Purification and characterization of two lignin peroxidase isozymes produced by Bjerkandera sp. strain BOS55

Rimko Ten Have, Sybe Hartmans, Pauline J.M. Teunissen, Jim A. Field

Research output: Contribution to journalArticle

37 Scopus citations

Abstract

The white-rot fungus Bjerkandera sp. strain BOS55 excretes at least seven lignin peroxidase (LIP) isozymes. Two of these, LiP-2 and LIP-5 (molecular weight 40-42 kDa), were purified to homogeneity. Both isozymes had the same N-terminal amino acid sequences which showed strong homology with LiP isozymes produced by other white-rot fungi. The kinetics of both isozymes were similar, LIP-5 oxidized veratryl alcohol optimally only in the presence of H2O2 near pH 3.0 (16.7 U/mg) and LiP-2 did this below pH 2.5 (33.8 U/mg). Also at normal physiological pHs for fungal growth (pH 5.0-6.5) both isozymes were still active. Further characterization of LiP-2 and LiP-5 revealed that the K(m) for H2O2 strongly decreased with increasing pH. As a result of this the catalytic efficiency (TN/K(m)) calculated on the basis of the K(m) for H2O2 in the oxidation of veratryl alcohol was constant over wide pH range.

Original languageEnglish (US)
Pages (from-to)391-394
Number of pages4
JournalFEBS Letters
Volume422
Issue number3
DOIs
StatePublished - Feb 6 1998
Externally publishedYes

Keywords

  • Bjerkandera sp. strain BOS55
  • Lignin peroxidase
  • N-terminal sequence
  • Purification

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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