{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["6(1)"],"submitter":["Shi H"],"pubmed_abstract":["<h4>Background</h4>β-Xylosidase is an important constituent of the hemicellulase system and it plays an important role in hydrolyzing xylooligosaccharides to xylose. Xylose, a useful monose, has been utilized in a wide range of applications such as food, light, chemical as well as energy industry. Therefore, the xylose-tolerant β-xylosidase with high specific activity for bioconversion of xylooligosaccharides has a great potential in the fields as above.<h4>Results</h4>A β-xylosidase gene (Tth xynB3) of 2,322 bp was cloned from the extremely thermophilic bacterium Thermotoga thermarum DSM 5069 that encodes a protein containing 774 amino acid residues, and was expressed in Escherichia coli BL21 (DE3). The phylogenetic trees of β-xylosidases were constructed using Neighbor-Joining (NJ) and M"],"journal":["Biotechnology for biofuels"],"pagination":["27"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3621209"],"repository":["biostudies-literature"],"pubmed_title":["Biochemical properties of a novel thermostable and highly xylose-tolerant β-xylosidase/α-arabinosidase from Thermotoga thermarum."],"pmcid":["PMC3621209"],"pubmed_authors":["Li X","Gu H","Huang Y","Zhang Y","Wang F","Shi H","Wang L"],"additional_accession":[]},"is_claimable":false,"name":"Biochemical properties of a novel thermostable and highly xylose-tolerant β-xylosidase/α-arabinosidase from Thermotoga thermarum.","description":"<h4>Background</h4>β-Xylosidase is an important constituent of the hemicellulase system and it plays an important role in hydrolyzing xylooligosaccharides to xylose. Xylose, a useful monose, has been utilized in a wide range of applications such as food, light, chemical as well as energy industry. Therefore, the xylose-tolerant β-xylosidase with high specific activity for bioconversion of xylooligosaccharides has a great potential in the fields as above.<h4>Results</h4>A β-xylosidase gene (Tth xynB3) of 2,322 bp was cloned from the extremely thermophilic bacterium Thermotoga thermarum DSM 5069 that encodes a protein containing 774 amino acid residues, and was expressed in Escherichia coli BL21 (DE3). The phylogenetic trees of β-xylosidases were constructed using Neighbor-Joining (NJ) and M","dates":{"release":"2013-01-01T00:00:00Z","publication":"2013 Feb","modification":"2025-04-19T15:19:53.822Z","creation":"2019-03-27T01:07:10Z"},"accession":"S-EPMC3621209","cross_references":{"pubmed":["23422003"],"doi":["10.1186/1754-6834-6-27"]}}