Characterization of recombinant E. coli expressing a novel fucosidase from Bacillus cereus 2-8 belonging to GH95 family.
Bacillus cereus
Fucoidan
Fucosidase
Function domain analysis
Journal
Protein expression and purification
ISSN: 1096-0279
Titre abrégé: Protein Expr Purif
Pays: United States
ID NLM: 9101496
Informations de publication
Date de publication:
10 2021
10 2021
Historique:
received:
02
03
2020
revised:
09
03
2021
accepted:
30
04
2021
pubmed:
16
5
2021
medline:
29
1
2022
entrez:
15
5
2021
Statut:
ppublish
Résumé
Fucoidan oligosaccharides possesses diverse physicochemical and biological activities. Specific glycoside hydrolases are valuable tools for degrading polysaccharides to produce oligosaccharides. In this study, BcFucA, a novel fucosidase belonging to GH95 family from Bacillus cereus 2-8, was cloned into pET21a vector, expressed in E. coli BL21 (DE3) and characterized. The protein consists of 1136 amino acid residues encoded by 3411 bases and has a molecular weight of 125.35 kDa. The optimal temperature and pH of this enzyme are 50 °C and pH 4.0. In addition, this study showed that the unknown function domain (encoding Lys261-Thr681) defined as a linker is quite important for its activity. The obtained novel enzyme BcFucA will contribute to the effective degradation of fucoidan and future industrial applications.
Identifiants
pubmed: 33991676
pii: S1046-5928(21)00080-2
doi: 10.1016/j.pep.2021.105897
pii:
doi:
Substances chimiques
Bacterial Proteins
0
Recombinant Fusion Proteins
0
alpha-L-Fucosidase
EC 3.2.1.51
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
105897Informations de copyright
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