ArticleExtremophiles : life under extreme conditions2018
A novel trifunctional, family GH10 enzyme from Acidothermus cellulolyticus 11B, exhibiting endo-xylanase, arabinofuranosidase and acetyl xylan esterase activities.
Article in Extremophiles : life under extreme conditions, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 28 citations in OpenAlex.
- Transcriptome sequencing of Bacillus sp. HMM and effect of GH gene overexpression on cellulase activities.Biotechnology letters · 2026Article
- Molecular cloning and characterization of a GH10 thermophilic xylanase from hot spring and its potential application in promoting probiotic growth.BMC biotechnology · 2026Article
- The Jarman-Bell principle revisited: Gut microbiota facilitate body size-dependent nutritional strategies in herbivores.Current research in microbial sciences · 2025Article
- Cloning, expression and characterization of a glycoside hydrolase family 51 α-l-arabinofuranosidase from3 Biotech · 2022Article
- The preparation technology and application of xylo-oligosaccharide as prebiotics in different fields: A review.Frontiers in nutrition · 2022Review
- Extremophiles, a Nifty Tool to Face Environmental Pollution: From Exploitation of Metabolism to Genome Engineering.International journal of environmental research and public health · 2021Review
- Xylan in the Middle: Understanding Xylan Biosynthesis and Its Metabolic Dependencies Toward Improving Wood Fiber for Industrial Processing.Frontiers in plant science · 2019Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A novel, family GH10 enzyme, Xyn10B from Acidothermus cellulolyticus 11B was cloned and expressed in Escherichia coli. This enzyme was purified to homogeneity by binding to regenerated amorphous cellulose. It had higher binding on Avicel as compared to insoluble xylan due to the presence of cellulose-binding domains, CBM3 and CBM2. This enzyme was optimally active at 70 °C and pH 6.0. It was stable up to 70 °C while the CD spectroscopy analysis showed thermal unfolding at 80 °C. Xyn10B was found to be a trifunctional enzyme having endo-xylanase, arabinofuranosidase and acetyl xylan esterase activities. Its activities against beechwood xylan, p-Nitrophenyl arabinofuranoside and p-Nitrophenyl acetate were found to be 126,480, 10,350 and 17,250 U μmol
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