ArticleExtremophiles : life under extreme conditions2014
Cloning, expression and characterization of a novel cold-active and halophilic xylanase from Zunongwangia profunda.
Article in Extremophiles : life under extreme conditions, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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20 citing papers in PubMed, 65 citations in OpenAlex.
- Utilization of sugarcane bagasse waste by Aspergillus welwitchiae SVUAw9 for production, purification, and characterization of cold-active xylanase under solid-state fermentation conditions.Microbial cell factories · 2026Article
- Molecular Identification and Engineering a Salt-Tolerant GH11 Xylanase for Efficient Xylooligosaccharides Production.Biomolecules · 2024Article
- Functional characterisation of a new halotolerant seawater active glycoside hydrolase family 6 cellobiohydrolase from a salt marsh.Scientific reports · 2024Article
- Metagenomic psychrohalophilic xylanase from camel rumen investigated for bioethanol production from wheat bran using Bacillus subtilis AP.Scientific reports · 2022Article
- Biotechnological potential of psychrophilic microorganisms as the source of cold-active enzymes in food processing applications.3 Biotech · 2021Review
- Identification and Characterization of a Novel, Cold-Adapted d-Xylobiose- and d-Xylose-Releasing Endo-β-1,4-xylanase from an Antarctic Soil Bacterium,Biomolecules · 2021Article
- Extremophilic Prokaryotic Endoxylanases: Diversity, Applicability, and Molecular Insights.Frontiers in microbiology · 2021Review
- Xylanase from Marine Filamentous FungusJournal of applied glycoscience · 2021Article
- Isolation and Characterization of a Novel Cold-Active, Halotolerant Endoxylanase fromMarine drugs · 2020Article
- Properties and Applications of Extremozymes from Deep-Sea Extremophilic Microorganisms: A Mini Review.Marine drugs · 2019Review
- An extreme halophilic xylanase from camel rumen metagenome with elevated catalytic activity in high salt concentrations.AMB Express · 2019Article
- Characterizing a Halo-Tolerant GH10 Xylanase fromInternational journal of molecular sciences · 2019Article
- Characterization of a novel cold-active xylanase from Luteimonas species.World journal of microbiology & biotechnology · 2018Article
- Distinctive molecular and biochemical characteristics of a glycoside hydrolase family 20 β-N-acetylglucosaminidase and salt tolerance.BMC biotechnology · 2017Article
- Review
- Characterization of a NaCl-tolerant β-N-acetylglucosaminidase from Sphingobacterium sp. HWLB1.Extremophiles : life under extreme conditions · 2016Article
- A trehalase from Zunongwangia sp.: characterization and improving catalytic efficiency by directed evolution.BMC biotechnology · 2016Article
- A Novel Multi-domain High Molecular, Salt-Stable Alkaline Xylanase fromFrontiers in microbiology · 2016Article
- Discovery, Molecular Mechanisms, and Industrial Applications of Cold-Active Enzymes.Frontiers in microbiology · 2016Review
- Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A new xylanase gene (xynA) from the marine microorganism Zunongwangia profunda was identified to encode 374 amino acid residues. Its product (XynA) showed the highest identity (42.78%) with a xylanase from Bacillus sp. SN5 among the characterized xylanases. XynA exhibited the highest activity at pH 6.5 and 30 °C, retaining 23 and 38% of the optimal activity at 0 and 5 °C, respectively. XynA was not only cold active, but also halophilic, and both its activity and thermostability could be significantly increased by NaCl, showing the highest activity (180% of the activity) at 3 M NaCl and retaining nearly 100% activity at 5 M NaCl, compared to the absence of NaCl. In the presence of 3 M NaCl, the k cat/K m value of XynA exhibited a 3.41-fold increase for beechwood xylan compared to no added NaCl, and the residual activity of XynA increased from 23% (no added NaCl) to 58% after 1 h incubation at 45 °C. This may be the first report concerning a cold-adapted xylanase from a non-halophilic species that displays the highest activity at a NaCl concentration range from 3 to 5 M. The features of cold activity and salt tolerance suggest the potential application of XynA in the food industry and bioethanol production from marine seaweeds.
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