XynDZ5: A New Thermostable GH10 Xylanase.
biocatalysis
biotechnology
genome analysis
mode of action
thermostability
xylanase
Journal
Frontiers in microbiology
ISSN: 1664-302X
Titre abrégé: Front Microbiol
Pays: Switzerland
ID NLM: 101548977
Informations de publication
Date de publication:
2020
2020
Historique:
received:
14
09
2019
accepted:
12
03
2020
entrez:
12
5
2020
pubmed:
12
5
2020
medline:
12
5
2020
Statut:
epublish
Résumé
Xylanolytic enzymes have a broad range of applications in industrial biotechnology as biocatalytic components of various processes and products, such as food additives, bakery products, coffee extraction, agricultural silage and functional foods. An increasing market demand has driven the growing interest for the discovery of xylanases with specific industrially relevant characteristics, such as stability at elevated temperatures and in the presence of other denaturing factors, which will facilitate their incorporation into industrial processes. In this work, we report the discovery and biochemical characterization of a new thermostable GH10 xylanase, termed XynDZ5, exhibiting only 26% amino acid sequence identity to the closest characterized xylanolytic enzyme. This new enzyme was discovered in an Icelandic hot spring enrichment culture of a
Identifiants
pubmed: 32390953
doi: 10.3389/fmicb.2020.00545
pmc: PMC7193231
doi:
Types de publication
Journal Article
Langues
eng
Pagination
545Informations de copyright
Copyright © 2020 Zarafeta, Galanopoulou, Leni, Kaili, Chegkazi, Chrysina, Kolisis, Hatzinikolaou and Skretas.
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