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King Oyster, Eryngii · 1999 · Research Support, Non U.S. Gov'T

High relevance

Heterologous expression of Pleurotus eryngii peroxidase confirms its ability to oxidize Mn(2+) and different aromatic substrates.

Pleurotus eryngii

Gut & microbiome
SpeciesKing Oyster, Eryngii
JournalApplied and environmental microbiology
Year1999

Key points

  • A versatile ligninolytic peroxidase has been cloned from Pleurotus eryngii and its allelic variant MnPL2 expressed in Aspergillus nidulans, with properties similar to those of the mature enzyme from P. eryngii
  • These include the ability to oxidize Mn(2+) and aromatic substrates, confirming that this is a new peroxidase type sharing catalytic properties of lignin peroxidase and manganese peroxidase

Metadata-grounded summary

Citation abstract

A versatile ligninolytic peroxidase has been cloned from Pleurotus eryngii and its allelic variant MnPL2 expressed in Aspergillus nidulans, with properties similar to those of the mature enzyme from P. eryngii. These include the ability to oxidize Mn(2+) and aromatic substrates, confirming that this is a new peroxidase type sharing catalytic properties of lignin peroxidase and manganese peroxidase.

Citation

Ruiz-Dueñas FJ, Martínez MJ, Martínez AT (1999). Heterologous expression of Pleurotus eryngii peroxidase confirms its ability to oxidize Mn(2+) and different aromatic substrates. Applied and environmental microbiology https://doi.org/10.1128/AEM.65.10.4705-4707.1999 PMID: 10508113

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