Biochemical characterization of a glycoside hydrolase family 43 β-D-galactofuranosidase from the fungus Aspergillus niger

Gregory S. Bulmer, Fang Wei Yuen, Naimah Begum, Bethan S. Jones, Sabine L. Flitsch, Jolanda M. van Munster*

*Corresponding author for this work

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β-D-Galactofuranose (Galf) and its polysaccharides are found in bacteria, fungi and protozoa but do not occur in mammalian tissues, and thus represent a specific target for anti-pathogenic drugs. Understanding the enzymatic degradation of these polysaccharides is therefore of great interest, but the identity of fungal enzymes with exclusively galactofuranosidase activity has so far remained elusive. Here we describe the identification and characterization of a galactofuranosidase from the industrially important fungus Aspergillus niger. Analysis of glycoside hydrolase family 43 subfamily 34 (GH43_34) members via conserved unique peptide patterns and phylogeny, revealed the occurrence of distinct clusters and, by comparison with specificities of characterized bacterial members, suggested a basis for prediction of enzyme specificity. Using this rationale, in tandem with molecular docking, we identified a putative β-D-galactofuranosidase from A. niger which was recombinantly produced in Escherichia coli. The Galf-specific hydrolase, encoded by xynD demonstrates maximum activity at pH 5, 25 °C towards 4-nitrophenyl-β-galactofuranoside (pNP-β-Galf), with a K m of 17.9 ± 1.9 mM and V max of 70.6 ± 5.3 µM min −1. The characterization of this first fungal GH43 galactofuranosidase offers further molecular insight into the degradation of Galf-containing structures.

Original languageEnglish
Article number110170
JournalEnzyme and Microbial Technology
Early online date5 Dec 2022
Publication statusPrint publication - Mar 2023


  • Aspergillus
  • Galactofuranose
  • Galactofuranosidase
  • Glycobiology
  • Polysaccharide
  • Recombinant protein expression
  • XynD
  • Polysaccharides
  • Aspergillus niger
  • Substrate Specificity
  • Molecular Docking Simulation
  • Glycoside Hydrolases/metabolism


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