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Manganese peroxidase (MnP), a crucial enzyme in biodegradation of lignin, is synthesized by most white rot fungi. To obtain novel enzymes with superior biodegradation potential, MnP-producing wild isolates were evaluated for their ability to degrade recalcitrant azo dyes, sulfonephthalein dyes, and kraft lignin. Of 30 wild isolates screened, 18 tested positive for lignin modifying enzymes (LMEs). Thirteen of these isolates were positive for both laccase and MnP, whereas four produced only laccase, and one produced lignin peroxidase alone. The isolates were identified as Clitopilus scyphoides MH172162 (AGUM004), Ganoderma rasinaceum MH172163 (AGUM007), and three Schizophyllum species: MH172164, MH172165, and MH172166 (KONA001, AGUM0011, and AGUM021). The Fourier-transform infrared spectroscopy (FTIR) analysis of dye degradation and kraft lignin samples with AGUM004 and AGUM007 revealed biotransformation. The former could not completely degrade Reactive Black 5 and bromocresol green, but it could completely (100%) decolorize bromophenyl blue, bromothymol blue, and Remazol brilliant blue R. The latter efficiently degraded almost all tested dyes. Both degraded kraft lignin. The screened hyper MnP-producing wild AGUM004 and AGUM007 were shown to be potential dye degraders in addition to having lignin degrading abilities.

Screening of wild basidiomycetes and evaluation of the biodegradation potential of dyes and lignin by manganese peroxidases