ArticleMolecular biotechnology2013
Overexpression, purification, and biochemical characterization of the esterase Est0796 from Lactobacillus plantarum WCFS1.
Article in Molecular biotechnology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 21 citations in OpenAlex.
- Assessment of the impact of manual curation in BioCyc.Frontiers in bioinformatics · 2026Article
- Exploring the Structural Insights of ThermostableACS omega · 2024Article
- Cloning, Expression, and Purification of a GDSL-like Lipase/Acylhydrolase from a Native Lipase-Producing Bacterium, Lactobacillus fermentumIranian biomedical journal · 2022Article
- Characteration of a novel arylesterase from probiotics3 Biotech · 2021Article
- Characterization of a feruloyl esterase from Lactobacillus plantarum.Applied and environmental microbiology · 2013Article
Corrections and comments
- Erratum issuedInmaculada, Navarro-González [corrected to Navarro-González, Inmaculada]
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lactobacillus plantarum is a lactic acid bacterium that is encountered in an extensive range of foods such as fermented dairy products, meat, vegetables, and bakery products. Given the little molecular information available on the lipolytic activity of L. plantarum, the aim of this study was to clone, purify, and biochemically characterize the esterase coded by gene lp_0796 (Est0796). The esterase was cloned in pET28a and purified in two steps, using solid ammonium sulfate and His tag affinity chromatography. The molecular mass of the purified Est0796 was 28.7 kDa (by SDS-PAGE) and 26.6 kDa (by gel filtration chromatography), pointing to a monomeric structure. Est0796 showed maximum activity at pH 8.0 and 35 °C and toward shorter acyl chain lengths (C2-C4). The activity was resistant to organic solvents and cations, suggesting that this esterase may play a role in the fermentation of food products.
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