ArticlePloS one2015
Est16, a New Esterase Isolated from a Metagenomic Library of a Microbial Consortium Specializing in Diesel Oil Degradation.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 34 citations in OpenAlex.
- Recombinant Esterase (BaCEApplied biochemistry and biotechnology · 2025Article
- Use of Taguchi design for optimization of diesel-oil biodegradation using consortium ofJournal of environmental health science & engineering · 2022Article
- Characterization and purification of esterase from Cellulomonas fimi DB19 isolated from Zanthoxylum armatum with its possible role in diesel biodegradation.Archives of microbiology · 2022Article
- From Data Mining ofMicroorganisms · 2021Article
- Metagenomic applications in exploration and development of novel enzymes from nature: a review.Journal, genetic engineering & biotechnology · 2020Review
- A novel bacterial carboxylesterase identified in a metagenome derived-clone from Brazilian mangrove sediments.Molecular biology reports · 2020Article
- Identification and characterization of a novel alkalistable and salt-tolerant esterase from the deep-sea hydrothermal vent of the East Pacific Rise.MicrobiologyOpen · 2018Article
- Halotolerant aminopeptidase M29 from Mesorhizobium SEMIA 3007 with biotechnological potential and its impact on biofilm synthesis.Scientific reports · 2017Article
- Construction of a novel lipolytic fusion biocatalyst GDEst-lip for industrial application.Journal of industrial microbiology & biotechnology · 2017Article
- Functional Metagenomics as a Tool for Identification of New Antibiotic Resistance Genes from Natural Environments.Microbial ecology · 2017Review
- Identification and Characterization of a Novel Salt-Tolerant Esterase from the Deep-Sea Sediment of the South China Sea.Frontiers in microbiology · 2017Article
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Authors and funding
5 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lipolytic enzymes have attracted attention from a global market because they show enormous biotechnological potential for applications such as detergent production, leather processing, cosmetics production, and use in perfumes and biodiesel. Due to the intense demand for biocatalysts, a metagenomic approach provides methods of identifying new enzymes. In this study, an esterase designated as Est16 was selected from 4224 clones of a fosmid metagenomic library, revealing an 87% amino acid identity with an esterase/lipase (accession number ADM63076.1) from an uncultured bacterium. Phylogenetic studies showed that the enzyme belongs to family V of bacterial lipolytic enzymes and has sequence and structural similarities with an aryl-esterase from Pseudomonas fluorescens and a patented Anti-Kazlauskas lipase (patent number US20050153404). The protein was expressed and purified as a highly soluble, thermally stable enzyme that showed a preference for basic pH. Est16 exhibited activity toward a wide range of substrates and the highest catalytic efficiency against p-nitrophenyl butyrate and p-nitrophenyl valerate. Est16 also showed tolerance to the presence of organic solvents, detergents and metals. Based on molecular modeling, we showed that the large alpha-beta domain is conserved in the patented enzymes but not the substrate pocket. Here, it was demonstrated that a metagenomic approach is suitable for discovering the lipolytic enzyme diversity and that Est16 has the biotechnological potential for use in industrial processes.
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