ArticleMolecular biotechnology2010
Cloning, expression, purification, and characterization of a novel esterase from Lactobacillus plantarum.
Article in Molecular biotechnology, 2010. 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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11 citing papers in PubMed, 40 citations in OpenAlex.
- Recent Applications and Prospects of Enzymes in Quality and Safety Control of Fermented Foods.Foods (Basel, Switzerland) · 2024Review
- Bioaccumulation and biotransformation of simvastatin in probiotic bacteria: A step towards better understanding of drug-bile acids-microbiome interactions.Frontiers in pharmacology · 2023Article
- Heterologous expression, molecular studies and biochemical characterization of a novel alkaline esterase gene fromRSC advances · 2022Article
- 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
- The Lp_3561 and Lp_3562 Enzymes Support a Functional Divergence Process in the Lipase/Esterase Toolkit from Lactobacillus plantarum.Frontiers in microbiology · 2016Article
- A Lactobacillus plantarum esterase active on a broad range of phenolic esters.Applied and environmental microbiology · 2015Article
- Characterization of a feruloyl esterase from Lactobacillus plantarum.Applied and environmental microbiology · 2013Article
- Overexpression, purification, and biochemical characterization of the esterase Est0796 from Lactobacillus plantarum WCFS1.Molecular biotechnology · 2013Article
- The PE-PPE domain in mycobacterium reveals a serine α/β hydrolase fold and function: an in-silico analysis.PloS one · 2011Article
- Biochemical and structural characterization of two site-directed mutants of Staphylococcus xylosus lipase.Molecular biotechnology · 2010Article
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Authors and funding
5 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Lactobacillus plantarum is an important lactic acid bacterium, usually found as natural inhabitant of food, such as fermented vegetables and meat products. However, little information about lactic acid bacteria, especially concerning L. plantarum, as a source of useful enzymes has been reported. The aim of this study was to clone, express in Escherichia coli, purify, and characterize an esterase from L. plantarum ATCC 8014. The esterase gene (1014 bp) was amplified and cloned in pET14b expression vector to express a His(6)-tagged protein in E. coli. Recombinant L. plantarum esterase was purified by Ni-NTA resin, presenting an apparent molecular mass of about 38 kDa. It presented highest activity at pH 6.0 and 40 degrees C. Also, it presented preference for p-nitrophenyl butyrate, but hydrolyzed more efficiently p-nitrophenyl acetate. Besides, this study shows, for the first time, CD data about secondary structure of an esterase from L. plantarum.
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