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

View ORCID ProfileGregory S. Bulmer, View ORCID ProfileFang Wei Yuen, View ORCID ProfileNaimah Begum, View ORCID ProfileBethan S. Jones, View ORCID ProfileSabine L. Flitsch, View ORCID ProfileJolanda M. van Munster
doi: https://doi.org/10.1101/2021.10.27.466152
Gregory S. Bulmer
1Manchester Institute of Biotechnology (MIB) & School of Natural Sciences, The University of Manchester, 131 Princess Street, Manchester, M1 7DN, United Kingdom
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Fang Wei Yuen
1Manchester Institute of Biotechnology (MIB) & School of Natural Sciences, The University of Manchester, 131 Princess Street, Manchester, M1 7DN, United Kingdom
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Naimah Begum
1Manchester Institute of Biotechnology (MIB) & School of Natural Sciences, The University of Manchester, 131 Princess Street, Manchester, M1 7DN, United Kingdom
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Bethan S. Jones
1Manchester Institute of Biotechnology (MIB) & School of Natural Sciences, The University of Manchester, 131 Princess Street, Manchester, M1 7DN, United Kingdom
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Sabine L. Flitsch
1Manchester Institute of Biotechnology (MIB) & School of Natural Sciences, The University of Manchester, 131 Princess Street, Manchester, M1 7DN, United Kingdom
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Jolanda M. van Munster
1Manchester Institute of Biotechnology (MIB) & School of Natural Sciences, The University of Manchester, 131 Princess Street, Manchester, M1 7DN, United Kingdom
2Scotland’s Rural College, West Mains Road, King’s Buildings, Edinburgh, EH9 3JG, United Kingdom
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  • For correspondence: jolanda.van-munster@sruc.ac.uk
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Abstract

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. Phylogenetic analysis of glycoside hydrolase family 43 subfamily 34 (GH43_34) members revealed the occurrence of three 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 expressed 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 Km of 17.9 ± 1.9 mM and Vmax of 70.6 ± 5.3 μmol min−1. The characterization of this first fungal GH43 galactofuranosidase offers further molecular insight into the degradation of Galf-containing structures and may inform clinical treatments against fungal pathogens.

Competing Interest Statement

The authors have declared no competing interest.

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The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY 4.0 International license.
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Posted October 27, 2021.
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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
bioRxiv 2021.10.27.466152; doi: https://doi.org/10.1101/2021.10.27.466152
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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
bioRxiv 2021.10.27.466152; doi: https://doi.org/10.1101/2021.10.27.466152

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