ArticleMicrobial cell factories2005
Industrial-scale production and purification of a heterologous protein in Lactococcus lactis using the nisin-controlled gene expression system NICE: the case of lysostaphin.
Article in Microbial cell factories, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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45 citing papers in PubMed, 111 citations in OpenAlex.
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- Functional expression and secretion of basic fibroblast growth factor inFrontiers in bioengineering and biotechnology · 2025Article
- Optimization of growth conditions and the inducer concentration for increasing spike protein expression in recombinantBioscience of microbiota, food and health · 2025Article
- Antimicrobial peptidase lysostaphin at subinhibitory concentrations modulates staphylococcal adherence, biofilm formation, and toxin production.BMC microbiology · 2023Article
- Lactococcus lactis, a bacterium with probiotic functions and pathogenicity.World journal of microbiology & biotechnology · 2023Review
- Lactiplantibacillus plantarum as a novel platform for production and purification of integral membrane proteins using RseP as the benchmark.Scientific reports · 2023Article
- Self-cleaved expression of recombinant lysostaphin from its cellulose binding domain fusion.Applied microbiology and biotechnology · 2022Article
- Biomaterial-based delivery of antimicrobial therapies for the treatment of bacterial infections.Nature reviews. Materials · 2022Article
- Heterologous production of active form of beta-lytic protease by Bacillus subtilis and improvement of staphylolytic activity by protein engineering.Microbial cell factories · 2021Article
- Functional Expression and Characterization of the Highly Promiscuous Lanthipeptide Synthetase SyncM, Enabling the Production of Lanthipeptides with a Broad Range of Ring Topologies.ACS synthetic biology · 2021Article
- Plasmid Replicons for the Production of Pharmaceutical-Grade pDNA, Proteins and Antigens byInternational journal of molecular sciences · 2021Review
- Design and High Expression of Non-glycosylated Lysostaphins inFrontiers in microbiology · 2021Article
- Surface Display of Heterologous β-Galactosidase in Food-Grade Recombinant Lactococcus lactis.Current microbiology · 2018Article
- The Lactococcus lactis KF147 nonribosomal peptide synthetase/polyketide synthase system confers resistance to oxidative stress during growth on plant leaf tissue lysate.MicrobiologyOpen · 2018Article
- Lactic Acid Bacteria for Delivery of Endogenous or Engineered Therapeutic Molecules.Frontiers in microbiology · 2018Review
- Development and evaluation of an efficient heterologous gene knock-in reporter system in Lactococcus lactis.Microbial cell factories · 2017Article
- Enhanced heterologous protein productivity by genome reduction in Lactococcus lactis NZ9000.Microbial cell factories · 2017Article
- RecombinantBioMed research international · 2017Article
- Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe NIsin-Controlled gene Expression system NICE of Lactococcus lactis is one of the most widespread used expression systems of Gram-positive bacteria. It is used in more than 100 laboratories for laboratory-scale gene expression experiments. However, L. lactis is also a micro-organism with a large biotechnological potential. Therefore, the aim of this study was to test whether protein production in L. lactis using the NICE system can also effectively be performed at the industrial-scale of fermentation.
resultsLysostaphin, an antibacterial protein (mainly against Staphylococcus aureus) from S. simulans biovar. Staphylolyticus, was used as a model system. Food-grade lysostaphin expression constructs in L. lactis were grown at 1L-, 300-L and 3000-L scale and induced with nisin for lysostaphin production. The induction process was equally effective at all scales and yields of about 100 mg/L were obtained. Up-scaling was easy and required no specific effort. Furthermore, we describe a simple and effective way of downstream processing to obtain a highly purified lysostaphin, which has been used for clinical phase I trials.
conclusionThis is the first example that shows that nisin-regulated gene expression in L. lactis can be used at industrial scale to produce large amounts of a target protein, such as lysostaphin. Downstream processing was simple and in a few steps produced a highly purified and active enzyme.
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