1.11.1.16: versatile peroxidase
This is an abbreviated version!
For detailed information about versatile peroxidase, go to the full flat file.
Word Map on EC 1.11.1.16
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1.11.1.16
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lignin
-
pleurotus
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peroxidases
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ligninolytic
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eryngii
-
laccase
-
white-rot
-
bjerkandera
-
ostreatus
-
veratryl
-
adusta
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chrysosporium
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phanerochaete
-
lignin-degrading
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non-phenolic
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2,6-dimethoxyphenol
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delignification
-
aryl-alcohols
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degradation
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synthesis
-
industry
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analysis
-
paper production
- 1.11.1.16
- lignin
- pleurotus
- peroxidases
-
ligninolytic
- eryngii
- laccase
-
white-rot
- bjerkandera
- ostreatus
-
veratryl
- adusta
- chrysosporium
-
phanerochaete
-
lignin-degrading
-
non-phenolic
- 2,6-dimethoxyphenol
-
delignification
-
aryl-alcohols
- degradation
- synthesis
- industry
- analysis
- paper production
Reaction
Synonyms
B-type dye-decolorizing peroxidase, bacterial lignin peroxidase, DypB, manganese peroxidase 4, Mb peroxidase, metMb peroxidase, Mnp4, More, myoglobin, R1B4, versatile peroxidase, versatile peroxidase MnP2, versatile peroxidase VPL2 precursor, VP1, Vpl2, VPS1
ECTree
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Substrates Products
Substrates Products on EC 1.11.1.16 - versatile peroxidase
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REACTION DIAGRAM
1,4-dimethoxybenzene + H2O2
1,4-benzoquinone + formaldehyde + H2O
-
Mn2+-independent activity
-
-
?
1-methylanthracene + H2O2
1-methylanthraquinone + H2O
-
at 43% of the rate with 9-methylanthracene
-
-
?
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
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H+ + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + H+
?
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + H+
? + H2O
-
-
-
?
2,7-diaminofluorene + H2O2
? + H2O
-
during oxidation of 2,7-diaminofluorene, both with and without Mn2+, biphasic kinetics with apparent saturation in both micromolar and millimolar ranges are obtained
-
-
?
2-chloro-1,4-dimethoxybenzene + H2O2
2-chloro-1,4-benzoquinone + H2O
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Mn2+-independent activity
-
-
?
2-methylanthracene + H2O2
2-methylanthraquinone + H2O
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at 24% of the rate with 9-methylanthracene
-
-
?
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+
-
-
?
anthracene + H2O2
anthraquinone + H2O
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at 4.8% of the rate with 9-methylanthracene
-
-
?
Azure B + 2 H+ + H2O2
oxidized Azure B + 2 H2O
dye decolorization, substrate of N246A mutant enzyme
-
-
?
bovine pancreatic RNase
oxidized bovine pancreatic RNase
-
no redox mediators involved
-
-
?
carbazole + H2O2
? + H2O
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at 4.8% of the rate with 9-methylanthracene
-
-
?
guaiacylglycerol-beta-guaiacyl ether + H2O2
glycerol + guaiacol + 2 H2O
GGE, substrate of mutant enzyme N246A
-
-
?
indigo carmine + 2 H+ + H2O2
oxidized indigo carmine + 2 H2O
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dye decolorization
-
-
?
manganese(II)-substituted polyoxometalate + H2O2
manganese(III)-substituted polyoxometalate + H2O2
-
-
-
-
?
methyl green + 2 H+ + H2O2
oxidized methyl green + 2 H2O
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dye decolorization
-
-
?
Mn2+ + H2O2 + remazol black-5
?
-
incubation of enzyme with dyes rose bengal, remazol brilliant violet, remazol black-5, remazol blue-19, and remazol orange-16, results in the decolorization of all the dyes tested within a range of 71-84% after 16 h incubation with the enzyme at 100 U/l
-
-
?
Mn2+ + H2O2 + remazol blue-19
?
-
incubation of enzyme with dyes rose bengal, remazol brilliant violet, remazol black-5, remazol blue-19, and remazol orange-16, results in the decolorization of all the dyes tested within a range of 71-84% after 16 h incubation with the enzyme at 100 U/l
-
-
?
Mn2+ + H2O2 + remazol brilliant violet
?
-
incubation of enzyme with dyes rose bengal, remazol brilliant violet, remazol black-5, remazol blue-19, and remazol orange-16, results in the decolorization of all the dyes tested within a range of 71-84% after 16 h incubation with the enzyme at 100 U/l
-
-
?
Mn2+ + H2O2 + remazol orange-16
?
-
incubation of enzyme with dyes rose bengal, remazol brilliant violet, remazol black-5, remazol blue-19, and remazol orange-16, results in the decolorization of all the dyes tested within a range of 71-84% after 16 h incubation with the enzyme at 100 U/l
-
-
?
Mn2+ + H2O2 + rose bengal
?
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incubation of enzyme with dyes rose bengal, remazol brilliant violet, remazol black-5, remazol blue-19, and remazol orange-16, results in the decolorization of all the dyes tested within a range of 71-84% after 16 h incubation with the enzyme at 100 U/l
-
-
?
p-dimethoxybenzene + H2O2
benzoquinone + H2O
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catalyzed by isoforms PS3, PS1
-
-
?
phenol red + H2O2
oxidized phenol red + H2O
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Mn2+-dependent activity
-
-
?
Remazol brilliant blue R + 2 H+ + H2O2
oxidized Remazol brilliant blue R + 2 H2O
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dye decolorization
-
-
?
remazol brilliant blue R + H2O2
? + 2 H2O
transformation of the bulky substrate remazol brilliant blue R (RBBR), is monitored at its maximum visible absorbance wavelength of 590 nm
-
-
?
remazol brilliant blue R + H2O2
oxidized remazol brilliant blue R + 2 H2O
substrate of N246A mutant enzyme
-
-
?
2 2,6-dimethoxyphenol + 2 H2O2
coerulignone + 2 H2O
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Mn2+-independent activity
-
-
?
2 2,6-dimethoxyphenol + 2 H2O2
coerulignone + 2 H2O
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Mn2+-independent activity
-
-
?
2 2,6-dimethoxyphenol + 2 H2O2
coerulignone + 2 H2O
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Mn2+-dependent and independent activity
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-
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
oxidation of Mn2+ to Mn3+ (manganese peroxidase activity) is measured as the H2O2-dependent formation of the complex malonate-Mn3+
-
-
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
activity of EC 1.11.1.13
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-
?
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
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-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H+ + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H+ + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H+ + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H+ + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
-
-
-
?
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H+ + H2O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H+ + H2O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H+ + H2O2
?
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H+ + H2O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H+ + H2O2
?
-
-
-
?
? + H2O
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
? + H2O
-
Mn2+-independent activity
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
? + H2O
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
? + H2O
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
? + H2O
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
? + H2O
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
? + H2O
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
? + H2O
-
-
-
-
?
oxidized 2,6-dimethoxyphenol + 2 H2O
substrate 2,6-dimethoxyphenol (DMP) is transformed at the distal site of heme prosthetic group (lignin peroxidase activity)
-
-
?
2,6-dimethoxyphenol + 2 H+ + H2O2
oxidized 2,6-dimethoxyphenol + 2 H2O
-
-
-
-
?
2,6-dimethoxyphenol + 2 H+ + H2O2
oxidized 2,6-dimethoxyphenol + 2 H2O
Lentinus squarrosulus TAMI004
-
-
-
-
?
2,6-dimethoxyphenol + 2 H+ + H2O2
oxidized 2,6-dimethoxyphenol + 2 H2O
-
-
-
-
?
2,6-dimethoxyphenol + 2 H+ + H2O2
oxidized 2,6-dimethoxyphenol + 2 H2O
-
-
-
-
?
2,6-dimethoxyphenol + 2 H+ + H2O2
oxidized 2,6-dimethoxyphenol + 2 H2O
-
-
-
?
? + H2O
-
lignin fraction from straw pulpin, versatile peroxidase reacts with soluble lignin fragments in the absence of added mediators, most probably causing extensive polymerisation of high and intermediate fractions of lignin, and an increase of the small-molecular-mass lignin fraction
-
-
?
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
-
-
?
Mn2+ + H2O2
Mn3+ + H2O
the Mn2+-binding site in versatile peroxidase is formed by the side-chains of Glu36, Glu40, and Asp175 located in front of the internal (i.e. more distant from the main haem access-channel) propionate of haem, and connected to the solvent by a narrow access-channel that presents a variable geometry during catalysis
-
-
?
oxidized Reactive Black 5 + 2 H2O
-
-
-
-
?
Reactive Black 5 + 2 H+ + H2O2
oxidized Reactive Black 5 + 2 H2O
Lentinus squarrosulus 12292 ITS
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-
-
-
?
Reactive Black 5 + 2 H+ + H2O2
oxidized Reactive Black 5 + 2 H2O
Lentinus squarrosulus TAMI004
-
-
-
-
?
Reactive Black 5 + 2 H+ + H2O2
oxidized Reactive Black 5 + 2 H2O
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dye decolorization
-
-
?
Reactive Black 5 + 2 H+ + H2O2
oxidized Reactive Black 5 + 2 H2O
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dye decolorization
-
-
?
Reactive Black 5 + 2 H+ + H2O2
oxidized Reactive Black 5 + 2 H2O
-
-
-
?
Reactive Black 5 + 2 H+ + H2O2
oxidized Reactive Black 5 + 2 H2O
dye decolorization, substrate of N246A mutant enzyme
-
-
?
Reactive Black 5 + H2O2
?
versatile peroxidase activity on Reactive Black 5 is eliminated by the R257D mutation
-
-
?
Reactive Black 5 + H2O2
oxidized Reactive Black 5 + H2O
-
-
-
?
Reactive Black 5 + H2O2
oxidized Reactive Black 5 + H2O
-
-
-
?
Reactive Black 5 + H2O2
oxidized Reactive Black 5 + H2O
-
catalyzed by isoform PS1
-
-
?
Reactive Blue 5 + H2O2 + H+
oxidized Reactive Blue 5 + H2O
-
-
-
-
?
veratryl alcohol + H2O2
3,4-dimethoxybenzoic acid + 2 H2O
substrate of N246A mutant enzyme
-
-
?
veratryl alcohol + H2O2 + H+
veratraldehyde + H2O
-
Mn2+-independent activity
-
-
?
veratryl alcohol + H2O2 + H+
veratraldehyde + H2O
-
catalyzed by isoforms PS2, PS1
-
-
?
veratryl alcohol + H2O2 + H+
veratraldehyde + H2O
-
Mn2+-independent activity
-
-
?
veratryl alcohol + H2O2 + H+
veratraldehyde + H2O
a solvent-exposed tryptophan is the catalytically-active residue in veratryl alcohol oxidation, initiating an electron transfer pathway to haem
-
-
?
veratryl alcohol + H2O2 + H+
veratraldehyde + H2O
-
-
-
-
?
?
-
-
enzyme is able to decolorize 27 out of 41 industrial dyes tested
-
-
?
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
-
-
?
additional information
?
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ability of versatile peroxidase to oxidize both Mn2+ and aromatic compounds
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-
additional information
?
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ability of versatile peroxidase to oxidize both Mn2+ and aromatic compounds
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-
-
additional information
?
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the oxidation of 2,6-dimethylphenol, Mn2+ and remazol brilliant blue R (RBBR) of the three different substrates occurs at different active sites of the enzyme molecule. Versatile peroxidase (VP) from Bjerkandera adusta is an enzyme able to oxidize bulky and high-redox substrates trough a long-range electron t (LRET) pathway. The catalytic rate of the LRET mediated transformation shows a good correlation with the ionization energy of the additional amino acid on the protein surface
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-
additional information
?
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the oxidation of 2,6-dimethylphenol, Mn2+ and remazol brilliant blue R (RBBR) of the three different substrates occurs at different active sites of the enzyme molecule. Versatile peroxidase (VP) from Bjerkandera adusta is an enzyme able to oxidize bulky and high-redox substrates trough a long-range electron t (LRET) pathway. The catalytic rate of the LRET mediated transformation shows a good correlation with the ionization energy of the additional amino acid on the protein surface
-
-
-
additional information
?
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versatile peroxidase has a high affinity for H2O2, Mn2+, ferulic acid, naphthol, and different hydroquinones and dyes, but their affinities for veratryl alcohol and substituted phenols are lower
-
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-
additional information
?
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versatile peroxidase has a high affinity for H2O2, Mn2+, ferulic acid, naphthol, and different hydroquinones and dyes, but their affinities for veratryl alcohol and substituted phenols are lower
-
-
-
additional information
?
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Bjerkandera adusta UAMH8258
ability of versatile peroxidase to oxidize both Mn2+ and aromatic compounds
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-
-
additional information
?
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Bjerkandera adusta UAMH8258
versatile peroxidase has a high affinity for H2O2, Mn2+, ferulic acid, naphthol, and different hydroquinones and dyes, but their affinities for veratryl alcohol and substituted phenols are lower
-
-
-
additional information
?
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oxidation of substrates may occur in two ways, either directly by the enzyme or by diffusible chelated Mn3+ as an oxidizing agent
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?
additional information
?
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enzyme is able to oxidize efficiently Mn2+ and phenolic and nonphenolic compounds in absence of this ion
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?
additional information
?
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substrate specificity analysis, overview
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-
-
additional information
?
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versatile peroxidase oxidizes high molecular weight substrates through catalytic tryptophan at the surface resembling lignin peroxidase and Mn2+ to Mn3+ as in manganese peroxidase
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-
-
additional information
?
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Fourier transform infrared (FTIR) analysis to assess the decolorization of Reactive Black 5 and kraft lignin by immobilized Lentinus squarrosulus in optimized production medium containing 0.01% RB5 and 0.02% kraft lignin
-
-
-
additional information
?
-
Lentinus squarrosulus 12292 ITS
-
Fourier transform infrared (FTIR) analysis to assess the decolorization of Reactive Black 5 and kraft lignin by immobilized Lentinus squarrosulus in optimized production medium containing 0.01% RB5 and 0.02% kraft lignin
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-
-
additional information
?
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Lentinus squarrosulus TAMI004
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versatile peroxidase oxidizes high molecular weight substrates through catalytic tryptophan at the surface resembling lignin peroxidase and Mn2+ to Mn3+ as in manganese peroxidase
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-
-
additional information
?
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humic acid degradation by versatile peroxidase and laccase using sod-podzolic soil, representative of the southern taiga region, decolorization of humic acids, overview. The soil sample is taken from the birch forest plot of forest experimental dacha of Russian state Agrarian University-Moscow Timiryazev agricultural academy (Moscow, Russia, N55°49008.4', E37°32042')
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-
-
additional information
?
-
Lentinus tigrinus VKM F-160
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humic acid degradation by versatile peroxidase and laccase using sod-podzolic soil, representative of the southern taiga region, decolorization of humic acids, overview. The soil sample is taken from the birch forest plot of forest experimental dacha of Russian state Agrarian University-Moscow Timiryazev agricultural academy (Moscow, Russia, N55°49008.4', E37°32042')
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-
additional information
?
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substrate specificity analysis, overview
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-
-
additional information
?
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in presence of H2O2 and Mn2+, a cell-free supernatant is capable to decolorize commercial azo dyes acid black 1 and reactive black 5, reaching efficiencies between 15 and 95%. For all assays performed with 33 microM Mn2+, the initial rate of the decolorization process is dependent on the dosage of H2O2
-
-
?
additional information
?
-
Phanerodontia chrysosporium BKM-F-1767
-
in presence of H2O2 and Mn2+, a cell-free supernatant is capable to decolorize commercial azo dyes acid black 1 and reactive black 5, reaching efficiencies between 15 and 95%. For all assays performed with 33 microM Mn2+, the initial rate of the decolorization process is dependent on the dosage of H2O2
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?
additional information
?
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-
highly efficient oxidation of synthetic and natural lignin-related compounds by Physisporinus vitreus versatile peroxidase
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-
additional information
?
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the enzyme performs decolorization of azo dyes. Most derivatives of G-type lignin increase slightly by the recombinant enzyme rVP1 treatment compared with the control. Pyrolysis-GC/MS analysis of lignin modified products, detailed overview
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-
additional information
?
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highly efficient oxidation of synthetic and natural lignin-related compounds by Physisporinus vitreus versatile peroxidase
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additional information
?
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the enzyme performs decolorization of azo dyes. Most derivatives of G-type lignin increase slightly by the recombinant enzyme rVP1 treatment compared with the control. Pyrolysis-GC/MS analysis of lignin modified products, detailed overview
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-
additional information
?
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in the absence of Mn2+, efficient hydroquinone oxidation is dependent on exogenous H2O2. In the presence of Mn2+, exogenous H2O2 is not required for complete oxidation of hydroquinones
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?
additional information
?
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versatile peroxidase is able to oxidize typical substrates of other peroxidases, these hybrid properties are due to the coexistence in a single protein of different catalytic sites reminiscent of those present in the other basidiomycete peroxidase families
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?
additional information
?
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presence of two independent catalytic sites for different phenols and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) in native enzyme, characterizedby high and low specificity constants, i.e. Km in the micromolar range and Km in the millimolar range, respcetively
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-
?
additional information
?
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presence of two independent catalytic sites for different phenols and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) in native enzyme, characterizedby high and low specificity constants, i.e. Km in the micromolar range and Km in the millimolar range, respcetively
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?
additional information
?
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the enzyme shows a broad substrate spectrum
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additional information
?
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the enzyme shows a broad substrate spectrum
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additional information
?
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no activity with Phenol Red and Remazol Brilliant Blue
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?
additional information
?
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no substrates: Fe2+, veratryl alcohol
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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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