2026-04-13T02:51:14Zhttps://recercat.cat/oai/requestoai:recercat.cat:20.500.12327/2062025-10-22T11:14:37Zcom_2072_4428com_2072_4427col_2072_487898
RECERCAT
author
Gifre-Renom, L.
author
Cano-Garrido, O.
author
Fàbregas, F.
author
Roca-Pinilla, R.
author
Seras-Franzoso, J.
author
Ferrer-Miralles, N.
author
Villaverde, A.
author
Bach, A.
author
Devant, M.
author
Arís, A.
author
Garcia-Fruitós, E.
other
Producció Animal
group
Producció de Remugants
2025-10-22T11:14:37Z
2025-10-22T11:14:37Z
2018-09-17
Gifre-Renom, L., O. Cano-Garrido, F. Fàbregas, R. Roca-Pinilla, J. Seras-Franzoso, N. Ferrer-Miralles, and A. Villaverde et al. 2018. "A New Approach To Obtain Pure And Active Proteins From Lactococcus Lactis Protein Aggregates". Scientific Reports 8 (1). Springer Nature America, Inc. doi:10.1038/s41598-018-32213-8.
2045-2322
http://hdl.handle.net/20.500.12327/206
https://doi.org/10.1038/s41598-018-32213-8
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 difcult-to-purify. Although Escherichia coli is
widely used for protein production, recombinant products must be co-purifed through costly processes
to remove lipopolysaccharide (LPS) and minimize adverse efects 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-specifc 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 afordable 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 difcult-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-efective and simple protocol with special relevance for difcult-to-purify or
highly aggregated proteins.
eng
Attribution 4.0 International
A new approach to obtain pure and active proteins from Lactococcus lactis protein aggregates
info:eu-repo/semantics/article