Skip to Content
Merck
All Photos(1)

Documents

40452

Sigma-Aldrich

Laccase from Agaricus bisporus

greener alternative

powder, deep brown, ≥4 U/mg

Synonym(s):

Uroshiol oxidase

Sign Into View Organizational & Contract Pricing
All Photos(1)

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

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.

color

deep brown

greener alternative category

, Enabling

shipped in

wet ice

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

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

Signal Word

Danger

Hazard Statements

H334

Precautionary Statements

P261 - P342 + P311

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

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
View All Related Papers

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service