ArticlePloS one2017
Recombinant laccase from Pediococcus acidilactici CECT 5930 with ability to degrade tyramine.
Article in PloS one, 2017. 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, 49 citations in OpenAlex.
- Bacterial laccases for green remediation of contaminants of emerging concern: from molecular cloning to metagenomic and computational insights.Biodegradation · 2026Review
- Beyond enzyme engineering: ordered enzyme immobilization drives enhanced productivityFrontiers in bioengineering and biotechnology · 2026Article
- Laccases from lactic acid bacteria show cuprous oxidase activity and capture Cu(II) and Ag(I) ions.Protein science : a publication of the Protein Society · 2026Article
- Screening of Lactic Acid Bacteria Strains for Potential Sourdough and Bread Applications: Enzyme Expression and Exopolysaccharide Production.Probiotics and antimicrobial proteins · 2025Article
- Leveraging bacterial laccases to facilitate the decomposition of xenobiotic compounds: a review.3 Biotech · 2024Review
- Biochemical and Structural Characterization of a Novel Psychrophilic Laccase (Multicopper Oxidase) Discovered fromInternational journal of molecular sciences · 2024Article
- Compositional Changes in the Gut Microbiota of Responders and Non-responders to Probiotic Treatment Among Patients With Diarrhea-predominant Irritable Bowel Syndrome: A Post Hoc Analysis of a Randomized Clinical Trial.Journal of neurogastroenterology and motility · 2022Article
- Structural analysis and biochemical properties of laccase enzymes from two Pediococcus species.Microbial biotechnology · 2021Article
- Probiotic properties of a phytase producing Pediococcus acidilactici strain SMVDUDB2 isolated from traditional fermented cheese product, Kalarei.Scientific reports · 2020Article
- Laccases: structure, function, and potential application in water bioremediation.Microbial cell factories · 2019Review
- Bacterial laccases: promising biological green tools for industrial applications.Cellular and molecular life sciences : CMLS · 2018Review
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Biogenic amines degradation by bacterial laccases is little known, so we have cloned and heterologously expressed, in E. coli, a new laccase from Pediococcus acidilactici CECT 5930 (Lpa5930), a lactic acid bacterium commonly found in foods able to degrade tyramine. The recombinant enzyme has been characterized by physical and biochemical assays. Here we report the optimization of expression and purification procedures of this laccase. DNA encoding sequence of laccase from P. acidilactici was amplified by PCR and cloned into the expression plasmid pET28a for induction by isopropyl-β-D-thiogalactoipyranoside. Protein expression was performed in E. coli BL21(DE3) harboring pGro7 plasmid expressing a chaperone folding assistant induced by arabinose. Purification was performed by column metal-chelating chromatography on Ni-NTA-agarose. The laccase enzyme obtained has an apparent molecular mass of ∼60 kDa, an optimum temperature activity toward 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) of 28°C, and was quickly inactivated at temperatures higher than 70°C. The apparent Km value for ABTS was 1.7 mM and the Vmax obtained was 24 U/mg. In addition to ABTS, recombinant Lpa5930 laccase degraded the biogenic amine tyramine at pH 9.5 and pH 4.0 with or without ABTS as a mediator. Tyramine degradation by laccases could solve the problems generated in food due to the presence of this toxic compound.
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