ArticleBiotechnology for biofuels and bioproducts2023
Functional characterization of fungal lytic polysaccharide monooxygenases for cellulose surface oxidation.
Article in Biotechnology for biofuels and bioproducts, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Who cites it
6 citing papers in PubMed.
- Review
- Characterization of an AA9 LPMO from Fusarium oxysporum and its role in cellulose hydrolysis and functionalization.Biotechnology for biofuels and bioproducts · 2026Article
- Carboxylation of lyocell fabrics using C-1 lytic polysaccharide monooxygenases (Cellulose (London, England) · 2026Article
- Enzymatic functionalization of bacterial nanocellulose: current approaches and future prospects.Journal of nanobiotechnology · 2025Review
- LPMO-Catalyzed Oxidation of Cellulosic Fibers with Controlled Addition of a Reductant and HACS sustainable chemistry & engineering · 2025Article
- The impact of the carbohydrate-binding module on how a lytic polysaccharide monooxygenase modifies cellulose fibers.Biotechnology for biofuels and bioproducts · 2024Article
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
backgroundMicrobial lytic polysaccharide monooxygenases (LPMOs) cleave diverse biomass polysaccharides, including cellulose and hemicelluloses, by initial oxidation at C1 or C4 of glycan chains. Within the Carbohydrate-Active Enzymes (CAZy) classification, Auxiliary Activity Family 9 (AA9) comprises the first and largest group of fungal LPMOs, which are often also found in tandem with non-catalytic carbohydrate-binding modules (CBMs). LPMOs originally attracted attention for their ability to potentiate complete biomass deconstruction to monosaccharides. More recently, LPMOs have been applied for selective surface modification of insoluble cellulose and chitin.
resultsTo further explore the catalytic diversity of AA9 LPMOs, over 17,000 sequences were extracted from public databases, filtered, and used to construct a sequence similarity network (SSN) comprising 33 phylogenetically supported clusters. From these, 32 targets were produced successfully in the industrial filamentous fungus Aspergillus niger, 25 of which produced detectable LPMO activity. Detailed biochemical characterization of the eight most highly produced targets revealed individual C1, C4, and mixed C1/C4 regiospecificities of cellulose surface oxidation, different redox co-substrate preferences, and CBM targeting effects. Specifically, the presence of a CBM correlated with increased formation of soluble oxidized products and a more localized pattern of surface oxidation, as indicated by carbonyl-specific fluorescent labeling. On the other hand, LPMOs without native CBMs were associated with minimal release of soluble products and comparatively dispersed oxidation pattern.
conclusionsThis work provides insight into the structural and functional diversity of LPMOs, and highlights the need for further detailed characterization of individual enzymes to identify those best suited for cellulose saccharification versus surface functionalization toward biomaterials applications.
Identifiers
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Registered trials
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