Enzymatic catalysis with selective cleavage of lignin bonds provides a sustainable option for lignin valorization. We present the first functionally characterized fungal intracellular β-etherase, Ds-GST1, from the wood-degrading white-rot basidiomycete Dichomitus squalens. It belongs to the glutathione-S-transferase superfamily and it selectively cleaves the β-O-4 aryl ether bond of a dimeric lignin model compound in a glutathione-dependent reaction. Ds-GST1 also demonstrates activity on polymeric synthetic lignin fractions, shown by a decrease in molecular weight distribution of the laccase-oxidized guaiacyl-DHP. In addition to a possible role of Ds-GST1 in intracellular catabolism of lignin-derived aromatic compounds, the cleavage of the most abundant linkages in lignin under mild reaction conditions makes this biocatalyst an attractive green alternative in biotechnological applications.

Selective cleavage of lignin β-O-4 aryl ether bond by β-etherase of the white-rot fungus Dichomitus squalens

2019 Spring National Meeting

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