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Applied Microbiology and Biotechnology

, Volume 57, Issue 1–2, pp 85–91 | Cite as

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

  •  A. Leontievsky
  •  N. Myasoedova
  •  B. Baskunov
  •  L. Golovleva
  •  C. Bucke
  •  C. Evans
Original Paper

Abstract.

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°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°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.

Keywords

Oxidation Enzyme Benzoquinone Glutaraldehyde Hydroquinone 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer-Verlag 2001

Authors and Affiliations

  •  A. Leontievsky
    • 1
  •  N. Myasoedova
    • 1
  •  B. Baskunov
    • 1
  •  L. Golovleva
    • 1
  •  C. Bucke
    • 2
  •  C. Evans
    • 2
  1. 1.Institute of Biochemistry and Physiology of Microorganisms of Russian Academy of Sciences (IBPM RAS), 142290 Pushchino Moscow region, Prospekt Nauki 5, Russia
  2. 2.School of Biosciences, University of Westminster, London W1W 6UW, UK

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