<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Torosian N</submitter><funding>NASA</funding><funding>National Aeronautics and Space Administration</funding><funding>U.S. Department of Energy &amp; Office of Science</funding><funding>National Science Foundation &amp; Directorate for Biological Sciences</funding><funding>National Science Foundation</funding><pagination>1629-1642</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC12485897</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>15(10)</volume><pubmed_abstract>Fervidibacter sacchari is an aerobic hyperthermophile belonging to the phylum Armatimonadota that degrades a variety of polysaccharides. Its genome encodes 117 enzymes with one or more annotated glycoside hydrolase (GH) domain, but the roles of these putative GHs in polysaccharide catabolism are poorly defined. Here, we describe one F. sacchari enzyme encoding a GH10 domain, Fsa02490Xyn, that was previously shown to be active on Miscanthus, oat β-glucan, and beech-wood xylan, with optimal activity at 90-100 °C. We show that Fsa02490Xyn is also active on birch-wood xylan and gellan gum. The pH range on beech-wood xylan was 4.5 to 9.5 (pH&lt;sub>opt&lt;/sub> 7.0-8.0). Fsa024940Xyn had a K&lt;sub>m&lt;/sub> of 2.375 mm, V&lt;sub>max&lt;/sub> of 1250 μm·min&lt;sup>-1&lt;/sup>, and k&lt;sub>cat&lt;/sub>/K&lt;sub>m&lt;/sub> of 1.2</pubmed_abstract><journal>FEBS open bio</journal><pubmed_title>Characterization of the thermophilic xylanase Fsa02490Xyn from the hyperthermophile Fervidibacter sacchari belonging to glycoside hydrolase family 10.</pubmed_title><pmcid>PMC12485897</pmcid><funding_grant_id>HRD‐1712523</funding_grant_id><funding_grant_id>DE-AC02-05CH11231</funding_grant_id><funding_grant_id>80NSSC20M0043</funding_grant_id><funding_grant_id>80NSSC21M0157</funding_grant_id><funding_grant_id>80NSSC17K0548</funding_grant_id><funding_grant_id>HRD-1712523</funding_grant_id><funding_grant_id>DBI REU 1757316</funding_grant_id><pubmed_authors>Mewalal R</pubmed_authors><pubmed_authors>Covington JK</pubmed_authors><pubmed_authors>Blaby IK</pubmed_authors><pubmed_authors>Nou NO</pubmed_authors><pubmed_authors>Torosian N</pubmed_authors><pubmed_authors>Hess M</pubmed_authors><pubmed_authors>Palmer M</pubmed_authors><pubmed_authors>Hedlund BP</pubmed_authors><pubmed_authors>Cook AM</pubmed_authors><pubmed_authors>Cheng JF</pubmed_authors><pubmed_authors>Harmon-Smith M</pubmed_authors></additional><is_claimable>false</is_claimable><name>Characterization of the thermophilic xylanase Fsa02490Xyn from the hyperthermophile Fervidibacter sacchari belonging to glycoside hydrolase family 10.</name><description>Fervidibacter sacchari is an aerobic hyperthermophile belonging to the phylum Armatimonadota that degrades a variety of polysaccharides. Its genome encodes 117 enzymes with one or more annotated glycoside hydrolase (GH) domain, but the roles of these putative GHs in polysaccharide catabolism are poorly defined. Here, we describe one F. sacchari enzyme encoding a GH10 domain, Fsa02490Xyn, that was previously shown to be active on Miscanthus, oat β-glucan, and beech-wood xylan, with optimal activity at 90-100 °C. We show that Fsa02490Xyn is also active on birch-wood xylan and gellan gum. The pH range on beech-wood xylan was 4.5 to 9.5 (pH&lt;sub>opt&lt;/sub> 7.0-8.0). Fsa024940Xyn had a K&lt;sub>m&lt;/sub> of 2.375 mm, V&lt;sub>max&lt;/sub> of 1250 μm·min&lt;sup>-1&lt;/sup>, and k&lt;sub>cat&lt;/sub>/K&lt;sub>m&lt;/sub> of 1.2</description><dates><release>2025-01-01T00:00:00Z</release><publication>2025 Oct</publication><modification>2026-06-04T00:22:47.741Z</modification><creation>2026-05-03T03:12:31.54Z</creation></dates><accession>S-EPMC12485897</accession><cross_references><pubmed>40880124</pubmed><doi>10.1002/2211-5463.70072</doi></cross_references></HashMap>