ArticleBiotechnology for biofuels2019
A novel thermostable GH10 xylanase with activities on a wide variety of cellulosic substrates from a xylanolytic
Article in Biotechnology for biofuels, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Targeted Preparation of Low-Degree Polymerization Xylooligosaccharides From Lignocellulosic Biomass: Advances, Structure-Activity Relationships, and Applications.Journal of food science · 2026Review
- A chemoproteomic biotechnological toolkit for resolving xylanase specificity in decorated xylan.Nature communications · 2026Article
- Molecular cloning and characterization of a GH10 thermophilic xylanase from hot spring and its potential application in promoting probiotic growth.BMC biotechnology · 2026Article
- Effective Degradation of Brewer Spent Grains by a Novel Thermostable GH10 Xylanase.Applied biochemistry and biotechnology · 2024Article
- Heteroxylan hydrolysis by a recombinant cellulase-free GH10 xylanase from the alkaliphilic bacterium Halalkalibacterium halodurans C-125.Archives of microbiology · 2024Article
- Alternative splicing analysis of lignocellulose-degrading enzyme genes and enzyme variants in Aspergillus niger.Applied microbiology and biotechnology · 2024Article
- Clustered surface amino acid residues modulate the acid stability of GH10 xylanase in fungi.Applied microbiology and biotechnology · 2024Article
- Article
- Gene cloning, expression, and characterization of two endo-xylanases fromFrontiers in microbiology · 2023Article
- Biochemical and Thermodynamic Studies on a Novel Thermotolerant GH10 Xylanase fromBiomolecules · 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
- Activity-based protein profiling reveals dynamic substrate-specific cellulase secretion by saprotrophic basidiomycetes.Biotechnology for biofuels and bioproducts · 2022Article
- ThermophilicFrontiers in microbiology · 2022Article
- A thermostable and CBM2-linked GH10 xylanase fromFrontiers in bioengineering and biotechnology · 2022Article
- Improvement of XYL10C_∆N catalytic performance through loop engineering for lignocellulosic biomass utilization in feed and fuel industries.Biotechnology for biofuels · 2021Article
- Phenotype Switching in Metal-Tolerant Bacteria Isolated from a Hyperaccumulator Plant.Biology · 2021Article
- Rational engineering of xylanase hyper-producing system in Trichoderma reesei for efficient biomass degradation.Biotechnology for biofuels · 2021Article
- Xylanolytic Bacillus species for xylooligosaccharides production: a critical review.Bioresources and bioprocessing · 2021Review
- Conversion of Wheat Bran to Xylanases and Dye Adsorbent byPolymers · 2021Article
- Extremophilic Prokaryotic Endoxylanases: Diversity, Applicability, and Molecular Insights.Frontiers in microbiology · 2021Review
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundCellulose and hemicellulose are the two largest components in lignocellulosic biomass. Enzymes with activities towards cellulose and xylan have attracted great interest in the bioconversion of lignocellulosic biomass, since they have potential in improving the hydrolytic performance and reducing the enzyme costs. Exploring glycoside hydrolases (GHs) with good thermostability and activities on xylan and cellulose would be beneficial to the industrial production of biofuels and bio-based chemicals.
resultsA novel GH10 enzyme (XynA) identified from a xylanolytic strain
conclusionsXynA is a novel thermostable GH10 xylanase with a wide substrate spectrum. It displays good stability in a broad range of pH and high temperatures, and exhibits activities towards xylans and a wide variety of cellulosic substrates, which are not found in other GH10 enzymes. The enzyme also has high capacity in saccharification of pretreated corn stover. These characteristics make XynA a good candidate not only for assisting cellulase in lignocellulosic biomass hydrolysis, but also for the research on structure-function relationship of bifunctional xylanase/cellulase.
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