New Enzyme from Reishi Mushroom Helps Clean and Detoxify Various Dyes

Jenn Hoskins
17th August, 2024

New Enzyme from Reishi Mushroom Helps Clean and Detoxify Various Dyes

Image Source: Natural Science News, 2024

Key Findings

  • Researchers from the Institute of Botany, Jiangsu Province, and Chinese Academy of Sciences studied the DyP enzyme GlDyP2 from the fungus Ganoderma lucidum
  • GlDyP2 can oxidize both phenolic and non-phenolic lignin components, crucial for effective lignin degradation
  • The enzyme also decolorizes and detoxifies various dyes, indicating potential for wastewater treatment and environmental pollution mitigation
The degradation of lignin, a complex and recalcitrant polymer found in lignocellulosic biomass, has significant implications for the production of renewable fuels and chemicals. Lignin's resistance to breakdown has been a major obstacle in utilizing this abundant biomass effectively. Traditional methods have focused on fungal enzymes, particularly heme peroxidases and laccases, to degrade lignin[2]. However, recent research has highlighted the potential of dye-decolorizing peroxidases (DyPs), a novel superfamily of heme peroxidases, in oxidizing stubborn compounds. In a recent study conducted by the Institute of Botany, Jiangsu Province, and Chinese Academy of Sciences, researchers explored the capabilities of a specific DyP enzyme, GlDyP2, from the fungus Ganoderma lucidum[1]. The GlDyP2 gene was successfully expressed in Escherichia coli, and the enzymatic properties of the recombinant GlDyP2 protein were thoroughly investigated. The study found that GlDyP2 could oxidize not only the typical peroxidase substrate ABTS but also two lignin substrates, guaiacol and 2,6-dimethoxy phenol (DMP). This is significant because it indicates that GlDyP2 can target both phenolic and non-phenolic components of lignin, a capability that is crucial for effective lignin degradation. The optimum pH and temperature for GlDyP2 activity were determined to be 4.0 and 35°C, respectively, with the enzyme showing stability in acidic environments and a T50 value of 51°C, indicating good thermal stability. Interestingly, the activity of GlDyP2 was inhibited by various metal ions and solvents, including Mg2+, Ni2+, Mn2+, ethanol, Cu2+, Zn2+, methanol, isopropyl alcohol, Na2EDTA·2H2O, Fe2+, and SDS. Despite these inhibitors, the kinetic analysis revealed that GlDyP2 exhibited the strongest affinity and catalytic efficiency towards guaiacol among the tested substrates. This suggests that GlDyP2 could be particularly effective in breaking down specific lignin compounds. The study also demonstrated the enzyme's ability to decolorize and detoxify a range of dyes, including Reactive Blue 19, Reactive Brilliant Blue X-BR, Reactive Black 5, Methyl Orange, Trypan Blue, and Malachite Green. This aligns with previous findings that DyPs from other fungi can degrade high redox potential dyes and lignin model compounds[3][4]. The ability to decolorize and detoxify dyes indicates that GlDyP2 could be valuable in wastewater treatment, addressing environmental pollution caused by dye effluents. Moreover, the findings build on earlier research that showed different DyPs have varying efficiencies and stability profiles. For example, DyPs from Auricularia auricula-judae and Bjerkandera adusta were stable at higher temperatures, whereas those from Marasmius scorodonius and Pleurotus ostreatus were more thermolabile[3]. The GlDyP2 enzyme's stability and efficiency in acidic conditions add to this understanding, suggesting that different DyPs could be tailored for specific industrial applications. The research also complements studies on laccases, another group of lignin-degrading enzymes. Laccases have shown high efficiency in decolorizing dyes and degrading lignin in the presence of redox mediators[5]. However, the unique properties of GlDyP2, particularly its strong affinity for guaiacol and its effective decolorization of multiple dyes, highlight its potential as a complementary tool in biotechnological applications. In conclusion, the study by the Institute of Botany, Jiangsu Province, and Chinese Academy of Sciences underscores the potential of GlDyP2 in lignin degradation and dye wastewater treatment. By expanding our understanding of DyPs and their capabilities, this research paves the way for more efficient and sustainable methods to utilize lignocellulosic biomass and mitigate environmental pollution.

BiotechBiochemMycology

References

Main Study

1) Heterologous expression and characterization of a dye-decolorizing peroxidase from Ganoderma lucidum, and its application in decolorization and detoxifization of different types of dyes.

Published 17th August, 2024

Journal: World journal of microbiology & biotechnology

Issue: Vol 40, Issue 10, Aug 2024

Related Studies

2) Insights into lignin degradation and its potential industrial applications.

https://doi.org/10.1016/B978-0-12-407679-2.00001-6

3) Comparative Cold Shock Expression and Characterization of Fungal Dye-Decolorizing Peroxidases.

https://doi.org/10.1007/s12010-016-2073-0

4) Characterization of a Dye-Decolorizing Peroxidase from Irpex lacteus Expressed in Escherichia coli: An Enzyme with Wide Substrate Specificity Able to Transform Lignosulfonates.

https://doi.org/10.3390/jof7050325

5) Efficient degradation and detoxification of structurally different dyes and mixed dyes by LAC-4 laccase purified from white-rot fungi Ganoderma lucidum.

https://doi.org/10.1016/j.ecoenv.2024.116450


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