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Merck
CN

51639

Laccase from Trametes versicolor

≥10 U/mg

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About This Item

CAS Number:
EC Number:
420-150-4
UNSPSC Code:
12352204
EC Number:
MDL number:
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form

powder

specific activity

≥10 U/mg

storage temp.

−20°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

Application

Laccase is polyphenol oxidase found in many plants, fungi and microorganisms. Laccases may be useful in enzymatic biofuel systems, teeth whitening, textile dyeing, and in other applications that require the removal of oxygen . Product 51639 is from Trametes versicolor.

Biochem/physiol Actions

Laccase is a blue copper oxidase that reduces molecular oxygen to water. Laccase oxidizes polyphenols, methoxy-substituted phenols and diamines, but not tyrosine. Oxidation by laccase is an one-electron reaction that generates a free radical .
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.

Other Notes

1 U corresponds to the amount of enzyme which converts 1 μmol catechol per minute at pH 4.5 and 25°C.
former nomenclature: Coriolus versicolor

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Storage Class

13 - Non Combustible Solids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

Regulatory Information

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C Madzak et al.
Protein engineering, design & selection : PEDS, 19(2), 77-84 (2005-12-22)
Laccases are oxidizing enzymes of interest because of their potential environmental and industrial applications. We performed site-directed mutagenesis of a laccase produced by Trametes versicolor in order to improve its catalytic properties. Considering a strong interaction of the Asp residue
The structure and function of fungal laccases
Christopher F. Thurston
Microbiology, 140, 19-26 (1994)
Applications of oxidoreductases: Recent progress.
Xu, Feng
Industrial Biotechnology (New Rochelle, N.Y.), 1, 38-50 (2005)
Noémie Lalaoui et al.
Chemical communications (Cambridge, England), 49(81), 9281-9283 (2013-09-03)
We report the functionalization of multi-walled carbon nanotube (MWCNT) electrodes by oxidative electropolymerization of pyrrole monomers bearing pyrene and N-hydroxysuccinimide groups. Both polymers were applied to the immobilization and electrical wiring of Trametes versicolor laccase via chemical grafting or non-covalent
Ngoc Han Tran et al.
Bioresource technology, 147, 667-671 (2013-09-17)
Numerous efforts have been made to remove emerging trace organic contaminants, such as pharmaceuticals and personal care products (PPCPs). This study examined the removal of N,N-diethyl-m-toluamide (DEET) by Trametes versicolor laccase and its laccase-mediator systems. Experimental results showed that DEET

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