38429
Laccase from Trametes versicolor
powder, light brown, ≥0.5 U/mg
Synonym(s):
Oxygen oxidoreductase
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About This Item
CAS Number:
NACRES:
NA.54
UNSPSC Code:
12352204
EC Number:
420-150-4
MDL number:
Product Name
Laccase from Trametes versicolor, powder, light brown, ≥0.5 U/mg
SMILES string
[n]1(c(c(cc1C)C=O)C)CC
InChI key
NWDZDFOKSUDVJV-UHFFFAOYSA-N
InChI
1S/C9H13NO/c1-4-10-7(2)5-9(6-11)8(10)3/h5-6H,4H2,1-3H3
form
powder
specific activity
≥0.5 U/mg
greener alternative product characteristics
Waste Prevention
Design for Energy Efficiency
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sustainability
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color
light brown
greener alternative category
storage temp.
2-8°C
Quality Level
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Application
Laccase from Trametes versicolor has been used:
- to assess the use of four laccase-producing strains in waste water treatment
- in laccase assay
- in screening the lignols
Biochem/physiol Actions
Laccase catalyzes the oxidation of phenol containing compounds, including lignin, through the reduction of oxygen to water. The presence of mediators will allow the oxidation of non-phenlic compounds as well. The primary function of laccase is to degrade lignin in fungi.
Some of the enzymatic actions of laccase are associated with sporulation, detoxification, morphogenesis, melanin polymerization and it offers protection to spore coat. Laccase can catalyse a number of substrates including medicinal drugs and halogenated pesticides. It utilizes oxygen for its catalysis. For these reasons, it might be useful in the biological degradation of micropollutants in wastewater treatment.
General description
Laccase is an enzyme, produced by ericoid mycorrhiza and ectomycorrhiza fungi. It belongs to the group of polyphenol oxidases. Laccase is also present in plants and bacteria.
We are committed to bringing you Greener Alternative Products, which adhere to one or more of The 12 Principles of Greener Chemistry. This product has been enhanced for energy efficiency and waste prevention when used in fuel cell and cellulosic ethanol research. For more information see the article in biofiles and Enzymes for Alternative Energy Research.
Other Notes
One unit corresponds to the amount of enzyme which converts 1 μmole of catechol per minute at pH 5.0 and 25 °C
former nomenclature: Coriolus versicolor
signalword
Danger
hcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Regulatory Information
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Jonas Margot et al.
AMB Express, 3(1), 63-63 (2013-10-25)
Relatively high concentrations of micropollutants in municipal wastewater treatment plant (WWTP) effluents underscore the necessity to develop additional treatment steps prior to discharge of treated wastewater. Microorganisms that produce unspecific oxidative enzymes such as laccases are a potential means to
Michael Clark et al.
ACS synthetic biology, 11(1), 308-316 (2021-12-10)
Inadequate management of household and industrial wastes poses major challenges to human and environmental health. Advances in synthetic biology may help address these challenges by engineering biological systems to perform new functions such as biomanufacturing of high-value compounds from low-value
Xuan Luo et al.
ACS applied materials & interfaces, 12(46), 51999-52007 (2020-11-06)
The fabrication of hybrid protein-Cu3(PO4)2 nanoflowers (NFs) via an intermediate toroidal structure is dramatically accelerated under shear using a vortex fluidic device (VFD), which possesses a rapidly rotating angled tube. As-prepared laccase NFs (LNFs) exhibit ≈1.8-fold increase in catalytic activity
Laccase-mediator catalyzed conversion of model lignin compounds
Rich JO, et al.
Biocatal. Agric. Biotechnol., ACS Symp.Ser., 5, 111-115 (2016)
Ana Luisa Parra Guardado et al.
Environmental science and pollution research international, 28(20), 25579-25593 (2021-01-19)
In the present work, pharmaceutical micropollutant degradation by laccase immobilized on silica through an innovative process is proposed. The influence of different parameters on the immobilization conditions was evaluated by a 23 full factorial design, and parameters leading to the
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