ArticleScientific reports2018
A new approach to obtain pure and active proteins from Lactococcus lactis protein aggregates.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 36 citations in OpenAlex.
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- Immunomodulation Evidence of Nanostructured Recombinant Proteins in Salmonid Cells.Animals : an open access journal from MDPI · 2024Article
- Lactiplantibacillus plantarum: a new example of inclusion body producing bacteria.Microbial cell factories · 2023Article
- The future of recombinant host defense peptides.Microbial cell factories · 2022Review
- Potential of Oral Nanoparticles Containing Cytokines as Intestinal Mucosal Immunostimulants in Pigs: A Pilot Study.Animals : an open access journal from MDPI · 2022Article
- Adenovirus Fibers as Ultra-Stable Vehicles for Intracellular Nanoparticle and Protein Delivery.Biomolecules · 2022Article
- Overcoming the Solubility Problem in E. coli: Available Approaches for Recombinant Protein Production.Methods in molecular biology (Clifton, N.J.) · 2022Review
- Recombinant Protein Production and Purification of Insoluble Proteins.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Solubilization and Refolding of Inclusion Body Proteins.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Toxicity Profiling of Bacterial Inclusion Bodies in Human Caco-2 Cells.Frontiers in bioengineering and biotechnology · 2022Article
- Exploring the RNase A scaffold to combine catalytic and antimicrobial activities. Structural characterization of RNase 3/1 chimeras.Frontiers in molecular biosciences · 2022Article
- Sequence edition of single domains modulates the final immune and antimicrobial potential of a new generation of multidomain recombinant proteins.Scientific reports · 2021Article
- Host Defence RNases as Antiviral Agents against Enveloped Single Stranded RNA Viruses.Virulence · 2021Review
- Selecting Subpopulations of High-Quality Protein Conformers among Conformational Mixtures of Recombinant Bovine MMP-9 Solubilized from Inclusion Bodies.International journal of molecular sciences · 2021Article
- Coiled-Coil Based Inclusion Bodies and Their Potential Applications.Frontiers in bioengineering and biotechnology · 2021Review
- Catalytically-active inclusion bodies for biotechnology-general concepts, optimization, and application.Applied microbiology and biotechnology · 2020Review
- A new generation of recombinant polypeptides combines multiple protein domains for effective antimicrobial activity.Microbial cell factories · 2020Article
- Recombinant Protein-Based Nanoparticles: Elucidating their Inflammatory Effects In Vivo and their Potential as a New Therapeutic Format.Pharmaceutics · 2020Article
- The Biological Potential Hidden in Inclusion Bodies.Pharmaceutics · 2020Article
Corrections and comments
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Authors and funding
11 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The production of pure and soluble proteins is a complex, protein-dependent and time-consuming process, in particular for those prone-to-aggregate and/or difficult-to-purify. Although Escherichia coli is widely used for protein production, recombinant products must be co-purified through costly processes to remove lipopolysaccharide (LPS) and minimize adverse effects in the target organism. Interestingly, Lactococcus lactis, which does not contain LPS, could be a promising alternative for the production of relevant proteins. However, to date, there is no universal strategy to produce and purify any recombinant protein, being still a protein-specific process. In this context and considering that L. lactis is also able to form functional protein aggregates under overproduction conditions, we explored the use of these aggregates as an alternative source of soluble proteins. In this study, we developed a widely applicable and economically affordable protocol to extract functional proteins from these nanoclusters. For that, two model proteins were used: mammary serum amyloid A3 (M-SAA3) and metalloproteinase 9 (MMP-9), a difficult-to-purify and a prone-to-aggregate protein, respectively. The results show that it is possible to obtain highly pure, soluble, LPS-free and active recombinant proteins from L. lactis aggregates through a cost-effective and simple protocol with special relevance for difficult-to-purify or highly aggregated proteins.
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