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Optimization, Purification and Characterization of Laccase from Ganoderma leucocontextum Along with its Phylogenetic Relationship

Summary

This research focused on studying and optimizing an important enzyme called laccase from a rare medicinal mushroom species. The enzyme was successfully isolated and shown to be very stable at high temperatures and acidic conditions, making it valuable for industrial uses. Impact on everyday life: – Could lead to more environmentally friendly industrial processes – May help develop new methods for treating industrial waste and pollutants – Could contribute to more sustainable manufacturing processes – Potential applications in paper processing and textile industries

Background

Ganoderma leucocontextum is a medicinal mushroom species commonly called ‘Zanglingzhi’ or ‘White Lingzhi’ in China. It contains numerous pharmacological bioactive compounds important for therapeutic effects. The species has been limitedly investigated due to its scarceness worldwide. Laccase, an extracellular isozyme belonging to the oxidoreductase family, is an eco-friendly green catalyst with flexible substrate accommodation and valuable industrial applications.

Objective

The aim of this study was to investigate laccase production from Ganoderma leucocontextum for the first time, optimize its production conditions, purify and characterize the enzyme, and establish its phylogenetic relationship through ITS regions of DNA.

Results

The optimal conditions for laccase production were: temperature 40°C, pH 5.0, 7 days incubation, and 100 rpm agitation. Glucose and sucrose were effective carbon sources, while beef extract (10 g/L) and yeast extract enhanced laccase production. The purified laccase (Glacc110) had a molecular weight of 65.0 kDa, optimal activity at pH 3.0 and 70°C, and showed good thermostability. The enzyme retained >90% activity for 16 minutes at 60°C in acidic medium. The Km and Vmax values were 1.658 mM and 2.452 mM/min respectively.

Conclusion

This study reports the first successful purification and characterization of laccase from G. leucocontextum. The enzyme showed interesting properties including stability at higher temperatures and acidic pH, making it suitable for industrial and biotechnological applications. The thermostability of the laccase produced through submerged fermentation demonstrates significant potential for various industrial uses.
  • Published in:Scientific Reports,
  • Study Type:Laboratory Research,
  • Source: 10.1038/s41598-022-06111-z
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