Molecular characterisation of a versatile peroxidase from a Bjerkandera strain

Abstract

The cloning and sequencing of the rbpa gene coding for a versatile peroxidase from a novel Bjerkandera strain is hereby reported. The 1777 bp isolated fragment contained a 1698 bp peroxidase-encoding gene, interrupted by 11 introns. The 367 amino acid-deduced sequence includes a 27 amino acid-signal peptide. The molecular model, built via homology modelling with crystal structures of four fungal peroxidases, highlighted the amino acid residues putatively involved in manganese binding and aromatic substrate oxidation. The potential heme pocket residues (R44, F47, H48, E79, N85, H177, F194 and D239) include both distal and proximal histidines (H48 and H177). RBP possesses potential calcium-binding residues (D49, G67, D69, S71, S178, D195, T197, I200 and D202) and eight cysteine residues (C3, C15, C16, C35, C121, C250, C286, C316). In addition, RBP includes residues involved in substrate oxidation: three acidic residues (E37, E41 and D183)-putatively involved in manganese binding and H83 and W172-potentially involved in oxidation of aromatic substrates. Characterisation of nucleotide and amino acid sequences include RBP in versatile peroxidase group sharing catalytic properties of both LiP and MnP. In addition, the RBP enzyme appears to be closely related with the ligninolytic peroxidases from the Trametes versicolor strain.

Decolorization of Remazol Brilliant Blue (RBBR) and Poly R-478 dyes by Bjerkandera adusta CCBAS 930

“…These enzymes catalyze the oxidative depolymerization of lignin in ligninocellulose wood complexes [6], and also other aromatic compounds possessing a lignin-like structure such as synthetic dyes [7,8]. Among white-rot basidiomycetes growing on wood, the ability to biodegrade synthetic dyes was reported for Phanerochaete chrysosporium, Trametes (Coriolus) versicolor, Pleurotus ostreatus, P. eryngii, Phlebia radiata, and Bjerkandera adusta [9][10][11][12][13][14]. P. chrysosporium demonstrated the greatest effectiveness at decolorization and biodegradation of anthraquinonic, azo and triphenylmethans dyes [9,11,12].…”

“…P. chrysosporium demonstrated the greatest effectiveness at decolorization and biodegradation of anthraquinonic, azo and triphenylmethans dyes [9,11,12]. Decolorization and biodegradation abilities of different Bjerkandera spp., including B. adusta strains, were widely studied, and basically include azo, anthraquinonic, triphenylmethans and heterocyclic dyes [2,5,[13][14][15][16][17][18][19][20]. A new strain Bjerkandera adusta CCBAS 930 isolated from soil was described [21].…”

Lignin‐modifying enzymes in filamentous basidiomycetes – ecological, functional and phylogenetic review

“…The third type of fungal class II LMP is a LIP-like MNP enzyme, so-called versatile peroxidase (VP, EC 1.11.1.16) that was first described in Pleurotus enryngii [26,71,72] and is also found in Bjerkandera spp. [73]. Physiological and functional features of basidiomycete LMPs are presented in Table 1.…”

Versatile Peroxidases: Super Peroxidases with Potential Biotechnological Applications-A Mini Review

“…Genetic architecture also confirms this concept where in the genetic elements of versatile peroxidase are shown to possess significant similarity to Lignin peroxidase and Manganese peroxidase genes. In Phanerochaete chrysosporium, the most extensively studied white rot fungus, the Lignin peroxidase gene is reported to exhibit high relativity to Versatile peroxidase of Bjerkandera than its Manganese peroxidase gene [13]. …”

“…The heme propionate is stabilized by two helices with Ca 2+ and two histidine residues one at proximity to heme and another at the distal end. The manganese cation binding site is stabilized by three acidic residues specifically tri-carboxylates of glutamate and aspartate residues [13]. The heme channel and tri-carboxylate manganese binding site of this peroxidase are illustrated in Figure 2.…”