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
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1.11.1.14
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chrysosporium
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phanerochaete
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manganese
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laccase
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melanin
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ligninolytic
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veratryl
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peroxidases
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melanoma
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melanogenesis
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white-rot
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kojic
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decolor
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l-dopa
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diphenolase
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basidiomycete
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trametes
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monophenolase
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versicolor
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hyperpigmentation
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lignin-degrading
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whitening
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textile
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anti-tyrosinase
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o-quinones
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manganese-dependent
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l-3,4-dihydroxyphenylalanine
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microphthalmia-associated
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anti-melanogenic
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o-diphenols
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bjerkandera
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arbutin
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skin-whitening
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non-phenolic
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1.14.18.1
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dopaquinone
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phlebia
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tyrosinase-related
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delignification
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dopachrome
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remazol
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lignocellulolytic
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anti-melanogenesis
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eryngii
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tyrosinases
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catecholase
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depigmenting
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biotechnology
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dye-decolorizing
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synthesis
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environmental protection
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lignocellulose-degrading
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analysis
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degradation
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industry
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irpex
- 1.11.1.14
- chrysosporium
- phanerochaete
- manganese
- laccase
- melanin
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ligninolytic
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veratryl
- peroxidases
- melanoma
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melanogenesis
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white-rot
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kojic
-
decolor
- l-dopa
- diphenolase
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basidiomycete
- trametes
- monophenolase
- versicolor
- hyperpigmentation
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lignin-degrading
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whitening
-
textile
-
anti-tyrosinase
- o-quinones
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manganese-dependent
- l-3,4-dihydroxyphenylalanine
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microphthalmia-associated
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anti-melanogenic
- o-diphenols
- bjerkandera
- arbutin
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skin-whitening
-
non-phenolic
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1.14.18.1
- dopaquinone
- phlebia
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tyrosinase-related
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delignification
- dopachrome
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remazol
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lignocellulolytic
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anti-melanogenesis
- eryngii
- tyrosinases
- catecholase
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depigmenting
- biotechnology
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dye-decolorizing
- synthesis
- environmental protection
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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
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Application
Application on EC 1.11.1.14 - lignin peroxidase
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analysis
biofuel production
the use of LiP may provide a cost-effective, efficient and greener route for the transformation of biomass into second-generation (2 G) biofuels. Lignin depolymerization is an important step in producing 2 G biofuels and other green chemicals as lignin protects cellulose and hemicellulose against the enzymes required to hydrolyse it to fermentable sugars
biotechnology
degradation
environmental protection
industry
synthesis
additional information
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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
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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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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
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degradation of different recalcitrant compounds, removal of toxic dyes
degradation
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the electroenzymatic method using in situ-generated hydrogen peroxide is effective for oxidation of veratryl alcohol by lignin peroxidase. The method may be easily applied to biodegradation systems
degradation
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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
LiPH8 showing high acid stability will be a crucial player in biomass valorization using selective depolymerization of lignin
degradation
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the enzyme can be used for PVC films biodegradation. Fungal metabolites are playing an immense role in developing various sustainable waste treatment processes. Production and characterization of a fungal lignin peroxidase with a potential to degrade polyvinyl chloride, method optimization, overview
degradation
the partially purified LiP is able to degrade toxic synthetic polymer polyvinyl chloride (PVC) films, resulting in a 31% weight reduction of the films. LiP can effectively transform an endocrine disruptive hormone known as 17beta-estradiol (E2), which is considered a pollutant once released into the environment. Veratryl alcohol facilitates the enhanced removal and transformation of E2 by LiP and can perhaps also remove other closely related endocrine-disrupting impurities
degradation
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degradation of different recalcitrant compounds, removal of toxic dyes
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degradation
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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
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degradation
Phanerodontia chrysosporium ATCC 24725
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the electroenzymatic method using in situ-generated hydrogen peroxide is effective for oxidation of veratryl alcohol by lignin peroxidase. The method may be easily applied to biodegradation systems
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degradation
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the enzyme can be used for PVC films biodegradation. Fungal metabolites are playing an immense role in developing various sustainable waste treatment processes. Production and characterization of a fungal lignin peroxidase with a potential to degrade polyvinyl chloride, method optimization, overview
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use of Phanerochaete chrysosporium and its enzyme lignin peroxidase in the degradation of environmental pollutants such as dye. High efficient degradation of dyes with lignin peroxidase coupled with glucose oxidase
environmental protection
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the enzyme shows the potential to be applied in the treatment of textile effluents (decolorization of dyes). The results from the selection of dyes such as methylene blue, malachite green and methyl orange show that the enzyme is able to remove a higher content of methylene blue (14%) compared to the other two dyes (3-8%). The optimization with the OFAT method determined the operating conditions of the decolorization of methylene blue dye at temperature 55°C, pH 5.0 (in 50 mM sodium acetate buffer) with H2O2 concentration 4.0 mM. The addition of veratryl alcohol to the reaction mixture has no affect on decolorization of dye
environmental protection
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a high and sustainable lignin peroxidase activity is achieved via in situ release of H2O2 by a co-immobilized glucose oxidase. The present co-immobilization system is demonstrated to be very effective for lignin peroxidase mediated dye decolourization
environmental protection
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lignin peroxidase enzyme production using sewage treatment plant sludge as a major substrate seems to be a promising and encouraging alternative for better sludge management. This is a new environmental biotechnological approach for the biodegradation of sludge, which, in addition to producing lignin peroxidase, would reduce treatment and production costs through the use of an environmentally friendly process
environmental protection
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lignin peroxidase has a applicable potential for the degradation of sulfonated azo dyes
environmental protection
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removal of four catechols (1,2-dihydroxybenzene), 4-chlorocatechol (4-CC), 4,5-dichlorocatechol (4,5-DCC) and 4-methylcatechol (4-MC) typical pollutants in wastewater derived from oil and paper industries
environmental protection
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the enzyme is able to decolorize synthetic dyes
environmental protection
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the enzyme is able to decolorize synthetic dyes
environmental protection
Lentinus strigellus
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the enzyme is able to decolorize synthetic dyes
environmental protection
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the enzyme is able to decolorize synthetic dyes
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environmental protection
Lentinus strigellus SXS355
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the enzyme is able to decolorize synthetic dyes
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environmental protection
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the enzyme is able to decolorize synthetic dyes
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environmental protection
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the enzyme is able to decolorize synthetic dyes
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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
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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
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evaluation of the effect of enzyme dosage, incubation time, and H2O2 addition profile on lignin activation by quantifying the phenoxy radicals formed using electron paramagnetic resonance spectroscopy. At optimal conditions, i.e. dose of 15 /g and continuous addition of H2O2, the content of phenoxy radicals is doubled as compared with an untreated control
synthesis
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immobilization of enzyme by entrapping in xerogel matrix of trimethoxysilane and proplytetramethoxysilane to maximum immobilization efficiency of 88.6%. The free and immobilized enzymes have optimum pH values of 6 and 5 while optimum temperatures are 60°C and 80°C, respectively. Immobilization enhances the activity and thermo-stability potential significantly and immobilized enzyme remains stable over broad pH and temperature range
synthesis
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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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lignin peroxidase has a broad spectrum of potential industrial and biotechnological applications attributed by its non-specific catalytic mechanism towards a variety of substrates. The use of LiP may provide a cost-effective, efficient and greener route for the transformation of biomass into second-generation (2 G) biofuels and other high-value green biochemicals, and thus effectively improve the economics of biorefineries. This biocatalyst can be applied in diverse industries such as pulp and paper mills, biofuels, food and feed, pharmaceuticals and also serve as a bioremediation agent, overview
additional information
peroxidases are well-known biocatalysts produced by all organisms, especially microorganisms, and used in a number of biotechnological applications
additional information
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peroxidases are well-known biocatalysts produced by all organisms, especially microorganisms, and used in a number of biotechnological applications