ArticleCommunications biology2021
A plant host, Nicotiana benthamiana, enables the production and study of fungal lignin-degrading enzymes.
Article in Communications biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 15 citations in OpenAlex.
- Iron-induced demethoxylation of lignin as an important source for methanol and its oxidation products in the environment.Nature communications · 2026Article
- Biodegradation and detoxification of malachite green dye by crude manganese peroxidase produced by Pseudomonas aeruginosa MF14446.1 and Enterobacter roggenkampii CP033800.1.Scientific reports · 2025Article
- Metabolic engineering inaBIOTECH · 2025Review
- ARTP Mutagenesis ofJournal of microbiology and biotechnology · 2025Article
- Industrial applications of Phanerochaete chrysosporium lignin-degrading enzymes: current status, production challenges, and future directions.World journal of microbiology & biotechnology · 2025Review
- Looking into the world's largest elephant population in search of ligninolytic microorganisms for biorefineries: a mini-review.Biotechnology for biofuels and bioproducts · 2022Review
- Could termites be hiding a goldmine of obscure yet promising yeasts for energy crisis solutions based on aromatic wastes? A critical state-of-the-art review.Biotechnology for biofuels and bioproducts · 2022Review
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
Lignin has significant potential as an abundant and renewable source for commodity chemicals yet remains vastly underutilized. Efforts towards engineering a biochemical route to the valorization of lignin are currently limited by the lack of a suitable heterologous host for the production of lignin-degrading enzymes. Here, we show that expression of fungal genes in Nicotiana benthamiana enables production of members from seven major classes of enzymes associated with lignin degradation (23 of 35 tested) in soluble form for direct use in lignin activity assays. We combinatorially characterized a subset of these enzymes in the context of model lignin dimer oxidation, revealing that fine-tuned coupling of peroxide-generators to peroxidases results in more extensive C-C bond cleavage compared to direct addition of peroxide. Comparison of peroxidase isoform activity revealed that the extent of C-C bond cleavage depends on peroxidase identity, suggesting that peroxidases are individually specialized in the context of lignin oxidation. We anticipate the use of N. benthamiana as a platform to rapidly produce a diverse array of fungal lignin-degrading enzymes will facilitate a better understanding of their concerted role in nature and unlock their potential for lignin valorization, including within the plant host itself.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.