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Extracellular Proteins of Trametes hirsuta st. 072 Induced by Copper Ions and a Lignocellulose Substrate

Summary

This research examined how a wood-degrading fungus produces different enzymes to break down plant material. The study revealed that the fungus uses a sophisticated system of proteins to efficiently decompose tough plant materials like straw and wood. This has important implications for both nature and industry. Impacts on everyday life: – Improved understanding of natural recycling processes in forests and agricultural systems – Potential development of more efficient biofuel production from plant waste – New approaches for breaking down agricultural residues like straw – Possible applications in paper and textile industries for eco-friendly processing – Development of new industrial enzymes for various biotechnology applications

Background

Fungi have the highest natural capacity to degrade lignocellulose substrates through complex systems of extracellular enzymes. The expression and secretion of these enzymes depend on substrate characteristics and environmental conditions. Lignocellulose is a major structural component of plants and an abundant renewable natural resource, but its bioconversion is challenging due to lignin’s resistance to degradation.

Objective

To analyze the secretome and enzymatic activities of the white-rot basidiomycete Trametes hirsuta st. 072 when cultivated on synthetic media and lignocellulose substrate, with and without copper ion induction.

Results

T. hirsuta produced multiple extracellular enzymes including ligninolytic, cellulolytic, hemicellulolytic, peroxide generating, and proteolytic enzymes, as well as cerato-platanins. The fungus predominantly expressed cellobiases and xylanases in response to lignocellulose, rather than glucanases and mannosidases seen in other white rot species. Lignin peroxidase activity was attributed to versatile peroxidase. The enzyme expression profiles changed dramatically between growth conditions, with surface cultivation on lignocellulose switching off certain enzymes while activating others. Cerato-platanin proteins were produced only in response to lignocellulose contact.

Conclusion

T. hirsuta employs a sequential mechanism for natural substrate degradation, producing different sets of enzymes to digest all main components of the substrate during cultivation. The fungus secretes distinct glycoside hydrolases with unique substrate specificity compared to other basidiomycetes, along with multiple isoforms of laccases and versatile peroxidase as key lignin-modifying enzymes. The presence of lignocellulose and copper ions significantly impacts enzyme expression patterns.
  • Published in:BMC Microbiology,
  • Study Type:Laboratory Research,
  • Source: 10.1186/s12866-016-0729-0
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