediate. The cationic radical intermediate formed from LiPH8/H2O2-catalyzed 1-electron oxidation of GGE dimer is capable of undergoing a variety of reactions such as side-chain oxidation, C-C bond, and beta-O-4' ether bond cleavage. The intermediates are predicted from a heterolytic bond cleavage reaction mechanism when the first step 1-electron oxidation takes place at lower redox potential-Ring A. The deprotonation of the short-lived cationic radical results in the formation of the phenoxy radical which sequentially cleaved into fragments. Protonation of hydroxyl group under acidic conditions is a key step in bond-cleavage pathways
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additional information
?
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lignin peroxidase is an extracellular hemeprotein that is H2O2-dependent, with an unusually high redox potential and low optimum pH. It is capable of oxidizing a variety of reducing substrates, including polymeric substrates. It has the distinction of being able to oxidize methoxylated aromatic rings without a free phenolic group, which generates cation radicals that can react further by a variety of pathways, including ring opening, demethylation, and phenol dimerization. In contrast with laccases, LiP does not require mediators to degrade high redox-potential compounds, but it needs H2O2 to initiate catalysis. Substrate specificity, no or poor activity with ferulic acid, vanillic acid, diaminobenzidine, and HoBT. Purified LiP obtained from immobilized Phanerochaete chrysosporium completely decolorizes bromophenyl blue, bromothymol blue, and bromocresol green, purified enzyme from immobilized Phanerochaete chrysosporium shows increased dye decolorization efficiency compared to the enzyme from non-immobilized Phanerochaete chrysosporium
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additional information
?
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lignin peroxidase isozyme H8 from the white-rot fungus Phanerochaete chrysosporium (LiPH8) demonstrates a high redox potential and can efficiently catalyze the oxidation of veratryl alcohol, as well as the degradation of recalcitrant lignin
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additional information
?
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lignin peroxidase isozyme H8 from the white-rot fungus Phanerochaete chrysosporium (LiPH8) demonstrates a high redox potential and can efficiently catalyze the oxidation of veratryl alcohol, as well as the degradation of recalcitrant lignin
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additional information
?
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partially purified lignin peroxidase is used for the degradation of polyvinyl chloride (PVC) films, a significant reduction in the weight of PVC film is observed (31%), measurement of CO2 as reaction product. FTIR spectra of the enzyme-treated plastic film reveal structural changes in the chemical composition, indicating a specific peak at 2943/cm that correspond to alkenyl C-H stretch. Deterioration on the surface of PVC films is confirmed by scanning electron microscopy tracked through activity assay for the lignin peroxidase
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additional information
?
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the fungal lignin peroxidase does not produce the veratryl alcohol cation radical as a diffusible ligninolytic oxidant. Reaction-diffusion model and solution-phase model, overview. The oxidation of veratryl alcohol (VA) by the enzyme in air at physiological pH 4.5 consumes O2 and produces about 1.1 veratraldehyde per H2O2 supplied. This finding suggests that some VAx02cation radical may escape oxidation at the enzyme's active site, hydrolyzing instead to give benzylic radicals that rapidly add O2. The resulting alpha-hydroxyperoxyl radicals would in turn eliminate the H2O2 precursor HO2 radical, thus accounting for the enhancement in veratraldehyde yield. VA is required for the enzyme to oxidize 4-methoxymandelic acid, which quenches the ESR signal of the VA produced, and veratraldehyde production during these reactions occurs only after all of the 4-methoxymandelic acid has been consumed. Moreover, the rate of 4-methoxymandelic acid oxidation by the enzyme exhibits saturation kinetics as the concentration of VA is increased. Enzymatic oxidations of dye-functionalized beads
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A140G/A243R/A317P
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kcat/Km for 2,4-dichlorophenol is 4fold higher than wild-type value, kcat/Km for H2O2 is 89fold higher than wild-type value
A140G/S190P/P193A/S196F/E208Q
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the variant shows increased 2,4-dichlorophenol degradation activity (ca. 1.6fold) and stability against H2O2. Kcat for H2O2 increases over the wild type value by about 6.5fold, the Km values for H2O2 is lower than wild type value
H102T/S119R/N120T/Q126K/A243R/A315G
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kcat/Km for 2,4-dichlorophenol is fold higher than wild-type value, kcat/Km for H2O2 is 89fold higher than wild-type value
N182D/D183K/A36E
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generating a Mn2+-binding site
P106R/Q210H/L211V/A243R/F255L
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kcat/Km for 2,4-dichlorophenol is 4fold higher than wild-type value, kcat/Km for H2O2 is 89fold higher than wild-type value
P106R/S119R/N120T/S228Y/A272G/L275V/A315G/A317T
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the variant shows increased 2,4-dichlorophenol degradation activity (ca. 1.6fold) and stability against H2O2. Kcat for H2O2 increases over the wild type value by about 6.5fold, the Km values for H2O2 is lower than wild type value
S274L/L275F/A292
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the variant shows increased 2,4-dichlorophenol degradation activity (ca. 1.6fold) and stability against H2O2. Kcat for H2O2 increases over the wild type value by about 6.5fold, the Km values for H2O2 is lower than wild type value
S49C/A67C/H239E
site-directed mutagenesis, improved thermostability of the synthetic LiPH8 variant (PDB ID 6ISS) capable of strengthening the helix-loop interactions under acidic conditions. The mutant retains excellent thermostability at pH 2.5 with a 10fold increase in t1/2 (2.52 h at 25°C) compared with that of the wild-type enzyme. The recombinant LiPH8 variant is the only unique lignin peroxidase containing five disulfide bridges, and the helix-loop interactions of the synthetic disulfide bridge and ionic salt bridge in its structure are responsible for stabilizing the Ca2+-binding region and heme environment, resulting in an increase in overall structural resistance against acidic conditions
W171F
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no activity towards veratryl alcohol
A55R/N156E/H239E
site-directed mutagenesis the triple mutant of LiPH8 with 2 additional saltbridges on the solvent-exposed regions shows excellent stability and oxidation activity under extremely acidic conditions down to pH 2.6. The stabilized mutant shows higher activity levels at all three pH levels tested, as compared to wild-type, with the highest activity at pH 2.6. Increased conversion of lignin dimer, convertion of 96.1% and 45.3% of the dimer at pH 2.6 and pH 5.0, respectively
A55R/N156E/H239E
site-directed mutagenesis, a rationally designed variant, that demonstrates a 12.5fold increased half-life under extremely acidic conditions, 9.9fold increased catalytic efficiency toward veratryl alcohol, and a 7.8fold enhanced lignin model dimer conversion efficiency compared to those of native LiPH8. The mutant has two constructed salt bridges. See for structure: PDB ID 6A6Q. Introduction of strong ionic salt bridges based on computational design results in a LiPH8 variant with markedly improved stability, as well as higher activity under acidic pH conditions
additional information
design of active LiPH8 variants for increased stability in intensively acidic environments. Introduction of new strong salt bridges at effective locations and optimized interactions between charged residues and their environments are vital for active and stable LiP at acidic pH. Molecular dynamics (MD) simulation of the solvated structure under the desired conditions and calculating the Gibbs free energy of the variant are used for creating an acid-stable LiP variant, followed by protein X-ray crystallography
additional information
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design of active LiPH8 variants for increased stability in intensively acidic environments. Introduction of new strong salt bridges at effective locations and optimized interactions between charged residues and their environments are vital for active and stable LiP at acidic pH. Molecular dynamics (MD) simulation of the solvated structure under the desired conditions and calculating the Gibbs free energy of the variant are used for creating an acid-stable LiP variant, followed by protein X-ray crystallography
additional information
engineering of lignin peroxidase isozyme H8 and other enzymes involved in lignin depolymerization including targeting stability at low pH. Catalysis of degradation of the dimer to products by an acid-stabilized variant of lignin peroxidase isozyme H8 increases from 38.4% at pH 5.0 to 92.5% at pH 2.6. At pH 2.6, the observed product distribution results from 65.5% beta-O-4' ether bond cleavage, 27.0% Calpha-C1 carbon bond cleavage, and 3.6% Calpha-oxidation as by-product
additional information
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engineering of lignin peroxidase isozyme H8 and other enzymes involved in lignin depolymerization including targeting stability at low pH. Catalysis of degradation of the dimer to products by an acid-stabilized variant of lignin peroxidase isozyme H8 increases from 38.4% at pH 5.0 to 92.5% at pH 2.6. At pH 2.6, the observed product distribution results from 65.5% beta-O-4' ether bond cleavage, 27.0% Calpha-C1 carbon bond cleavage, and 3.6% Calpha-oxidation as by-product
additional information
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enzyme LiP obtained from a wild isolate of Phanerochaete chrysosporium immobilized on polyurethane foam cubes is purified 21fold using ammonium sulfate precipitation and size exclusion chromatography. The enzyme with a molecular mass of 55 kDa exhibited a considerably higher pH tolerance and thermostability compared with the native enzyme. It shows a strong affinity for the substrate veratryl alcohol and has kinetic constant values of 142.86 micromol and 0.065 mM. inhibited the activity, while ethanol, EDTA, Cu2+, Mn+, Na+, and Fe2+ exhibited induction. Purified LiP completely decolorizes (100%) bromophenyl blue, bromothymol blue, and bromocresol green. The 96% and 72% degradation obtained with phenol and Congo red is also higher compared to crude LiP. Treatment with LiP shows reduction in acid detergent lignin (ADL) as compared to untreated straws, with a maximum of 2.87 units obtained in jowar followed by 2.66 units in paddy straw. The digestibility of all straws increased, the response varying from a maximum of 21.27 units in proso millet to a minimum of 12.32 units obtained in little millet. The enzyme from immobilized organism exhibits an enhanced pH stability compared with the native enzyme obtained in the submerged cultures. It retains over 75% of activity at pH 6.5 for over 15 min
additional information
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fungal metabolites are playing an immense role in developing various sustainable waste treatment processes. Production and characterization of a fungal lignin peroxidase with a potential to degrade polyvinyl chloride, method optimization, overview
additional information
improving the thermostability of LiP in acidic environments is required for effective lignin depolymerization in practical applications
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Paszczynski, A.; Huynh, V.B.; Crawford, R.L.
Comparison of ligninase-I and peroxidase-M2 from the white-rot fungus Phanerochaete chrysosporium
Arch. Biochem. Biophys.
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750-765
1986
Phanerodontia chrysosporium, Phanerodontia chrysosporium BKM-F-1767
brenda
Tien, M.; Kirk, T.K.
Lignin-degrading enzyme from Phanerochaete chrysosporium: Purification, characterization, and catalytic properties of a unique H2O2-requiring oxygenase
Proc. Natl. Acad. Sci. USA
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1984
Phanerodontia chrysosporium, Phanerodontia chrysosporium BKM-F-1767
brenda
Renganathan, V.; Miki, K.; Gold, M.H.
Multiple molecular forms of diarylpropane oxygenase, an H2O2-requiring, lignin-degrading enzyme from Phanerochaete chrysosporium
Arch. Biochem. Biophys.
241
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1985
Phanerodontia chrysosporium
brenda
Andersson, L.A.; Renganathan, V.; Chiu, A.A.; Loehr, T.M.; Gold, M.H.
Spectral characterization of diarylpropane oxygenase, a novel peroxide-dependent, lignin-degrading heme enzyme
J. Biol. Chem.
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1985
Phanerodontia chrysosporium
brenda
Gold, M.H.; Kuwahara, M.; Chiu, A.A.; Glenn, J.K.
Purification and characterization of an extracellular H2O2-requiring diarylpropane oxygenase from the white rot basidiomycete, Phanerochaete chrysosporium
Arch. Biochem. Biophys.
234
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1984
Phanerodontia chrysosporium
brenda
Aitken, M.; Irvine, R.L.
Stability testing of ligninase and Mn-peroxidase from Phanerochaete chrysosporium
Biotechnol. Bioeng.
34
1251-1260
1989
Phanerodontia chrysosporium, Phanerodontia chrysosporium VKM F-1767
brenda
Khindaria, A.; Nie, G.; Aust, S.D.
Detection and characterization of the lignin peroxidase compound II-veratryl alcohol cation radical complex
Biochemistry
36
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1997
Phanerodontia chrysosporium
brenda
Blodig, W.; Smith, A.T.; Doyle, W.A.; Piontek, K.
Crystal structures of pristine and oxidatively processed lignin peroxidase expressed in Escherichia coli and of the W171F variant that eliminates the redox active tryptophan 171. Implications for the reaction mechanism
J. Mol. Biol.
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2001
Phanerodontia chrysosporium
brenda
Mester, T.; Tien, M.
Engineering of a manganese-binding site in lignin peroxidase isozyme H8 from Phanerochaete chrysosporium
Biochem. Biophys. Res. Commun.
284
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2001
Phanerodontia chrysosporium
brenda
Liu, A.; Huang, X.; Song, S.; Wang, D.; Lu, X.; Qu, Y.; Gao, P.
Kinetics of the H2O2-dependent ligninase-catalyzed oxidation of veratryl alcohol in the presence of cationic surfactant studied by spectrophotometric technique
Spectrochim. Acta A
59
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2003
Phanerodontia chrysosporium
brenda
Zhang, W.; Huang, X.; Li, Y.; Qu, Y.; Gao, P.
Catalytic activity of lignin peroxidase and partition of veratryl alcohol in AOT/isooctane/toluene/water reverse micelles
Appl. Microbiol. Biotechnol.
70
315-320
2006
Phanerodontia chrysosporium
brenda
Ferapontova, E.E.; Castillo, J.; Gorton, L.
Bioelectrocatalytic properties of lignin peroxidase from Phanerochaete chrysosporium in reactions with phenols, catechols and lignin-model compounds
Biochim. Biophys. Acta
1760
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2006
Phanerodontia chrysosporium
brenda
Lan, J.; Huang, X.; Hu, M.; Li, Y.; Qu, Y.; Gao, P.; Wu, D.
High efficient degradation of dyes with lignin peroxidase coupled with glucose oxidase
J. Biotechnol.
123
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2006
Phanerodontia chrysosporium
brenda
Pointing, S.B.; Pelling, A.L.; Smith, G.J.; Hyde, K.D.; Reddy, C.A.
Screening of basidiomycetes and xylariaceous fungi for lignin peroxidase and laccase gene-specific sequences
Mycol. Res.
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2005
Trametes versicolor, Trametes coccinea, Trametes sanguinea, Panus sp., Perenniporia medulla-panis, Phanerodontia chrysosporium (P06181), Phanerodontia chrysosporium (P11543), Phanerodontia chrysosporium (Q9UW80), Phanerodontia chrysosporium H10 (P11543), Phanerodontia chrysosporium H2 (Q9UW80), Phanerodontia chrysosporium H8 (P06181)
brenda
Zhang, Y.; Huang, X.R.; Huang, F.; Li, Y.Z.; Qu, Y.B.; Gao, P.J.
Catalytic performance of lignin peroxidase in a novel reverse micelle
Colloids Surf. B Biointerfaces
65
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2008
Phanerodontia chrysosporium
brenda
Ryu, K.; Hwang, S.Y.; Kim, K.H.; Kang, J.H.; Lee, E.K.
Functionality improvement of fungal lignin peroxidase by DNA shuffling for 2,4-dichlorophenol degradability and H2O2 stability
J. Biotechnol.
133
110-115
2008
Phanerodontia chrysosporium
brenda
Ryu, K.; Kang, J.H.; Wang, L.; Lee, E.K.
Expression in yeast of secreted lignin peroxidase with improved 2,4-dichlorophenol degradability by DNA shuffling
J. Biotechnol.
135
241-246
2008
Phanerodontia chrysosporium
brenda
Alam, M.Z.; Mansor, M.F.; Jalal, K.C.
Optimization of decolorization of methylene blue by lignin peroxidase enzyme produced from sewage sludge with Phanerocheate chrysosporium
J. Hazard. Mater.
162
708-715
2009
Phanerodontia chrysosporium
brenda
Cohen, S.; Belinky, P.A.; Hadar, Y.; Dosoretz, C.G.
Characterization of catechol derivative removal by lignin peroxidase in aqueous mixture
Biores. Technol.
100
2247-2253
2009
Phanerodontia chrysosporium
brenda
Qiu, H.; Li, Y.; Ji, G.; Zhou, G.; Huang, X.; Qu, Y.; Gao, P.
Immobilization of lignin peroxidase on nanoporous gold: enzymatic properties and in situ release of H2O2 by co-immobilized glucose oxidase
Biores. Technol.
100
3837-3842
2009
Phanerodontia chrysosporium
brenda
Sharma, J.; Yadav, R.; Singh, N.; Yadav, K.
Secretion and characterisation of ligninperoxidases by some new indigenous lignolytic fungi
Biosci. Biotechnol. Res. Asia
5
673-678
2008
Agaricus campestris, Phanerodontia chrysosporium, Trametes hirsuta, Trametes versicolor, Pleurotus ostreatus, Lentinus sajor-caju, Volvariella volvacea, Tropicoporus linteus, Polyporous velutinus, Trametes elegans, Pleurotus sapidus, Lentinus sajor-caju MTCC 141, Trametes hirsuta MTCC 136, Pleurotus ostreatus MTCC 1803, Trametes versicolor MTCC 138, Pleurotus sapidus MTCC 1807, Volvariella volvacea MTCC 957, Polyporous velutinus MTCC 1813, Trametes elegans MTCC 1812, Agaricus campestris MTCC 972, Tropicoporus linteus MTCC 1175, Phanerodontia chrysosporium MTCC 787
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brenda
Lan, J.; Zhang, Y.; Huang, X.; Hu, M.; Liu, W.; Li, Y.; Qu, Y.; Gao, P.
Improvement of the catalytic performance of lignin peroxidase in reversed micelles
J. Chem. Technol. Biotechnol.
83
64-70
2008
Phanerodontia chrysosporium, Phanerodontia chrysosporium F. F. Lombard / ME-446 / ATCC 43541
-
brenda
Ruiz-Duenas, F.J.; Morales, M.; Garcia, E.; Miki, Y.; Martinez, M.J.; Martinez, A.T.
Substrate oxidation sites in versatile peroxidase and other basidiomycete peroxidases
J. Exp. Bot.
60
441-452
2009
Phanerodontia chrysosporium (P49012)
brenda
Alam, M.Z.; Mansor, M.F.; Jalal, K.C.
Optimization of lignin peroxidase production and stability by Phanerochaete chrysosporium using sewage-treatment-plant sludge as substrate in a stirred-tank bioreactor
J. Ind. Microbiol. Biotechnol.
36
757-764
2009
Phanerodontia chrysosporium
brenda
Wang, P.; Hu, X.; Cook, S.; Begonia, M.; Lee, K.; Hwang, H.
Effect of culture conditions on the production of ligninolytic enzymes by white rot fungi Phanerochaete chrysosporium (ATCC 20696) and separation of its lignin peroxidase
World J. Microbiol. Biotechnol.
24
2205-2212
2008
Phanerodontia chrysosporium, Phanerodontia chrysosporium ATCC 20696
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brenda
Lee, K.; Pi, K.; Lee, K.
Synthesis of veratraldehyde from veratryl alcohol by lignin peroxidase with in situ electrogeneration of hydrogen peroxide in an electrochemical reactor
World J. Microbiol. Biotechnol.
25
1691-1694
2009
Phanerodontia chrysosporium, Phanerodontia chrysosporium ATCC 24725
brenda
Brueck, T.B.; Brueck, D.W.
Oxidative metabolism of the anti-cancer agent mitoxantrone by horseradish, lacto-and lignin peroxidase
Biochimie
93
217-226
2011
Phanerodontia chrysosporium
brenda
Wen, X.; Jia, Y.; Li, J.
Degradation of tetracycline and oxytetracycline by crude lignin peroxidase prepared from Phanerochaete chrysosporium--a white rot fungus
Chemosphere
75
1003-1007
2009
Phanerodontia chrysosporium, Phanerodontia chrysosporium BKM-F-1767
brenda
Tuisel, H.; Sinclair, R.; Bumpus, J.A.; Ashbaugh, W.; Brock, B.J.; Aust, S.D.
Lignin peroxidase H2 from Phanerochaete chrysosporium purification, characterization and stability to temperature and pH
Arch. Biochem. Biophys.
279
158-166
1990
Phanerodontia chrysosporium (P11542), Phanerodontia chrysosporium
brenda
Min, K.; Yum, T.; Kim, J.; Woo, H.M.; Kim, Y.; Sang, B.I.; Yoo, Y.J.; Kim, Y.H.; Um, Y.
Perspectives for biocatalytic lignin utilization cleaving 4-O-5 and Calpha-Cbeta bonds in dimeric lignin model compounds catalyzed by a promiscuous activity of tyrosinase
Biotechnol. Biofuels
10
212
2017
Agaricus bisporus, Phanerodontia chrysosporium
brenda
Vandana, T.; Kumar, S.; Swaraj, S.; Manpal, S.
Purification, characterization, and biodelignification potential of lignin peroxidase from immobilized Phanerochaete chrysosporium
BioResources
14
5380-5399
2019
Phanerodontia chrysosporium
-
brenda
Pham, L.T.M.; Seo, H.; Kim, K.J.; Kim, Y.H.
In silico-designed lignin peroxidase from Phanerochaete chrysosporium shows enhanced acid stability for depolymerization of lignin
Biotechnol. Biofuels
11
325
2018
Phanerodontia chrysosporium (P06181), Phanerodontia chrysosporium
brenda
Pham, L.T.M.; Deng, K.; Northen, T.R.; Singer, S.W.; Adams, P.D.; Simmons, B.A.; Sale, K.L.
Experimental and theoretical insights into the effects of pH on catalysis of bond-cleavage by the lignin peroxidase isozyme H8 from Phanerochaete chrysosporium
Biotechnol. Biofuels
14
108
2021
Phanerodontia chrysosporium (P06181), Phanerodontia chrysosporium
brenda
Khatoon, N.; Jamal, A.; Ali, M.I.
Lignin peroxidase isoenzyme a novel approach to biodegrade the toxic synthetic polymer waste
Environ. Technol.
40
1366-1375
2019
Phanerodontia chrysosporium, Phanerodontia chrysosporium NK-1
brenda
Biko, O.; Viljoen-Bloom, M.; van Zyl, W.
Microbial lignin peroxidases applications, production challenges and future perspectives
Enzyme Microb. Technol.
141
109669
2020
Phanerodontia chrysosporium (D1M7B6)
brenda
Son, H.; Seo, H.; Han, S.; Kim, S.M.; Pham, L.T.M.; Khan, M.F.; Sung, H.J.; Kang, S.H.; Kim, K.J.; Kim, Y.H.
Extra disulfide and ionic salt bridge improves the thermostability of lignin peroxidase H8 under acidic condition
Enzyme Microb. Technol.
148
109803
2021
Phanerodontia chrysosporium (P06181)
brenda
Houtman, C.J.; Maligaspe, E.; Hunt, C.G.; Fernandez-Fueyo, E.; Martinez, A.T.; Hammel, K.E.
Fungal lignin peroxidase does not produce the veratryl alcohol cation radical as a diffusible ligninolytic oxidant
J. Biol. Chem.
293
4702-4712
2018
Phanerodontia chrysosporium (P06181)
brenda
Sadaqat, B.; Khatoon, N.; Malik, A.Y.; Jamal, A.; Farooq, U.; Ali, M.I.; He, H.; Liu, F.J.; Guo, H.; Urynowicz, M.; Wang, Q.; Huang, Z.
Enzymatic decolorization of melanin by lignin peroxidase from Phanerochaete chrysosporium
Sci. Rep.
10
20240
2020
Phanerodontia chrysosporium, Phanerodontia chrysosporium NK-1
brenda
Ecker, J.; Fueloep, L.
Lignin peroxidase ligand access channel dysfunction in the presence of atrazine
Sci. Rep.
8
5989
2018
Phanerodontia chrysosporium
brenda