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
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pleurotus
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peroxidases
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ligninolytic
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eryngii
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laccase
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white-rot
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bjerkandera
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ostreatus
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veratryl
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adusta
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chrysosporium
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phanerochaete
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lignin-degrading
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non-phenolic
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2,6-dimethoxyphenol
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delignification
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aryl-alcohols
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degradation
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synthesis
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industry
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analysis
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paper production
- 1.11.1.16
- lignin
- pleurotus
- peroxidases
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ligninolytic
- eryngii
- laccase
-
white-rot
- bjerkandera
- ostreatus
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veratryl
- adusta
- chrysosporium
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phanerochaete
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lignin-degrading
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non-phenolic
- 2,6-dimethoxyphenol
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delignification
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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
1.11.1.16 versatile peroxidaseAdvanced search results
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Application on EC 1.11.1.16 - versatile peroxidase
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APPLICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
agriculture
analysis
degradation
environmental protection
industry
paper production
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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
synthesis
additional information
peroxidases are well-known biocatalysts produced by all organisms, especially microorganisms, and used in a number of biotechnological applications
agriculture
overproducing the VP gene in plants increases significantly their biomass and the abiotic stress tolerance. The versatile peroxidase enzyme is an effective biotechnological tool to protect organisms against ROS. In transgenic tobacco plants, it improves drought, salt, and oxidative stress tolerance. Thus, the versatile peroxidase gene represents a great potential for obtaining stress-tolerant crops. The enzyme from Bjerkandera adusta can mitigate oxidative stress induced by paraquat, salt- (NaCl), drought- and osmotic-stress (sorbitol)
agriculture
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use of versatile peroxidase in enhancing the digestibility of straws is substantiated through proximate and in vitro digestibility analysis, use of versatile peroxidase in increasing the in vitro degradation of straws for enhancing feed utilization in ruminants. Usage of commonly available crop residues such as paddy straw, finger millet straw, foxtail millet straw, little millet straw, and barnyard millet straw (milled to 1 to 2 cm length and dried at a constant temperature of 70°C) in biodegradation studies
agriculture
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use of versatile peroxidase in increasing the in vitro degradation of straws for enhancing feed utilization in ruminants
agriculture
Lentinus squarrosulus TAMI004
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use of versatile peroxidase in enhancing the digestibility of straws is substantiated through proximate and in vitro digestibility analysis, use of versatile peroxidase in increasing the in vitro degradation of straws for enhancing feed utilization in ruminants. Usage of commonly available crop residues such as paddy straw, finger millet straw, foxtail millet straw, little millet straw, and barnyard millet straw (milled to 1 to 2 cm length and dried at a constant temperature of 70°C) in biodegradation studies
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agriculture
Bjerkandera adusta UAMH8258
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overproducing the VP gene in plants increases significantly their biomass and the abiotic stress tolerance. The versatile peroxidase enzyme is an effective biotechnological tool to protect organisms against ROS. In transgenic tobacco plants, it improves drought, salt, and oxidative stress tolerance. Thus, the versatile peroxidase gene represents a great potential for obtaining stress-tolerant crops. The enzyme from Bjerkandera adusta can mitigate oxidative stress induced by paraquat, salt- (NaCl), drought- and osmotic-stress (sorbitol)
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agriculture
Lentinus squarrosulus 12292 ITS
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use of versatile peroxidase in increasing the in vitro degradation of straws for enhancing feed utilization in ruminants
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analysis
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detection and quantification of soluble lignin transformation by measuring changes in the true colour of the system solution
analysis
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evaluation of the effect of enzyme dosage, incubation time, and H2O2 addition profile on lignin activation by quantifying the phenoxy radicals formed using electron paramagnetic resonance spectroscopy. At optimal conditions, i.e. dose of 15 /g and continuous addition of H2O2, the content of phenoxy radicals is doubled as compared with an untreated control
analysis
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evaluation of the effect of enzyme dosage, incubation time, and H2O2 addition profile on lignin activation by quantifying the phenoxy radicals formed using electron paramagnetic resonance spectroscopy. At optimal conditions, i.e. dose of 15 /g and continuous addition of H2O2, the content of phenoxy radicals is doubled as compared with an untreated control
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degradation
versatile peroxidase presents particular interest due to its catalytic versatility including the degradation of compounds that other peroxidases are not able to oxidize directly, versatile peroxidase versatility permits its application in Mn3+-mediated or Mn-independent reactions on both low and high redox-potential aromatic substrates and dyes, versatile peroxidase can be used to reoxidize Mn-containing polyoxometalates, which are efficient oxidizers in paper pulp delignification
degradation
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in presence of H2O2 and Mn2+, a cell-free subpernatant 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
degradation
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the allosteric behaviour of the VP enzyme promotes a high level of regulation of activity during the breakdown of model and industrial ligninolytic substrates, such as effluent from a pulp and paper plant, and fouled membrane solids extracted from a ground water treatment membrane
degradation
Phanerodontia chrysosporium BKM-F-1767
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in presence of H2O2 and Mn2+, a cell-free subpernatant 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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environmental protection
the enzyme immobilized on yeast cell wall fragments can be used for longterm bioremediation of environments contaminated with azo dyes
environmental protection
versatile peroxidases form an attractive ligninolytic enzyme group due to their dual oxidative ability to oxidize Mn(II) and also phenolic and nonphenolic aromatic compounds, and can be used in programs for phytoremediation
environmental protection
Bjerkandera adusta UAMH8258
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versatile peroxidases form an attractive ligninolytic enzyme group due to their dual oxidative ability to oxidize Mn(II) and also phenolic and nonphenolic aromatic compounds, and can be used in programs for phytoremediation
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industry
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the enzyme can be used in the treatment of industrial dye effluents. Paper pulp industries presently employ these ligninolytic enzymes for their pulp bleaching applications
industry
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the enzyme can be used in the treatment of industrial dye effluents. Paper pulp industries presently employ these ligninolytic enzymes for their pulp bleaching applications
industry
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the enzyme can be used in the treatment of industrial dye effluents. Paper pulp industries presently employ these ligninolytic enzymes for their pulp bleaching applications
industry
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the enzyme can be used in the treatment of industrial dye effluents. Paper pulp industries presently employ these ligninolytic enzymes for their pulp bleaching applications
synthesis
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expression of enzyme under control of the alcohol dehydrogenase promoter of Aspergillus nidulans in this host. Culture temperature of 19°C enhances the level of peroxidase 5.8-fold and reduces the effective proteolytic activity twofold giving a peroxidase activity of 466 units per l. Application of the same conditions to expression in Aspergillus niger does not result in improved peroxidase activity, while the effective proteolytic activity is increased
synthesis
production of the oxidase in strain BL21(DE3)pLysS, cultivated at 25°C in auto-induction medium and presence of heme
synthesis
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evaluation of the effect of enzyme dosage, incubation time, and H2O2 addition profile on lignin activation by quantifying the phenoxy radicals formed using electron paramagnetic resonance spectroscopy. At optimal conditions, i.e. dose of 15 /g and continuous addition of H2O2, the content of phenoxy radicals is doubled as compared with an untreated control
synthesis
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enzyme is produced by solid-state fermentation, using the agricultural residue banana peel as growth medium. An enzymatic activity of 10800 U/l i.e. 36 U/g of substrate is detected after 18 days, whereas only 1800 U/l are reached by conventional submerged fermentation with glucose-based medium
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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