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Sigma-Aldrich

Laccase from Trametes versicolor

greener alternative

powder, light brown, ≥0.5 U/mg

Synonym(s):

Oxygen oxidoreductase

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About This Item

CAS Number:
80498-15-3
Enzyme Commission number:
1.10.3.2 (BRENDA, IUBMB)
EC Number:
420-150-4
MDL number:
MFCD00131475
UNSPSC Code:
12352204
NACRES:
NA.54

form

powder

specific activity

≥0.5 U/mg

greener alternative product characteristics

Waste Prevention
Design for Energy Efficiency
Learn more about the Principles of Green Chemistry.

sustainability

Greener Alternative Product

color

light brown

greener alternative category

Enabling,

storage temp.

2-8°C

InChI

1S/C9H13NO/c1-4-10-7(2)5-9(6-11)8(10)3/h5-6H,4H2,1-3H3

InChI key

NWDZDFOKSUDVJV-UHFFFAOYSA-N

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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.

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

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.
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.

Unit Definition

One unit corresponds to the amount of enzyme which converts 1 μmole of catechol per minute at pH 5.0 and 25 °C

Other Notes

former nomenclature: Coriolus versicolor

pictograms

Health hazard
GHS08

signalword

Danger

hcodes

H334

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Laccases and other polyphenol oxidases in ecto-and ericoid mycorrhizal fungi
Burke R and Cairney J
Mycorrhiza, 12(3), 105-116 (2002)
Komal Agrawal et al.
Heliyon, 6(5), e03972-e03972 (2020-05-22)
Multicopper oxidases (MCOs) has a unique feature of having the presence of four Cu atoms arranged into three (Type I, II and III) spectral classification. MCOs laccase due to its broad range of substrate specificity has numerous biotechnological applications. The
Qimiao Shao et al.
The Journal of biological chemistry, 287(17), 14270-14279 (2012-03-01)
Many insects eat the green leaves of plants but excrete black feces in an as yet unknown mechanism. Insects cannot avoid ingesting pathogens with food that will be specifically detected by the midgut immune system. However, just as in mammals
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
Laccase-mediator catalyzed conversion of model lignin compounds
Rich JO, et al.
Biocatal. Agric. Biotechnol., ACS Symp.Ser., 5, 111-115 (2016)
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