biostudies-literatureChorozian KHellenic Foundation for Research and InnovationMinistry of Science, Technological Development and Innovations of the Republic of Serbia27https://www.ebi.ac.uk/biostudies/studies/S-EPMC12949506biostudies-literatureUnknown19(1)<h4>Background</h4>Fungal AA9 lytic polysaccharide monooxygenases (LPMOs) play a central role in oxidative cellulose degradation and are key contributors to biomass conversion. While widely distributed in fungal genomes, many LPMOs remain uncharacterized, limiting our understanding of their functional diversity and biotechnological potential. Fusarium oxysporum, a genetically rich but underexplored species, contains several AA9 LPMOs. This study focuses on the characterization of one such enzyme named FoLPMO9A, demonstrating its role in lignocellulose degradation and its potential for cellulose-based material functionalization.<h4>Results</h4>The gene encoding FoLPMO9A was heterologously expressed in Pichia pastoris, and the produced recombinant protein was evaluated for its biochemical anBiotechnology for biofuels and bioproductsCharacterization of an AA9 LPMO from Fusarium oxysporum and its role in cellulose hydrolysis and functionalization.PMC12949506015795451-03-136/2025-03/200042Dimarogona MChorozian KKarnaouri ANikodinovic-Runic JPonjavic MTopakas EfalseCharacterization of an AA9 LPMO from Fusarium oxysporum and its role in cellulose hydrolysis and functionalization.<h4>Background</h4>Fungal AA9 lytic polysaccharide monooxygenases (LPMOs) play a central role in oxidative cellulose degradation and are key contributors to biomass conversion. While widely distributed in fungal genomes, many LPMOs remain uncharacterized, limiting our understanding of their functional diversity and biotechnological potential. Fusarium oxysporum, a genetically rich but underexplored species, contains several AA9 LPMOs. This study focuses on the characterization of one such enzyme named FoLPMO9A, demonstrating its role in lignocellulose degradation and its potential for cellulose-based material functionalization.<h4>Results</h4>The gene encoding FoLPMO9A was heterologously expressed in Pichia pastoris, and the produced recombinant protein was evaluated for its biochemical an2026-01-01T00:00:00Z2026 Jan2026-07-16T23:21:23.121Z2026-07-12T03:11:18.857ZS-EPMC129495064160668010.1186/s13068-026-02742-w