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Research article - Peer-reviewed, 2023

Multiple enzymatic approaches to hydrolysis of fungal beta-glucans by the soil bacterium Chitinophaga pinensis

Lu, Zijia; Ramgard, Carl; Ergenlioglu, Irem; Sandin, Lova; Hammar, Hugo; Andersson, Helena; King, Katharine; Inman, Annie R.; Hao, Mengshu; Bulone, Vincent; McKee, Lauren S.

Abstract

The genome of the soil Bacteroidota Chitinophaga pinensis encodes a large number of glycoside hydrolases (GHs) with noteworthy features and potentially novel functions. Several are predicted to be active on polysaccharide components of fungal and oomycete cell walls, such as chitin, beta-1,3-glucan and beta-1,6-glucan. While several fungal beta-1,6-glucanase enzymes are known, relatively few bacterial examples have been characterised to date. We have previously demonstrated that C. pinensis shows strong growth using beta-1,6-glucan as the sole carbon source, with the efficient release of oligosaccharides from the polymer. We here characterise the capacity of the C. pinensis secretome to hydrolyse the beta-1,6-glucan pustulan and describe three distinct enzymes encoded by its genome, all of which show different levels of beta-1,6-glucanase activity and which are classified into different GH families. Our data show that C. pinensis has multiple tools to deconstruct pustulan, allowing the species' broad utility of this substrate, with potential implications for bacterial biocontrol of pathogens via cell wall disruption. Oligosaccharides derived from fungal beta-1,6-glucans are valuable in biomedical research and drug synthesis, and these enzymes could be useful tools for releasing such molecules from microbial biomass, an underexploited source of complex carbohydrates.

Keywords

beta-1,3-glucanase; beta-1,6-glucanase; carbohydrate-binding module; glycoside hydrolase; pustulan

Published in

The Febs Journal
2023, Volume: 290, number: 11, pages: 2909-2922
Publisher: WILEY

    UKÄ Subject classification

    Biochemistry and Molecular Biology

    Publication identifier

    DOI: https://doi.org/10.1111/febs.16720

    Permanent link to this page (URI)

    https://res.slu.se/id/publ/121518