Purification, characterization and sequence analysis of a laccase from the ascomycete Mauginiella sp.

Hetti Palonen, Markku Saloheimo, Liisa Viikari, Kristiina Kruus (Corresponding Author)

Research output: Contribution to journalArticleScientificpeer-review

85 Citations (Scopus)


A laccase from the ascomycete Mauginiella sp. was purified to electrophoretic homogeneity and biochemically characterized. The molecular mass of the laccase was 63 kDa as determined by mass spectrometry and it existed as six isoforms with isoelectric points in the range of 4.8–6.4. The laccase showed activity towards the typical substrates: 2,2′-azinobis-(3-ethylbenzothiazoline)-6-sulphonate (ABTS), guaiacol, dimethoxyphenol (2,6-DMP), and syringaldazine. The pH optima on guaiacol, 2,6-DMP and ABTS were 4, 3.5 and 2.4, respectively. The enzyme was strongly, 98%, inhibited by 1 mM NaN3 and 88% by 1 mM KCN. The laccase was stable at neutral pH, retaining 80% activity after 24 h at pH 6–8. The enzyme was sensitive to high temperatures: the half-life at 70 °C was only 3 min. A fragment of the laccase gene was isolated and its nucleotide sequence was determined. The laccase gene showed high identity to the laccase genes lcc1 and lcc2 of the basidiomycetes Trametes versicolor and Trametes villosa, respectively.
Original languageEnglish
Pages (from-to)854-862
Number of pages9
JournalEnzyme and Microbial Technology
Issue number6
Publication statusPublished - 2003
MoE publication typeA1 Journal article-refereed


  • Laccase
  • Mauginiella sp.
  • Purification
  • Characterization
  • Amino acid sequence
  • Gene sequence

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