Identification of a novel glycoside hydrolase family 8 xylanase from Deinococcus geothermalis and its application at low temperatures.
Deinococcus
/ enzymology
Substrate Specificity
Endo-1,4-beta Xylanases
/ genetics
Xylans
/ metabolism
Enzyme Stability
Cold Temperature
Bacterial Proteins
/ genetics
Hydrogen-Ion Concentration
Glycoside Hydrolases
/ genetics
Amino Acid Sequence
Hydrolysis
Recombinant Proteins
/ metabolism
Sequence Alignment
Cloning, Molecular
Kinetics
Molecular Weight
Disaccharides
Deinococcus geothermalis
Cold-adapted enzyme
DgeoXyn
GH8
Xylanase
Journal
Archives of microbiology
ISSN: 1432-072X
Titre abrégé: Arch Microbiol
Pays: Germany
ID NLM: 0410427
Informations de publication
Date de publication:
17 Jun 2024
17 Jun 2024
Historique:
received:
04
05
2024
accepted:
15
06
2024
revised:
12
06
2024
medline:
17
6
2024
pubmed:
17
6
2024
entrez:
17
6
2024
Statut:
epublish
Résumé
Xylanase is the most important hydrolase in the xylan hydrolase system, the main function of which is β-1,4-endo-xylanase, which randomly cleaves xylans to xylo-oligosaccharides and xylose. Xylanase has wide ranging of applications, but there remains little research on the cold-adapted enzymes required in some low-temperature industries. Glycoside hydrolase family 8 (GH8) xylanases have been reported to have cold-adapted enzyme activity. In this study, the xylanase gene dgeoxyn was excavated from Deinococcus geothermalis through sequence alignment. The recombinant xylanase DgeoXyn encodes 403 amino acids with a theoretical molecular weight of 45.39 kDa. Structural analysis showed that DgeoXyn has a (α/α)6-barrel fold structure typical of GH8 xylanase. At the same time, it has strict substrate specificity, is only active against xylan, and its hydrolysis products include xylobiose, xylotrinose, xytetranose, xylenanose, and a small amount of xylose. DgeoXyn is most active at 70 ℃ and pH 6.0. It is very stable at 10, 20, and 30 ℃, retaining more than 80% of its maximum enzyme activity. The enzyme activity of DgeoXyn increased by 10% after the addition of Mn
Identifiants
pubmed: 38884653
doi: 10.1007/s00203-024-04055-8
pii: 10.1007/s00203-024-04055-8
doi:
Substances chimiques
Endo-1,4-beta Xylanases
EC 3.2.1.8
Xylans
0
Bacterial Proteins
0
Glycoside Hydrolases
EC 3.2.1.-
Recombinant Proteins
0
xylobiose
ID02R0EG7P
Disaccharides
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
307Subventions
Organisme : National Key R&D Program of China
ID : 2023YFF1000300
Organisme : National Natural Science Foundation of China
ID : 31930004
Organisme : National Natural Science Foundation of China
ID : 32270067
Organisme : Agricultural Science and Technology Innovation Program of the Chinese Academy of Agricultural Sciences
ID : CAAS-ZDRW202305
Organisme : Third Xinjiang Scientific Expedition
ID : 2022xjkk020602
Informations de copyright
© 2024. The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature.
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