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 language | English (US) |
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Pages (from-to) | 391-394 |
Number of pages | 4 |
Journal | FEBS Letters |
Volume | 422 |
Issue number | 3 |
DOIs | |
State | Published - Feb 6 1998 |
Externally published | Yes |
Keywords
- Bjerkandera sp. strain BOS55
- Lignin peroxidase
- N-terminal sequence
- Purification
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology