Purification, characterization and partial amino acid sequences of thermo-alkali-stable and mercury ion-tolerant xylanase from Thermomyces dupontii KKU–CLD–E2–3

• Published in: Scientific reports Vol. 10; no. 1; pp. 21663 - 10
• Main Authors: Seemakram, Wasan, Boonrung, Santhaya, Aimi, Tadanori, Ekprasert, Jindarat, Lumyong, Saisamorn, Boonlue, Sophon
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 10.12.2020; Nature Publishing Group; Nature Portfolio
• Subjects: 631/326; 631/45; 631/61; Alkalies; Amino Acid Sequence; Amino acids; Ammonium; Ammonium sulfate; Bleaching; Carbon dioxide; Cellulose; Cobalt; Column chromatography; Copper; Disaccharides; Endo-1,4-beta Xylanases - chemistry; Endo-1,4-beta Xylanases - isolation & purification; endo-1,4-β-Xylanase; Enzyme Stability; Eurotiales - enzymology; Homology; Hot Temperature; Humanities and Social Sciences; Hydrogen-Ion Concentration; Hydrolysis; Industry; Mercury; Molecular weight; multidisciplinary; pH effects; Protein folding; Protein purification; Pulp; Pulp & paper industry; Science; Science (multidisciplinary); Sodium lauryl sulfate; Substrate Specificity; Xylan; Xylans

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...