<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Zhuang J</submitter><funding>Hubei Provincial Department of Science and Technology</funding><pagination>3215</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC11989904</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>26(7)</volume><pubmed_abstract>This study investigates the biochemical properties of two xylanases, ZgXyn10A and CaXyn10B, which are members of the glycoside hydrolase family 10 (GH10) and originate from the marine Bacteroidetes species &lt;i>Zobellia galactanivorans&lt;/i> and &lt;i>Cellulophaga algicola&lt;/i>, respectively. Utilizing an auto-induction expression system in &lt;i>Escherichia coli&lt;/i>, high-purity recombinant forms of these enzymes were successfully produced. Biochemical assays revealed that ZgXyn10A and CaXyn10B exhibit optimal activities at 40 °C and 30 °C, respectively, and demonstrate a high sensitivity to temperature fluctuations. Unlike conventional low-temperature enzymes, these xylanases retain only a fraction of their maximal activity at lower temperatures. To gain deeper insights into the structural and func</pubmed_abstract><journal>International journal of molecular sciences</journal><pubmed_title>Loop Dynamics Mediate Thermal Adaptation of Two Xylanases from Marine Bacteria.</pubmed_title><pmcid>PMC11989904</pmcid><funding_grant_id>2024JDC050</funding_grant_id><pubmed_authors>Yang J</pubmed_authors><pubmed_authors>Zhang Y</pubmed_authors><pubmed_authors>Han Z</pubmed_authors><pubmed_authors>Wang Y</pubmed_authors><pubmed_authors>Zhuang J</pubmed_authors></additional><is_claimable>false</is_claimable><name>Loop Dynamics Mediate Thermal Adaptation of Two Xylanases from Marine Bacteria.</name><description>This study investigates the biochemical properties of two xylanases, ZgXyn10A and CaXyn10B, which are members of the glycoside hydrolase family 10 (GH10) and originate from the marine Bacteroidetes species &lt;i>Zobellia galactanivorans&lt;/i> and &lt;i>Cellulophaga algicola&lt;/i>, respectively. Utilizing an auto-induction expression system in &lt;i>Escherichia coli&lt;/i>, high-purity recombinant forms of these enzymes were successfully produced. Biochemical assays revealed that ZgXyn10A and CaXyn10B exhibit optimal activities at 40 °C and 30 °C, respectively, and demonstrate a high sensitivity to temperature fluctuations. Unlike conventional low-temperature enzymes, these xylanases retain only a fraction of their maximal activity at lower temperatures. To gain deeper insights into the structural and func</description><dates><release>2025-01-01T00:00:00Z</release><publication>2025 Mar</publication><modification>2026-04-08T19:01:12.332Z</modification><creation>2025-07-02T03:05:03.122Z</creation></dates><accession>S-EPMC11989904</accession><cross_references><pubmed>40244048</pubmed><doi>10.3390/ijms26073215</doi></cross_references></HashMap>