ArticleBiotechnology for biofuels2018
Insight into the functional roles of Glu175 in the hyperthermostable xylanase XYL10C-ΔN through structural analysis and site-saturation mutagenesis.
Article in Biotechnology for biofuels, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 28 citations in OpenAlex.
- Screening, Characterization and Comparison of Endoglucanases/Xylanases from Thermophilic Fungi: AInternational journal of molecular sciences · 2025Article
- Genomic insights into the phylogeny and biomass-degrading enzymes of rumen ciliates.The ISME journal · 2022Article
- The Emergence of New Catalytic Abilities in an Endoxylanase from Family GH10 by Removing an Intrinsically Disordered Region.International journal of molecular sciences · 2022Article
- Improvement of XYL10C_∆N catalytic performance through loop engineering for lignocellulosic biomass utilization in feed and fuel industries.Biotechnology for biofuels · 2021Article
- Extremophilic Prokaryotic Endoxylanases: Diversity, Applicability, and Molecular Insights.Frontiers in microbiology · 2021Review
- Improvement in catalytic activity and thermostability of a GH10 xylanase and its synergistic degradation of biomass with cellulase.Biotechnology for biofuels · 2019Article
- Biochemical characterization of a novel exo-oligoxylanase fromBiotechnology for biofuels · 2019Article
- A novel thermostable GH10 xylanase with activities on a wide variety of cellulosic substrates from a xylanolyticBiotechnology for biofuels · 2019Article
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Authors and funding
9 authors at 4 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
backgroundImproving the hydrolytic performance of hemicellulases to degrade lignocellulosic biomass is of considerable importance for second-generation biorefinery. Xylanase, as the crucial hemicellulase, must be thermostable and have high activity for its potential use in the bioethanol industry. To obtain excellent xylanase candidates, it is necessary to understand the structure-function relationships to provide a meaningful reference to improve the enzyme properties. This study aimed to investigate the catalytic mechanism of a highly active hyperthermophilic xylanase variant, XYL10C-ΔN, for hemicellulose degradation.
resultsBy removing the N-terminal 66 amino acids, the variant XYL10C-ΔN showed a 1.8-fold improvement in catalytic efficiency and could hydrolyze corn stover more efficiently in hydrolysis of corn stover; however, it retained similar thermostability to the wild-type XYL10C. Based on the crystal structures of XYL10C-ΔN and its complex with xylobiose, Glu175 located on loop 3 was found to be specific to GH10 xylanases and probably accounts for the excellent enzyme properties by interacting with Lys135 and Met137 on loop 2. Site-saturation mutagenesis confirmed that XYL10C-ΔN with glutamate acid at position 175 had the highest catalytic efficiency, specific activity, and the broadest pH-activity profile. The functional roles of Glu175 were also verified in the mutants of another two GH10 xylanases, XylE and XynE2, which showed increased catalytic efficiencies and wider pH-activity profiles.
conclusionsXYL10C-ΔN, with excellent thermostability, high catalytic efficiency, and great lignocellulose-degrading capability, is a valuable candidate xylanase for the biofuel industry. The mechanism underlying improved activity of XYN10C-ΔN was thus investigated through structural analysis and functional verification, and Glu175 was identified to play the key role in the improved catalytic efficiency. This study revealed the importance of a key residue (Glu175) in XYN10C-ΔN and provides a reference to modify GH10 xylanases for improved catalytic performance.
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