ArticleWorld journal of microbiology & biotechnology2014
Characterization of a novel cold-active esterase isolated from swamp sediment metagenome.
Article in World journal of microbiology & biotechnology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 17 citations in OpenAlex.
- A fast workflow to explore active enzymes from environmental samples through functional metagenomics.Applied microbiology and biotechnology · 2026Article
- Metagenomic Screening for Lipolytic Genes Reveals an Ecology-Clustered Distribution Pattern.Frontiers in microbiology · 2022Article
- A novel cold-adapted and highly salt-tolerant esterase from Alkalibacterium sp. SL3 from the sediment of a soda lake.Scientific reports · 2016Article
- Improved cultivation and metagenomics as new tools for bioprospecting in cold environments.Extremophiles : life under extreme conditions · 2015Review
- Est16, a New Esterase Isolated from a Metagenomic Library of a Microbial Consortium Specializing in Diesel Oil Degradation.PloS one · 2015Article
- Partial characterization of a crude cold-active lipase from Rhodococcus cercidiphylli BZ22.Folia microbiologica · 2014Article
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
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Abstract
A functional screen of a metagenomic library from "Upo" swamp sediment in Korea identified a gene EstL28, the product of which displayed lipolytic properties on a tributyrin-supplemented medium. The EstL28 sequence encodes a 290 amino acid protein (designated as EstL28), with a predicted molecular weight of 31.3 kDa. The encoded EstL28 protein exhibited the highest sequence similarity (45 %) to a hydrolase found in Streptococcus sanguinis. Phylogenetic analysis indicated that EstL28 belongs to a currently uncharacterized family of esterases. Within the conserved α/β-hydrolase 6 domain, the EstL28 retains the catalytic triad Ser₁₀₃-Asp₂₄₈-His₂₆₈ that is typical of esterases. The Ser103 residue in the catalytic triad is located in the consensus pentapeptide motif GXSXG. The purified EstL28 enzyme worked optimally at 35 °C and pH 8.5 and remained stable at temperatures lower than 20 °C. The catalytic activity of EstL28 was maximal with p-nitrophenyl butyrate, indicating that it was an esterase. This enzyme also exhibited stable activity in the presence of methanol, ethanol, isopropanol, and dimethyl sulfoxide. Therefore, the level of stability in organic solvents and cold temperature suggests that EstL28 has potential for many biotechnological applications.
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