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

Zijia Lu, Carl Rämgård, İrem Ergenlioğlu, Lova Sandin, Hugo Hammar, Helena Andersson, Katharine King, Annie R. Inman, Mengshu Hao, Vincent Bulone, Lauren S. McKee

Research output: Contribution to journalArticlepeer-review

4 Citations (Scopus)
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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, β-1,3-glucan and β-1,6-glucan. While several fungal β-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 β-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 β-1,6-glucan pustulan and describe three distinct enzymes encoded by its genome, all of which show different levels of β-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 β-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.

Original languageEnglish
Pages (from-to)2909-2922
Number of pages14
JournalFEBS Journal
Issue number11
Early online date6 Jan 2023
Publication statusPublished - Jun 2023


  • carbohydrate-binding module
  • glycoside hydrolase
  • pustulan
  • β-1,3-glucanase
  • β-1,6-glucanase


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