ArticleFrontiers in microbiology2024
Improvement of thermostability and catalytic efficiency of xylanase from
Article in Frontiers in microbiology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed, 15 citations in OpenAlex.
- Review of Xylanases: Sources, Engineering and Biotechnological Use.Microorganisms · 2026Review
- Exploring black soil microbiota for industrial enzymes: cellulase and xylanase characterization from Bacillus subtilis SSMK413.Microbial cell factories · 2025Article
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7 authors at 2 institutions in 1 country.
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Abstract
Introduction: Extracting xylanase from thermophilic filamentous fungi is a feasible way to obtain xylanase with good thermal stability. Methods: The transcriptomic data of Results and discussion: 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 increased by 9.3 times, the optimal temperature was increased by 5°C, and the residual enzyme activity remained above 80% after 30 min at 50-65°C, indicating that redundant C-terminal truncation can improve the thermal stability and catalytic performance of GH11 xylanase.
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