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40452

Sigma-Aldrich

Laccase from Agaricus bisporus

greener alternative

powder, deep brown, ≥4 U/mg

Synonym(s):

Uroshiol oxidase

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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

biological source

fungus (Agaricus bisporus)

form

powder

specific activity

≥4 U/mg

greener alternative product characteristics

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

sustainability

Greener Alternative Product

color

deep brown

greener alternative category

, Enabling

shipped in

wet ice

storage temp.

−20°C

SMILES string

[n]1(c(c(cc1C)C=O)C)CC

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

Related Categories

General description

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 used as enzyme for alternative energy. For more information see the Enzymes for Alternative Energy Research.

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 .

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 .

Unit Definition

1 U corresponds to the amount of enzyme which converts 1 μmol catechol per minute at pH 6.0 and 25°C

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)

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Applications of oxidoreductases: Recent progress.
Xu, Feng
Industrial Biotechnology (New Rochelle, N.Y.), 1, 38-50 (2005)
The structure and function of fungal laccases
Christopher F. Thurston
Microbiology, 140, 19-26 (1994)
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
Meng-Hsuan Wu et al.
Scientific reports, 9(1), 9754-9754 (2019-07-07)
Laccases that are tolerant to organic solvents are powerful bio-catalysts with broad applications in biotechnology. Most of these uses must be accomplished at high concentration of organic solvents, during which proteins undergo unfolding, thereby losing enzyme activity. Here we show
Shanfa Lu et al.
Proceedings of the National Academy of Sciences of the United States of America, 110(26), 10848-10853 (2013-06-12)
Laccases, as early as 1959, were proposed to catalyze the oxidative polymerization of monolignols. Genetic evidence in support of this hypothesis has been elusive due to functional redundancy of laccase genes. An Arabidopsis double mutant demonstrated the involvement of laccases
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