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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
1,4-dimethoxybenzene + H2O2
?
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
-
-
-
?
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 2,6-dimethoxyphenol + 2 H2O2
coerulignone + 2 H2O
2 guaiacol + H2O2
3,3'-dimethoxy-4,4'-biphenylquinone + H2O
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2
? + H2O
2,4,6-trichlorophenol + H2O2
? + H2O
2,4-dichlorophenol + H2O2
?
2,4-dichlorophenol + H2O2
? + H2O
-
best substrate
-
-
?
2-chloro-1,4-dimethoxybenzene
?
3,4-dimethoxybenzyl alcohol + H2O2
3,4-dimethoxybenzaldehyde + 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-chlorophenol + H2O2
? + H2O
-
45% of the activity with 2,4-dichlorophenol
-
-
?
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
-
-
?
4-phenoxyphenol + H2O2
phenol + 1,4-benzoquinone
-
cleavage of 4-O-5 bond in 4-phenoxyphenol by the catalytic promiscuity of tyrosinase
-
-
?
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
-
?
Direct Blue GLL dye + H2O2
?
ferrocytochrome c + H2O2
?
-
-
-
?
fuchsine + H2O2
?
-
-
-
-
?
guaiacyl glycerol-beta-guaiacyl ether + H2O2
vanillin + guaiacol + 2-hydroxyacetaldehyde + H2O
-
a dimeric lignin model compound, derivatization with tetramethylsilane is carried out to analyze guaiacyl glycerol-beta-guaiacyl ether, GGE. The catalytic promiscuity of tyrosinase seemed to cleave the Calpha-Cbeta bond in GGE, yielding vanillin and possibly an unstable o-(2-hydroxyethyl)guaiacol radical. The unstable o-(2-hydroxyethyl)guaiacol radical might be further catalyzed to guaiacol and 2-hydroxyacetaldehyde by the tyrosinase, and then guaiacol might be polymerized to an unidentified product
-
-
?
humic acid + H2O2
? + H2O
lignocellulose + H2O2
? + H2O
substrate is wheat straw lignocellulose
-
-
?
methylene blue + H2O2
? + H2O
-
-
-
-
?
mitoxantrone + H2O2
hexahydronaphtho-[2,3-f]-quinoxaline-7,12-dione + H2O
-
low efficiency
-
-
?
n-propanol + H2O2
?
-
-
-
-
?
n-propanol + H2O2
propanal + H2O
n-propanol + H2O2
propanaldehyde + H2O
n-propanol + H2O2
propionaldehyde + H2O
-
-
-
-
?
non-phenolic substrates + H2O2
?
o-dianisidine + H2O2
? + H2O
pyrogallol red + H2O2
?
-
-
-
-
?
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
-
-
-
?
rhodamine B + H2O2
?
-
-
-
-
?
veratryl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
veratryl alcohol + H2O2
?
veratryl alcohol + H2O2
veratraldehyde + H2O
veratryl alcohol + H2O2 + H+
veratraldehyde + H2O
xylene cyanol + H2O2
?
-
-
-
-
?
additional information
?
-
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
-
-
-
-
?
1,4-dimethoxybenzene + H2O2

?
-
-
-
-
?
1,4-dimethoxybenzene + H2O2
?
-
-
-
-
?
1,4-dimethoxybenzene + H2O2
?
-
-
-
?
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
-
olefinic hydroxylation
-
-
?
2 2,6-dimethoxyphenol + 2 H2O2

coerulignone + 2 H2O
-
-
-
?
2 2,6-dimethoxyphenol + 2 H2O2
coerulignone + 2 H2O
-
-
-
?
2 guaiacol + H2O2

3,3'-dimethoxy-4,4'-biphenylquinone + H2O
-
27% of the activity with 2,4-dichlorophenol
-
-
?
2 guaiacol + H2O2
3,3'-dimethoxy-4,4'-biphenylquinone + H2O
-
27% of the activity with 2,4-dichlorophenol
-
-
?
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2

? + H2O
-
-
-
?
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2
? + H2O
-
92% of the activity with 2,4-dichlorophenol
-
-
?
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2
? + H2O
-
92% of the activity with 2,4-dichlorophenol
-
-
?
2,4,6-trichlorophenol + H2O2

? + H2O
-
63% of the activity with 2,4-dichlorophenol
-
-
?
2,4,6-trichlorophenol + H2O2
? + H2O
-
63% of the activity with 2,4-dichlorophenol
-
-
?
2,4-dichlorophenol + H2O2

?
-
-
-
-
?
2,4-dichlorophenol + H2O2
?
-
-
-
-
?
2,4-dichlorophenol + H2O2
?
-
-
-
-
?
2-chloro-1,4-dimethoxybenzene

?
-
-
-
-
?
2-chloro-1,4-dimethoxybenzene
?
-
-
-
-
?
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
-
?
Direct Blue GLL dye + H2O2

?
-
-
-
-
r
Direct Blue GLL dye + H2O2
?
-
-
-
-
r
humic acid + H2O2

?
-
-
-
-
?
humic acid + H2O2
?
-
-
-
-
?
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
-
?
humic acid + H2O2
? + H2O
-
-
-
-
?
humic acid + H2O2
? + H2O
-
-
-
-
?
L-Dopa + H2O2

?
-
-
-
-
?
L-Dopa + 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
-
-
?
lignin + H2O2
? + H2O
substrate is Kraft lignin
-
-
?
mimosine + H2O2

?
-
-
-
-
?
mimosine + H2O2
?
-
-
-
-
?
n-propanol + H2O2

propanal + H2O
-
-
-
-
?
n-propanol + H2O2
propanal + H2O
-
-
-
-
?
n-propanol + H2O2

propanaldehyde + H2O
-
-
-
-
?
n-propanol + H2O2
propanaldehyde + H2O
-
-
-
-
?
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
-
-
?
o-dianisidine + H2O2

? + H2O
-
76% of the activity with 2,4-dichlorophenol
-
-
?
o-dianisidine + H2O2
? + H2O
-
76% of the activity with 2,4-dichlorophenol
-
-
?
oxytetracycline + H2O2

?
-
LiP shows strong degrading ability
-
-
?
oxytetracycline + H2O2
?
-
LiP shows strong degrading ability
-
-
?
tetracycline + 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
-
-
-
-
?
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
Lentinus strigellus
-
-
-
-
?
veratryl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
Lentinus strigellus SXS355
-
-
-
-
?
veratryl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
-
-
-
-
?
veratryl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
-
-
-
-
?
veratryl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
Loweporus lividus
-
-
-
-
?
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 7â9. 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
Phanerochaete chrysosporium F. F. Lombard / ME-446 / ATCC 43541
-
-
-
-
?
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
-
-
-
-
?
veratryl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
-
-
-
-
?
veratryl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
Polyporous velutinus
-
-
-
-
?
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
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
-
-
-
-
?
veratryl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
-
-
-
-
?
veratryl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
-
-
-
-
?
veratryl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
-
-
-
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?
veratryl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
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-
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-
?
veratryl alcohol + H2O2

?
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-
-
-
?
veratryl alcohol + H2O2
?
-
-
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-
?
veratryl alcohol + H2O2
?
-
-
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-
?
veratryl alcohol + H2O2
?
-
-
-
?
veratryl alcohol + H2O2

veratraldehyde + H2O
-
-
-
-
?
veratryl alcohol + H2O2
veratraldehyde + H2O
-
-
-
-
?
veratryl alcohol + H2O2
veratraldehyde + H2O
-
-
-
?
veratryl alcohol + H2O2 + H+

veratraldehyde + H2O
-
-
-
-
?
veratryl alcohol + H2O2 + H+
veratraldehyde + H2O
-
-
-
?
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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-
?
veratryl alcohol + H2O2 + H+
veratraldehyde + H2O
-
-
-
-
?
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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-
?
veratryl alcohol + H2O2 + H+
veratraldehyde + H2O
-
-
-
?
veratryl alcohol + H2O2 + H+
veratraldehyde + H2O
-
-
-
-
?
veratryl alcohol + H2O2 + H+
veratraldehyde + H2O
-
-
-
-
?
additional information

?
-
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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)
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?
additional information
?
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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)
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?
additional information
?
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tyrosinase (EC 1.14.18.1) has a promiscuous activity for oxidizing the lignin-related nonphenolic substrate veratryl alcohol, catalyzing the reaction of heme-containing lignin peroxidase, LiP, EC 1.11.1.14. Tyrosinase exhibits a broad substrate specificity for various phenolic compounds
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
-
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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
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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
?
-
-
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
?
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of the aryl-CalphaHOH-CbetaHR-CgammaH2OH-type (R being aryl or O-aryl)
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-
?
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
?
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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
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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
-
-
?
additional information
?
-
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
?
-
-
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
?
-
Phanerochaete chrysosporium F. F. Lombard / ME-446 / ATCC 43541
-
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
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-
?
additional information
?
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first enzyme connected to oxidative breakdown of the aromatic plant heteropolymer lignin and related xenobiotics
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-
?
additional information
?
-
first enzyme connected to oxidative breakdown of the aromatic plant heteropolymer lignin and related xenobiotics
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-
?
additional information
?
-
-
first enzyme connected to oxidative breakdown of the aromatic plant heteropolymer lignin and related xenobiotics
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-
?
additional information
?
-
-
oxidation of various phenolic and non-phenolic lignin model-compounds
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-
?
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
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?
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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Breast Neoplasms
Orf239342 from the mushroom Agaricus bisporus is a mannose binding protein.
Cardiovascular Diseases
PXDN reduces autophagic flux in insulin-resistant cardiomyocytes via modulating FoxO1.
Herpes Simplex
Antiviral melanization reaction of Heliothis virescens hemolymph against DNA and RNA viruses in vitro.
Hyperpigmentation
Optimization of Phenolics Extracted from Idesia polycarpa Defatted Fruit Residue and Its Antioxidant and Depigmenting Activity In Vitro and In Vivo.
Hyperpigmentation
Oxyresveratrol and hydroxystilbene compounds. Inhibitory effect on tyrosinase and mechanism of action.
Hyperpigmentation
Screening of Nepalese crude drugs traditionally used to treat hyperpigmentation: in vitro tyrosinase inhibition.
Melanoma
Anti-melanogenic activity of Viola odorata different extracts on B16F10 murine melanoma cells.
Melanoma
Antimelanogenesis Effects of Fungal Exopolysaccharides Prepared from Submerged Culture of Fomitopsis castanea Mycelia.
Melanoma
Byelyankacin: a novel melanogenesis inhibitor produced by Enterobacter sp. B20.
Melanoma
Chemical and bioactivity of flavanones obtained from roots of Dalea pazensis Rusby.
Melanoma
Comparative study of tyrosinases from different sources: relationship between halide inhibition and the enzyme active site.
Melanoma
Design, synthesis, and anti-melanogenic effects of (E)-2-benzoyl-3-(substituted phenyl)acrylonitriles.
Melanoma
Dual Bioactivities of Essential Oil Extracted from the Leaves of Artemisia argyi as an Antimelanogenic versus Antioxidant Agent and Chemical Composition Analysis by GC/MS.
Melanoma
Effects of quercetin on mushroom tyrosinase and B16-F10 melanoma cells.
Melanoma
Ethyl acetate extract from Panax ginseng C.A. Meyer and its main constituents inhibit ?-melanocyte-stimulating hormone-induced melanogenesis by suppressing oxidative stress in B16 mouse melanoma cells.
Melanoma
Evaluation of depigmenting activity by 8-hydroxydaidzein in mouse b16 melanoma cells and human volunteers.
Melanoma
Free-Radical-Scavenging, Antityrosinase, and Cellular Melanogenesis Inhibitory Activities of Synthetic Isoflavones.
Melanoma
Halogenated aromatic thiosemicarbazones as potent inhibitors of tyrosinase and melanogenesis.
Melanoma
Inhibitory effect of ephedrannins A and B from roots of Ephedra sinica STAPF on melanogenesis.
Melanoma
Inhibitory effect of Gastrodia elata extract on melanogenesis in HM3KO melanoma cells.
Melanoma
Inhibitory Effect of Phlorotannins Isolated from Ecklonia cava on Mushroom Tyrosinase Activity and Melanin Formation in Mouse B16F10 Melanoma Cells.
Melanoma
Inhibitory effect of [6]-gingerol on melanogenesis in B16F10 melanoma cells and a possible mechanism of action.
Melanoma
Inhibitory Effects of (2'R)-2',3'-dihydro-2'-(1-hydroxy-1-methylethyl)-2,6'-bibenzofuran-6,4'-diol on Mushroom Tyrosinase and Melanogenesis in B16-F10 Melanoma Cells.
Melanoma
Inhibitory effects of phytoncide solution on melanin biosynthesis.
Melanoma
Inhibitory effects of Sargassum polycystum on tyrosinase activity and melanin formation in B16F10 murine melanoma cells.
Melanoma
Involvement of the p38 MAPK and ERK signaling pathway in the anti-melanogenic effect of methyl 3,5-dicaffeoyl quinate in B16F10 mouse melanoma cells.
Melanoma
Lightening effect on ultraviolet-induced pigmentation of guinea pig skin by oral administration of a proanthocyanidin-rich extract from grape seeds.
Melanoma
Mechanism and inhibitory effect of galangin and its flavonoid mixture from Alpinia officinarum on mushroom tyrosinase and B16 murine melanoma cells.
Melanoma
Melanogenesis effect of Cordyceps militaris culture broth on the melanin formation of B16F0 melanoma cells.
Melanoma
Melanogenic inhibitory effects of Triangularin in B16F0 melanoma cells, in vitro and molecular docking studies.
Melanoma
Molecular docking studies of a phlorotannin, dieckol isolated from Ecklonia cava with tyrosinase inhibitory activity.
Melanoma
Papuabalanols A and B, new tannins from Balanophora papuana.
Melanoma
pH-dependent interconvertible forms of mushroom tyrosinase with different kinetic properties.
Melanoma
Piceatannol inhibits melanogenesis by its antioxidative actions.
Melanoma
Skin-whitening mechanism of cumin (Cuminum cyminum L.) extract.
Melanoma
Spiro-acridine inhibiting tyrosinase enzyme: Kinetic, protein-ligand interaction and molecular docking studies.
Melanoma
Structural requirement of phenylthiourea analogs for their inhibitory activity of melanogenesis and tyrosinase.
Melanoma
Synthesis and antityrosinase mechanism of benzaldehyde thiosemicarbazones: novel tyrosinase inhibitors.
Melanoma
Synthesis and preliminary in vitro biological evaluation of 4-[(4-hydroxyphenyl)sulfanyl]but-3-en-2-one, a 4-mercaptophenol derivative designed as a novel bifunctional antimelanoma agent.
Melanoma
The Organogermanium Compound THGP Suppresses Melanin Synthesis via Complex Formation with L-DOPA on Mushroom Tyrosinase and in B16 4A5 Melanoma Cells.
Melanoma
The role of sulfhydryl compounds in mammalian melanogenesis: the effect of cysteine and glutathione upon tyrosinase and the intermediates of the pathway.
Melanoma
[8]-Gingerol inhibits melanogenesis in murine melanoma cells through down-regulation of the MAPK and PKA signal pathways.
Melanoma, Experimental
Acetoside inhibits alpha-MSH-induced melanin production in B16 melanoma cells by inactivation of adenyl cyclase.
Melanoma, Experimental
Antimelanogenic and antioxidant properties of gallic acid.
Melanoma, Experimental
Antioxidant and antimelanogenic activities of polyamine conjugates from corn bran and related hydroxycinnamic acids.
Melanoma, Experimental
Effects of salicylic acid on mushroom tyrosinase and B16 melanoma cells.
Melanoma, Experimental
Inhibitory effect of artocarpanone from Artocarpus heterophyllus on melanin biosynthesis.
Melanoma, Experimental
Inhibitory effects of hinokitiol on tyrosinase activity and melanin biosynthesis and its antimicrobial activities.
Melanoma, Experimental
Inhibitory effects of Na7PMo11CuO40 on mushroom tyrosinase and melanin formation and its antimicrobial activities.
Melanoma, Experimental
Melanin biosynthesis inhibitory and antioxidant activities of quercetin-3'-O-beta-D-glucoside isolated from Allium cepa.
Melanoma, Experimental
Melanocins A, B and C, new melanin synthesis inhibitors produced by Eupenicillium shearii. I. Taxonomy, fermentation, isolation and biological properties.
Melanoma, Experimental
Poly-?-glutamate from Bacillus subtilis inhibits tyrosinase activity and melanogenesis.
Melanoma, Experimental
Quantitative proteomic analysis uncovers inhibition of melanin synthesis by silk fibroin via MITF/tyrosinase axis in B16 melanoma cells.
Melanoma, Experimental
ROS-scavenging and anti-tyrosinase properties of crocetin on B16F10 murine melanoma cells.
Melanoma, Experimental
The effects of areca catechu L extract on anti-inflammation and anti-melanogenesis.
Melanosis
Reduction of facial pigmentation of melasma by topical lignin peroxidase: A novel fast-acting skin-lightening agent.
Melanosis
Topical Treatments for Melasma: A Systematic Review of Randomized Controlled Trials
Neoplasms
Biological activities of phenolic compounds isolated from galls of Terminalia chebula Retz. (Combretaceae).
Neoplasms
Biological activity and molecular docking studies of curcumin-related ?,?-unsaturated carbonyl-based synthetic compounds as anticancer agents and mushroom tyrosinase inhibitors.
Neoplasms
Stimulation of erythrocyte cell membrane scrambling by mushroom tyrosinase.
Parkinson Disease
Role of peroxidases in Parkinson disease: a hypothesis.
Starvation
Disordered ultrastructure in lignin-peroxidase-secreting hyphae of the white-rot fungus Phanerochaete chrysosporium.
Starvation
Effect of Environmental Conditions on Extracellular Protease Activity in Lignolytic Cultures of Phanerochaete chrysosporium.
Tuberculosis
Reaction of haem containing proteins and enzymes with hydroperoxides: the radical view.
Vitiligo
Inhibition of experimental autoimmune vitiligo by oral administration of mushroom tyrosinase.
Vitiligo
Tyrosinase as an autoantigen in patients with vitiligo.
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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
-
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

-
degradation of different recalcitrant compounds, removal of toxic dyes
degradation
-
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
-
enzyme shows marked dye-decolorization efficiency and stability toward denaturing, oxidizing, and bleaching agents, and compatibility with EcoVax and Dipex as laundry detergents for 48 h at 40°C
degradation
-
degradation of different recalcitrant compounds, removal of toxic dyes
-
degradation
-
enzyme shows marked dye-decolorization efficiency and stability toward denaturing, oxidizing, and bleaching agents, and compatibility with EcoVax and Dipex as laundry detergents for 48 h at 40°C
-
degradation
-
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
-
environmental protection

-
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
-
decolorization of textile dyes
environmental protection
-
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
-
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
-
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
-
lignin peroxidase has a applicable potential for the degradation of sulfonated azo dyes
environmental protection
-
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
-
the enzyme is able to decolorize synthetic dyes
environmental protection
-
the enzyme is able to decolorize synthetic dyes
environmental protection
-
the enzyme is able to decolorize synthetic dyes
environmental protection
-
the enzyme is able to decolorize synthetic dyes
environmental protection
Lentinus strigellus
-
the enzyme is able to decolorize synthetic dyes
environmental protection
-
the enzyme is able to decolorize synthetic dyes
-
environmental protection
Lentinus strigellus SXS355
-
the enzyme is able to decolorize synthetic dyes
-
environmental protection
-
decolorization of textile dyes
-
environmental protection
-
the enzyme is able to decolorize synthetic dyes
-
environmental protection
-
the enzyme is able to decolorize synthetic dyes
-
environmental protection
-
the enzyme is able to decolorize synthetic dyes
-
industry

-
the enzyme can be used as biocatalytic in delignification (which is emerging owing to its superior selectivity, low energy consumption, and unparalleled sustainability) iIn the biorefinery utilizing lignocellulosic biomasses, lignin decomposition to value-added phenolic derivatives
industry
-
the enzyme can be used as biocatalytic in delignification (which is emerging owing to its superior selectivity, low energy consumption, and unparalleled sustainability) iIn the biorefinery utilizing lignocellulosic biomasses, lignin decomposition to value-added phenolic derivatives
synthesis

-
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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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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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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