<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Yang Y</submitter><funding>National Natural Science Foundation of China</funding><pagination>1385329</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC11039872</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>15</volume><pubmed_abstract>&lt;h4>Introduction&lt;/h4>Extracting xylanase from thermophilic filamentous fungi is a feasible way to obtain xylanase with good thermal stability.&lt;h4>Methods&lt;/h4>The transcriptomic data of &lt;i>Myceliophthora thermophilic destructive&lt;/i> ATCC42464 were differentially expressed and enriched. By comparing the sequences of Mtxylan2 and more than 10 xylanases, the N-terminal and C-terminal of Mtxylan2 were truncated, and three mutants 28N, 28C and 28NC were constructed.&lt;h4>Results and discussion&lt;/h4>GH11 xylan Mtxylan2 was identified by transcriptomic analysis, the specific enzyme activity of Mtxylan2 was 104.67 U/mg, and the optimal temperature was 65°C. Molecular modification of Mtxylan2 showed that the catalytic activity of the mutants was enhanced. Among them, the catalytic activity of 28C was i</pubmed_abstract><journal>Frontiers in microbiology</journal><pubmed_title>Improvement of thermostability and catalytic efficiency of xylanase from &lt;i>Myceliophthora thermophilar&lt;/i> by N-terminal and C-terminal truncation.</pubmed_title><pmcid>PMC11039872</pmcid><funding_grant_id>32001638</funding_grant_id><funding_grant_id>31972016</funding_grant_id><pubmed_authors>Li W</pubmed_authors><pubmed_authors>Li X</pubmed_authors><pubmed_authors>Yang Y</pubmed_authors><pubmed_authors>Lu H</pubmed_authors><pubmed_authors>Wu Q</pubmed_authors><pubmed_authors>Zhang C</pubmed_authors><pubmed_authors>Wu Y</pubmed_authors></additional><is_claimable>false</is_claimable><name>Improvement of thermostability and catalytic efficiency of xylanase from &lt;i>Myceliophthora thermophilar&lt;/i> by N-terminal and C-terminal truncation.</name><description>&lt;h4>Introduction&lt;/h4>Extracting xylanase from thermophilic filamentous fungi is a feasible way to obtain xylanase with good thermal stability.&lt;h4>Methods&lt;/h4>The transcriptomic data of &lt;i>Myceliophthora thermophilic destructive&lt;/i> ATCC42464 were differentially expressed and enriched. By comparing the sequences of Mtxylan2 and more than 10 xylanases, the N-terminal and C-terminal of Mtxylan2 were truncated, and three mutants 28N, 28C and 28NC were constructed.&lt;h4>Results and discussion&lt;/h4>GH11 xylan Mtxylan2 was identified by transcriptomic analysis, the specific enzyme activity of Mtxylan2 was 104.67 U/mg, and the optimal temperature was 65°C. Molecular modification of Mtxylan2 showed that the catalytic activity of the mutants was enhanced. Among them, the catalytic activity of 28C was i</description><dates><release>2024-01-01T00:00:00Z</release><publication>2024</publication><modification>2026-05-26T11:10:24.837Z</modification><creation>2026-05-24T03:07:35.747Z</creation></dates><accession>S-EPMC11039872</accession><cross_references><pubmed>38659990</pubmed><doi>10.3389/fmicb.2024.1385329</doi></cross_references></HashMap>