ArticleScientific reports2020
Purification, characterization and partial amino acid sequences of thermo-alkali-stable and mercury ion-tolerant xylanase from Thermomyces dupontii KKU-CLD-E2-3.
Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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6 citing papers in PubMed, 18 citations in OpenAlex.
- Optimization and comparative evaluation of fungal laccase-based biobleaching of pineapple leaf pulp: toward sustainable non-wood pulp processing using Paramarasmius palmivorus.Biotechnology letters · 2026Article
- Cloning, heterologus expression and characterization of a thermophilic and salt tolerant GH11 xylanase from Allostreptomyces psammosilenae YIM DR4008Antonie van Leeuwenhoek · 2025Article
- Microbially Induced Calcium Carbonate Precipitation Using Lysinibacillus sp.: A Ureolytic Bacterium from Uttarakhand for Soil Stabilization.Current microbiology · 2024Article
- Exploring the potential of a new thermotolerant xylanase from3 Biotech · 2024Article
- Purification of xylanases from Aureobasidium pullulans CCT 1261 and its application in the production of xylooligosaccharides.World journal of microbiology & biotechnology · 2022Article
- Application of surfactants in papermaking industry and future development trend of green surfactants.Applied microbiology and biotechnology · 2021Review
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Authors and funding
6 authors at 4 institutions in 2 countries.
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Abstract
We investigated the properties of the low molecular weight thermo-alkali-stable and mercury ion-tolerant xylanase production from Thermomyces dupontii KKU-CLD-E2-3. The xylanase was purified to homogeneity by ammonium sulfate, Sephadex G-100 and DEAE-cellulose column chromatography which resulted 27.92-fold purification specific activity of 56.19 U/mg protein and a recovery yield of 2.01%. The purified xylanase showed a molecular weight of 25 kDa by SDS-PAGE and the partial peptide sequence showed maximum sequence homology to the endo-1,4-β-xylanase. The optimum temperature and pH for its activity were 80 °C and pH 9.0, respectively. Furthermore, the purified xylanase can maintain more than 75% of the original activity in pH range of 7.0-10.0 after incubation at 4 °C for 24 h, and can still maintain more than 70% of original activity after incubating at 70 °C for 90 min. Our purified xylanase was activated by Cu
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