MYCOLab Ai Logo - gold and army green

Enhanced Extracellular Production of Laccase in Coprinopsis cinerea by Silencing Chitinase Gene

Summary

This research demonstrates a new method to increase production of an important industrial enzyme called laccase by genetically modifying fungi. By silencing specific genes that control cell wall properties, researchers were able to create fungal strains that produce significantly more enzyme. This advance could make industrial enzyme production more efficient and cost-effective. Impacts on everyday life: • More efficient production of enzymes used in eco-friendly industrial processes • Potential cost reduction for products that use these enzymes • Development of better methods for sustainable manufacturing • Advancement of biotechnology techniques for protein production • Contribution to greener industrial processes by improving production of environmentally friendly catalysts

Background

Laccase is a copper-containing polyphenol oxidase and important green biocatalyst with industrial applications due to its ability to oxidize various compounds with water as the only byproduct. While basidiomycetes laccase occupies over 90% of the current laccase market share, the yield and efficiency of naturally secreted laccase is relatively low, leading to high production costs that limit industrial applications.

Objective

This study aimed to achieve efficient homologous recombinant expression of laccase Lcc5 in Coprinopsis cinerea by silencing chitinase genes to enhance production. The researchers sought to identify and silence critical chitinase genes to modify cell wall properties and improve laccase yields.

Results

Silencing either ChiEn1 or ChiE2 reduced sporulation and growth rate while increasing cell wall sensitivity. The ChiE2-silenced strain Cclcc5-antiChiE2-5 showed highest extracellular laccase activity of 38.2 U/mL at 250 rpm agitation speed in 3-L fermenter culture, compared to 25.5 U/mL for the control strain at 150 rpm. The silenced strain showed increased tolerance to shear forces and achieved 2.6-fold higher laccase activity than the control when both were run at 250 rpm.

Conclusion

Silencing the chitinase gene ChiE2 successfully enhanced laccase production in C. cinerea by increasing cell wall shear tolerance while altering growth characteristics. The engineered strain achieved 1.6-fold higher laccase activity and 1.8-fold higher productivity compared to controls in scaled-up fermentation. This approach provides a novel strategy for enhancing protein production in C. cinerea.
  • Published in:Applied Microbiology and Biotechnology,
  • Study Type:Laboratory Research,
  • Source: 10.1007/s00253-024-13164-9
Scroll to Top