ArticleExtremophiles : life under extreme conditions2005
Hyperthermophilic alpha-L: -arabinofuranosidase from Thermotoga maritima MSB8: molecular cloning, gene expression, and characterization of the recombinant protein.
Article in Extremophiles : life under extreme conditions, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed, 40 citations in OpenAlex.
- Recombinant Production and Biochemical Characterization of Thermostable Arabinofuranosidase from Acidothermophilic Alicyclobacillus Acidocaldarius.The protein journal · 2023Article
- Structure and function characterization of the α-L-arabinofuranosidase from the white-rot fungus Trametes hirsuta.Applied microbiology and biotechnology · 2023Article
- Isolation of Saccharibacillus WB17 strain from wheat bran phyllosphere and genomic insight into the cellulolytic and hemicellulolytic complex of the Saccharibacillus genus.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2022Article
- Biochemical and Molecular Dynamics Study of a Novel GH 43 α-l-Arabinofuranosidase/β-Xylosidase FromFrontiers in bioengineering and biotechnology · 2022Article
- Complete Genome Sequence of Pedobacter sp. PAMC26386 and Their Low Temperature Application in Arabinose-containing Polysaccharides Degradation.Current microbiology · 2021Article
- Characterisation of three novel α-L-arabinofuranosidases from a compost metagenome.BMC biotechnology · 2019Article
- Enzymatic Mechanism for Arabinan Degradation and Transport in the Thermophilic Bacterium Caldanaerobius polysaccharolyticus.Applied and environmental microbiology · 2017Article
- Optimization of expression and properties of the recombinant acetohydroxyacid synthase of Thermotoga maritima.Data in brief · 2015Article
- Overexpression, purification and characterisation of homologous α-L-arabinofuranosidase and endo-1,4-β-D-glucanase in Aspergillus vadensis.Journal of industrial microbiology & biotechnology · 2014Article
- 6-pyruvoyltetrahydropterin synthase paralogs replace the folate synthesis enzyme dihydroneopterin aldolase in diverse bacteria.Journal of bacteriology · 2009Article
- Alpha-L-arabinofuranosidases: the potential applications in biotechnology.Journal of industrial microbiology & biotechnology · 2006Review
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1 author at 1 institution in 1 country.
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Abstract
A putative alpha-L: -arabinofuranosidase (AFase) gene belonging to family 51 of glycosyl hydrolases of a hyperthermophilic bacterium Thermotoga maritima MSB8 was cloned, sequenced, and overexpressed in Escherichia coli. The recombinant protein (Tm-AFase) was purified to apparent homogeneity by heat treatment (80 degrees C, 30 min), followed by hydrophobic interaction, anion-exchange, and gel permeation column chromatography. Tm-AFase had a molecular mass of 55,284 Da on matrix assisted laser desorption ionization time-of-flight mass spectrometry and approximately 332 kDa on gel permeation column chromatography. Therefore, Tm-AFase comprised six identical subunits as in the case of homologous AFase from Geobacillus stearothermophilus. Regarding substrate specificity, Tm-AFase was active with p-nitrophenyl alpha-L: -arabinofuranoside but not with p-nitrophenyl alpha-L: -arabinopyranoside. Regarding polysaccharides, Tm-AFase hydrolyzed arabinan and debranched arabinan but not arabinoxylan, arabinogalactan, and carboxymethyl cellulose. Tm-AFase was extremely thermophilic, displaying an optimal reaction temperature of 90 degrees C in a 10 min assay. When Tm-AFase was heated at 90 degrees C, no loss of activity was observed for at least 24 h. At 100 degrees C, the activity dropped to approximately 50% in 20 min; thereafter, inactivation occurred very slowly exhibiting a half-life of approximately 2.7 h, characterizing the enzyme to be the most thermophilic AFase reported thus far.
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