ArticleBMC biotechnology2014
Expression and characterization of a GH43 endo-arabinanase from Thermotoga thermarum.
Article in BMC biotechnology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 29 citations in OpenAlex.
- Decoding dietary pectin: from structural complexity and microbial CAZyme-PUL networks to cross-feeding and host-beneficial metabolites.Gut microbes · 2026Review
- Exo- and Endo-1,5-α-L-Arabinanases and Prebiotic Arabino-Oligosaccharides Production.Journal of microbiology and biotechnology · 2025Review
- Review
- Functional annotation of rhizospheric phageome of the wild plant speciesFrontiers in microbiology · 2023Article
- Engineering Caldicellulosiruptor bescii with Surface Layer Homology Domain-Linked Glycoside Hydrolases Improves Plant Biomass Solubilization.Applied and environmental microbiology · 2022Article
- Proteome specialization of anaerobic fungi during ruminal degradation of recalcitrant plant fiber.The ISME journal · 2021Article
- Cultivation of Mushrooms and Their Lignocellulolytic Enzyme Production Through the Utilization of Agro-Industrial Waste.Molecules (Basel, Switzerland) · 2020Review
- Enzymatic Mechanism for Arabinan Degradation and Transport in the Thermophilic Bacterium Caldanaerobius polysaccharolyticus.Applied and environmental microbiology · 2017Article
- Discovery and characterization of family 39 glycoside hydrolases from rumen anaerobic fungi with polyspecific activity on rare arabinosyl substrates.The Journal of biological chemistry · 2017Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundArabinan is an important plant polysaccharide degraded mainly by two hydrolytic enzymes, endo-arabinanase and α-L-arabinofuranosidase. In this study, the characterization and application in arabinan degradation of an endo-arabinanase from Thermotoga thermarum were investigated.
resultsThe recombinant endo-arabinanase was expressed in Escherichia coli BL21 (DE3) and purified by heat treatment followed by purification on a nickel affinity column chromatography. The purified endo-arabinanase exhibited optimal activity at pH 6.5 and 75°C and its residual activity retained more than 80% of its initial activity after being incubated at 80°C for 2 h. The results showed that the endo-arabinanase was very effective for arabinan degradation at higher temperature. When linear arabinan was used as the substrate, the apparent K(m) and V(max) values were determined to be 12.3 ± 0.15 mg ml⁻¹ and 1,052.1 ± 12.7 μmol ml⁻¹ min⁻¹, respectively (at pH 6.5, 75°C), and the calculated kcat value was 349.3 ± 4.2 s⁻¹.
conclusionsThis work provides a useful endo-arabinanase with high thermostability andcatalytic efficiency, and these characteristics exhibit a great potential for enzymatic conversion of arabinan.
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