Functional analysis of a novel lytic polysaccharide monooxygenase from Streptomyces griseus on cellulose and chitin.
Bacterial Proteins
/ metabolism
Biomass
Catalytic Domain
/ physiology
Cellulases
/ metabolism
Cellulose
/ metabolism
Chitin
/ metabolism
Glycoside Hydrolases
/ metabolism
Mixed Function Oxygenases
/ metabolism
Oligosaccharides
/ metabolism
Oxidation-Reduction
Polysaccharides
/ metabolism
Protein Binding
/ physiology
Streptomyces griseus
/ metabolism
Substrate Specificity
Cellulose
Lytic polysaccharide monooxygenases (LPMO)
Streptomyces griseus
Journal
International journal of biological macromolecules
ISSN: 1879-0003
Titre abrégé: Int J Biol Macromol
Pays: Netherlands
ID NLM: 7909578
Informations de publication
Date de publication:
01 Dec 2020
01 Dec 2020
Historique:
received:
16
07
2020
revised:
28
07
2020
accepted:
03
08
2020
pubmed:
9
8
2020
medline:
7
4
2021
entrez:
9
8
2020
Statut:
ppublish
Résumé
Lytic polysaccharide monooxygenases (LPMOs) are enzymes that degrade polysaccharides with an oxidative mechanism and contributed to the efficiency in biomass degradation by glycoside hydrolases (GHs). In this study, the substrate and reaction specificity of SgLPMO10A that was an auxiliary activity family 10 (AA10) enzyme with a carbohydrate binding module family 2 (CBM2) domain from Streptomyces griseus, was analyzed. This enzyme produced oxidized cello-oligosaccharides from cellulose and boosted cellulose degradation by cellulases. Detailed study of the AA10 and CBM2 domains revealed that the binding ability of SgLPMO10A depended on CBM2 and that only the AA10 domain functions more effectively in the presence of a certain amount of substrates.
Identifiants
pubmed: 32763398
pii: S0141-8130(20)34102-7
doi: 10.1016/j.ijbiomac.2020.08.015
pii:
doi:
Substances chimiques
Bacterial Proteins
0
Oligosaccharides
0
Polysaccharides
0
Chitin
1398-61-4
Cellulose
9004-34-6
Mixed Function Oxygenases
EC 1.-
Cellulases
EC 3.2.1.-
Glycoside Hydrolases
EC 3.2.1.-
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
2085-2091Informations de copyright
Copyright © 2020 Elsevier B.V. All rights reserved.