Purification, characterization and partial amino acid sequences of thermo-alkali-stable and mercury ion-tolerant xylanase from Thermomyces dupontii KKU–CLD–E2–3
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 re...
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| Auteurs principaux: | , , , , , |
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| Format: | article |
| Langue: | EN |
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Nature Portfolio
2020
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| Accès en ligne: | https://doaj.org/article/db64466b69614148b7f4a952f76502e3 |
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