{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Yang Y"],"funding":["National Natural Science Foundation of China"],"pagination":["1385329"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11039872"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["15"],"pubmed_abstract":["<h4>Introduction</h4>Extracting xylanase from thermophilic filamentous fungi is a feasible way to obtain xylanase with good thermal stability.<h4>Methods</h4>The transcriptomic data of <i>Myceliophthora thermophilic destructive</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.<h4>Results and discussion</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"],"journal":["Frontiers in microbiology"],"pubmed_title":["Improvement of thermostability and catalytic efficiency of xylanase from <i>Myceliophthora thermophilar</i> by N-terminal and C-terminal truncation."],"pmcid":["PMC11039872"],"funding_grant_id":["32001638","31972016"],"pubmed_authors":["Li W","Li X","Yang Y","Lu H","Wu Q","Zhang C","Wu Y"],"additional_accession":[]},"is_claimable":false,"name":"Improvement of thermostability and catalytic efficiency of xylanase from <i>Myceliophthora thermophilar</i> by N-terminal and C-terminal truncation.","description":"<h4>Introduction</h4>Extracting xylanase from thermophilic filamentous fungi is a feasible way to obtain xylanase with good thermal stability.<h4>Methods</h4>The transcriptomic data of <i>Myceliophthora thermophilic destructive</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.<h4>Results and discussion</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","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024","modification":"2026-05-26T11:10:24.837Z","creation":"2026-05-24T03:07:35.747Z"},"accession":"S-EPMC11039872","cross_references":{"pubmed":["38659990"],"doi":["10.3389/fmicb.2024.1385329"]}}