A Novel Dimeric Exoglucanase (GH5_38): Biochemical and Structural Characterisation towards its Application in Alkyl Cellobioside Synthesis.
Animals
Bacterial Proteins
/ chemistry
Binding Sites
Cloning, Molecular
Escherichia coli
/ genetics
Gene Expression
Genetic Vectors
/ chemistry
Glucans
/ chemistry
Glycoside Hydrolases
/ chemistry
Glycosides
/ biosynthesis
Hydrogen-Ion Concentration
Isoptera
/ microbiology
Kinetics
Microbiota
/ physiology
Models, Molecular
Protein Binding
Protein Conformation, alpha-Helical
Protein Conformation, beta-Strand
Protein Interaction Domains and Motifs
Protein Multimerization
Recombinant Proteins
/ chemistry
Substrate Specificity
beta-Glucans
/ chemistry
Alkyl cellobiosides
GH5_38
dimeric protein
exoglucanase
transglycosylation
Journal
Molecules (Basel, Switzerland)
ISSN: 1420-3049
Titre abrégé: Molecules
Pays: Switzerland
ID NLM: 100964009
Informations de publication
Date de publication:
09 Feb 2020
09 Feb 2020
Historique:
received:
18
12
2019
revised:
14
01
2020
accepted:
21
01
2020
entrez:
14
2
2020
pubmed:
14
2
2020
medline:
24
11
2020
Statut:
epublish
Résumé
An exoglucanase (Exg-D) from the glycoside hydrolase family 5 subfamily 38 (GH5_38) was heterologously expressed and structurally and biochemically characterised at a molecular level for its application in alkyl glycoside synthesis. The purified Exg-D existed in both dimeric and monomeric forms in solution, which showed highest activity on mixed-linked β-glucan (88.0 and 86.7 U/mg protein, respectively) and lichenin (24.5 and 23.7 U/mg protein, respectively). They displayed a broad optimum pH range from 5.5 to 7 and a temperature optimum from 40 to 60 °C. Kinetic studies demonstrated that Exg-D had a higher affinity towards β-glucan, with a
Identifiants
pubmed: 32050450
pii: molecules25030746
doi: 10.3390/molecules25030746
pmc: PMC7036808
pii:
doi:
Substances chimiques
Bacterial Proteins
0
Glucans
0
Glycosides
0
Recombinant Proteins
0
beta-Glucans
0
Glycoside Hydrolases
EC 3.2.1.-
lichenin
M7F3LRN53I
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Department of Science and Technology, Republic of South Africa
ID : CSIR National Biocatalysis Initiative Project
Organisme : Department of Science and Technology, Republic of South Africa
ID : NRF South African Research Chair in Protein Biochemistry and Structural Biology
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