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Description of the First Fungal Dye-Decolorizing Peroxidase Oxidizing Manganese(II)

Summary

This research discovered and characterized a new type of enzyme from oyster mushroom that can break down tough chemical compounds and potentially help in industrial processes. The enzyme shows exceptional stability and versatility in its activities. Impacts on everyday life: – Could lead to more environmentally friendly methods for treating industrial dyes and wastewater – May help develop better processes for converting plant waste into useful products – Could contribute to development of new biocatalysts for various industrial applications – Advances our understanding of how mushrooms break down wood in nature – May lead to improved methods for recycling plant-based materials

Background

Dye-decolorizing peroxidases (DyPs) are a newly discovered family of enzymes that can oxidize various dye compounds. While several bacterial DyPs have been characterized, fungal DyPs remain less studied. The genome of Pleurotus ostreatus (oyster mushroom) contains multiple DyP genes, but their properties and functions are not well understood.

Objective

To identify, express, and characterize DyP enzymes from the P. ostreatus genome, particularly focusing on their ability to oxidize different substrates including manganese, and to understand their evolutionary relationships and potential roles in lignin degradation.

Results

Both enzymes efficiently oxidized anthraquinoid dyes and low redox-potential substrates, but only Pleos-DyP4 could oxidize the high redox-potential dye Reactive Black 5. Unexpectedly, both enzymes could oxidize Mn2+ to Mn3+, with Pleos-DyP4 showing activity comparable to manganese peroxidases. Pleos-DyP4 demonstrated high thermal stability (T50 = 73°C) and pH stability. Secretome analysis confirmed Pleos-DyP4 was secreted during growth on lignocellulosic substrates along with other peroxidases.

Conclusion

This study reveals the first fungal DyP capable of oxidizing Mn2+, with activity levels comparable to classic manganese-oxidizing peroxidases. The results suggest DyPs may play a role in lignin degradation through Mn3+ generation, particularly given that P. ostreatus expresses three different families of Mn2+-oxidizing peroxidases during lignocellulose breakdown.
  • Published in:Applied Microbiology and Biotechnology,
  • Study Type:Experimental Research,
  • Source: 10.1007/s00253-015-6665-3
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