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SAE0050

Sigma-Aldrich

Laccase from Aspergillus sp.

Synonym(s):

Laccase from Aspergillus sp., Novozym 51003

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About This Item

CAS Number:
EC Number:
UNSPSC Code:
12352204
NACRES:
NA.54

Quality Level

shipped in

ambient

storage temp.

2-8°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

General description

Laccase EC 1.10.3.2, a glycoprotein, is an extracellular multicopper enzyme and is considered as a metal. Laccase is widely distributed in fungi and also found among the higher plants, bacteria and insects.

Biochem/physiol Actions

Laccase oxidizes aromatic and nonaromatic compounds. Various compounds are used for detecting laccase production. These include guaiacol, syringaldazine and polymeric dyes like remazol brilliant blue-R. Laccase is involved in lignin degradation and thereby has industrial as well as food applications. Laccase is commonly used for delignification, dye bleaching, paper processing, waste detoxification, textile dye transformation, plant fiber modification and ethanol production.

Unit Definition

One Unit: LAMU (Laccase Unit). 1 LAMU is defined as the amount of enzyme which oxidizes 1 micromole of syringaldazine per minute, at pH 7.5 and 30 deg C.

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

Storage Class Code

10 - Combustible liquids

WGK

WGK 1


Certificates of Analysis (COA)

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Laccase: new functions for an old enzyme.
Mayer A M and Staples R C
Phytochemistry, 60(6), 551-565 (2002)
Screening and induction of laccase activity in fungal species and its application in dye decolorization.
Kumar V V, et al.
African Journal of Microbiology Research, 5(11), 1261-1267 (2011)
Microwave-assisted covalent immobilization of enzymes on inorganic surfaces.
Plagemann, R., et al.
Engineering in Life Sciences, 14, 493-499 (2014)
Screening and induction of laccase activity in fungal species and its application in dye decolorization.
Kumar VV
African Journal of Microbiology Research, 5, 1261-1267 (2011)
Meng-Hsuan Wu et al.
FEBS open bio, 8(8), 1230-1246 (2018-08-09)
A high-efficiency laccase, DLac, was isolated from Cerrena sp. RSD1. The kinetic studies indicate that DLac is a diffusion-limited enzyme. The crystal structure of DLac was determined to atomic resolution, and its overall structure shares high homology to monomeric laccases

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