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      Discovery of a bifunctional xylanolytic enzyme with arabinoxylan arabinofuranohydrolase‐d3 and endo‐xylanase activities and its application in the hydrolysis of cereal arabinoxylans

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          Abstract

          Xylanolytic enzymes, with both endo‐xylanase and arabinoxylan arabinofuranohydrolase (AXH) activities, are attractive for the economically feasible conversion of recalcitrant arabinoxylan. However, their characterization and utilization of these enzymes in biotechnological applications have been limited. Here, we characterize a novel bifunctional enzyme, rAbf43A, cloned from a bacterial consortium that exhibits AXH and endo‐xylanase activities. Hydrolytic pattern analyses revealed that the AXH activity belongs to AXHd3 because it attacked only the C(O)‐3‐linked arabinofuranosyl residues of double‐substituted xylopyranosyl units of arabinoxylan and arabinoxylan‐derived oligosaccharides, which are usually resistant to hydrolysis. The enzyme rAbf43A also liberated a series of xylo‐oligosaccharides (XOSs) from beechwood xylan, xylohexaose and xylopentaose, indicating that rAbf43A exhibited endo‐xylanase activity. Homology modelling based on AlphaFold2 and site‐directed mutagenesis identified three non‐catalytic residues (H161, A270 and L505) located in the substrate‐binding pocket essential for its dual‐functionality, while the mutation of A117 located in the −1 subsite to the proline residue only affected its endo‐xylanase activity. Additionally, rAbf43A showed significant synergistic action with the bifunctional xylanase/feruloyl esterase rXyn10A/Fae1A from the same bacterial consortium on insoluble wheat arabinoxylan and de‐starched wheat bran degradation. When rXyn10A/Fae1A was added to the rAbf43A pre‐hydrolyzed reactions, the amount of released reducing sugars, xylose and ferulic acid increased by 9.43% and 25.16%, 189.37% and 93.54%, 31.39% and 32.30%, respectively, in comparison with the sum of hydrolysis products released by each enzyme alone. The unique characteristics of rAbf43A position it as a promising candidate not only for designing high‐performance enzyme cocktails but also for investigating the structure–function relationship of GH43 multifunctional enzymes.

          Abstract

          1. A novel bifunctional xylanolytic enzyme (rAbf43A) was obtained.2. rAbf43A exhibits arabinoxylan arabinofuranohydrolase‐d3 and endo‐xylanase activities.3. rAbf43A shows obvious synergy with cognate bifunctional xylanase/feruloyl esterase.

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          Glycan complexity dictates microbial resource allocation in the large intestine

          The structure of the human gut microbiota is controlled primarily through the degradation of complex dietary carbohydrates, but the extent to which carbohydrate breakdown products are shared between members of the microbiota is unclear. We show here, using xylan as a model, that sharing the breakdown products of complex carbohydrates by key members of the microbiota, such as Bacteroides ovatus, is dependent on the complexity of the target glycan. Characterization of the extensive xylan degrading apparatus expressed by B. ovatus reveals that the breakdown of the polysaccharide by the human gut microbiota is significantly more complex than previous models suggested, which were based on the deconstruction of xylans containing limited monosaccharide side chains. Our report presents a highly complex and dynamic xylan degrading apparatus that is fine-tuned to recognize the different forms of the polysaccharide presented to the human gut microbiota.
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            Towards enzymatic breakdown of complex plant xylan structures: State of the art.

            Significant progress over the past few years has been achieved in the enzymology of microbial degradation and saccharification of plant xylan, after cellulose being the most abundant natural renewable polysaccharide. Several new types of xylan depolymerizing and debranching enzymes have been described in microorganisms. Despite the increasing variety of known glycoside hydrolases and carbohydrate esterases, some xylan structures still appear quite recalcitrant. This review focuses on the mode of action of different types of depolymerizing endoxylanases and their cooperation with β-xylosidase and accessory enzymes in breakdown of complex highly branched xylan structures. Emphasis is placed on the enzymatic hydrolysis of alkali-extracted deesterified polysaccharide as well as acetylated xylan isolated from plant cell walls under non-alkaline conditions. It is also shown how the combination of selected endoxylanases and debranching enzymes can determine the nature of prebiotic xylooligosaccharides or lead to complete hydrolysis of the polysaccharide. The article also highlights the possibility for discovery of novel xylanolytic enzymes, construction of multifunctional chimeric enzymes and xylanosomes in parallel with increasing knowledge on the fine structure of the polysaccharide.
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              Bio-based products from xylan: A review

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                Author and article information

                Contributors
                hlyuan@cau.edu.cn
                Journal
                Microb Biotechnol
                Microb Biotechnol
                10.1111/(ISSN)1751-7915
                MBT2
                Microbial Biotechnology
                John Wiley and Sons Inc. (Hoboken )
                1751-7915
                25 April 2023
                July 2023
                : 16
                : 7 ( doiID: 10.1111/mbt2.v16.7 )
                : 1536-1547
                Affiliations
                [ 1 ] State Key Laboratory of Animal Biotech Breeding, College of Biological Sciences China Agricultural University Beijing China
                [ 2 ] College of Life Science Luoyang Normal University Luoyang China
                Author notes
                [*] [* ] Correspondence

                Hongli Yuan, State Key Laboratory of Animal Biotech Breeding, College of Biological Sciences, China Agricultural University, Beijing, China.

                Email: hlyuan@ 123456cau.edu.cn

                Author information
                https://orcid.org/0000-0003-0307-7065
                https://orcid.org/0000-0001-5218-0523
                Article
                MBT214267 MICROBIO-2023-132-RA.R1
                10.1111/1751-7915.14267
                10281360
                37096984
                83c15b8f-beec-415b-b4f1-dc7e1c082d40
                © 2023 The Authors. Microbial Biotechnology published by Applied Microbiology International and John Wiley & Sons Ltd.

                This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc-nd/4.0/ License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non‐commercial and no modifications or adaptations are made.

                History
                : 11 April 2023
                : 04 February 2023
                : 13 April 2023
                Page count
                Figures: 6, Tables: 0, Pages: 12, Words: 6998
                Funding
                Funded by: the Henan Province Science and Technology Breakthrough Project
                Award ID: 222102320318
                Funded by: the National Key Research and Development Program of China
                Award ID: 2022YFA0912103
                Categories
                Research Article
                Research Articles
                Custom metadata
                2.0
                July 2023
                Converter:WILEY_ML3GV2_TO_JATSPMC version:6.2.9 mode:remove_FC converted:20.06.2023

                Biotechnology
                Biotechnology

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