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Information on EC 1.10.3.2 - laccase and Organism(s) Trametes versicolor and UniProt Accession Q12719
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1.10.3.2 laccaseIUBMB Comments
A group of multi-copper proteins of low specificity acting on both o- and p-quinols, and often acting also on aminophenols and phenylenediamine. The semiquinone may react further either enzymically or non-enzymically.
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Word Map
- 1.10.3.2
- trametes
-
decolor
- versicolor
- abts
-
white-rot
- manganese
-
basidiomycete
- pleurotus
- oxidases
-
wastewater
-
textile
-
effluent
- ostreatus
-
bioremediation
-
electrode
-
lignocellulosic
-
recalcitrant
- pulp
- guaiacol
- straw
- wood
- tyrosinase
- mushroom
-
solid-state
-
submerged
- cellulase
- xylanase
-
brilliant
- phanerochaete
-
chemoradiation
- chrysosporium
- malachite
-
trinuclear
-
veratryl
-
kraft
-
chemoradiotherapy
-
copper-containing
-
reusability
- monophenols
- indigo
- edodes
-
humic
- bagasse
-
brachytherapy
-
bioelectrocatalytic
-
copper-binding
- azoreductase
- monolignols
- industry
-
para-aortic
- food industry
- degradation
- biofuel production
- energy production
- medicine
- environmental protection
- biotechnology
- analysis
- cmcase
- synthesis
The taxonomic range for the selected organisms is: Trametes versicolor
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
laccase, lacc, phenol oxidase, laccase a, cota-laccase, lac i, diphenol oxidase, poxa1b, laccase2, cota laccase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Benzenediol:oxygen oxidoreductase
-
-
-
-
Diphenol oxidase
-
-
-
-
Laccase allele OR
-
-
-
-
Laccase allele TS
-
-
-
-
Lcc2
Ligninolytic phenoloxidase
-
-
-
-
p-diphenol oxidase
-
-
-
-
urishiol oxidase
-
-
-
-
urushiol oxidase
-
-
-
-
Lcc2
Lcc2 is comprised of 5 individual isoforms with pI values ranging from 3.5 to 5.8
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4 benzenediol + O2 = 4 benzosemiquinone + 2 H2O
two site ping-pong bi-bi mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
benzenediol:oxygen oxidoreductase
A group of multi-copper proteins of low specificity acting on both o- and p-quinols, and often acting also on aminophenols and phenylenediamine. The semiquinone may react further either enzymically or non-enzymically.
CAS REGISTRY NUMBER
COMMENTARY
80498-15-3
-
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
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate) + O2
? + H2O
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
? + H2O
-
44% of the activity with phenol
-
-
?
2,2-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,4-dichlorophenol + 4-aminoantipyrine + O2
? + H2O
-
93% of the activity with phenol
-
-
?
2,5-xylidine + O2
?
the enzyme also transforms the non-phenolic substrate at pH 5.0, native and recombinant enzymes, wild-type and mutant enzymes, overview
-
-
?
2,6-dichlorophenol + 4-aminoantipyrine + O2
? + H2O
-
258% of the activity with phenol
-
-
?
2,6-dimethoxyphenol + 4-aminoantipyrine + O2
? + H2O
-
159% of the activity with phenol
-
-
?
4 syringic acid + O2
4 4-carboxy-2,6-dimethoxyphenoxyl + 2 H2O
-
-
-
-
?
4-hydroxy-3,5-dimethoxybenzaldehyde azine + O2
?
-
i.e. syringaldazine
-
-
?
caffeic acid + 4-aminoantipyrine + O2
? + H2O
-
39% of the activity with phenol
-
-
?
catechol + 4-aminoantipyrine + O2
? + H2O
-
176% of the activity with phenol
-
-
?
coniferyl alcohol + O2
?
the enzyme transforms the non-phenolic substrate at pH 4.5 only when recombinantly expressed in the yeast Yarrowia lipolytica strain Po1t, overview
-
-
?
diethylaniline + 4-aminoantipyrine + O2
? + H2O
-
103% of the activity with phenol
-
-
?
dimethylaniline + 4-aminoantipyrine + O2
? + H2O
-
165% of the activity with phenol
-
-
?
ferulic acid + O2
3-(4-hydroxy-3-oxo-cyclohexa-1,5-dienyl)-acrylic acid + H2O
-
-
-
-
?
guaiacol + 4-aminoantipyrine + O2
? + H2O
-
61% of the activity with phenol
-
-
?
hydrocaffeic acid + 4-aminoantipyrine + O2
? + H2O
-
185% of the activity with phenol
-
-
?
hydroquinone + 4-aminoantipyrine + O2
? + H2O
-
89% of the activity with phenol
-
-
?
m-chlorophenol + 4-aminoantipyrine + O2
? + H2O
-
50% of the activity with phenol
-
-
?
N,N-dimethyl-p-phenylenediamine + 4-aminoantipyrine + O2
? + H2O
-
377% of the activity with phenol
-
-
?
N-ethyl-N-(2-hydroxy-3-sulfopropyl)-3-methylaniline + 4-aminoantipyrine + O2
? + H2O
-
198% of the activity with phenol
-
-
?
o-chlorophenol + 4-aminoantipyrine + O2
? + H2O
-
150% of the activity with phenol
-
-
?
o-cresol + 4-aminoantipyrine + O2
? + H2O
-
39% of the activity with phenol
-
-
?
p-hydroxybenzoic acid + 4-aminoantipyrine + O2
? + H2O
-
3% of the activity with phenol
-
-
?
p-toluidine + 4-aminoantipyrine + O2
? + H2O
-
51% of the activity with phenol
-
-
?
pyrogallol + 4-aminoantipyrine + O2
? + H2O
-
10% of the activity with phenol
-
-
?
resorcinol + 4-aminoantipyrine + O2
? + H2O
-
73% of the activity with phenol
-
-
?
sinapic acid + O2
3-(3,5-dimethoxy-4-oxo-cyclohexa-1,5-dienyl)-acrylic acid + H2O
-
-
-
-
?
tyrosine + O2
?
the enzyme catalyzes oxidative cross-linking of tyrosine and potato patatin and lysozyme-derived peptides
-
-
?
vanillic acid + O2
4-carboxy-2-methoxycyclohexa-2,4-dienone + H2O
-
-
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,6-dimethoxyphenol + O2
3,3',5,5'-tetramethoxy-4-diphenoquinone + H2O
-
-
-
-
?
2,6-dimethoxyphenol + O2
3,3',5,5'-tetramethoxy-4-diphenoquinone + H2O
-
-
-
?
2,6-dimethoxyphenol + O2
?
-
-
-
?
guaiacol + O2
?
-
-
-
?
syringaldazine + O2
?
-
-
-
?
additional information
?
-
-
degradation of polychlorinated phenols and guaiacols
-
-
?
additional information
?
-
the enzyme is involved in bioremdiation
-
-
?
additional information
?
-
-
the enzyme is involved in bioremdiation
-
-
?
additional information
?
-
-
purified recombinant laccase decolorizes more than 90% of Remazol Brilliant Blue R initially at 80 mg/l1 after 16 h at 45°C and pH 5 when 25 U laccase/ml is used. The purified recombinant laccase can efficiently decolorize Remazol Brilliant Blue R without additional redox mediators
-
-
?
NATURAL SUBSTRATE
NATURAL 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
additional information
?
-
the enzyme is involved in bioremdiation
-
-
?
additional information
?
-
-
the enzyme is involved in bioremdiation
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
copper
Cu2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
chitosan
-
conjugated to the enzyme, with 81-93% laccase being conjugated, a moderate activity loss of 16-28% occurs in conjugation solution, a second severe activity loss of 63-78% occurs during a cycle of phase change consisting of precipitation, centrifugation and re-dissolution of the enzymechitosan conjugates, the chitosan molecular size has little effect, overview
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.13
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 5.0, 25°C
0.01
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
pH and temperature not specified in the publication
0.43
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
pH 4.5, 55°C
0.01
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.0, 30°C, recombinant mutant D206A
0.0128
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 3.0, 50°C
0.016
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.0, 30°C, recombinant mutant D206N
0.026
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.0, 30°C, recombinant mutant D206E
0.038
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 4.5, 25°C
0.0423
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
free enzyme
0.0452
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
enzyme conjugated with chitosan of 505 kDa
0.0498
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
enzyme conjugated with chitosan of 214 kDa
0.05
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.0, 30°C, recombinant wild-type enzyme
0.0852
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
enzyme conjugated with chitosan of 432 kDa
0.095
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
enzyme conjugated with chitosan of 131 kDa
12
2,2-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
pH 3.0, 23°C
45
2,2-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
pH 3.0, 23°C
0.19
2,6-dimethoxyphenol
pH 3.4, 30°C, recombinant wild-type enzyme
0.5
2,6-dimethoxyphenol
pH and temperature not specified in the publication
2.23
guaiacol
pH and temperature not specified in the publication
3.77
syringaldazine
pH and temperature not specified in the publication
additional information
additional information
-
Michaelis-Menten steady-state kinetics, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.064
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
enzyme conjugated with chitosan of 505 kDa
0.08
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
enzyme conjugated with chitosan of 214 kDa
0.101
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
enzyme conjugated with chitosan of 432 kDa
0.168
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
enzyme conjugated with chitosan of 131 kDa
0.252
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
-
free enzyme
1.3
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.0, 30°C, recombinant wild-type enzyme
1.6
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.0, 30°C, recombinant mutant D206A
3.3
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.0, 30°C, recombinant mutant D206E
4.3
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid)
pH 3.0, 30°C, recombinant mutant D206N
0.51
2,6-dimethoxyphenol
pH 3.4, 30°C, recombinant wild-type enzyme
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1024
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 5.0, 25°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
28.8
pH 4.5, 55°C, substrate: 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
additional information
additional information
-
relative activity of laccase in conjugation with chitosans of different molecular weights, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2
substrate: 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
3.5
5.5
3
substrate: 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) or 2,6-dimethoxyphenol
3
substrate: 2,2-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) or 2,6-dimethoxyphenol
3
substrate: 2,2-azino-bis-(3-ethylbenzthiazoline-6-sulfonix acid) or 2,6-dimethoxyphenol
3.5
substrate: guaiacol
5.5
substrate: syringaldazine
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 7.5
-
pH 6.0: about 55% of maximal activity, pH 7.5: about 55% of maximal activity, immobilized enzyme, substrate: 2,6-dimethoxyphenol
additional information
-
pH profiles of free and chitosan-conjugated enzyme
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
50
substrate: 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
50
substrate: 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 70
25°C: about 75% of maximal activity, 70°C: about 55% of maximal activity
30 - 80
30°C: about 70% of maximal activity, 80°C: about 45% of maximal activity, substrate: 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
35 - 60
-
35°C: about 60% of maximal activity, 60°C: about 60% of maximal activity, immobilized enzyme, substrate: 2,6-dimethoxyphenol
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.8
Lcc2 is comprised of 5 individual isoforms with pI values ranging from 3.5 to 5.8
5.9
Lcc2 is comprised of 5 individual isoforms with pI values ranging from 3.5 to 5.8
6
Lcc2 is comprised of 5 individual isoforms with pI values ranging from 3.5 to 5.8
6.1
Lcc2 is comprised of 5 individual isoforms with pI values ranging from 3.5 to 5.8
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
culture in a medium containing groundnut shell and cyanobacterial bloom in a ratio of 9:1 dry weight basis in submerged fermentation at initial pH 5.0 and 28°C temperature
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
plant, bacterial, and insect laccases have a polymerizing role in nature, implicated in biosynthesis of lignin, melanin formation, and cuticle hardening, respectively. On the other hand, fungal laccases carry out both polymerizing (melanin synthesis and fruit body formation) as well as depolymerizing roles (lignin degradation)
additional information
-
the laccase from Trametes versicolor is a high redox potential enzyme. Structure-function study, mass spectrometry, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). LAC4_TRAVE
520
0
55644
Swiss-Prot
Secretory Pathway (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
?
x * 100000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D206A
site-directed mutagenesis, the Asn mutation leads to a significant shift of pH optimum for activity with 2,6-dimethoxyphenol, the mutant shows several fold increased activity compared to the wild-type enzyme
D206E
site-directed mutagenesis, the Asn mutation leads to a significant shift of pH optimum for activity with 2,6-dimethoxyphenol, the mutant shows several fold increased activity compared to the wild-type enzyme
D206N
site-directed mutagenesis, the Asn mutation leads to a significant shift of pH optimum for activity with 2,6-dimethoxyphenol, the mutant shows several fold increased activity compared to the wild-type enzyme
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2 - 7
6 h, 25°C, in the absence of the substrate, recombinant laccase is stable
741665
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 30
-
at pH 6, the rate of inactivation increases as the temperature is elevated from 10 to 60°C, with good stability observed in the range of 10 to 30°C
50
after 20 min the enzyme loses 60% of its initial activity
60
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
activity and stability of laccase in conjugation with chitosan is reduced, overview
-
co-cross-linking method is superior to the other methods of immobilization in terms of operating stability. In co-cross-linking method of immobilization, laccase is mixed with bovine serum albumin as protein-based stabilizing agent and glutaraldehyde as crosslinking agent
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme 209fold from strain 951022 by ethanol precipitation, anion exchange and hydrophobic interaction chromatography, and gel filtration, to homogeneity
-
recombinant enzyme
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of wild-type and mutant enzymes in Yarrowia lipolytica Po1t prototrophic strain
gene lcc1 or lccalpha, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression of a soluble enzyme in Saccharomyces cerevisiae strain W303-1a
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
purification and recovery of immobilized and extractable transgenic enzyme, treatment with copper for activation of apoenzyme and as purification step
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
sensitive, rapid, and precise determination of phenols and their derivatives is important in environmental control and protection. An amperometric principle-based biosensor, employing immobilized laccase enzyme from Trametes versicolor, is developed for the detection of disubstituted methyl and methoxy phenols (industrial effluents). Evaluation of the influence of different enzyme immobilization techniques, on nylon membrane, on the performances of laccase-based Clark-type electrodes. The analytical properties and operating stabilities of the resulting biosensors are tested with different disubstituted methyl and methoxy derivatives of phenol substrates. Co-cross-linking method is superior to the other methods of immobilization in terms of sensitivity, limit of detection, response time, and operating stability. In co-cross-linking method of immobilization, laccase is mixed with bovine serum albumin as protein-based stabilizing agent and glutaraldehyde as crosslinking agent
degradation
energy production
-
combination oflaccase and catalase in construction of H2O2-O2 based biocathode for applications in glucose biofuel cells. The deposited enzymes laccase and catalase by means of alternating current electrophoretic deposition (AC-EPD) do not inhibit each other and carry out about 90% of the catalytic reduction process of O2-H2O2
environmental protection
industry
-
laccases can be considered as one of the most important biocatalyst which can be exploited for divergent industrial applications viz. paper pulp bleaching, fiber modification, dye decolorization, bioremediation as well as organic synthesis
synthesis
-
the enzyme from Trametes versicolor synthesizes 1. polycatechol, a valuable polymer used as a chromatographic resin and in the formation of thin films for biosensors, 2. benzofuranones for medicinal chemistry, 3. poly allylamine with high antioxidant potential, 4. dyes used in hair dyeing, 5. benzoquinones used as intermediates in pharmaceuticals, 6. phenazine and phenoxazinone chromopheres for synthetic dyes
additional information
-
environmental protection, potential application of waste water cyanobacterial bloom and dyeing effluent as a medium for laccase production by Coriolus versicolor strain MTCC138
degradation
-
enzyme shows dye-decolourizing activity against several anthraquinone dyes, azo dyes, polymeric dyes and others
environmental protection
-
sensitive, rapid, and precise determination of phenols and their derivatives is important in environmental control and protection. An amperometric principle-based biosensor, employing immobilized laccase enzyme from Trametes versicolor, is developed for the detection of disubstituted methyl and methoxy phenols (industrial effluents). Evaluation of the influence of different enzyme immobilization techniques, on nylon membrane, on the performances of laccase-based Clark-type electrodes. The analytical properties and operating stabilities of the resulting biosensors are tested with different disubstituted methyl and methoxy derivatives of phenol substrates. Co-cross-linking method is superior to the other methods of immobilization in terms of sensitivity, limit of detection, response time, and operating stability. In co-cross-linking method of immobilization, laccase is mixed with bovine serum albumin as protein-based stabilizing agent and glutaraldehyde as crosslinking agent
environmental protection
the enzyme has potential for application in the treatment of contaminated water with low pH values and high phenolic content
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rogalski, J.; Wojtas-Wasilewska, M.; Apalovic, R.; Leonowicz, A.
Affinity chromatography: a convenient method for purification of fungal lactases
Biotechnol. Bioeng.
37
770-777
1991
Trametes versicolor, Fomes fomentarius
Rogalski, J.; Dawidowicz, A.L.; Leonowicz, A.
Purification and immobilization of the inducible form of extracellular laccase of the fungus Trametes versicolor
Acta Biotechnol.
10
261-269
1990
Trametes versicolor
-
Wrigley, S.K.; Gibson, J.F.
Electron paramagnetic resonance studies of type 1 copper in type 2 depleted fungal laccase A
Biochim. Biophys. Acta
916
259-264
1987
Trametes versicolor
Brown, M.A.; Zhao, Z.; Grant Mauk, A.
Expression and characterization of a recombinant multi-copper oxidase: laccase IV from Trametes versicolor
Inorg. Chim. Acta
331
232-238
2002
Trametes versicolor
-
Salas, C.; Lobos, S.; Larrain, J.; Salas, L.; Cullen, D.; Vicuna, R.
Properties of laccase isoenzymes produced by the basidiomycete Ceriporiopsis subvermispora
Biotechnol. Appl. Biochem.
21
323-333
1995
Gelatoporia subvermispora, Trametes versicolor
-
Bertrand, T.; Jolivalt, C.; Briozzo, P.; Caminade, E.; Joly, N.; Madzak, C.; Mougin, C.
Crystal structure of a four-copper laccase complexed with an arylamine: insights into substrate recognition and correlation with kinetics
Biochemistry
41
7325-7333
2002
Trametes versicolor (Q96UT7), Trametes versicolor
Johannes, C.; Majcherczyk, A.
Laccase activity tests and laccase inhibitors
J. Biotechnol.
78
193-199
2000
Trametes versicolor
Roy-Arcand, L.; Archibald, F.S.
Direct dechlorination of chlorophenolic compounds by laccases from Trametes (Coriolus) versicolor
Enzyme Microb. Technol.
13
194-201
1991
Trametes versicolor
-
Bailey, M.R.; Woodard, S.L.; Callaway, E.; Beifuss, K.; Magallanes-Lundback, M.; Lane, J.R.; Horn, M.E.; Mallubhotla, H.; Delaney, D.D.; Ward, M.; Van Gastel, F.; Howard, J.A.; Hood, E.E.
Improved recovery of active recombinant laccase from maize seed
Appl. Microbiol. Biotechnol.
63
390-397
2004
Trametes versicolor
Sulistyaningdyah, W.T.; Ogawa, J.; Tanaka, H.; Maeda, C.; Shimizu, S.
Characterization of alkaliphilic laccase activity in the culture supernatant of Myrothecium verrucaria 24G-4 in comparison with bilirubin oxidase
FEMS Microbiol. Lett.
230
209-214
2004
Trametes versicolor, Albifimbria verrucaria, Trametes sp., Trametes sp. Ha-1, Albifimbria verrucaria 24G-4
Piontek, K.; Antorini, M.; Choinowski, T.
Crystal structure of a laccase from the fungus Trametes versicolor at 1.90-A resolution containing a full complement of coppers
J. Biol. Chem.
277
37663-37669
2002
Trametes versicolor
Lorenzo, M.; Moldes, D.; Rodriguez Couto, S.; Sanroman, M.A.
Inhibition of laccase activity from Trametes versicolor by heavy metals and organic compounds
Chemosphere
60
1124-1128
2005
Trametes versicolor
Necochea, R.; Valderrama, B.; Diaz-Sandoval, S.; Folch-Mallol, J.L.; Vazquez-Duhalt, R.; Iturriaga, G.
Phylogenetic and biochemical characterisation of a recombinant laccase from Trametes versicolor
FEMS Microbiol. Lett.
244
235-241
2005
Trametes versicolor (Q5IR80), Trametes versicolor, Trametes versicolor UAMH 8272 (Q5IR80)
Delanoy, G.; Li, Q.; Yu, J.
Activity and stability of laccase in conjugation with chitosan
Int. J. Biol. Macromol.
35
89-95
2005
Trametes versicolor
Han, M.J.; Han, M.J.; Choi, H.T.; Song, H.G.
Purification and characterization of laccase from the white rot fungus Trametes versicolor
J. Microbiol.
43
555-560
2005
Trametes versicolor, Trametes versicolor 951022
Madzak, C.; Mimmi, M.C.; Caminade, E.; Brault, A.; Baumberger, S.; Briozzo, P.; Mougin, C.; Jolivalt, C.
Shifting the optimal pH of activity for a laccase from the fungus Trametes versicolor by structure-based mutagenesis
Protein Eng. Des. Sel.
19
77-84
2006
Trametes versicolor (Q96UT7), Trametes versicolor
Koschorreck, K.; Richter, S.M.; Swierczek, A.; Beifuss, U.; Schmid, R.D.; Urlacher, V.B.
Comparative characterization of four laccases from Trametes versicolor concerning phenolic C-C coupling and oxidation of PAHs
Arch. Biochem. Biophys.
474
213-219
2008
Trametes versicolor (O13456), Trametes versicolor (O94222), Trametes versicolor (Q12719), Trametes versicolor (Q5IR80), Trametes versicolor
Kurniawati, S.; Nicell, J.A.
Characterization of Trametes versicolor laccase for the transformation of aqueous phenol
Biores. Technol.
99
7825-7834
2008
Trametes versicolor
Guo, M.; Lu, F.; Liu, M.; Li, T.; Pu, J.; Wang, N.; Liang, P.; Zhang, C.
Purification of recombinant laccase from Trametes versicolor in Pichia methanolica and its use for the decolorization of anthraquinone dye
Biotechnol. Lett.
30
2091-2096
2008
Trametes versicolor
Mishra, A.; Kumar, S.
Kinetic studies of laccase enzyme of Coriolus versicolor MTCC 138 in an inexpensive culture medium
Biochem. Eng. J.
46
252-256
2009
Trametes versicolor, Trametes versicolor MTCC 138
-
Erden, E.; Cigdem Ucar, M.; Gezer, T.; Pazarlioglu, N.
Screening for ligninolytic enzymes from autochthonous fungi and applications for decolorization of Remazole Marine Blue
Braz. J. Microbiol.
40
346-353
2009
Agaricus sp., Trametes hirsuta, Trametes versicolor, Pleurotus ostreatus, Cyclocybe aegerita, Inocybe lacera, Inocybe longicystis, Lactarius deliciosus, Lepista nuda, Lepiota sp. 1, Lepiota sp. 2, Leptonia lazunila, Lyophyllum subglobisporium, Ramaria stricta, Russula rosacea, Russula sp., Agrocybe sp. 1, Agrocybe sp. 2, Clitocybe sp., Coprinopsis atramentaria, Parasola plicatilis, Cortinarius sp. 1, Cortinarius sp. 2, Lepista nuda ECN 100605, Pleurotus ostreatus ECN 100607, Cortinarius sp. 2 ECN 100602, Lyophyllum subglobisporium ECN 100606, Trametes versicolor ECN 100609, Ramaria stricta ECN 100608
Frasconi, M.; Favero, G.; Boer, H.; Koivula, A.; Mazzei, F.
Kinetic and biochemical properties of high and low redox potential laccases from fungal and plant origin
Biochim. Biophys. Acta
1804
899-908
2010
Trametes versicolor, Melanocarpus albomyces, Trametes hirsuta (Q02497), Toxicodendron vernicifluum (Q8H979), Trametes hirsuta VTT D-95443 (Q02497)
Li, Q.; Pei, J.; Zhao, L.; Xie, J.; Cao, F.; Wang, G.
Overexpression and characterization of laccase from Trametes versicolor in Pichia pastoris
Appl. Biochem. Microbiol.
50
140-147
2014
Trametes versicolor (I6QS85), Trametes versicolor
Sarika, C.; Rekha, K.; Narasimha Murthy, B.
Immobilized laccase-based biosensor for the detection of disubstituted methyl and methoxy phenols - application of Box-Behnken design with response surface methodology for modeling and optimization of performance parameters
Artif. Cells Nanomed. Biotechnol.
44
1741-1752
2016
Trametes versicolor
Martinez-Morales, F.; Bertrand, B.; Pasion Nava, A.A.; Tinoco, R.; Acosta-Urdapilleta, L.; Trejo-Hernandez, M.R.
Production, purification and biochemical characterization of two laccase isoforms produced by Trametes versicolor grown on oak sawdust
Biotechnol. Lett.
37
391-396
2015
Trametes versicolor (Q12718), Trametes versicolor (Q5IR80), Trametes versicolor, Trametes versicolor HEMIM-9 (Q12718), Trametes versicolor HEMIM-9 (Q5IR80)
Bertrand, B.; Martinez-Morales, F.; Tinoco-Valencia, R.; Rojas, S.; Acosta-Urdapilleta, L.; Trejo-Hernandez, M.
Biochemical and molecular characterization of laccase isoforms produced by the white-rot fungus Trametes versicolor under submerged culture conditions
J. Mol. Catal. B
122
339-347
2015
Trametes versicolor (A0A144KZD6), Trametes versicolor (A0A144KZF3), Trametes versicolor (A0A144KZI7), Trametes versicolor (A0A144KZJ7), Trametes versicolor (A0A144KZK6)
-
Ammam, M.; Fransaer, J.
Combination of laccase and catalase in construction of H2O2-O2 based biocathode for applications in glucose biofuel cells
Biosens. Bioelectron.
39
274-281
2013
Trametes versicolor
Sharma, A.; Jain, K.K.; Jain, A.; Kidwai, M.; Kuhad, R.C.
Bifunctional in vivo role of laccase exploited in multiple biotechnological applications
Appl. Microbiol. Biotechnol.
102
10327-10343
2018
Trametes hirsuta, Trametes versicolor, Trametes cinnabarina, Trametes villosa, Ustilago maydis, Crinipellis sp.
Stanzione, I.; Pezzella, C.; Giardina, P.; Sannia, G.; Piscitelli, A.
Beyond natural laccases extension of their potential applications by protein engineering
Appl. Microbiol. Biotechnol.
104
915-924
2020
Bacillus licheniformis, Bacillus pumilus, Trametes versicolor, Lentinula edodes, Lentinula edodes (C5NN27), Rheinheimera sp., Thermothelomyces thermophilus, Pleurotus ostreatus (O60199)
Li, M.; Liu, L.; Kermasha, S.; Karboune, S.
Laccase-catalyzed oxidative cross-linking of tyrosine and potato patatin- and lysozyme-derived peptides Molecular and kinetic study
Enzyme Microb. Technol.
143
109694
2021
Trametes hirsuta (B2L9C1), Trametes hirsuta, Trametes versicolor (Q12718), Trametes versicolor
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