ArticleBioresource technology2013
Molecular characterization of a cold-active recombinant xylanase from Flavobacterium johnsoniae and its applicability in xylan hydrolysis.
Article in Bioresource technology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 56 citations in OpenAlex.
- Solid-State Fermentation of Green Coconut Husk byACS omega · 2026Article
- A Glycosyl Hydrolase 30 Family Xylanase from the Rumen Metagenome and Its Effects on In Vitro Ruminal Fermentation of Wheat Straw.Animals : an open access journal from MDPI · 2023Article
- Novel Virulence Factors DecipheringInternational journal of molecular sciences · 2022Article
- Biochemical and Thermodynamic Studies on a Novel Thermotolerant GH10 Xylanase fromBiomolecules · 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
- Isolation and Characterization of a Novel Cold-Active, Halotolerant Endoxylanase fromMarine drugs · 2020Article
- Extremophile Microbial Communities and Enzymes for Bioenergetic Application Based on Multi-Omics Tools.Current genomics · 2020Review
- Carbohydrate Binding Modules: Diversity of Domain Architecture in Amylases and Cellulases From Filamentous Microorganisms.Frontiers in bioengineering and biotechnology · 2020Review
- Article
- Molecular and Biochemical Characterization of a Bimodular Xylanase FromFrontiers in microbiology · 2019Article
- Characterization of a novel cold-active xylanase from Luteimonas species.World journal of microbiology & biotechnology · 2018Article
- Article
- Discovery, Molecular Mechanisms, and Industrial Applications of Cold-Active Enzymes.Frontiers in microbiology · 2016Review
- NaCl-, protease-tolerant and cold-active endoglucanase from Paenibacillus sp. YD236 isolated from the feces of Bos frontalis.SpringerPlus · 2016Article
- Kinetic and thermodynamic characterization of a novel low-temperature-active xylanase from Arthrobacter sp. GN16 isolated from the feces of Grus nigricollis.Bioengineered · 2015Article
- Cold and Hot Extremozymes: Industrial Relevance and Current Trends.Frontiers in bioengineering and biotechnology · 2015Review
- Purification and characterization of cellulase-free low molecular weight endo β-1,4 xylanase from an alkalophilic Cellulosimicrobium cellulans CKMX1 isolated from mushroom compost.World journal of microbiology & biotechnology · 2014Article
- A thermo-halo-tolerant and proteinase-resistant endoxylanase from Bacillus sp. HJ14.Folia microbiologica · 2014Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
A novel xylanase gene, xyn10A, was cloned from Flavobacterium johsoniae, overexpressed in a flavobacterial expression system, the recombinant enzyme purified by Ni-affinity chromatography, and enzyme structure and activity analyzed. Xyn10A was found to be a modular xylanase with an Fn3 accessory domain on its N-terminal and a catalytic region on the C-terminal. The optimum pH and temperature for Xyn10A was 8.0 and 30 °C, but Xyn10A retained 50% activity at 4 °C, indicating that Xyn10A is a cold-active xylanase. A Fn3-deletion xylanase had relative activity ca. 3.6-fold lower than the wild-type, indicating that Fn3 promotes xylanase activity. The Fn3 region also contributed to stability of the enzyme at elevated temperatures. However, Fn3 did not bind this xylanase to insoluble substrates. The enzyme hydrolyzed xylo-oligosaccharides into xylobiose, and xylose with xylobiose as the main product, confirming that Xyn10A is a strict endo-β-1,4-xylanase. Xyn10A also hydrolyzed birchwood and beechwood xylan to yield mainly xylose, xylobiose and xylotriose.
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