Heterologous expression and biochemical characterization of novel multifunctional thermostable α-amylase from hot-spring metagenome.
Hot-spring metagenome
Multifunctional enzyme
Recombinant protein
Thermophilic bacteria
Thermostability
α-Amylase
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 Jul 2023
01 Jul 2023
Historique:
received:
22
02
2023
revised:
24
04
2023
accepted:
07
05
2023
medline:
19
6
2023
pubmed:
15
5
2023
entrez:
14
5
2023
Statut:
ppublish
Résumé
Hot-springs are regarded as the best source of industrially significant biocules and one of the unique locations for extremophiles. The α-amylase is one of the most important enzymes used in starch consuming industries, where the need of thermostability is paramount. In this study, the full metagenome sequences obtained from the soil of Tuwa hot-spring (Gujarat, India) were examined for the presence of several thermostable enzymes using bioinformatic techniques. The whole gene sequence for α-amylase was found from the metagenome. The α-amylase gene was amplified, cloned, and expressed in Escherichia coli and further characterized in vitro. The rm-α-amylase was found optimally active at 60 °C and at pH 6.0 and showed significantly high activity in 0.1 mM Co
Identifiants
pubmed: 37182622
pii: S0141-8130(23)01704-X
doi: 10.1016/j.ijbiomac.2023.124810
pii:
doi:
Substances chimiques
alpha-Amylases
EC 3.2.1.1
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
124810Informations de copyright
Copyright © 2023. Published by Elsevier B.V.
Déclaration de conflit d'intérêts
Declaration of competing interest The authors declare that they have no known competing interests that could have appeared to influence the work reported in this paper.