ArticleMolecular biotechnology2019
A Novel VIII Carboxylesterase with High Hydrolytic Activity Against Ampicillin from a Soil Metagenomic Library.
Article in Molecular biotechnology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Bacterial family-VIII esterase displays dual activities: hydrolysis of polyester bioplastics and β-lactam antibiotics.The ISME journal · 2026Article
- Thermostable Esterase from ThermophilicGenes · 2025Article
- Enhancing the Hydrolysis and Acyl Transfer Activity of Carboxylesterase DLFae4 by a Combinational Mutagenesis and In-Silico Method.Foods (Basel, Switzerland) · 2023Article
- Genome-wide analysis of lipolytic enzymes and characterization of a high-tolerant carboxylesterase fromFrontiers in microbiology · 2023Article
- Molecular Cloning and Characterization of a New Family VI Esterase from an Activated Sludge Metagenome.Microorganisms · 2022Article
- Metagenomic survey of the microbiome of ancient Siberian permafrost and modern Kamchatkan cryosols.microLife · 2022Article
- Molecular Characterization of Novel Family IV and VIII Esterases from a Compost Metagenomic Library.Microorganisms · 2021Article
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Authors and funding
8 authors.
Funding
Abstract
A novel carboxylesterase gene, named dlfae4, was discovered and sequenced from a soil metagenomic library. The dlfae4 gene was composed of 1017 base pairs encoding 338 amino acid residues with a predicted molecular mass of 37.2 kDa. DLFae4 exhibited strong hydrolytic activity towards methyl ferulate under optimum pH and temperature conditions (pH 8.6, 50 °C) and displayed remarkable thermostability, with residual activity as high as 50% after incubation for 3 h at 60 °C. A family VIII esterase DLFae4 was found to contain a typical serine residue within the S-X-X-K motif, which serves as a catalytic nucleophile in class C β-lactamases and family VIII esterases. As a consequence of its high sequence similarity with β-lactamases, DLFae4 exhibited significant hydrolytic activity towards ampicillin. In addition, DLFae4 was found to be the first known member of family VIII carboxylesterases with phthalate-degrading ability. Site-directed mutagenesis studies revealed that Ser11, Lys14, and Tyr121 residues play an essential catalytic role in DLFae4. These new findings, which are of great importance for further in-depth research and engineering development of carboxylesterases, should advance the implementation of biotechnological applications.
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Registered trials
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