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XynDZ5: A New Thermostable GH10 Xylanase
Dimitra Zarafeta1, Anastasia P Galanopoulou1,2, Maria Evangelia Leni1
1Institute of Chemical Biology, National Hellenic Research Foundation, Athens, Greece.
Frontiers in Microbiology
|May 12, 2020
Summary
A novel thermostable xylanase, XynDZ5, was discovered in an Icelandic hot spring. This enzyme shows high efficiency and stability at high temperatures and in denaturing conditions, making it ideal for industrial biotechnology applications.
Area of Science:
- Biotechnology
- Enzymology
- Microbial biochemistry
Background:
- Xylanolytic enzymes (xylanases) are crucial biocatalysts in industrial biotechnology.
- Market demand for xylanases with enhanced stability (thermal, chemical) is increasing.
- Discovery of novel xylanases with specific industrial characteristics is essential.
Purpose of the Study:
- To discover and biochemically characterize a new thermostable GH10 xylanase.
- To assess the enzyme's suitability for high-temperature industrial applications.
Main Methods:
- Bioinformatic analysis of an Icelandic hot spring enrichment culture.
- Recombinant production of the xylanase (XynDZ5) in *Escherichia coli*.
- Biochemical characterization including optimal temperature, pH, and stability assays.
- Computational modeling of the enzyme's three-dimensional structure.
Main Results:
- Discovery of XynDZ5, a GH10 xylanase with 26% sequence identity to its closest relative.
- Optimal activity at 65-75°C and pH 7.5.
- High catalytic efficiency and stability at elevated temperatures, in metal ions, and denaturing agents.
- Exhibited significant exo-activity, an atypical characteristic.
- Modeled structure revealed a (β/α)8 TIM barrel fold.
Conclusions:
- XynDZ5 is a promising thermostable biocatalyst for various high-temperature industrial processes.
- Its unique biochemical profile and stability enhance its biotechnological potential.
- Further structural insights may explain its catalytic performance.
