1.11.1.14: lignin peroxidase
This is an abbreviated version!
For detailed information about lignin peroxidase, go to the full flat file.
Word Map on EC 1.11.1.14
-
1.11.1.14
-
chrysosporium
-
phanerochaete
-
manganese
-
laccase
-
melanin
-
ligninolytic
-
veratryl
-
peroxidases
-
melanoma
-
melanogenesis
-
white-rot
-
kojic
-
decolor
-
l-dopa
-
diphenolase
-
basidiomycete
-
trametes
-
monophenolase
-
versicolor
-
hyperpigmentation
-
lignin-degrading
-
whitening
-
textile
-
anti-tyrosinase
-
o-quinones
-
manganese-dependent
-
l-3,4-dihydroxyphenylalanine
-
microphthalmia-associated
-
anti-melanogenic
-
o-diphenols
-
bjerkandera
-
arbutin
-
skin-whitening
-
non-phenolic
-
1.14.18.1
-
dopaquinone
-
phlebia
-
tyrosinase-related
-
delignification
-
dopachrome
-
remazol
-
lignocellulolytic
-
anti-melanogenesis
-
eryngii
-
tyrosinases
-
catecholase
-
depigmenting
-
biotechnology
-
dye-decolorizing
-
synthesis
-
environmental protection
-
lignocellulose-degrading
-
analysis
-
degradation
-
industry
-
irpex
- 1.11.1.14
- chrysosporium
- phanerochaete
- manganese
- laccase
- melanin
-
ligninolytic
-
veratryl
- peroxidases
- melanoma
-
melanogenesis
-
white-rot
-
kojic
-
decolor
- l-dopa
- diphenolase
-
basidiomycete
- trametes
- monophenolase
- versicolor
- hyperpigmentation
-
lignin-degrading
-
whitening
-
textile
-
anti-tyrosinase
- o-quinones
-
manganese-dependent
- l-3,4-dihydroxyphenylalanine
-
microphthalmia-associated
-
anti-melanogenic
- o-diphenols
- bjerkandera
- arbutin
-
skin-whitening
-
non-phenolic
-
1.14.18.1
- dopaquinone
- phlebia
-
tyrosinase-related
-
delignification
- dopachrome
-
remazol
-
lignocellulolytic
-
anti-melanogenesis
- eryngii
- tyrosinases
- catecholase
-
depigmenting
- biotechnology
-
dye-decolorizing
- synthesis
- environmental protection
-
lignocellulose-degrading
- analysis
- degradation
- industry
- irpex
Reaction
Synonyms
ALiP-P3, bacterial lignin peroxidase, diarylpropane oxygenase, diarylpropane peroxidase, diarylpropane:oxygen,hydrogen-peroxide oxidoreductase (C-C-bond-cleaving), DypB, fungal lignin peroxidase, Glg4, H2O2-dependent ligninase, heme-containing lignin peroxidase, heme-containing peroxidase, lignin peroxidase, lignin peroxidase H8, lignin peroxidase isozyme H8, lignin peroxidase LIII, ligninase, ligninase H2, ligninase H8, ligninase I, ligninase LG5, LIP, Lip1, LIP2, LiPH8, lipJ, LPA, LPOA, microbial lignin peroxidase, More, mushroom tyrosinase, oxygenase, diarylpropane, Pr-lip1, Pr-lip4
ECTree
1.11.1.14 lignin peroxidaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 1.11.1.14 - lignin peroxidase
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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
-
?
1-phenyl-1,2-ethandiol + H2O2
? + 2 H2O
substrate of N246A mutant enzyme
-
-
?
1-phenyl-1-propanol + H2O2
? + 2 H2O
substrate of N246A mutant enzyme
-
-
?
1-phenyl-2-propanol + H2O2
? + 2 H2O
substrate of N246A mutant enzyme
-
-
?
1-phenylethanol + H2O2
? + 2 H2O
substrate of N246A mutant enzyme
-
-
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
activity of EC 1.11.1.13
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H+ + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
-
-
-
?
2,6-dimethoxyphenol + 2 H+ + H2O2
oxidized 2,6-dimethoxyphenol + 2 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
-
-
?
Azure B + 2 H+ + H2O2
oxidized Azure B + 2 H2O
dye decolorization, substrate of N246A mutant enzyme
-
-
?
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
-
?
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
-
-
?
guaiacylglycerol-beta-guaiacyl ether + H2O2
glycerol + guaiacol + 2 H2O
GGE, substrate of mutant enzyme N246A
-
-
?
lignocellulose + H2O2
? + H2O
substrate is wheat straw lignocellulose
-
-
?
mitoxantrone + H2O2
hexahydronaphtho-[2,3-f]-quinoxaline-7,12-dione + H2O
-
low efficiency
-
-
?
Reactive Black 5 + 2 H+ + H2O2
oxidized Reactive Black 5 + 2 H2O
dye decolorization, substrate of N246A mutant enzyme
-
-
?
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
-
-
-
?
remazol brilliant blue R + H2O2
oxidized remazol brilliant blue R + 2 H2O
substrate of N246A mutant enzyme
-
-
?
veratryl alcohol + H2O2
3,4-dimethoxybenzoic acid + 2 H2O
substrate of N246A mutant enzyme
-
-
?
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
Phanerodontia chrysosporium BKM-F 1767
-
-
-
-
?
1,2-bis(3,4-dimethoxyphenyl)propane-1,3-diol + H2O2
3,4-dimethoxybenzaldehyde + 1-(3,4-dimethyl-phenyl)ethane-1,2-diol + H2O
Phanerodontia chrysosporium BKM-F-1767
-
-
-
-
?
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
?
Phanerodontia chrysosporium BKM-F 1767
-
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
?
Phanerodontia chrysosporium BKM-F-1767
-
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
?
Phanerodontia chrysosporium VKM F-1767
-
-
-
-
?
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
?
Phlebia radiata 79 / ATCC 64658
-
-
-
-
?
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 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 veratryl alcohol + H2O2
2 veratryl aldehyde + 2 H2O
-
-
-
-
?
2 veratryl alcohol + H2O2
2 veratryl aldehyde + 2 H2O
-
-
-
?
2 veratryl alcohol + H2O2
2 veratryl aldehyde + 2 H2O
-
-
-
?
2 veratryl alcohol + H2O2
2 veratryl aldehyde + 2 H2O
-
-
-
-
?
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
-
-
?
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
Phanerodontia chrysosporium BKM-F 1767
-
veratryl alcohol
-
-
?
3,4-dimethoxybenzyl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
Phanerodontia chrysosporium BKM-F-1767
-
veratryl alcohol
-
-
?
3,4-dimethoxybenzyl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
-
veratryl alcohol
-
?
3,4-dimethoxybenzyl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
Phlebia radiata 79 / ATCC 64658
-
veratryl alcohol
-
?
coomassie brilliant blue + H2O2
?
-
decolorization of a textile dye
-
-
?
coomassie brilliant blue + H2O2
?
Pseudomonas fluorescens LiP-RL5
-
decolorization of a textile dye
-
-
?
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
-
-
?
melanin + H2O2
?
-
pH 3, 40 °C, 15 IU/ml, and 10 h incubation are the optimal conditions for the degradation of the melanin. The use of the mediator veratryl alcohol is effective to enhance the efficacy of the melanin degradation, with up to 92% decolorization, method evaluation and optimization, overview
-
-
?
melanin + H2O2
?
-
pH 3, 40 °C, 15 IU/ml, and 10 h incubation are the optimal conditions for the degradation of the melanin. The use of the mediator veratryl alcohol is effective to enhance the efficacy of the melanin degradation, with up to 92% decolorization, method evaluation and optimization, overview
-
-
?
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
?
Phanerodontia chrysosporium BKM-F 1767
-
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
?
Phanerodontia chrysosporium BKM-F-1767
-
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
?
Phanerodontia chrysosporium BKM-F-1767
-
LiP shows strong degrading ability
-
-
?
tetracycline + H2O2
?
Phanerodontia chrysosporium BKM-F-1767
-
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
-
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 79. 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
Phanerodontia chrysosporium ATCC 20696
-
optimum culture conditions
-
-
?
veratryl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
Phanerodontia chrysosporium BKM-F-1767
-
-
-
-
?
veratryl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
Phanerodontia chrysosporium F. F. Lombard / ME-446 / ATCC 43541
-
-
-
-
?
veratryl alcohol + H2O2
3,4-dimethoxybenzaldehyde + H2O
Phanerodontia chrysosporium MTCC 787
-
-
-
-
?
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
3,4-dimethoxybenzaldehyde + H2O
-
-
-
-
?
veratryl alcohol + H2O2 + H+
veratraldehyde + H2O
-
-
-
-
?
veratryl alcohol + H2O2 + H+
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 + H+
veratraldehyde + H2O
Phanerodontia chrysosporium ATCC 24725
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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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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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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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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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oxidation degradation reaction of lignin in the corn stover (CS) is catalyzed by LiP from Aspergillus oryzae, optimization of a biodegradation process, overview
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LiP uses H2O2 to catalyze one-electron oxidation of chemicals to free radicals. Hydrogen peroxide oxidizes the heme-LiP by two electrons to LiP I, a ferryl (Fe(IV)) n-porphyrin cation radical of LiP. A substrate molecule can then be oxidized by one electron to a radical, and LiP I is reduced by one electron to LiP II. A subsequent oxidation of another substrate molecule by LiP II returns the LiP to its ferric resting state. The presence of excess H2O2 or slow reduction of LiP II to resting state may lead to the oxidation of LiP II to LiP III, an inactivated enzyme form. This is called LiP cycle. Optimization of enzyme activity measurement and assay condition, overview. The optimum combination of parameters for the maximum is as follows, including pretreatment temperature of 120°C, pretreatment time of 5 min, reaction temperature of 30°C, enzyme amount of 3.75 U/100 ml, 50 mM sodium lactate-hydrochloric acid buffer of pH 1.5, H2O2 concentration of 20 mM and H2O2 amount of 1 ml
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the maximal yield of total reducing sugar (Ytrs) by synergistic effect analysis between LiP and three enzyme components of cellulase (endo-beta-1,4-glucanase, exo-beta-1,4-glucanase and beta-glucosidase), oxidation and degradation of lignin, overview
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Aspergillus oryzae CGMCC5992
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the maximal yield of total reducing sugar (Ytrs) by synergistic effect analysis between LiP and three enzyme components of cellulase (endo-beta-1,4-glucanase, exo-beta-1,4-glucanase and beta-glucosidase), oxidation and degradation of lignin, overview
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Aspergillus oryzae CGMCC5992
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oxidation degradation reaction of lignin in the corn stover (CS) is catalyzed by LiP from Aspergillus oryzae, optimization of a biodegradation process, overview
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Aspergillus oryzae CGMCC5992
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LiP uses H2O2 to catalyze one-electron oxidation of chemicals to free radicals. Hydrogen peroxide oxidizes the heme-LiP by two electrons to LiP I, a ferryl (Fe(IV)) n-porphyrin cation radical of LiP. A substrate molecule can then be oxidized by one electron to a radical, and LiP I is reduced by one electron to LiP II. A subsequent oxidation of another substrate molecule by LiP II returns the LiP to its ferric resting state. The presence of excess H2O2 or slow reduction of LiP II to resting state may lead to the oxidation of LiP II to LiP III, an inactivated enzyme form. This is called LiP cycle. Optimization of enzyme activity measurement and assay condition, overview. The optimum combination of parameters for the maximum is as follows, including pretreatment temperature of 120°C, pretreatment time of 5 min, reaction temperature of 30°C, enzyme amount of 3.75 U/100 ml, 50 mM sodium lactate-hydrochloric acid buffer of pH 1.5, H2O2 concentration of 20 mM and H2O2 amount of 1 ml
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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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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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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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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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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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oxidation of various phenolic and non-phenolic lignin model-compounds
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oxidation of various phenolic and non-phenolic lignin model-compounds
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additional information
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oxidation of various phenolic and non-phenolic lignin model-compounds
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additional information
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oxidation of various phenolic and non-phenolic lignin model-compounds
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additional information
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oxidation of various phenolic and non-phenolic lignin model-compounds
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of the aryl-CalphaHOH-CbetaHR-CgammaH2OH-type (R being aryl or O-aryl)
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intradiol cleavage in phenylglycol structures, hydroxylation of benzylic methylene groups, oxidative coupling of phenols, all reactions require H2O2, Calpha-Cbeta cleavage and methylene hydroxylation involve substrate oxygenation, the oxygen atom originates from O2 not H2O2: thus the enzyme acts as oxygenase which requires H2O2
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additional information
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intradiol cleavage in phenylglycol structures, hydroxylation of benzylic methylene groups, oxidative coupling of phenols, all reactions require H2O2, Calpha-Cbeta cleavage and methylene hydroxylation involve substrate oxygenation, the oxygen atom originates from O2 not H2O2: thus the enzyme acts as oxygenase which requires H2O2
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with concomitant insertion of 1 atom of molecular oxygen
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with concomitant insertion of 1 atom of molecular oxygen
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oxidation of benzyl alcohols to aldehydes or ketones
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oxidation of benzyl alcohols to aldehydes or ketones
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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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decolourization of two waterless-soluble aromatic dyes (pyrogallol red and bromopyrogallol red) using lignin peroxidase coupled with glucose oxidase in the medium demonstrates that a higher decolourization percentage is obtained if H2O2 is supplied enzymatically
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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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the removal mechanism of catechol derivatives seems to be different for each catecholic substrate in terms of substrate consumption and transformation, and of enzyme activity
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selective and efficient lignin peroxidase isozyme H8 catalyzed depolymerization of the phenolic lignin dimer
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selective and efficient lignin peroxidase isozyme H8 catalyzed depolymerization of the phenolic lignin dimer
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catalysis of degradation of the dimer to products by an acid-stabilized variant of lignin peroxidase isozyme H8 increases from 38.4% at pH 5.0 to 92.5% at pH 2.6. At pH 2.6, the observed product distribution results from 65.5% beta-O-4' ether bond cleavage, 27.0% Calpha-C1 carbon bond cleavage, and 3.6% Calpha-oxidation as by-product. Enzyme LiPH8 catalyzes the oxidative cleavage of both beta-O-4' ether and C-C bonds in aryl ether dimers and catalyzes breaking of beta-O-4' ether, C-C, and C-H bonds in trimeric lignin model compounds. The distribution of products is pH-dependent. Study catalysis of bond cleavage events in a phenolic lignin dimer by quantitative analysis of product formation during LiPH8-catalyzed degradation of a GGE model compound (GGE-NIMS compound) using nanostructure-initiator mass spectrometry. Low pH conditions drive reaction equilibrium toward the favorable formation of the active cationic radical intermediate. The cationic radical intermediate formed from LiPH8/H2O2-catalyzed 1-electron oxidation of GGE dimer is capable of undergoing a variety of reactions such as side-chain oxidation, C-C bond, and beta-O-4' ether bond cleavage. The intermediates are predicted from a heterolytic bond cleavage reaction mechanism when the first step 1-electron oxidation takes place at lower redox potential-Ring A. The deprotonation of the short-lived cationic radical results in the formation of the phenoxy radical which sequentially cleaved into fragments. Protonation of hydroxyl group under acidic conditions is a key step in bond-cleavage pathways
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catalysis of degradation of the dimer to products by an acid-stabilized variant of lignin peroxidase isozyme H8 increases from 38.4% at pH 5.0 to 92.5% at pH 2.6. At pH 2.6, the observed product distribution results from 65.5% beta-O-4' ether bond cleavage, 27.0% Calpha-C1 carbon bond cleavage, and 3.6% Calpha-oxidation as by-product. Enzyme LiPH8 catalyzes the oxidative cleavage of both beta-O-4' ether and C-C bonds in aryl ether dimers and catalyzes breaking of beta-O-4' ether, C-C, and C-H bonds in trimeric lignin model compounds. The distribution of products is pH-dependent. Study catalysis of bond cleavage events in a phenolic lignin dimer by quantitative analysis of product formation during LiPH8-catalyzed degradation of a GGE model compound (GGE-NIMS compound) using nanostructure-initiator mass spectrometry. Low pH conditions drive reaction equilibrium toward the favorable formation of the active cationic radical intermediate. The cationic radical intermediate formed from LiPH8/H2O2-catalyzed 1-electron oxidation of GGE dimer is capable of undergoing a variety of reactions such as side-chain oxidation, C-C bond, and beta-O-4' ether bond cleavage. The intermediates are predicted from a heterolytic bond cleavage reaction mechanism when the first step 1-electron oxidation takes place at lower redox potential-Ring A. The deprotonation of the short-lived cationic radical results in the formation of the phenoxy radical which sequentially cleaved into fragments. Protonation of hydroxyl group under acidic conditions is a key step in bond-cleavage pathways
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lignin peroxidase is an extracellular hemeprotein that is H2O2-dependent, with an unusually high redox potential and low optimum pH. It is capable of oxidizing a variety of reducing substrates, including polymeric substrates. It has the distinction of being able to oxidize methoxylated aromatic rings without a free phenolic group, which generates cation radicals that can react further by a variety of pathways, including ring opening, demethylation, and phenol dimerization. In contrast with laccases, LiP does not require mediators to degrade high redox-potential compounds, but it needs H2O2 to initiate catalysis. Substrate specificity, no or poor activity with ferulic acid, vanillic acid, diaminobenzidine, and HoBT. Purified LiP obtained from immobilized Phanerochaete chrysosporium completely decolorizes bromophenyl blue, bromothymol blue, and bromocresol green, purified enzyme from immobilized Phanerochaete chrysosporium shows increased dye decolorization efficiency compared to the enzyme from non-immobilized Phanerochaete chrysosporium
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lignin peroxidase isozyme H8 from the white-rot fungus Phanerochaete chrysosporium (LiPH8) demonstrates a high redox potential and can efficiently catalyze the oxidation of veratryl alcohol, as well as the degradation of recalcitrant lignin
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lignin peroxidase isozyme H8 from the white-rot fungus Phanerochaete chrysosporium (LiPH8) demonstrates a high redox potential and can efficiently catalyze the oxidation of veratryl alcohol, as well as the degradation of recalcitrant lignin
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partially purified lignin peroxidase is used for the degradation of polyvinyl chloride (PVC) films, a significant reduction in the weight of PVC film is observed (31%), measurement of CO2 as reaction product. FTIR spectra of the enzyme-treated plastic film reveal structural changes in the chemical composition, indicating a specific peak at 2943/cm that correspond to alkenyl C-H stretch. Deterioration on the surface of PVC films is confirmed by scanning electron microscopy tracked through activity assay for the lignin peroxidase
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the fungal lignin peroxidase does not produce the veratryl alcohol cation radical as a diffusible ligninolytic oxidant. Reaction-diffusion model and solution-phase model, overview. The oxidation of veratryl alcohol (VA) by the enzyme in air at physiological pH 4.5 consumes O2 and produces about 1.1 veratraldehyde per H2O2 supplied. This finding suggests that some VAx02cation radical may escape oxidation at the enzyme's active site, hydrolyzing instead to give benzylic radicals that rapidly add O2. The resulting alpha-hydroxyperoxyl radicals would in turn eliminate the H2O2 precursor HO2 radical, thus accounting for the enhancement in veratraldehyde yield. VA is required for the enzyme to oxidize 4-methoxymandelic acid, which quenches the ESR signal of the VA produced, and veratraldehyde production during these reactions occurs only after all of the 4-methoxymandelic acid has been consumed. Moreover, the rate of 4-methoxymandelic acid oxidation by the enzyme exhibits saturation kinetics as the concentration of VA is increased. Enzymatic oxidations of dye-functionalized beads
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Phanerodontia chrysosporium BKM-F 1767
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oxidation of various phenolic and non-phenolic lignin model-compounds
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Phanerodontia chrysosporium BKM-F-1767
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oxidation of various phenolic and non-phenolic lignin model-compounds
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additional information
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Phanerodontia chrysosporium BKM-F-1767
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oxidation of various phenolic and non-phenolic lignin model-compounds
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additional information
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Phanerodontia chrysosporium BKM-F-1767
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of the aryl-CalphaHOH-CbetaHR-CgammaH2OH-type (R being aryl or O-aryl)
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additional information
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Phanerodontia chrysosporium BKM-F-1767
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intradiol cleavage in phenylglycol structures, hydroxylation of benzylic methylene groups, oxidative coupling of phenols, all reactions require H2O2, Calpha-Cbeta cleavage and methylene hydroxylation involve substrate oxygenation, the oxygen atom originates from O2 not H2O2: thus the enzyme acts as oxygenase which requires H2O2
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additional information
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Phanerodontia chrysosporium BKM-F-1767
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with concomitant insertion of 1 atom of molecular oxygen
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Phanerodontia chrysosporium BKM-F-1767
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oxidation of benzyl alcohols to aldehydes or ketones
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Phanerodontia chrysosporium F. F. Lombard / ME-446 / ATCC 43541
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decolourization of two waterless-soluble aromatic dyes (pyrogallol red and bromopyrogallol red) using lignin peroxidase coupled with glucose oxidase in the medium demonstrates that a higher decolourization percentage is obtained if H2O2 is supplied enzymatically
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additional information
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partially purified lignin peroxidase is used for the degradation of polyvinyl chloride (PVC) films, a significant reduction in the weight of PVC film is observed (31%), measurement of CO2 as reaction product. FTIR spectra of the enzyme-treated plastic film reveal structural changes in the chemical composition, indicating a specific peak at 2943/cm that correspond to alkenyl C-H stretch. Deterioration on the surface of PVC films is confirmed by scanning electron microscopy tracked through activity assay for the lignin peroxidase
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additional information
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oxidation of various phenolic and non-phenolic lignin model-compounds
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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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first enzyme connected to oxidative breakdown of the aromatic plant heteropolymer lignin and related xenobiotics
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first enzyme connected to oxidative breakdown of the aromatic plant heteropolymer lignin and related xenobiotics
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first enzyme connected to oxidative breakdown of the aromatic plant heteropolymer lignin and related xenobiotics
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Phlebia radiata 79 / ATCC 64658
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oxidation of various phenolic and non-phenolic lignin model-compounds
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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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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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enzyme DypB degrades solvent-obtained fractions of a Kraft lignin. The recombinant mutant enzyme Rh_DypB shows a classical peroxidase activity which is significantly increased by adding Mn2+ ions, kinetic parameters for H2O2, Mn2+, ABTS, and 2,6-DMP are determined. The enzyme shows broad dye-decolorization activity, especially in the presence of Mn2+, oxidizes various aromatic monomers from lignin, and cleaves the guaiacylglycerol-beta-guaiacyl ether (GGE), i.e., the Calpha-Cbeta bond of the dimeric lignin model molecule of beta-O-4 linkages. Under optimized conditions, 2 mM GGE is fully cleaved by recombinant Rh_DypB, generating guaiacol in only 10 min, at a rate of 12.5 micromol/min/mg enzyme. Screening of oxidation activity on monomeric lignin model compounds, overview
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additional information
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enzyme DypB degrades solvent-obtained fractions of a Kraft lignin. The recombinant mutant enzyme Rh_DypB shows a classical peroxidase activity which is significantly increased by adding Mn2+ ions, kinetic parameters for H2O2, Mn2+, ABTS, and 2,6-DMP are determined. The enzyme shows broad dye-decolorization activity, especially in the presence of Mn2+, oxidizes various aromatic monomers from lignin, and cleaves the guaiacylglycerol-beta-guaiacyl ether (GGE), i.e., the Calpha-Cbeta bond of the dimeric lignin model molecule of beta-O-4 linkages. Under optimized conditions, 2 mM GGE is fully cleaved by recombinant Rh_DypB, generating guaiacol in only 10 min, at a rate of 12.5 micromol/min/mg enzyme. Screening of oxidation activity on monomeric lignin model compounds, overview
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additional information
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oxidation of various phenolic and non-phenolic lignin model-compounds
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