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Applied Microbiology and Biotechnology

, Volume 59, Issue 2–3, pp 198–204 | Cite as

Purification and characterisation of a novel laccase from the ascomycete Melanocarpus albomyces

  •  L.-L. Kiiskinen
  •  L. Viikari
  •  K. Kruus
Original Paper

Abstract.

A novel laccase from the ascomycete Melanocarpus albomyces was purified and characterised. The enzyme was purified using anion exchange chromatography, hydrophobic interaction chromatography and gel filtration, and the purified laccase was biochemically characterised. It had activity towards typical substrates of laccases including 2,2′-azinobis-(3-ethylbenzthiazoline-6-sulphonate), dimethoxyphenol, guaiacol, and syringaldazine. The laccase showed good thermostability and it had a pH optimum at neutral pH, both unusual properties for most known fungal laccases. The activity of the laccase from M. albomyces was highest at 60–70°C. With guaiacol and syringaldazine the pH optima were rather broad: 5–7.5 and 6–7, respectively. It retained 50% of its activity after 5 h incubation at 60°C. The molecular weight of the laccase was about 80 kDa and the isoelectric point 4.0. The ultraviolet-visible absorption and electron paramagnetic resonance spectra of the purified laccase indicated that the typical three types of copper were present.

Keywords

Electron Paramagnetic Resonance Hydrophobic Interaction Anion Exchange Isoelectric Point Electron Paramagnetic Resonance Spectrum 
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 2002

Authors and Affiliations

  •  L.-L. Kiiskinen
    • 1
  •  L. Viikari
    • 1
  •  K. Kruus
    • 1
  1. 1.VTT Biotechnology, P.O. Box 1500, 02044 VTT, Finland

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