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Comparative Analysis of the Secretomes of Schizophyllum commune and Other Wood-Decay Basidiomycetes During Solid-State Fermentation Reveals its Unique Lignocellulose-Degrading Enzyme System

Summary

This research investigated how a unique fungus, Schizophyllum commune, breaks down plant material in ways different from other wood-degrading fungi. The study found that S. commune uses a hybrid approach combining chemical modification with an extensive set of enzymes to efficiently break down tough plant materials into simple sugars. This discovery has important implications for biofuel production and industrial applications. Impacts on everyday life: – Could lead to more efficient and cost-effective biofuel production from plant waste – May help develop better enzyme products for various industrial processes – Offers potential solutions for converting agricultural waste into valuable products – Could contribute to more environmentally friendly paper and textile processing – May help reduce dependence on fossil fuels through improved biomass conversion

Background

The genome of Schizophyllum commune encodes a diverse repertoire of degradative enzymes for plant cell wall breakdown. Recent comparative genomics studies suggest this wood decayer likely has a mode of biodegradation distinct from established white-rot/brown-rot models. However, much remains unknown about its extracellular enzyme system during lignocellulose deconstruction and the underlying mechanism is poorly understood.

Objective

To identify potentially important enzymes and provide insight into the mechanism of plant cell wall deconstruction by S. commune through analysis of its degradation dynamics and lignocellulolytic enzyme patterns during solid-state fermentation on Jerusalem artichoke stalk.

Results

S. commune displayed significantly higher levels of hydrolytic enzyme activities compared to the other fungi. It modified lignin polymer through hydroxyl radical attack, similar to brown-rot fungi. The crude enzyme cocktail from S. commune demonstrated superior performance over commercial enzyme preparations in biomass hydrolysis at low enzyme loadings. Secretome analysis revealed S. commune produced a higher diversity of carbohydrate-degrading enzymes, especially hemicellulases and pectinases, along with enzymes supporting hydroxyl radical generation. Multiple non-hydrolytic proteins including lytic polysaccharide monooxygenases and expansin-like proteins were also identified.

Conclusion

S. commune employs a unique hybrid decay mechanism combining Fenton chemistry-based oxidative modification with an extensive enzymatic system for polysaccharide degradation. Its enzyme cocktail shows high efficiency in biomass saccharification due to synergistic actions between cellulases and accessory enzymes. These findings provide new insights into S. commune’s complex degradative system and highlight the importance of accessory enzymes in lignocellulose breakdown.
  • Published in:Biotechnology for Biofuels,
  • Study Type:Comparative Analysis,
  • Source: 10.1186/s13068-016-0461-x
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