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Pell, G., Taylor, E.J., Gloster, T.M., Turkenburg, J.P., Fontes, C.M., Ferreira, L.M., Nagy, T., Clark, S.J., Davies, G.J. and Gilbert, H.J. (2004) The Mechanism by Which Family 10 Glycoside Hydrolase Bind Decorated Substrates. Journal of Biological Chemistry, 279, 9597-9605.
https://doi.org/10.1074/jbc.M312278200

has been cited by the following article:

• TITLE: Release of Arabinose from Wheat Insoluble Arabinoxylan by the Action of α-L-Arabinofuranosidase in Synergism with Endo-Xylanases

  AUTHORS: Dominic W. S. Wong, Sarah Batt

  KEYWORDS: α-L-Arabinofuranosidase, Mono-Substituted Xylopyranosyl Residuet, Di-Substituted Xylopyranosyl Unit, Arabinoxylan Arabinofuranohydrolase (AXH)

  JOURNAL NAME: Advances in Enzyme Research, Vol.11 No.4, December 29, 2023

  ABSTRACT: Wheat arabinoxylan (water-insoluble fraction) contains ~36% arabinose which may include both singly or doubly substitutions at C2/C3 of the Xylp units. α-L-Arabinofuranosidses (ABFs) of two GH families were analyzed for their respective activities on the hydrolysis of Xylp-Araf. BaABF (GH43) produced twice the yield of arabinose residues from the heteroxylan compared to AnABF (GH51) under the same reaction conditions. Two endo-xylanases (of GH10 and 11) also showed differential hydrolytic activities on the Xylp chain, with the GH10 XYN-ATM double the amount of reducing sugar yield (as xylose equivalent) than using the GH11 XYN-M3. When the ABF and XYN were combined in optimial ratios, a synergistic increase of 73.8% in arabinose yield was observed.