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Because there is some controversy concerning the ligninolytic enzymes produced byPleurotus species, ethylene release from α-keto-γ-thiomethylbutyric acid (KTBA), as described previously forPhanerochaete chrysosporium lignin peroxidase (LiP), was used to assess the oxidative power ofPleurotus eryngii cultures and extracellular proteins. Lignin model dimers were used to confirm the ligninolytic capabilities of enzymes isolated from liquid and solid-state fermentation (SSF) cultures. Three proteins that oxidized KTBA in the presence of veratryl alcohol and H2 O2 were identified (two proteins were found in liquid cultures, and one protein was found in SSF cultures). These proteins are versatile peroxidases that act on Mn2+ , as well as on simple phenols and veratryl alcohol. The two peroxidases obtained from the liquid culture were able to degrade a nonphenolic β-O-4 dimer, yielding veratraldehyde, as well as a phenolic dimer which is not efficiently oxidized byP. chrysosporium peroxidases. The former reaction is characteristic of LiP. The third KTBA-oxidizing peroxidase oxidized only the phenolic dimer (in the presence of Mn2+ ). Finally, a fourth Mn2+ -oxidizing peroxidase was identified in the SSF cultures on the basis of its ability to oxidize KTBA in the presence of Mn2+ . This enzyme is related to the Mn-dependent peroxidase ofP. chrysosporium because it did not exhibit activity with veratryl alcohol and Mn-independent activity with dimers. These results show thatP. eryngii produces three types of peroxidases that have the ability to oxidize lignin but lacks a typical LiP. Similar enzymes (in terms of N-terminal sequence and catalytic properties) are produced by otherPleurotus species. Some structural aspects ofP. eryngii peroxidases related to the catalytic properties are discussed.

A Search for Ligninolytic Peroxidases in the Fungus Pleurotus eryngii Involving α-Keto-γ-Thiomethylbutyric Acid and Lignin Model Dimers