A multi-omics approach to lignocellulolytic enzyme discovery reveals a new ligninase activity from Parascedosporium putredinis NO1
N.C. Oates et al. "A multi-omics approach to lignocellulolytic enzyme discovery reveals a new ligninase activity from Parascedosporium putredinis NO1" PNAS 118,18 (2021) [DOI:10.1073/pnas.2008888118]
Lignocellulose, in the form of crop residues, presents an attractive alternative to crude oil for both the production of renewable fuels and chemicals. Its large-scale application as a feedstock, however, remains limited. A bottleneck in its implementation is the presence of lignin that envelopes the structure, physically blocking access to sugar-rich polymers that lie beneath. Here, we describe the isolation of an exceptional lignocellulose-degrading fungus that produces new oxidase activity with no cofactor requirements. This enzyme cleaves β-ether units in lignin-releasing tricin, a flavonoid of pharmaceutical potential, from the lignin macromolecule. Furthermore, we demonstrate that treatments with this enzyme can increase the digestibility of lignocellulosic biomass, offering the possibility of producing a valuable product from lignin while decreasing processing costs.
Metaproteomic and metatranscriptomic databases generated during this research are available at MassIVE MSV000084758 and ProteomeXchange PXD016952. A curated dataset, which includes annotations, is available in the Dataset S1. Amplicon sequences are deposited at the European Nucleotide Archive under the accession PRJEB38167.