ArticlePloS one2019
Design, expression and functional characterization of a thermostable xylanase from Trichoderma reesei.
Article in PloS one, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 36 citations in OpenAlex.
- Biochemical Characterization of a GH11 Xylanase from Xylanase-Producing Trichoderma citrinoviride.Applied biochemistry and biotechnology · 2025Article
- Alteration of the Rhizosphere Microbiota and Growth Performance of Barley Infected withMicroorganisms · 2025Article
- Improved Enzymatic Properties of Chitosanase CsnMY002 fromInternational journal of molecular sciences · 2025Article
- Characterization and structural analysis of the endo-1,4-β-xylanase GH11 from the hemicellulose-degrading Thermoanaerobacterium saccharolyticum useful for lignocellulose saccharification.Scientific reports · 2023Article
- Characterization of a GH10 extremely thermophilic xylanase from the metagenome of hot spring for prebiotic production.Scientific reports · 2023Article
- Analyzing Current Trends and Possible Strategies to Improve Sucrose Isomerases' Thermostability.International journal of molecular sciences · 2023Review
- Thermostability improvement of sucrose isomerase PalI NX-5: a comprehensive strategy.Biotechnology letters · 2023Article
- Three Molecular Modification Strategies to Improve the Thermostability of Xylanase XynA fromFoods (Basel, Switzerland) · 2023Article
- Heterologous expression and characterization of two novel glucanases derived from sheep rumen microbiota.World journal of microbiology & biotechnology · 2022Article
- Uses and Abuses of the Atomic Displacement Parameters in Structural Biology.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Engineering mesophilic GH11 xylanase fromFrontiers in bioengineering and biotechnology · 2022Article
- Comparative transcriptomic analysis-based identification of the regulation of foreign proteins with different stabilities expressed inFrontiers in microbiology · 2022Article
- Extremophilic Prokaryotic Endoxylanases: Diversity, Applicability, and Molecular Insights.Frontiers in microbiology · 2021Review
- Computational design of noncanonical amino acid-based thioether staples at N/C-terminal domains of multi-modular pullulanase for thermostabilization in enzyme catalysis.Computational and structural biotechnology journal · 2021Article
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9 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Xylanases isolated from microorganisms such as the Trichoderma reesei have attracted considerable research interest because of their potential in various industrial applications. However, naturally isolated xylanases cannot withstand harsh conditions such as high temperature and basic pH. In this study, we performed structural analysis of the major T. reesei xylanase (Xyn2), and novel flexible regions of the enzyme were identified based on B-factor, a molecular dynamics (MD) parameter. To improve thermostability of the Xyn2, disulfide bonds were introduced into the unstable flexible region by using site-directed mutagenesis and two recombinant xylanases, XM1 (Xyn2Cys12-52) and XM2 (Xyn2Cys59-149) were successfully expressed in Pichia pastoris. Secreted recombinant Xyn2 was estimated by SDS-PAGE to be 24 kDa. Interestingly, the half-lives of XM1 and XM2 at 60°C were 2.5- and 1.8- fold higher, respectively than those of native Xyn2. The XM1 also exhibited improved pH stability and maintained more than 60% activity over pH values ranging from 2.0 to 10.0. However, the specific activity and catalytic efficiency of XM1 was decreased as compared to those of XM2 and native Xyn2. Our results will assist not only in elucidating of the interactions between protein structure and function, but also in rational target selection for improving the thermostability of enzymes.
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