Summary
Lactococcus lactis
is a bacteria with high biotechnological potential, where is frequently used in the amino acid production and production of fermented dairy products, as well as drug delivery systems and mucosal vaccine vector. The knowledge of a functional core proteome is important extremely for both fundamental understanding of cell functions and for synthetic biology applications. In this study, we characterized the
L. lacits
proteome from proteomic analysis of four biotechnological strains
L. lactis
:
L. lactis
subsp.
lactis
NCDO
2118,
L. lactis
subsp.
lactis
IL
1403,
L. lactis
subsp.
cremoris
NZ
9000 and
L. lactis
subsp.
cremoris
MG
1363. Our label‐free quantitative proteomic analysis of the whole bacterial lysates from each strains resulted in the characterization of the
L. lactis
core proteome that was composed by 586 proteins, which might contribute to resistance of this bacterium to different stress conditions as well as involved in the probiotic characteristic of
L. lactis
. Kegg enrichment analysis shows that ribosome, metabolic pathways, pyruvate metabolism and microbial metabolism in diverse environments were the most enriched. According to our quantitative proteomic analysis, proteins related to translation process were the more abundant in the core proteome, which represent an important step in the synthetic biology. In addition, we identified a subset of conserved proteins that are exclusive of the
L. lactis
subsp.
cremoris
or
L. lactis
subsp.
lactis
, which some are related to metabolic pathway exclusive. Regarding specific proteome of
NCDO
2118, we detected ‘strain‐specific proteins’. Finally, proteogenomics analysis allows the identification of proteins, which were not previously annotated in
IL
1403 and
MG
1363. The results obtained in this study allowed to increase our knowledge about the biology of
L. lactis
, which contributes to the implementation of strategies that make it possible to increase the biotechnological potential of this bacterium.