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    Author(s): Mun Su Rhee; Neha Sawhney; Young Sik Kim; Hyun Jee Rhee; Jason C. Hurlbert; Franz J. St. John; Guang Nong; John D. Rice; James F. Preston
    Date: 2017
    Source: Applied Microbiology and Biotechnology. 101(4): 1465-1476.
    Publication Series: Scientific Journal (JRNL)
    Station: Forest Products Laboratory
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    Description

    Paenibacillus sp. JDR-2 (Pjdr2) has been studied as a model for development of bacterial biocatalysts for efficient processing of xylans, methylglucuronoxylan, and methylglucuronoarabinoxylan, the predominant hemicellulosic polysaccharides found in dicots and monocots, respectively. Pjdr2 produces a cell-associated GH10 endoxylanase (Xyn10A1) that catalyzes depolymerization of xylans to xylobiose, xylotriose, and methylglucuronoxylotriose with methylglucuronate-linked α-1,2 to the nonreducing terminal xylose. A GH10/GH67 xylan utilization regulon includes genes encoding an extracellular cell-associated Xyn10A1 endoxylanase and an intracellular GH67 α-glucuronidase active on methylglucuronoxylotriose generated by Xyn10A1 but without activity on methylglucuronoxylotetraose generated by a GH11 endoxylanase. The sequenced genome of Pjdr2 contains three paralogous genes potentially encoding GH115 α- glucuronidases found in certain bacteria and fungi. One of these, Pjdr2_5977, shows enhanced expression during growth on xylans along with Pjdr2_4664 encoding a GH11 endoxylanase. Here, we show that Pjdr2_5977 encodes a GH115 α-glucuronidase, Agu115A, with maximal activity on the aldouronate methylglucuronoxylotetraose selectively generated by a GH11 endoxylanase Xyn11 encoded by Pjdr2_4664. Growth of Pjdr2 on this methylglucuronoxylotetraose supports a process for Xyn11-mediated extracellular depolymerization of methylglucuronoxylan and Agu115A-mediated intracellular deglycosylation as an alternative to the GH10/GH67 system previously defined in this bacterium. A recombinantly expressed enzyme encoded by the Pjdr2 agu115A gene catalyzes removal of 4-O-methylglucuronate residues α-1,2 linked to internal xylose residues in oligoxylosides generated by GH11 and GH30 xylanases and releases methylglucuronate from polymeric methylglucuronoxylan. The GH115 α- glucuronidase from Pjdr2 extends the discovery of this activity to members of the phylum Firmicutes and contributes to a novel system for bioprocessing hemicelluloses.

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    Citation

    Rhee, Mun Su; Sawhney, Neha; Kim, Young Sik; Rhee, Hyun Jee; Hurlbert, Jason C.; St. John, Franz J.; Nong, Guang; Rice, John D.; Preston, James F. 2017. GH115 α-glucuronidase and GH11 xylanase from Paenibacillus sp. JDR-2: potential roles in processing glucuronoxylans. Applied Microbiology and Biotechnology. 101(4): 1465-1476.

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    Keywords

    Paenibacillus sp. JDR-2, xylans, GH11 endoxylanase, GH115 α-glucuronidase, biofuels and chemicals

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https://www.fs.usda.gov/treesearch/pubs/56756