Biochemical characterization of an esterase from Thermobifida fusca YX with acetyl xylan esterase activity.
Acetylesterase
/ metabolism
Hydrogen-Ion Concentration
Kinetics
Substrate Specificity
Thermobifida
/ enzymology
Esterases
/ metabolism
Enzyme Stability
Temperature
Escherichia coli
/ genetics
Cloning, Molecular
/ methods
Hydrolysis
Xylans
/ metabolism
Butyrates
/ metabolism
Bacterial Proteins
/ metabolism
Nitrophenols
Thermobifida fusca
Acetyl xylan esterase activity
Esterase
Thermostable enzyme
Journal
Molecular biology reports
ISSN: 1573-4978
Titre abrégé: Mol Biol Rep
Pays: Netherlands
ID NLM: 0403234
Informations de publication
Date de publication:
15 Jun 2024
15 Jun 2024
Historique:
received:
25
02
2024
accepted:
01
05
2024
medline:
15
6
2024
pubmed:
15
6
2024
entrez:
15
6
2024
Statut:
epublish
Résumé
Esterases (EC 3.1.1.X) are enzymes that catalyze the hydrolysis ester bonds. These enzymes have large potential for diverse applications in fine industries, particularly in pharmaceuticals, cosmetics, and bioethanol production. In this study, a gene encoding an esterase from Thermobifida fusca YX (TfEst) was successfully cloned, and its product was overexpressed in Escherichia coli and purified using affinity chromatography. The TfEst kinetic assay revealed catalytic efficiencies of 0.58 s The enzyme stability over a broad pH range and its activity at elevated temperatures make it an appealing candidate for industrial processes. Overall, TfEst emerges as a promising enzymatic tool with significant implications for the advancement of biotechnology and biofuels industries.
Sections du résumé
BACKGROUND
BACKGROUND
Esterases (EC 3.1.1.X) are enzymes that catalyze the hydrolysis ester bonds. These enzymes have large potential for diverse applications in fine industries, particularly in pharmaceuticals, cosmetics, and bioethanol production.
METHODS AND RESULTS
RESULTS
In this study, a gene encoding an esterase from Thermobifida fusca YX (TfEst) was successfully cloned, and its product was overexpressed in Escherichia coli and purified using affinity chromatography. The TfEst kinetic assay revealed catalytic efficiencies of 0.58 s
CONCLUSIONS
CONCLUSIONS
The enzyme stability over a broad pH range and its activity at elevated temperatures make it an appealing candidate for industrial processes. Overall, TfEst emerges as a promising enzymatic tool with significant implications for the advancement of biotechnology and biofuels industries.
Identifiants
pubmed: 38878205
doi: 10.1007/s11033-024-09601-7
pii: 10.1007/s11033-024-09601-7
doi:
Substances chimiques
acetylxylan esterase
EC 3.1.1.72
Acetylesterase
EC 3.1.1.6
Esterases
EC 3.1.-
Xylans
0
Butyrates
0
4-nitrophenyl butyrate
2635-84-9
4-nitrophenyl acetate
830-03-5
Bacterial Proteins
0
Nitrophenols
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
767Subventions
Organisme : Conselho Nacional de Desenvolvimento Científico e Tecnológico
ID : 142311/2016-2
Organisme : Conselho Nacional de Desenvolvimento Científico e Tecnológico
ID : 308223/2023-3
Organisme : Fundação de Amparo à Pesquisa do Estado de São Paulo
ID : 2017/25705-8
Organisme : Fundação de Amparo à Pesquisa do Estado de São Paulo
ID : 2022/12234-5
Informations de copyright
© 2024. The Author(s), under exclusive licence to Springer Nature B.V.
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