LCC1 and LCC5 are the main laccases secreted in liquid cultures of Coprinopsis cinerea strains

Summary

This research investigated how different strains of the fungus Coprinopsis cinerea produce laccase enzymes under various growing conditions. Laccases are important enzymes that can break down various organic compounds. The study revealed that temperature and growth medium composition strongly influence laccase production, with cooler temperatures generally resulting in better enzyme production. The researchers identified five different types of laccases, with two (Lcc1 and Lcc5) being the main ones produced across all strains. Impacts on everyday life: – Improved understanding of enzyme production could lead to more efficient industrial processes – Better knowledge of fungal enzymes helps develop environmental applications like waste treatment – Understanding how temperature affects enzyme production can optimize biotechnology processes – Insights into fungal genetics and protein production advance biological research methods – Knowledge gained could help develop new applications for these versatile enzymes

Background

Laccases are four copper-containing oxidases capable of oxidizing phenolic and aromatic compounds. The litter-degrading dung fungus Coprinopsis cinerea has seventeen different laccase genes, presenting one of the largest groups of laccase genes described for a fungus. Prior to this study, little was known about the expression of these multiple laccase genes in C. cinerea.

Objective

To analyze and compare laccase production in different C. cinerea monokaryotic strains under varying culture conditions and identify which specific laccase isoenzymes are secreted into the culture medium.

Results

Most strains showed negligible laccase activity at 37°C but produced significant amounts at 25°C, particularly in mKjalke medium where 9 of 10 strains showed activities between 0.2-5.9 U/mL. Through proteomic analysis, five different laccases (Lcc1, Lcc2, Lcc5, Lcc9 and Lcc10) were identified. Lcc1 and Lcc5 were found to be the main laccases secreted by all laccase-positive strains, with Lcc1 appearing in three distinct forms and Lcc5 in two forms. Lcc2, Lcc9 and Lcc10 occurred only as minor laccases in three strains.

Conclusion

Laccase secretion in C. cinerea is strongly influenced by cultivation temperature and medium composition. Of the seventeen laccase genes, at least five are functionally expressed, with Lcc1 and Lcc5 being the predominant universal laccases across strains while others appear strain-specific. The multiple forms of Lcc1 and Lcc5 suggest post-translational modifications or protein dimerization occurs.
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