ArticleJournal of industrial microbiology & biotechnology2013
Isolation and characterization of a thermostable esterase from a metagenomic library.
Article in Journal of industrial microbiology & biotechnology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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12 citing papers in PubMed.
- Identification, Characterization, and Computer-Aided Rational Design of a Novel Thermophilic Esterase from Geobacillus subterraneus, and Application in the Synthesis of Cinnamyl Acetate.Applied biochemistry and biotechnology · 2024Article
- Molecular Cloning and Characterization of a New Family VI Esterase from an Activated Sludge Metagenome.Microorganisms · 2022Article
- Microbial elimination of pyrethroids: specific strains and involved enzymes.Applied microbiology and biotechnology · 2022Review
- Recombinant acetylxylan esterase of Halalkalibacterium halodurans NAH-Egypt: molecular and biochemical study.AMB Express · 2022Article
- An artificial self-assembling peptide with carboxylesterase activity and substrate specificity restricted to short-chain acid p-nitrophenyl esters.Frontiers in chemistry · 2022Article
- Metagenomic Screening for Lipolytic Genes Reveals an Ecology-Clustered Distribution Pattern.Frontiers in microbiology · 2022Article
- Characterization of a carboxylesterase with hyper-thermostability and alkali-stability from Streptomyces lividans TK24.Extremophiles : life under extreme conditions · 2021Article
- Discovery and characterizaton of a novel lipase with transesterification activity from hot spring metagenomic library.Biotechnology reports (Amsterdam, Netherlands) · 2017Article
- Metagenomics of Thermophiles with a Focus on Discovery of Novel Thermozymes.Frontiers in microbiology · 2016Review
- Expression and display of a novel thermostable esterase from Clostridium thermocellum on the surface of Bacillus subtilis using the CotB anchor protein.Journal of industrial microbiology & biotechnology · 2015Article
- Characterization of a novel thermophilic phospholipase B from Thermotoga lettingae TMO: applicability in enzymatic degumming of vegetable oils.Journal of industrial microbiology & biotechnology · 2015Article
- Biochemical characterization of a carboxylesterase from the archaeon Pyrobaculum sp. 1860 and a rational explanation of its substrate specificity and thermostability.International journal of molecular sciences · 2014Article
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3 authors.
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Abstract
A novel esterase gene was isolated by functional screening of a metagenomic library prepared from an activated sludge sample. The gene (est-XG2) consists of 1,506 bp with GC content of 74.8 %, and encodes a protein of 501 amino acids with a molecular mass of 53 kDa. Sequence alignment revealed that Est-XG2 shows a maximum amino acid identity (47 %) with the carboxylesterase from Thermaerobacter marianensis DSM 12885 (YP_004101478). The catalytic triad of Est-XG2 was predicted to be Ser₁₉₂-Glu₃₁₃-His₄₁₂ with Ser₉₂ in a conserved pentapeptide (GXSXG), and further confirmed by site-directed mutagenesis. Phylogenetic analysis suggested Est-XG2 belongs to the bacterial lipase/esterase family VII. The recombinant Est-XG2, expressed and purified from Escherichia coli, preferred to hydrolyze short and medium length p-nitrophenyl esters with the best substrate being p-nitrophenyl acetate (K(m) and k(cat) of 0.33 mM and 36.21 s⁻¹, respectively). The purified enzyme also had the ability to cleave sterically hindered esters of tertiary alcohols. Biochemical characterization of Est-XG2 revealed that it is a thermophilic esterase that exhibits optimum activity at pH 8.5 and 70 °C. Est-XG2 had moderate tolerance to organic solvents and surfactants. The unique properties of Est-XG2, high thermostability and stability in the presence of organic solvents, may render it a potential candidate for industrial applications.
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