Laccases are multi-copper oxidases that use molecular oxygen as the electron acceptor to oxidize both phenolic and, indirectly also non-phenolic substrates by mechanisms involving radicals. Due to their eco-friendliness and broad substrate specificity, laccases span a wide range of biotechnological applications. Here we present research performed in EU Horizon 2020-project FALCON, Fuel and Chemicals from Lignin through Enzymatic and Chemical Conversion. FALCON aims to valorize this lignin waste stream by enzymatic and mild chemical conversion to produce fuels, such as low sulfur marine fuel, fuel additives and chemical building blocks. We have heterologously expressed laccase from the litter-degrading basidiomycete Coprinopsis cinerea (CcLcc9) in methylotrophic Pichia pastoris yeast. The recombinant CcLcc9 oxidized 2,6-dimethoxyphenol in neutral pH range and showed thermostability. The oxidation of non-phenolic compounds by CcLcc9 was tested with low molecular weight mediators, such as syringyl-type plant phenols, which have shown potential as natural co-oxidants for lignocellulosic materials. The results show that syringyl nitrile and methyl syringate efficiently mediate the oxidation of veratryl alcohol to veratraldehyde. In addition, in the presence of these mediators CcLcc9 is able to oxidize lignin fractionated from steam-exploded poplar wood by hot ethanol. The depolymerization of lignin by Cclcc9 enzyme combined with formic acid treatment harbors a great potential for the sustainable processes of circular economy and modern biorefineries.

Alkaline thermostable recombinant laccase from Coprinopsis cinerea uses syringyl-type phenols as mediators and effectively oxidizes lignin

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.