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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Transformation of 2,4,6-trichlorophenol by free and immobilized fungal laccase.

Laccase from the white rot fungus Coriolus versicolor was immobilized on Celite R-637 by covalent binding with glutaraldehyde. After a sharp primary decline in activity (up to 50%), the retained enzyme activity was stable over a storage period of 33 days at 4 degrees C. A comparative study of soluble and immobilized laccases revealed the increased resistance of immobilized enzyme to the unfavourable effects of alkaline pH, high temperature and the action of inhibitors. A combination of these properties of immobilized laccase resulted in the ability to oxidize 2,4,6-trichlorophenol (2,4,6-TCP) at 50 degrees C at pH 7. 0. The reactions of soluble and immobilized laccase with 2,4,6-TCP were examined in the presence and absence of redox mediators. 3,5-Dichlorocatechol, 2,6-dichloro-1,4-benzoquinone and 2,6-dichloro-1,4-hydroquinone were found to be the primary products of 2,4,6-TCP oxidation by laccase; oligo- and polymeric compounds were also found.[1]

References

  1. Transformation of 2,4,6-trichlorophenol by free and immobilized fungal laccase. Leontievsky, A.A., Myasoedova, N.M., Baskunov, B.P., Golovleva, L.A., Bucke, C., Evans, C.S. Appl. Microbiol. Biotechnol. (2001) [Pubmed]
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