SAE0050
Laccase from Aspergillus sp.
Sinónimos:
Laccase from Aspergillus sp., Novozym 51003
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Permítanos ayudarleSMILES string
[n]1(c(c(cc1C)C=O)C)CC
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
shipped in
ambient
storage temp.
2-8°C
Quality Level
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.
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.
Other Notes
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.
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Clase de almacenamiento
10 - Combustible liquids
wgk
WGK 1
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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)
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 VV
African Journal of Microbiology Research, 5, 1261-1267 (2011)
Microwave-assisted covalent immobilization of enzymes on inorganic surfaces.
Plagemann, R., et al.
Engineering in Life Sciences, 14, 493-499 (2014)
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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