40452
Laccase from Agaricus bisporus
powder, deep brown, ≥4 U/mg
Synonym(s):
Uroshiol oxidase
Sign Into View Organizational & Contract Pricing
All Photos(1)
About This Item
Recommended Products
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
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
Signal Word
Danger
Hazard Statements
Precautionary Statements
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
Choose from one of the most recent versions:
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Customers Also Viewed
Applications of oxidoreductases: Recent progress.
Industrial Biotechnology (New Rochelle, N.Y.), 1, 38-50 (2005)
The structure and function of fungal laccases
Microbiology, 140, 19-26 (1994)
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
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
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
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