Abstract
A novel extracellular lignin peroxidase (LiP) has been produced (65 U/mL) in potato dextrose broth (PDB)-optimized media by a white-rot Agaricomycetes fungus strain KB-DZ15 newly isolated from dead deciduous trees at Zimoula Forest (Tizi-Ouzou, Algeria). This strain was identified as Phlebia radiata based on internal transcribed spacer (ITS) rDNA gene sequencing. The peroxidase enzyme (called LiP PR40) was purified and characterised. The matrix-assisted laser desorption-ionization – time of flight mass spectrometry (MALDI-TOF/MS) analysis revealed that LiP PR40 enzyme was a monomer with a molecular mass of 40,125.31 Da. The 25 N-terminal residue sequence of LiP PR40 showed high similarity with those of fungi LiPs. Interestingly, LiP PR40 presents premium activity at pH 3 and 80 °C with specific activity and Reinheitzahl (RZ) level of 510 U/mg and 2.81, respectively. Furthermore, it was completely inhibited by sodium azide (NaN3) and potassium cyanide (KCN), suggesting the presence of haem components in its tertiary structure. More interestingly, LiP PR40 illustrated more upper catalytic efficiency and dye-decolorisation aptitude than that of commercial well-known horseradish peroxidase (HRP) from roots of Armoracia rustanica and the purified reported LiP BA45 from Bjerkandera adusta strain CX-9. Consequently, these properties make LiP PR40 a potential candidate for destaining synthetic-dyes and lignin-biodegradation.
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