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Laccase

Laccases are copper-containing oxidase enzymes that are found in many plants, fungi and microorganisms. The copper can be bound in several sites; Type 1, Type 2, and/or Type 3. When types 2 and 3 are bound together, the enzyme is called a trinuclear cluster. Laccases are enzymatically active on phenols and similar molecules, and perform a one-electron oxidation. Laccases can be polymeric, and the enzymatically active form can be a dimer or trimer. The easiest way to detect activity in Laccases is with a spectrophotometer. Substrates that are commonly used with this method are ABTS, syringaldazine, 2,6-dimethoxyphenol, and dimethyl-p-phenylenediamine. Also, activity can be monitored with an oxygen sensor as the oxidation of the substrate is paired with the reduction of oxygen to water. Laccases can also be used as the cathode in an enzyme catalyzed fuel cell. They can be paired with an electron mediator to facilitate electron transfer to a solid electrode wire. Laccase is one of the few oxidoreductases commercialized as industrial catalysts. The enzyme can be used for textile dyeing/finishing, wine cork making, and many other industrial, environmental, diagnostic, and synthetic uses Applications of oxidoreductases: Recent progress, Industrial Biotechnology 1, 38-50[http://www.liebertonline.com/doi/pdf/10.1089/ind.2005.1.38?cookieSet=1]). (From the Wikpedia article Laccase.)

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Recent Publications on Laccase:

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Decolourization of recalcitrant dyes with a laccase from Streptomyces coelicolor under alkaline conditions.
Colored wastewater from textile industries is a consequence of dye...
18th July, 2008
Departement de chimie-biologie, Universite du Quebec a Trois-Rivieres, J Ind Microbiol Biotechnol. 2008 Jul 17;.
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Lignocellulolytic enzymes profile during growth and fruiting of Pleurotus ostreatus on wheat straw and tree leaves.
Cultivation of two commercial Pleurotus ostreatus (oyster mushroom)...
18th July, 2008
Durmishidze Institute of Biochemistry and Biotechnology, 0159 Tbilisi, Acta Microbiol Immunol Hung. 2008 Jun;55(2):157-68.
Efficient expression of laccase gene from white-rot fungus Schizophyllum commune in a transgenic tobacco plant.
Ligninolytic enzymes produced by white-rot fungi are effective degraders...
16th July, 2008
Department of Applied Biological Chemistry, Faculty of Agriculture, FEMS Microbiol Lett. 2008 Jul 2;.
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Purification and Characterization of Laccase Secreted by L. lividus.
The culture conditions for maximum secretion of laccase by Loweporus...
9th July, 2008
Department of Chemistry, D.D.U. Gorakhpur University, Gorakhpur, 273 009, Appl Biochem Biotechnol. 2008 Jul 8;.
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Catalytic activities of fungal oxidases in hydrophobic ionic liquid 1-butyl-3-methylimidazolium hexafluorophosphate-based microemulsion.
For hydrophobic ionic liquid 1-butyl-3-methylimidazolium...
8th July, 2008
Key Laboratory of Colloid & Interface Chemistry of the Education Ministry Colloids Surf B Biointerfaces. 2008 Jul 3;.
DOI Direct Link

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Laccase Patents:

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US Patent No.Title
7297527 Highly productive .alpha.-amylases
7329424 Process for manufacturing cheeses and other dairy products and products thereof
7329441 Water-soluble pouches
7329528 Enzyme multimer and process of producing same
7332297 Enzymatic polymerization

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Wikipedia excerpt, where present, licenced under the GNU Free Documentation License. Resources from the NCBI applied. Selected MeSH subject headings created and maintained by the US NLM are used in conjunction with additional keywords. 2006-2008 MeSH.
 

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