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
MDL number:
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
≥10 U/mg
storage temp.
−20°C
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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 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.
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 .
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
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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)
Ian R Wheeldon et al.
Proceedings of the National Academy of Sciences of the United States of America, 105(40), 15275-15280 (2008-10-01)
Here, we present two bifunctional protein building blocks that coassemble to form a bioelectrocatalytic hydrogel that catalyzes the reduction of dioxygen to water. One building block, a metallopolypeptide based on a previously designed triblock polypeptide, is electron-conducting. A second building
Ngoc Han Tran et al.
Bioresource technology, 146, 721-731 (2013-08-21)
Many efforts have been made to understand the biodegradation of emerging trace organic contaminants (EOCs) in the natural and engineered systems. This review summarizes the current knowledge on the biodegradation of EOCs while having in-depth discussion on metabolism and cometabolism
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