ArticleMolecular biotechnology2015
Characterization of Novel Family IV Esterase and Family I.3 Lipase from an Oil-Polluted Mud Flat Metagenome.
Article in Molecular biotechnology, 2015. 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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Who cites it
12 citing papers in PubMed, 27 citations in OpenAlex.
- Microbial lipases: advances in metagenomics and artificial intelligence for enzyme discovery and engineering.Archives of microbiology · 2026Review
- Screening of Marine Bacteria for Lipase Activity and Application as Whole-Cell Biocatalysts.Microorganisms · 2026Article
- An uncharacterized protein from the metagenome with no obvious homology to known lipases shows excellent alkaline lipase properties and potential applications in the detergent industry.Biotechnology letters · 2021Article
- Molecular Characterization of Novel Family IV and VIII Esterases from a Compost Metagenomic Library.Microorganisms · 2021Article
- Gene cloning, heterologous expression, and partial characterization of a novel cold-adapted subfamily I.3 lipase from Pseudomonas fluorescence KE38.Scientific reports · 2020Article
- Characterization of Novel Salt-Tolerant Esterase Isolated from the Marine BacteriumJournal of microbiology and biotechnology · 2020Article
- First Evidence of Acyl-Hydrolase/Lipase Activity From Human Probiotic Bacteria:Frontiers in microbiology · 2020Article
- Crystal structure of PMGL2 esterase from the hormone-sensitive lipase family with GCSAG motif around the catalytic serine.PloS one · 2020Article
- Characterization of a Novel Moderately Thermophilic Solvent-Tolerant Esterase Isolated From a Compost Metagenome Library.Frontiers in microbiology · 2019Article
- Functional Metagenomics as a Tool for Identification of New Antibiotic Resistance Genes from Natural Environments.Microbial ecology · 2017Review
- Integrative computational approach for genome-based study of microbial lipid-degrading enzymes.World journal of microbiology & biotechnology · 2016Review
- Metagenomics of Thermophiles with a Focus on Discovery of Novel Thermozymes.Frontiers in microbiology · 2016Review
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Two genes encoding lipolytic enzymes were isolated from a metagenomic library constructed from oil-polluted mud flats. An esterase gene, est3K, encoded a protein of 299 amino acids (ca. 32,364 Da). Est3K was a family IV esterase with typical motifs, HGGG, and HGF. Although est3K showed high identity to many genes with no information on their enzymatic properties, Est3K showed the highest identity (36 %) to SBLip5.1 from forest soil metagenome when compared to the enzymes with reported properties. A lipase gene, lip3K, encoded a protein of 616 amino acids (ca. 64,408 Da). Lip3K belonged to family I.3 lipase with a C-terminal secretion signal and showed the highest identity (93 %) to the lipase of Pseudomonas sp. MIS38. The presence of several newly identified conserved motifs in Est3K and Lip3K are suggested. Both Est3K and Lip3K exerted their maximal activity at pH 9.0 and 50 °C. The activity of Lip3K was significantly increased by the presence of 30 % methanol. The ability of the enzymes to retain activities in the presence of methanol and the substrates may offer a merit to the biotechnological applications of the enzymes such as transesterification. The activity and the thermostability of Lip3K were increased by Ca(2+). Est3K and Lip3K preferred p-nitrophenyl butyrate (C4) and octanoate (C8), respectively, as the substrate and acted independently on the substrates with no synergistic effect.
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