ArticleApplied and environmental microbiology2000
Sequencing and expression of additional xylanase genes from the hyperthermophile Thermotoga maritima FjSS3B.1.
Article in Applied and environmental microbiology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
8 citing papers in PubMed.
- Thermophilic Degradation of Hemicellulose, a Critical Feedstock in the Production of Bioenergy and Other Value-Added Products.Applied and environmental microbiology · 2020Review
- Hyperthermostable Thermotoga maritima xylanase XYN10B shows high activity at high temperatures in the presence of biomass-dissolving hydrophilic ionic liquids.Extremophiles : life under extreme conditions · 2016Article
- Cloning, purification and characterization of an alkali-stable endoxylanase from thermophilic Geobacillus sp. 71.World journal of microbiology & biotechnology · 2012Article
- Characterization of a thermostable and alkaline xylanase from Bacillus sp. and its bleaching impact on wheat straw pulp.World journal of microbiology & biotechnology · 2012Article
- Thermostable enzymes as biocatalysts in the biofuel industry.Advances in applied microbiology · 2010Review
- Thermophilic bacterial DNA polymerases with reverse-transcriptase activity.Extremophiles : life under extreme conditions · 2004Article
- Characterization of a thermostable L-arabinose (D-galactose) isomerase from the hyperthermophilic eubacterium Thermotoga maritima.Applied and environmental microbiology · 2004Article
- Suppressive subtractive hybridization detects extensive genomic diversity in Thermotoga maritima.Journal of bacteriology · 2002Article
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Two genes, xynB and xynC, coding for xylanases were isolated from Thermotoga maritima FjSS3B.1 by a genomic-walking-PCR technique. Sequencing of the genes showed that they encode multidomain family 10 xylanases. Only XynB exhibited activity against xylan substrates. The temperature optimum (87 degrees C) and pH optimum (pH 6.5) of XynB are different from the previously reported xylanase, XynA (also a family 10 enzyme), from this organism. The catalytic domain expressed without other domains has a lower temperature optimum, is less thermostable, and has optimal activity at pH 6.5. Despite having a high level of sequence similarity to xynB, xynC appears to be nonfunctional since its encoded protein did not show significant activity on xylan substrates.
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