Structural and biochemical insights into the substrate-binding mechanism of a glycoside hydrolase family 12 β-1,3-1,4-glucanase from Chaetomium sp.
Catalytic mechanism
Characterization
Crystal structure
Substrate binding
β-1,3-1,4-Glucanase
Journal
Journal of structural biology
ISSN: 1095-8657
Titre abrégé: J Struct Biol
Pays: United States
ID NLM: 9011206
Informations de publication
Date de publication:
09 2021
09 2021
Historique:
received:
29
04
2021
revised:
16
07
2021
accepted:
22
07
2021
pubmed:
31
7
2021
medline:
5
4
2022
entrez:
30
7
2021
Statut:
ppublish
Résumé
β-1,3-1,4-Glucanases are a type of hydrolytic enzymes capable of catalyzing the strict cleavage of β-1,4 glycosidic bonds adjacent to β-1,3 linkages in β-D-glucans and have exhibited great potential in food and feed industrials. In this study, a novel glycoside hydrolase (GH) family 12 β-1,3-1,4-glucanase (CtGlu12A) from the thermophilic fungus Chaetomium sp. CQ31 was identified and biochemically characterized. CtGlu12A was most active at pH 7.5 and 65 °C, respectively, and exhibited a high specific activity of 999.9 U mg
Identifiants
pubmed: 34329700
pii: S1047-8477(21)00079-4
doi: 10.1016/j.jsb.2021.107774
pii:
doi:
Substances chimiques
Glycoside Hydrolases
EC 3.2.1.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
107774Informations de copyright
Copyright © 2021 Elsevier Inc. All rights reserved.