ArticleApplied and environmental microbiology2013
Reconstitution of a thermostable xylan-degrading enzyme mixture from the bacterium Caldicellulosiruptor bescii.
Article in Applied and environmental microbiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- Characterization of the thermophilic xylanase Fsa02490Xyn from the hyperthermophile Fervidibacter sacchari belonging to glycoside hydrolase family 10.FEBS open bio · 2025Article
- Optimization of Fermentation Conditions for Enhanced Single Cell Protein Production byFoods (Basel, Switzerland) · 2025Article
- Biosynthesis of value-added bioproducts from hemicellulose of biomass through microbial metabolic engineering.Metabolic engineering communications · 2022Review
- Biochemical and Regulatory Analyses of Xylanolytic Regulons in Caldicellulosiruptor bescii Reveal Genus-Wide Features of Hemicellulose Utilization.Applied and environmental microbiology · 2022Article
- Caldicellulosiruptor bescii Adheres to Polysaccharides via a Type IV Pilin-Dependent Mechanism.Applied and environmental microbiology · 2020Article
- Thermophilic Degradation of Hemicellulose, a Critical Feedstock in the Production of Bioenergy and Other Value-Added Products.Applied and environmental microbiology · 2020Review
- Insights into Thermophilic Plant Biomass Hydrolysis fromMicroorganisms · 2020Review
- The biology and biotechnology of the genus Caldicellulosiruptor: recent developments in 'Caldi World'.Extremophiles : life under extreme conditions · 2020Review
- A novel thermostable GH10 xylanase with activities on a wide variety of cellulosic substrates from a xylanolyticBiotechnology for biofuels · 2019Article
- The diversity and specificity of the extracellular proteome in the cellulolytic bacteriumBiotechnology for biofuels · 2018Article
- Isolation of highly thermostable β-xylosidases from a hot spring soil microbial community using a metagenomic approach.DNA research : an international journal for rapid publication of reports on genes and genomes · 2017Article
- Insights into the roles of non-catalytic residues in the active site of a GH10 xylanase with activity on cellulose.The Journal of biological chemistry · 2017Article
- SGNH hydrolase-type esterase domain containing Cbes-AcXE2: a novel and thermostable acetyl xylan esterase from Caldicellulosiruptor bescii.Extremophiles : life under extreme conditions · 2017Article
- Oxidation of a non-phenolic lignin model compound by twoBiotechnology for biofuels · 2017Article
- Article
- Heterologous expression of family 10 xylanases from Acidothermus cellulolyticus enhances the exoproteome of Caldicellulosiruptor bescii and growth on xylan substrates.Biotechnology for biofuels · 2016Article
- The N-Terminal GH10 Domain of a Multimodular Protein from Caldicellulosiruptor bescii Is a Versatile Xylanase/β-Glucanase That Can Degrade Crystalline Cellulose.Applied and environmental microbiology · 2015Article
- Anaerobic thermophiles.Life (Basel, Switzerland) · 2014Review
- Biochemical characterization of two thermostable xylanolytic enzymes encoded by a gene cluster of Caldicellulosiruptor owensensis.PloS one · 2014Article
- Seven N-terminal residues of a thermophilic xylanase are sufficient to confer hyperthermostability on its mesophilic counterpart.PloS one · 2014Article
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Authors and funding
7 authors.
Funding
Abstract
Xylose, the major constituent of xylans, as well as the side chain sugars, such as arabinose, can be metabolized by engineered yeasts into ethanol. Therefore, xylan-degrading enzymes that efficiently hydrolyze xylans will add value to cellulases used in hydrolysis of plant cell wall polysaccharides for conversion to biofuels. Heterogeneous xylan is a complex substrate, and it requires multiple enzymes to release its constituent sugars. However, the components of xylan-degrading enzymes are often individually characterized, leading to a dearth of research that analyzes synergistic actions of the components of xylan-degrading enzymes. In the present report, six genes predicted to encode components of the xylan-degrading enzymes of the thermophilic bacterium Caldicellulosiruptor bescii were expressed in Escherichia coli, and the recombinant proteins were investigated as individual enzymes and also as a xylan-degrading enzyme cocktail. Most of the component enzymes of the xylan-degrading enzyme mixture had similar optimal pH (5.5 to ∼6.5) and temperature (75 to ∼90°C), and this facilitated their investigation as an enzyme cocktail for deconstruction of xylans. The core enzymes (two endoxylanases and a β-xylosidase) exhibited high turnover numbers during catalysis, with the two endoxylanases yielding estimated k(cat) values of ∼8,000 and ∼4,500 s(-1), respectively, on soluble wheat arabinoxylan. Addition of side chain-cleaving enzymes to the core enzymes increased depolymerization of a more complex model substrate, oat spelt xylan. The C. bescii xylan-degrading enzyme mixture effectively hydrolyzes xylan at 65 to 80°C and can serve as a basal mixture for deconstruction of xylans in bioenergy feedstock at high temperatures.
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