Structure and function characterization of the α-L-arabinofuranosidase from the white-rot fungus Trametes hirsuta.
Arabinoxylan
Crystal structure
Glycoside hydrolase 51 family
Synergistic degradation
Trametes hirsuta
α-L-Arabinofuranosidases
Journal
Applied microbiology and biotechnology
ISSN: 1432-0614
Titre abrégé: Appl Microbiol Biotechnol
Pays: Germany
ID NLM: 8406612
Informations de publication
Date de publication:
Jun 2023
Jun 2023
Historique:
received:
07
02
2023
accepted:
19
04
2023
revised:
17
04
2023
medline:
5
6
2023
pubmed:
14
5
2023
entrez:
13
5
2023
Statut:
ppublish
Résumé
α-L-Arabinofuranosidases (Abfs) play a crucial role in the degradation of hemicelluloses, especially arabinoxylans (AX). Most of the available characterized Abfs are from bacteria, while fungi, as natural decomposers, contain Abfs with little attention given. An arabinofuranosidase (ThAbf1), belonging to the glycoside hydrolase 51 (GH51) family, from the genome of the white-rot fungus Trametes hirsuta, was recombinantly expressed, characterized, and functionally determined. The general biochemical properties showed that the optimal conditions for ThAbf1 were pH 6.0 and 50°C. In substrate kinetics assays, ThAbf1 preferred small fragment arabinoxylo-oligosaccharides (AXOS) and could surprisingly hydrolyze di-substituted 2
Identifiants
pubmed: 37178306
doi: 10.1007/s00253-023-12561-w
pii: 10.1007/s00253-023-12561-w
doi:
Substances chimiques
alpha-N-arabinofuranosidase
EC 3.2.1.55
Xylans
0
Oligosaccharides
0
Glycoside Hydrolases
EC 3.2.1.-
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
3967-3981Informations de copyright
© 2023. The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature.
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