ArticleBiotechnology for biofuels2013
A novel highly thermostable xylanase stimulated by Ca2+ from Thermotoga thermarum: cloning, expression and characterization.
Article in Biotechnology for biofuels, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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28 citing papers in PubMed, 94 citations in OpenAlex.
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- Intracellular self-assembly and metabolite analysis of key enzymes for L-lysine synthesis based on key components of cellulosomes.Frontiers in microbiology · 2025Article
- Development of a RobustMicroorganisms · 2024Article
- Improvement of thermostability and catalytic efficiency of xylanase fromFrontiers in microbiology · 2024Article
- Review
- Endo-xylanases from Cohnella sp. AR92 aimed at xylan and arabinoxylan conversion into value-added products.Applied microbiology and biotechnology · 2021Article
- Role of extremophiles and their extremozymes in biorefinery process of lignocellulose degradation.Extremophiles : life under extreme conditions · 2021Review
- Phylogenetic, functional and structural characterization of a GH10 xylanase active at extreme conditions of temperature and alkalinity.Computational and structural biotechnology journal · 2021Article
- Extremophilic Prokaryotic Endoxylanases: Diversity, Applicability, and Molecular Insights.Frontiers in microbiology · 2021Review
- Characterization and functional analysis of two novel thermotolerant α-L-arabinofuranosidases belonging to glycoside hydrolase family 51 from Thielavia terrestris and family 62 from Eupenicillium parvum.Applied microbiology and biotechnology · 2020Article
- Tailoring Hydrothermal Vent Biodiversity Toward Improved Biodiscovery Using a NovelFrontiers in microbiology · 2020Article
- Xylanolytic Extremozymes Retrieved From Environmental Metagenomes: Characteristics, Genetic Engineering, and Applications.Frontiers in microbiology · 2020Review
- Heterologous expression and functional characterization of a GH10 endoxylanase fromBiotechnology reports (Amsterdam, Netherlands) · 2019Article
- The extracellular endo-β-1,4-xylanase with multidomain from the extreme thermophileBiotechnology for biofuels · 2019Article
- Thermostable Xylanase Production byMicroorganisms · 2018Article
- Effect of CBM1 and linker region on enzymatic properties of a novel thermostable dimeric GH10 xylanase (Xyn10A) from filamentous fungus Aspergillus fumigatus Z5.AMB Express · 2018Article
- Improved thermostability of an acidic xylanase from Aspergillus sulphureus by combined disulphide bridge introduction and proline residue substitution.Scientific reports · 2017Article
- Gene Expression and Molecular Characterization of a Xylanase from Chicken Cecum Metagenome.International journal of microbiology · 2017Article
- Metagenomics of Thermophiles with a Focus on Discovery of Novel Thermozymes.Frontiers in microbiology · 2016Review
- Overexpression and characterization of a Ca(2+) activated thermostable β-glucosidase with high ginsenoside Rb1 to ginsenoside 20(S)-Rg3 bioconversion productivity.Journal of industrial microbiology & biotechnology · 2015Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundXylanase is an important component of hemicellulase enzyme system. Since it plays an important role in the hydrolysis of hemicellulose into xylooligosaccharides (XOs), high thermostable xylanase has been the focus of much recent attention as powerful enzyme as well as in the field of biomass utilization.
resultsA xylanase gene (xyn10A) with 3,474 bp was cloned from the extremely thermophilic bacterium Thermotoga thermarum that encodes a protein containing 1,158 amino acid residues. Based on amino acid sequence homology, hydrophobic cluster and three dimensional structure analyses, it was attested that the xylanase belongs to the glycoside hydrolase (GH) families 10 with five carbohydrate binding domains. When the xylanase gene was cloned and expressed in Escherichia coli BL21 (DE3), the specific enzyme activity of xylanase produced by the recombinant strain was up to 145.8 U mg-1. The xylanase was optimally active at 95°C, pH 7.0. In addition, it exhibited high thermostability over broad range of pH 4.0-8.5 and temperature 55-90°C upon the addition of 5 mM Ca2+. Confirmed by Ion Chromatography System (ICS) analysis, the end products of the hydrolysis of beechwood xylan were xylose, xylobiose, xylotriose, xylotetraose, xylopentaose and xylohexaose.
conclusionsThe xylanase from T. thermarum is one of the hyperthermophilic xylanases that exhibits high thermostability, and thus, is a suitable candidate for generating XOs from cellulosic materials such as agricultural and forestry residues for the uses as prebiotics and precursors for further preparation of furfural and other chemicals.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.