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ARS Home » Pacific West Area » Albany, California » Western Regional Research Center » Bioproducts Research » Research » Publications at this Location » Publication #408764
Research Project: Zero Waste Agricultural Processing

Location: Bioproducts Research

Title: Release of arabinose from wheat insoluble arabinoxylan by the action of a-L-arabinofuranosidases in synergism with endo-xylanases

Author
item Batt-Throne, Sarah
item Wong, Dominic

Submitted to: Advances in Enzyme Research
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 12/26/2023
Publication Date: 12/29/2023
Citation: Batt Throne, S.B., Wong, D. 2023. Release of arabinose from wheat insoluble arabinoxylan by the action of a-L-arabinofuranosidases in synergism with endo-xylanases. Advances in Enzyme Research. 11,147-153. https://doi.org/10.4236/aer.2023.114007.
DOI: https://doi.org/10.4236/aer.2023.114007

Interpretive Summary: The structural complexity of biomass arises from its large fraction of heteroxylan, which comprises polysaccharides of '-1,4-xylopyranosyl (Xylp) backbone chain decorated with a variety of side groups. The key process in biomass degradation involves the cooperative interaction between the main chain enzymes and accessory enzymes targeting the cleavage of side group substitutions. This report describes the release of arabinose residues from wheat insoluble arabinoxylan by analyzing the activities of two families of a-L-arabinofuranosidase (on arabinose side groups) and two families of endo-xylanases (on the xylan main chain) and their cooperative interactions in enhancing the arabinose yield.

Technical Abstract: Wheat arabinoxylan (water-insoluble fraction) contains ~36% arabinose, which may include singly or doubly substitutions at C2/C3 of the Xylp units. -L-Arabinofuranosidases (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 different hydrolytic activities on the Xylp chain, with the GH10 XYN-ATM doubling 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.