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Enzyme Nomenclature
Information on EC 1.11.1.14 - lignin peroxidase
Word Map on EC 1.11.1.14
- 1.11.1.14
- chrysosporium
- phanerochaete
- manganese
- fungus
-
veratryl
- laccase
- peroxidases
-
ligninolytic
-
white-rot
-
decolor
-
basidiomycete
-
biodegradation
- versicolor
- trametes
-
lignin-degrading
-
wood
-
manganese-dependent
-
textile
- bjerkandera
- pleurotus
-
lignocellulose
- veratraldehyde
- xylanase
-
straw
- ostreatus
- eryngii
- phlebia
- adusta
- biotechnology
- coriolus
- 2,4-dichlorophenol
-
lignocellulolytic
-
delignification
-
transient-state
- irpex
-
bagasse
-
hardwood
-
peroxidase-catalyzed
- degradation
- analysis
- polyporus
-
dye-decolorizing
-
ceriporiopsis
-
triphenylmethane
-
kirk
-
mn-dependent
- sordida
- environmental protection
-
kraft
-
remazol
- subvermispora
-
n-limited
-
nonphenolic
-
decolourisation
- synthesis
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
1.11.1.14
-
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RECOMMENDED NAME
GeneOntology No.
lignin peroxidase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
1-(3,4-dimethoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H2O2 = 3,4-dimethoxybenzaldehyde + 2-methoxyphenol + glycolaldehyde + H2O
(1)
-
-
-
2 (3,4-dimethoxyphenyl)methanol + H2O2 = 2 (3,4-dimethoxyphenyl)methanol radical + 2 H2O
(2)
-
-
-
2 (3,4-dimethoxyphenyl)methanol + H2O2 = 2 (3,4-dimethoxyphenyl)methanol radical + 2 H2O
mechanism
-
2 (3,4-dimethoxyphenyl)methanol + H2O2 = 2 (3,4-dimethoxyphenyl)methanol radical + 2 H2O
mechanism
-
-
2 (3,4-dimethoxyphenyl)methanol + H2O2 = 2 (3,4-dimethoxyphenyl)methanol radical + 2 H2O
mechanism
-
-
2 (3,4-dimethoxyphenyl)methanol + H2O2 = 2 (3,4-dimethoxyphenyl)methanol radical + 2 H2O
mechanism
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
1-(3,4-dimethoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol:hydrogen-peroxide oxidoreductase
A hemoprotein, involved in the oxidative breakdown of lignin by white-rot basidiomycete fungi. The reaction involves an initial oxidation of the heme iron by hydrogen peroxide, forming compound I (FeIV=O radical cation) at the active site. A single one-electron reduction of compound I by an electron derived from a substrate molecule yields compound II (FeIV=O non-radical cation), followed by a second one-electron transfer that returns the enzyme to the ferric oxidation state. The electron transfer events convert the substrate molecule into a transient cation radical intermediate that fragments spontaneously. The enzyme can act on a wide range of aromatic compounds, including methoxybenzenes and nonphenolic beta-O-4 linked arylglycerol beta-aryl ethers, but cannot act directly on the lignin molecule, which is too large to fit into the active site. However larger lignin molecules can be degraded in the presence of veratryl alcohol. It has been suggested that the free radical that is formed when the enzyme acts on veratryl alcohol can diffuse into the lignified cell wall, where it oxidizes lignin and other organic substrates. In the presence of high concentration of hydrogen peroxide and lack of substrate, the enzyme forms a catalytically inactive form (compound III). This form can be rescued by interaction with two molecules of the free radical products. In the case of veratryl alcohol, such an interaction yields two molecules of veratryl aldehyde.
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CAS REGISTRY NUMBER
COMMENTARY
93792-13-3
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
LiP shows lignin degrading and coal depolymerization activity
physiological function
wild-type Rhodococcus jostii RHA1 shows hydrogen peroxide-dependent activity, whereas the DypB knockout strain shows no observable activity in the presence or absence of hydrogen peroxide and a significant decrease in activity compared to that of the wild-type strain
physiological function
-
LiP shows lignin degrading and coal depolymerization activity
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,2-bis(3,4-dimethoxyphenyl)propane-1,3-diol + H2O2
3,4-dimethoxybenzaldehyde + 1-(3,4-dimethyl-phenyl)ethane-1,2-diol + H2O
1-(3,4-diethoxyphenyl)-1,3-dihydroxy-2-(4-methoxy-phenyl)propane + O2 + H2O2
1-(4'-methoxyphenyl)-1,2-dihydroxyethane + 3,4-diethoxybenzaldehyde
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
-
-
-
?
1-(4-hydroxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H2O2
vanillin + hydroxyacetaldehyde + guaiacol
-
Calpha-Cbeta bond cleavage of substrate takes place. This reaction is inhibited by addition of diaphorase, consistent with a radical mechanism for C-C bond cleavage
-
?
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2
? + H2O
-
-
-
?
3-methyl-2-benzothiazolinone hydrazone + H2O2
? + H2O
-
enzyme has several substrate binding sites for 3-methyl-2-benzothiazolinone hydrazone, in addition to low and high affinity binding sites for Mn2+
-
-
?
4,5-dichlorocatechol + H2O2
?
-
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
-
?
4-chlorocatechol + H2O2
?
-
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
-
?
4-methylcatechol + H2O2
?
-
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
-
?
4-methylthio-2-oxobutanoate + H2O2
?
-
only in presence of veratryl alcohol, it possibly reacts with a veratryl alcohol radical to produce ethylene
-
-
?
catechol + H2O2
?
-
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
-
?
lignocellulose + H2O2
? + H2O
substrate is wheat straw lignocellulose
-
-
?
mitoxantrone + H2O2
hexahydronaphtho-[2,3-f]-quinoxaline-7,12-dione + H2O
-
low efficiency
-
-
?
Reactive Black 5 + H2O2
?
lignin peroxidase can only oxidize Reactive Black 5 in the presence of redox mediators such as veratryl alcohol
-
-
?
reduced 2,2'-azino-bis-(3-ethylbenzthiazole-6-sulfonic acid) + H2O2
oxidized 2,2'-azino-bis-(3-ethylbenzthiazole-6-sulfonic acid) + H2O
-
-
-
?
1,2-bis(3,4-dimethoxyphenyl)propane-1,3-diol + H2O2
3,4-dimethoxybenzaldehyde + 1-(3,4-dimethyl-phenyl)ethane-1,2-diol + H2O
-
-
-
-
?
1,2-bis(3,4-dimethoxyphenyl)propane-1,3-diol + H2O2
3,4-dimethoxybenzaldehyde + 1-(3,4-dimethyl-phenyl)ethane-1,2-diol + H2O
-
-
-
-
?
1,2-bis(3,4-dimethoxyphenyl)propane-1,3-diol + H2O2
3,4-dimethoxybenzaldehyde + 1-(3,4-dimethyl-phenyl)ethane-1,2-diol + H2O
-
-
-
-
?
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-methoxy-phenyl)propane + O2 + H2O2
1-(4'-methoxyphenyl)-1,2-dihydroxyethane + 3,4-diethoxybenzaldehyde
-
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
-
?
1-(3,4-diethoxyphenyl)-1,3-dihydroxy-2-(4-methoxyphenyl)-propane + O2 + H2O2
?
-
-
-
-
?
1-(3,4-diethoxyphenyl)-1,3-dihydroxy-2-(4-methoxyphenyl)-propane + O2 + H2O2
?
-
-
-
-
?
1-(3,4-diethoxyphenyl)-1,3-dihydroxy-2-(4-methoxyphenyl)-propane + O2 + H2O2
?
-
-
-
-
?
1-(3,4-diethoxyphenyl)-1,3-dihydroxy-2-(4-methoxyphenyl)-propane + O2 + H2O2
?
-
i.e. diarylpropane, involved in the oxidative breakdown of lignin in white rot basidiomycetes, induced by veratryl alcohol
-
-
?
1-(3,4-diethoxyphenyl)-1,3-dihydroxy-2-(4-methoxyphenyl)-propane + O2 + H2O2
?
-
i.e. diarylpropane, involved in the oxidative breakdown of lignin in white rot basidiomycetes, induced by veratryl alcohol
-
-
?
1-(3,4-diethoxyphenyl)-1,3-dihydroxy-2-(4-methoxyphenyl)-propane + O2 + H2O2
?
-
i.e. diarylpropane, involved in the oxidative breakdown of lignin in white rot basidiomycetes, induced by veratryl alcohol
-
-
?
1-(3,4-diethoxyphenyl)-1,3-dihydroxy-2-(4-methoxyphenyl)-propane + O2 + H2O2
?
-
-
-
-
?
1-(3,4-diethoxyphenyl)-1,3-dihydroxy-2-(4-methoxyphenyl)-propane + O2 + H2O2
?
-
-
-
-
?
1-(3,4-diethoxyphenyl)-1,3-dihydroxy-2-(4-methoxyphenyl)-propane + O2 + H2O2
?
-
-
-
-
?
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
-
olefinic hydroxylation
-
?
1-(4-ethoxy-3-methoxyphenyl)-1,2-propene + O2 + H2O2
1-(4-ethoxy-3-methoxyphenyl)-1,2-dihydroxypropane
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olefinic hydroxylation
-
-
?
3,4-dimethoxybenzyl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
-
veratryl alcohol
-
?
3,4-dimethoxybenzyl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
-
veratryl alcohol
-
?
3,4-dimethoxybenzyl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
-
veratryl alcohol
-
?
3,4-dimethoxybenzyl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
-
veratryl alcohol
-
?
3,4-dimethoxybenzyl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
-
veratryl alcohol
-
-
?
3,4-dimethoxybenzyl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
-
veratryl alcohol
-
?
3,4-dimethoxybenzyl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
-
veratryl alcohol
-
?
3,4-dimethoxybenzyl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
-
veratryl alcohol
-
?
3,4-dimethoxybenzyl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
-
veratryl alcohol
-
-
?
3,4-dimethoxybenzyl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
-
veratryl alcohol
-
-
?
3,4-dimethoxybenzyl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
-
veratryl alcohol
-
-
?
3,4-dimethoxybenzyl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
-
veratryl alcohol
-
?
3,4-dimethoxybenzyl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
-
veratryl alcohol
-
?
humic acid + H2O2
? + H2O
-
-
purified enzyme depolymerises humic acid as a model of coal in presence of H2O2
-
?
humic acid + H2O2
? + H2O
-
-
purified enzyme depolymerises humic acid as a model of coal in presence of H2O2
-
?
lignin + H2O2
? + H2O
-
substrate Kraft lignin. The highest production of radicals with minimal loss of activity, is obtained by using an enzyme dose of 15 U/g, with a continuous addition of H2O2 during 1 h. Enzymatically generated Mn(III)-malonate is able to activate lignin
-
-
?
lignin + H2O2
? + H2O
-
substrate Kraft lignin. The highest production of radicals with minimal loss of activity, is obtained by using an enzyme dose of 15 U/g, with a continuous addition of H2O2 during 1 h. Enzymatically generated Mn(III)-malonate is able to activate lignin
-
-
?
non-phenolic substrates + H2O2
?
-
e.g. 1,2,4-trimethoxybenzene, 4,4'-dimethoxybiphenyl, isoeugenol methylether, 1-(3,4-dimethoxyphenyl)-2-(2, 4-dichlorophenoxyl)-ethanol, guaiacyl glycerolether
-
-
?
non-phenolic substrates + H2O2
?
-
e.g. 1,2,4-trimethoxybenzene, 4,4'-dimethoxybiphenyl, isoeugenol methylether, 1-(3,4-dimethoxyphenyl)-2-(2, 4-dichlorophenoxyl)-ethanol, guaiacyl glycerolether
-
-
?
non-phenolic substrates + H2O2
?
-
e.g. 1,2,4-trimethoxybenzene, 4,4'-dimethoxybiphenyl, isoeugenol methylether, 1-(3,4-dimethoxyphenyl)-2-(2, 4-dichlorophenoxyl)-ethanol, guaiacyl glycerolether
-
-
?
oxytetracycline + H2O2
?
-
LiP shows strong degrading ability
-
-
?
oxytetracycline + H2O2
?
-
LiP shows strong degrading ability
-
-
?
tetracycline + H2O2
?
-
LiP shows strong degrading ability
-
-
?
veratryl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
-
-
-
-
?
veratryl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
-
-
-
-
?
veratryl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
-
-
-
-
?
veratryl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
-
-
-
-
?
veratryl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
-
-
-
-
?
veratryl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
-
-
-
-
?
veratryl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
-
ping pong mechanism
-
-
?
veratryl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
-
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 7–9. Under optimum conditions, the half-life of LiP is circa 12 h
-
-
?
veratryl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
-
optimum culture conditions
-
-
?
veratryl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
-
optimum culture conditions
-
-
?
veratryl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
-
-
-
-
?
veratryl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
-
-
-
-
?
veratryl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
-
-
-
-
?
veratryl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
-
-
-
-
?
veratryl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
Polyporous velutinus MTCC 1813
-
-
-
-
?
veratryl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
-
-
-
-
?
veratryl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
-
-
-
-
?
veratryl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
-
-
-
-
?
veratryl alcohol + H2O2
veratraldehyde + H2O
-
synthesis of veratraldehyde from veratryl alcohol by Phanerochaete chrysosporium lignin peroxidase with in situ electrogeneration of hydrogen peroxide in an electroenzymatic reactor
-
-
?
veratryl alcohol + H2O2
veratraldehyde + H2O
-
-
-
-
?
veratryl alcohol + H2O2
veratraldehyde + H2O
-
synthesis of veratraldehyde from veratryl alcohol by Phanerochaete chrysosporium lignin peroxidase with in situ electrogeneration of hydrogen peroxide in an electroenzymatic reactor
-
-
?
additional information
?
-
-
the enzyme shows a higher decolorization rate for monoazo dyes than for thiazin and heterocyclic textile dyes. A high decolorization rate is observed for the azo-dye such as Methyl red 98% and Methyl orange 96% within 24 h, while Direct blue GLL, Direct red 5B, Direct brown MR, Reactive red 2, and Ethylene blue decolorize up to 87%, 79%, 75%, 73%, and 84%, within 48 h, respectively. Direct brown T4LL, Disperse red DK, and Congo red show comparatively less decolorization than the others (63.2%, 63.3%, and 67.9%, within 48 h, respectively)
-
-
-
additional information
?
-
-
the enzyme shows a higher decolorization rate for monoazo dyes than for thiazin and heterocyclic textile dyes. A high decolorization rate is observed for the azo-dye such as Methyl red 98% and Methyl orange 96% within 24 h, while Direct blue GLL, Direct red 5B, Direct brown MR, Reactive red 2, and Ethylene blue decolorize up to 87%, 79%, 75%, 73%, and 84%, within 48 h, respectively. Direct brown T4LL, Disperse red DK, and Congo red show comparatively less decolorization than the others (63.2%, 63.3%, and 67.9%, within 48 h, respectively)
-
-
-
additional information
?
-
-
manganese peroxidase activity is more efficient than lignin peroxidase activity, with activity increasing with increasing concentrations of Mn2+ due to a second metal binding site involved in homotropic substrate Mn2+ activation. The activation of maganese peroxidase is also accompanied by a decrease in both activation energy and substrate Mn2+ affinity
-
-
-
additional information
?
-
-
Sulfonated azo dyes such as Methyl orange and Blue-2B are degraded by the purified lignin peroxidase. Degradation of the dyes is confirmed by HPLC, GC-MS, and FTIR spectroscopy. The mainly elected products of Methyl orange are 4-substituted hexanoic acid (m/z = 207), 4-cyclohexenone lactone cation (m/z = 191), and 4-isopropanal-2, 5-cyclohexa-dienone (m/z = 149) and for Blue-2B are 4-(2-hexenoic acid)-2, 5-cyclohexa-diene-one (m/z = 207) and dehydro-acetic acid derivative (m/z = 223), proposed pathway of degradation
-
-
-
additional information
?
-
-
Comamonas sp UVS decolorizes Direct Blue GLL dye (50 mg/l) within 13 h at static condition in yeast extract broth. It can degrade up to 300 mg/l of dye within 55 h. The maximum rate (Vmax) of decolorization is 12.41 mg dye/gcell h with the Michaelis constant (KM) value as 6.20 mg/l. The biodegradation is monitored by UV-Vis, GC-MS and HPLC, no decolorization is found under shaking conditions
-
-
-
additional information
?
-
-
Comamonas sp UVS decolorizes Direct Blue GLL dye (50 mg/l) within 13 h at static condition in yeast extract broth. It can degrade up to 300 mg/l of dye within 55 h. The maximum rate (Vmax) of decolorization is 12.41 mg dye/gcell h with the Michaelis constant (KM) value as 6.20 mg/l. The biodegradation is monitored by UV-Vis, GC-MS and HPLC, no decolorization is found under shaking conditions
-
-
-
additional information
?
-
-
catalyzes non-specifically several oxidations in the alkyl-side-chains of lignin-related compounds, Calpha-Cbeta cleavage in lignin model-compounds
-
-
?
additional information
?
-
-
oxidation of various phenolic and non-phenolic lignin model-compounds
-
-
?
additional information
?
-
-
oxidation of various phenolic and non-phenolic lignin model-compounds
-
-
?
additional information
?
-
-
oxidation of various phenolic and non-phenolic lignin model-compounds
-
-
?
additional information
?
-
-
oxidation of various phenolic and non-phenolic lignin model-compounds
-
-
?
additional information
?
-
-
oxidation of various phenolic and non-phenolic lignin model-compounds
-
-
?
additional information
?
-
-
of the aryl-CalphaHOH-CbetaHR-CgammaH2OH-type (R being aryl or O-aryl)
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
with concomitant insertion of 1 atom of molecular oxygen
-
-
?
additional information
?
-
-
with concomitant insertion of 1 atom of molecular oxygen
-
-
?
additional information
?
-
-
oxidation of benzyl alcohols to aldehydes or ketones
-
-
?
additional information
?
-
-
oxidation of benzyl alcohols to aldehydes or ketones
-
-
?
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
lignin peroxidase is not able to oxidize phenolic compounds efficiently because of inactivation in the absence of veratryl alcohol or related substrates
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
oxidation of various phenolic and non-phenolic lignin model-compounds
-
-
?
additional information
?
-
-
oxidation of various phenolic and non-phenolic lignin model-compounds
-
-
?
additional information
?
-
-
oxidation of various phenolic and non-phenolic lignin model-compounds
-
-
?
additional information
?
-
-
of the aryl-CalphaHOH-CbetaHR-CgammaH2OH-type (R being aryl or O-aryl)
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
with concomitant insertion of 1 atom of molecular oxygen
-
-
?
additional information
?
-
-
oxidation of benzyl alcohols to aldehydes or ketones
-
-
?
additional information
?
-
-
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
-
-
-
additional information
?
-
-
oxidation of various phenolic and non-phenolic lignin model-compounds
-
-
?
additional information
?
-
first enzyme connected to oxidative breakdown of the aromatic plant heteropolymer lignin and related xenobiotics
-
-
-
additional information
?
-
first enzyme connected to oxidative breakdown of the aromatic plant heteropolymer lignin and related xenobiotics
-
-
-
additional information
?
-
first enzyme connected to oxidative breakdown of the aromatic plant heteropolymer lignin and related xenobiotics
-
-
-
additional information
?
-
-
oxidation of various phenolic and non-phenolic lignin model-compounds
-
-
?
additional information
?
-
enzyme DypB has a significant role in lignin degradation in Rhodococcus jostii RHA1, is able to oxidize both polymeric lignin and a lignin model compound, and appears to have both Mn(II) and lignin oxidation sites
-
-
-
additional information
?
-
-
oxidation of various phenolic and non-phenolic lignin model-compounds
-
-
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-(3,4-diethoxyphenyl)-1,3-dihydroxy-2-(4-methoxyphenyl)-propane + O2 + H2O2
?
-
-
-
-
?
1-(3,4-diethoxyphenyl)-1,3-dihydroxy-2-(4-methoxyphenyl)-propane + O2 + H2O2
?
-
-
-
-
?
1-(3,4-diethoxyphenyl)-1,3-dihydroxy-2-(4-methoxyphenyl)-propane + O2 + H2O2
?
-
-
-
-
?
1-(3,4-diethoxyphenyl)-1,3-dihydroxy-2-(4-methoxyphenyl)-propane + O2 + H2O2
?
-
i.e. diarylpropane, involved in the oxidative breakdown of lignin in white rot basidiomycetes, induced by veratryl alcohol
-
-
?
1-(3,4-diethoxyphenyl)-1,3-dihydroxy-2-(4-methoxyphenyl)-propane + O2 + H2O2
?
-
i.e. diarylpropane, involved in the oxidative breakdown of lignin in white rot basidiomycetes, induced by veratryl alcohol
-
-
?
1-(3,4-diethoxyphenyl)-1,3-dihydroxy-2-(4-methoxyphenyl)-propane + O2 + H2O2
?
-
i.e. diarylpropane, involved in the oxidative breakdown of lignin in white rot basidiomycetes, induced by veratryl alcohol
-
-
?
1-(3,4-diethoxyphenyl)-1,3-dihydroxy-2-(4-methoxyphenyl)-propane + O2 + H2O2
?
-
-
-
-
?
1-(3,4-diethoxyphenyl)-1,3-dihydroxy-2-(4-methoxyphenyl)-propane + O2 + H2O2
?
-
-
-
-
?
1-(3,4-diethoxyphenyl)-1,3-dihydroxy-2-(4-methoxyphenyl)-propane + O2 + H2O2
?
-
-
-
-
?
1-(3,4-diethoxyphenyl)-1,3-dihydroxy-2-(4-methoxyphenyl)-propane + O2 + H2O2
?
-
-
-
-
?
additional information
?
-
Q3L2T9
first enzyme connected to oxidative breakdown of the aromatic plant heteropolymer lignin and related xenobiotics
-
-
-
additional information
?
-
Q3L452
first enzyme connected to oxidative breakdown of the aromatic plant heteropolymer lignin and related xenobiotics
-
-
-
additional information
?
-
Q53WT9
first enzyme connected to oxidative breakdown of the aromatic plant heteropolymer lignin and related xenobiotics
-
-
-
additional information
?
-
Q0SE24
enzyme DypB has a significant role in lignin degradation in Rhodococcus jostii RHA1, is able to oxidize both polymeric lignin and a lignin model compound, and appears to have both Mn(II) and lignin oxidation sites
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Iron
Mn2+
Iron
-
hemoprotein containing protoporphyrin IX, high-spin ferri-heme-complex, 0.7 heme per enzyme molecule
Iron
-
1.08 atom Fe per enzyme molecule; 1 mol protoheme IX per mol enzyme
Mn2+
-
activity of manganese peroxidase progressively increases with concentration of Mn2+ to a maximum at about 1.8 mM, with a corresponding decrease in lignin peroxidase activity to less than 10%
Mn2+
1 mM, 5.4fold activation in assay with lignin. Presence of Mn2+ is required, Km value is 8.4 mM, and data are not consistent with DypB acting as a Mn peroxidase. Breakdown of wheat straw lignocellulose by recombinant enzyme is observed over 24-48 h in the presence of 1 mM MnCl2
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ag+
-
1 mM, about 80% inhibition of native enzyme, about 15% inhibition of enzyme immobilized in xerogel matrix of trimethoxysilane and proplytetramethoxysilane
L-cysteine
-
1 mM, complete inhibition of native enzyme, about 30% inhibition of enzyme immobilized in xerogel matrix of trimethoxysilane and proplytetramethoxysilane
sodium bis (2-ethylhexyl)-sulfosuccinate
-
a mixed reversed micelle formed by anionic surfactant sodium bis (2-ethylhexyl)-sulfosuccinate and non-ionic surfactant polyoxyethylene lauryl ether (Brij30) is used to increase the catalytic activity
EDTA
-
1 mM, about 75% inhibition of native enzyme, about 20% inhibition of enzyme immobilized in xerogel matrix of trimethoxysilane and proplytetramethoxysilane
H2O2
-
the inhibitory concentration of H2O2 might be different for different dyes
H2O2
-
based on the characteristics of reversed micelles (the water content is under control), the glucose oxidase-catalyzed oxidation of glucose (as an H2O2 source) is used to couple to the lignin peroxidase-catalyzed oxidation of substrates to control the level of H2O2in the mixed reversed micellar medium
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
H2O2
-
degradation of tetracycline and oxytetracycline is not detected without the addition of H2O2, but enhances greatly with the addition of 0.1 mM H2O2
veratryl alcohol
-
without veratryl alcohol in the reaction system, there are only 18% of tetracycline removal and 14% of oxytetracycline removal. The degradation percentage reaches its maximum with veratryl alcohol concentration larger than 2.0 mM for tetracycline and 1.5 mM for oxytetracycline
additional information
-
Under the optimized conditions,the catalytic efficiency of lignin peroxidase in the N-gluconyl glutamic acid didecyl ester/Triton X-100 reverse micelle is 40times higher than that in the sodium bis (2-ethylhexyl) sulfosuccinate reverse micelle. The full expression of catalytic activity of lignin peroxidase in this medium is mainly due to the lack of electrostatic interaction between lignin peroxidase and the head group of N-gluconyl glutamic acid didecyl ester and Triton X-100 and to the size fit between lignin peroxidase and the inner water cavity of the reverse micelle
-
additional information
-
in order to obtain a high and sustainable activity of lignin peroxidase, H2O2 is supplied through a co-immobilized glucose oxidase (GOD)-catalyzed oxidation reaction
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
bioelectric oxidation of organic substrates by LiP immobilized on graphite electrode
-
0.163
2,4-Dichlorophenol
-
mutant enzyme A140G/S190P/P193A/S196F/E208Q
0.19
2,4-Dichlorophenol
-
mutant enzyme P106R/S119R/N120T/S228Y/A272G/L275V/A315G/A317T
0.74
2,4-Dichlorophenol
-
mutant enzyme H102T/S119R/N120T/Q126K/A243R/A315G
0.755
2,4-Dichlorophenol
-
mutant enzyme P106R/Q210H/L211V/A243R/F255L
0.083
H2O2
Loweporus lividus
-
2 mM veratryl alcohol, 50 mM sodium tartrate buffer pH 2.5, 25°C
4.09
H2O2
-
mutant enzyme P106R/S119R/N120T/S228Y/A272G/L275V/A315G/A317T
0.054
veratryl alcohol
-
in 50 mM sodium tartrate buffer, at pH 2.5, 25°C
0.058
veratryl alcohol
Loweporus lividus
-
0.4 mM H2O2, 50 mM sodium tartrate buffer pH 2.5, 25°C
0.588
veratryl alcohol
-
enzyme immobilized in xerogel matrix of trimethoxysilane and proplytetramethoxysilane, 25°C, pH 5.0
2.79
veratryl alcohol
-
recombinant enzyme without veratryl alcohol-H2O2 pretreatment, in 20 mM sodium succinate buffer (pH 3.0)
3.24
veratryl alcohol
-
recombinant enzyme with veratryl alcohol-H2O2 pretreatment, in 20 mM sodium succinate buffer (pH 3.0)
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
58.7
2,4-Dichlorophenol
Phanerochaete chrysosporium
-
mutant enzyme A140G/S190P/P193A/S196F/E208Q
66
2,4-Dichlorophenol
Phanerochaete chrysosporium
-
mutant enzyme P106R/S119R/N120T/S228Y/A272G/L275V/A315G/A317T
313.3
2,4-Dichlorophenol
Phanerochaete chrysosporium
-
mutant enzyme H102T/S119R/N120T/Q126K/A243R/A315G
316.7
2,4-Dichlorophenol
Phanerochaete chrysosporium
-
mutant enzyme P106R/Q210H/L211V/A243R/F255L
68.2
H2O2
Phanerochaete chrysosporium
-
mutant enzyme P106R/S119R/N120T/S228Y/A272G/L275V/A315G/A317T
2.5
veratryl alcohol
Loweporus lividus
-
0.4 mM H2O2, 50 mM sodium tartrate buffer pH 2.5, 25°C
16.3
veratryl alcohol
Trametopsis cervina
-
recombinant enzyme without veratryl alcohol-H2O2 pretreatment, in 20 mM sodium succinate buffer (pH 3.0)
17.7
veratryl alcohol
Trametopsis cervina
-
recombinant enzyme with veratryl alcohol-H2O2 pretreatment, in 20 mM sodium succinate buffer (pH 3.0)
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
Loweporus lividus
-
the purified enzyme does not show any manganese peroxidase activity and hence it is not a versatile peroxidase
additional information
-
4.0 U/ml veratryl alcohol activity, pH 3.5, 30°C
additional information
-
the activity of lignin peroxidase in the AOT/Brij30 mixed reversed micelles is much higher than that in a single sodium bis (2-ethylhexyl)-sulfosuccinate reversed micelle due to modification of the charge density of the interfacial membrane
additional information
-
the maximum activity of lignin peroxidase is 744 U/l after 5 days of fermentation using sewage treatment plant (STP) sludge as the major substrate
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.4
2.5
2.6
3.5
3.6
4.2
-
optimum pH for tetracycline and oxytetracycline degradation
4.8
-
in the AOT/Brij30 mixed reversed micelles. The optimum pH occurres at ca. 4.8, which is higher than that in a single AOT reversed micelle
5
-
enzyme immobilized in xerogel matrix of trimethoxysilane and proplytetramethoxysilane
additional information
3.5
-
similar pH activity profile for the immobilizied and the free enzyme
3.6
-
catalytic activity of lignin peroxidase in sodium bis(2-ethylhexyl)sulfosuccinate /isooctane/toluene/water reverse micelles
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.8 - 5.4
-
pH range for tetracycline and oxytetracycline degradation, no removal is observed when pH was below 2.8 or above 5.4. The degradation percentage is comparatively stable and high when pH is between 3.6 and 4.2 for tetracycline and oxytetracycline
3 - 11
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
24
25
30
37
40
80
-
enzyme immobilized in xerogel matrix of trimethoxysilane and proplytetramethoxysilane
37
-
optimum temperature for tetracycline and oxytetracycline degradation
40
-
immobilized lignin peroxidase, 10°C higher than that of free lignin peroxidase
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 90
20 - 40
-
at 30°C, tetracycline is nearly totally removed and this degradation percentage keeps unchanged until 37°C, whereas the degradation of oxytetracycline reaches about 90% at 30°C and increases with temperature until it is 37°C. At 20°C, the degradation of tetracycline reaches about 78%, the value for oxytetracycline is 83%. When temperature exceeds 37°C, the degradation of both tetracycline and oxytetracycline decreases
25 - 75
-
pH 5, 100% lignin peroxidase activity is retained at 55°C after incubation. The lignin peroxidase activity drops more than 75% at temperatures below 35°C and loses about 66% of its activity at a temperature of 75°C
30 - 40
Pycnoporus sp.
-
highest LiP activity is detected at 37°C, followed by 30°C, and no activity is obeserved at 40°C
10 - 90
-
lignin peroxidase is active in a broad range of temperature where higher temperature of about 90°C affects not the enzymatic configuration (thermal denaturation)
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
-
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
-
-
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40000
42000
43000
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
?
-
x * 39000, isozyme I, SDS-PAGE; x * 41000, isozyme II, SDS-PAGE; x * 43000, isozyme III, SDS-PAGE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 11
-
the lignin peroxidase activity is stable at pH 5, lower at a low pH of 3 and is high below pH 7, more than 70% of activity is lost at pH 7-11
704959
3 - 6
-
native enzyme, stable for 1 h, enzyme immobilized in xerogel matrix of trimethoxysilane and proplytetramethoxysilane, stable for 24 h
724663
3 - 7
-
the recombiannt enzyme is stable from pH 3.5 to neutral pH, but unstable over pH 7.0 and below pH 3.0
701072
4.5 - 5.5
Lentinus strigellus
-
pH range preserving 70-100% of initial activity, 25°C, 24 h
702977
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 70
-
temperature range preserving 70-100% of initial activity, pH 5.0, 1 h
10 - 40
10 - 70
-
temperature range preserving 70-100% of initial activity, pH 5.0, 1 h
10 - 40
-
temperature range preserving 70-100% of initial activity, pH 5.0, 1 h
23
-
retains nearly 30% of initial activity after 18 h, in presence of veratryl alcohol
25 - 75
-
pH 5, 100% lignin peroxidase activity is retained at 55°C after incubation. The lignin peroxidase activity drops more than 75% at temperatures below 35°C and loses about 66% of its activity at a temperature of 75°C
30 - 60
-
the recombinant enzyme is fully stable up to 30°C but unstable at 37°C, and is completely inactivated after 30 min at 60°C
45
-
after 2 h incubation at 45°C, 55% of the initial activity of the immobilized lignin peroxidase (on nanoporous gold) is still retained while the free lignin peroxidase is completely deactivated, pH 3.5 citrate buffer
10 - 40
Lentinus strigellus
-
temperature range preserving 70-100% of initial activity, pH 5.0, 1 h
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
lignin peroxidase in sodium bis(2-ethylhexyl)sulfosuccinate/isooctane/toluene/water reverse micelles reverse micelles shoes a the half-life of circa 12 h. under optimal conditions, 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 7–9
-
The results for the tests of the stability of lignin peroxidase show that the activity is more than 80% of the maximum for the first 12 h of incubation at an optimum pH of 5 and temperature of 55°C.
-
tryptophan stabilizes the lignin peroxidase activity during decolorization of dyes
-
veratryl alcohol stabilizes at pH 3.5 and 23°C, lag-phases are not observed
-
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acetone
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
at 4°C the activity of the immobilized lignin peroxidase decreases slowly. After 1 month, about 95% activity is still retained, free lignin peroxidase loses about 30% of its initial activity, indicating that the storage stability of lignin peroxidase considerably increases after the immobilization on nanoporous gold
-
frozen, in crude concentrates of growth medium complete loss of activity within a month
-
the concentrated enzyme can be stored without lost of activity for 2 months at 4°C in the refrigerator
Loweporus lividus
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
10 kDa ultrafiltration, 3 M ammonium sulphate precipitation, hydrophobic interaction chromatography, reversed phase chromatography
-
salt precipitation with 60% (NH4)2SO4, desalting column, Q FF ion exchange column and Sepharyl S-300 HR gel filtration
-
to homogeneity using Amicon concentration and DEAE cellulose chromatography
Loweporus lividus
-
ultrafiltration, anion-exchange and size exclusion chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3)pLysS cells, recombinant LiP protein accumulates in inclusion bodies as an inactive form
-
homologous overexpression in Phanerochaete sordida YK-624 uracil auxotrophic mutant UV-64
overexpression of isozyme H8 and W171 mutant in Escherichia coli
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the C/N ratio of the optimized medium for LiP production composed of asparagines 9.967 g/l, urea 16.247 g/l, fructose 13.953 g/l, malt extract 12.58 g/l, and (NH4)2SO4 13.92 g/l is 1.433
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A140G/A243R/A317P
-
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
-
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
-
kcat/Km for 2,4-dichlorophenol is fold higher than wild-type value, kcat/Km for H2O2 is 89fold higher than wild-type value
P106R/Q210H/L211V/A243R/F255L
-
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
-
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
-
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
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Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
the optimal refolding solution contains of 0.4 M urea, 5 mM CaCl2, 0.0005 mM hemin, and 0.6 mM oxidized glutathione in Tris-HCl buffer, at pH 9.5
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
biotechnology
degradation
environmental protection
synthesis
analysis
-
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
analysis
-
evaluation of the effect of enzyme dosage, incubation time, and H2O2 addition profile on lignin activation by quantifying the phenoxy radicals formed using electron paramagnetic resonance spectroscopy. At optimal conditions, i.e. dose of 15 /g and continuous addition of H2O2, the content of phenoxy radicals is doubled as compared with an untreated control
analysis
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evaluation of the effect of enzyme dosage, incubation time, and H2O2 addition profile on lignin activation by quantifying the phenoxy radicals formed using electron paramagnetic resonance spectroscopy. At optimal conditions, i.e. dose of 15 /g and continuous addition of H2O2, the content of phenoxy radicals is doubled as compared with an untreated control
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biotechnology
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Pleurotus ostreatus is a good candidate for scale-up ligninolytic enzyme production
biotechnology
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Pleurotus ostreatus is a good candidate for scale-up ligninolytic enzyme production
degradation
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degradation of different recalcitrant compounds, removal of toxic dyes
degradation
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the electroenzymatic method using in situ-generated hydrogen peroxide is effective for oxidation of veratryl alcohol by lignin peroxidase. The method may be easily applied to biodegradation systems
degradation
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degradation of different recalcitrant compounds, removal of toxic dyes
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degradation
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the electroenzymatic method using in situ-generated hydrogen peroxide is effective for oxidation of veratryl alcohol by lignin peroxidase. The method may be easily applied to biodegradation systems
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environmental protection
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use of Phanerochaete chrysosporium and its enzyme lignin peroxidase in the degradation of environmental pollutants such as dye. High efficient degradation of dyes with lignin peroxidase coupled with glucose oxidase
environmental protection
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the enzyme shows the potential to be applied in the treatment of textile effluents (decolorization of dyes). The results from the selection of dyes such as methylene blue, malachite green and methyl orange show that the enzyme is able to remove a higher content of methylene blue (14%) compared to the other two dyes (3-8%). The optimization with the OFAT method determined the operating conditions of the decolorization of methylene blue dye at temperature 55°C, pH 5.0 (in 50 mM sodium acetate buffer) with H2O2 concentration 4.0 mM. The addition of veratryl alcohol to the reaction mixture has no affect on decolorization of dye
environmental protection
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removal of four catechols (1,2-dihydroxybenzene), 4-chlorocatechol (4-CC), 4,5-dichlorocatechol (4,5-DCC) and 4-methylcatechol (4-MC) typical pollutants in wastewater derived from oil and paper industries
environmental protection
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a high and sustainable lignin peroxidase activity is achieved via in situ release of H2O2 by a co-immobilized glucose oxidase. The present co-immobilization system is demonstrated to be very effective for lignin peroxidase mediated dye decolourization
environmental protection
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lignin peroxidase has a applicable potential for the degradation of sulfonated azo dyes
environmental protection
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the enzyme is able to decolorize synthetic dyes
environmental protection
Lentinus strigellus
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the enzyme is able to decolorize synthetic dyes
environmental protection
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the enzyme is able to decolorize synthetic dyes
environmental protection
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lignin peroxidase enzyme production using sewage treatment plant sludge as a major substrate seems to be a promising and encouraging alternative for better sludge management. This is a new environmental biotechnological approach for the biodegradation of sludge, which, in addition to producing lignin peroxidase, would reduce treatment and production costs through the use of an environmentally friendly process
environmental protection
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the enzyme is able to decolorize synthetic dyes
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environmental protection
Lentinus strigellus SXS355
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the enzyme is able to decolorize synthetic dyes
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environmental protection
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the enzyme is able to decolorize synthetic dyes
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environmental protection
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the enzyme is able to decolorize synthetic dyes
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synthesis
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evaluation of the effect of enzyme dosage, incubation time, and H2O2 addition profile on lignin activation by quantifying the phenoxy radicals formed using electron paramagnetic resonance spectroscopy. At optimal conditions, i.e. dose of 15 /g and continuous addition of H2O2, the content of phenoxy radicals is doubled as compared with an untreated control
synthesis
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immobilization of enzyme by entrapping in xerogel matrix of trimethoxysilane and proplytetramethoxysilane to maximum immobilization efficiency of 88.6%. The free and immobilized enzymes have optimum pH values of 6 and 5 while optimum temperatures are 60°C and 80°C, respectively. Immobilization enhances the activity and thermo-stability potential significantly and immobilized enzyme remains stable over broad pH and temperature range
synthesis
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evaluation of the effect of enzyme dosage, incubation time, and H2O2 addition profile on lignin activation by quantifying the phenoxy radicals formed using electron paramagnetic resonance spectroscopy. At optimal conditions, i.e. dose of 15 /g and continuous addition of H2O2, the content of phenoxy radicals is doubled as compared with an untreated control
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synthesis
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immobilization of enzyme by entrapping in xerogel matrix of trimethoxysilane and proplytetramethoxysilane to maximum immobilization efficiency of 88.6%. The free and immobilized enzymes have optimum pH values of 6 and 5 while optimum temperatures are 60°C and 80°C, respectively. Immobilization enhances the activity and thermo-stability potential significantly and immobilized enzyme remains stable over broad pH and temperature range
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