Fig 1.
Macro–, fruiting-bodies morphology and Azure B decolorization of Junghuhnia nitida LE-BIN 2013 (1) and Steccherinum bourdotii LE-BIN 2738 (2): colonies on BWA medium (A); fruiting bodies on sawdust substrate (B); decolorization of Azure B in MEA medium (C).
Bars –10 mm. Control–: plate without fungus. Control+: plate with Trametes hirsuta LE-BIN 072.
Fig 2.
Maximum likelihood (ML) phylogenetic tree of ribosomal gene sequences.
Numbers at nodes are bootstrap percentages from 100 replicates. Fungi from the residual and the core polyporoid clades are highlighted in yellow and green respectively. Three ascomycete sequences used as the outgroup are highlighted in violet.
Table 1.
Oxidative potential of Junghuhnia nitida and Steccherinum bourdotii strains evaluated by the express method.
Fig 3.
The activity profiles of the lignin degrading enzymes during J. nitida (red circles) and S. bourdotii (black squares) static surface cultivation on LC medium.
Panels A-C show the activities of laccase, manganese peroxidase and Mn2+- independent peroxidases (versatile peroxidase and/or lignin peroxidase), respectively.
Fig 4.
The de novo sequenced peptides of JnL and SbL aligned with the amino acid sequences of laccase 2 from S. murashkinskyi (SmL) and laccase A from A. faginea (AfL).
The glycosylated peptides are shown in red. The potential glycosylation sites are highlighted in grey, and the occupied glycosylation sites are highlighted in red. The coordinating ligands of the copper ions are highlighted in turquoise.
Table 2.
Physicochemical characteristics of the laccases.
Fig 5.
Lines: M—molecular mass markers, 1 –JnL, 2 –JnL treated with PNGase F, 3 –SbL, 4 –SbL treated with PNGase F.
Fig 6.
Azure B decolorization by different laccases.
1 –Azure B+HOBt, 2 –Azure B + HOBt+enzyme, 3 –Azure B.
Fig 7.
DSC melting curves of ThL, CcL, JnL and SbL laccases.
Table 3.
The kinetic parameters of oxidation of the various substrates by the laccases.