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Fungal glucuronoyl esterases: Genome mining based enzyme discovery and biochemical characterization

Adiphol Dilokpimol ¹´²     Miia R Mäkelä ¹‘²         Gabriella Cerullo²         Miaomiao Zhou³      Simona Varriale¹‘² Loknath Gidijala ¹´²     Joana L A Brás ¹‘²        Peter Jütten²         Alexander Piechot³      Raymond Verhaert¹‘²  Vincenza Faraco²         Kristiina S Hilden³      Ronald P de Vries


4-O-Methyl-d-glucuronic acid (MeGlcA) is a side-residue of glucuronoarabinoxylan and can form ester linkages to lignin, contributing significantly to the strength and rigidity of the plant cell wall. Glucuronoyl esterases (4-O-methyl-glucuronoyl methylesterases, GEs) can cleave this ester bond, and therefore may play a significant role as auxiliary enzymes in biomass saccharification for the production of biofuels and biochemicals. GEs belong to a relatively new family of carbohydrate esterases (CE15) in the CAZy database (, and so far around ten fungal GEs have been characterized. To explore additional GE enzymes, we used a genome mining strategy. BLAST analysis with characterized GEs against approximately 250 publicly accessible fungal genomes identified more than 150 putative fungal GEs, which were classified into eight phylogenetic sub-groups. To validate the genome mining strategy, 21 selected GEs from both ascomycete and basidiomycete fungi were heterologously produced in Pichia pastoris. Of these enzymes, 18 were active against benzyl d-glucuronate demonstrating the suitability of our genome mining strategy for enzyme discovery.

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