ArticleExtremophiles : life under extreme conditions2021
Characterization of a carboxylesterase with hyper-thermostability and alkali-stability from Streptomyces lividans TK24.
Article in Extremophiles : life under extreme conditions, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Identification and characterization of a novel halolysin from Halostella sp. PRR32 with two C-terminal extensions.Extremophiles : life under extreme conditions · 2025Article
- AMWEst, a new thermostable and detergent-tolerant esterase retrieved from the Albian aquifer.Applied microbiology and biotechnology · 2024Article
- Identification and biochemical characterization of a novel halolysin from Halorubellus sp. PRR65 with a relatively high temperature activity.World journal of microbiology & biotechnology · 2024Article
- Expression, Characterization, Fermentation, Immobilization, and Application of a Novel Esterase Est804 From Metagenomic Library in Pesticide Degradation.Frontiers in microbiology · 2022Article
- An artificial self-assembling peptide with carboxylesterase activity and substrate specificity restricted to short-chain acid p-nitrophenyl esters.Frontiers in chemistry · 2022Article
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Authors and funding
8 authors.
Funding
Abstract
A gene (estA', 804 bp) from Streptomyces lividans TK24 was artificially synthesized and successfully overexpressed as a 6His-tagged fusion protein in Escherichia coli. It encoded a carboxylesterase (EstA) that composed of 267 amino acids with a predicted molecular weight of 28.56 kDa. Multiple sequence alignment indicated that EstA has typical characteristics of esterases, including a catalytic triad (Ser93-Asp194-His224) and a conserved pentapeptide motif (Gly91-Leu92-Ser93-Met94-Gly95). Simultaneously, phylogenetic analysis indicated that EstA belongs to family VI. Biochemical characterization displayed its optimum enzyme activity was at 55 ℃ and pH 8.5. Additionally, EstA exhibited higher activity towards short carbon substrates and showed the outstanding catalytic efficiency for pNPA2 with k
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