Penicillium species have been studied as producers of plant cell wall degrading enzymes to deconstruct agricultural residues and to be applied in industrial processes. Natural environments containing decaying plant matter are ideal places for isolating fungal strains with cellulolytic and xylanolytic activities. In the present study, Cerrado soil samples were used as source of filamentous fungi able to degrade xylan and cellulose. Penicillium was the most abundant genus among the obtained xylan and carboxymethylcellulose degraders. Penicillium polonicum was one of the best enzyme producers in agar-plate assays. In addition, it secretes CMCase, Avicelase, pectinase, mannanase, and xylanase during growth in liquid media containing sugarcane bagasse as carbon source. The highest value for endo-β-1,4-xylanase activity was obtained after 4 days of growth. Xyl PP, a 20 kDa endo-β-1,4-xylanase, was purified and partially characterized. The purified enzyme presented the remarkable feature of being resistant to the lignin-derived phenolic compounds, p-coumaric and trans-ferulic acids. This feature calls for its further use in bioprocesses that use lignocellulose as feedstock. Furthermore, future work should explore its structural features which may contribute to the understanding of the relationship between its structure and resistance to phenolic compounds.
Supplementary information: The online version contains supplementary material available at 10.1007/s13205-022-03405-x.
Keywords: Cerrado soil; Endo-β-1,4-xylanase; Penicillium; Sugarcane bagasse.
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