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

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Seemakram, Wasan, Boonrung, Santhaya, Aimi, Tadanori, Ekprasert, Jindarat, Lumyong, Saisamorn, Boonlue, Sophon
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2020
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7730141/
https://www.ncbi.nlm.nih.gov/pubmed/33303944
http://dx.doi.org/10.1038/s41598-020-78670-y

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7730141/
https://www.ncbi.nlm.nih.gov/pubmed/33303944
http://dx.doi.org/10.1038/s41598-020-78670-y

Ejemplares similares