Journal
FOODS
Volume 11, Issue 8, Pages -Publisher
MDPI
DOI: 10.3390/foods11081157
Keywords
Streptococcus thermophilus; cell surface proteins; tryptic hydrolysis; anti-inflammatory
Categories
Funding
- Ministere de l'Enseignement Superieur, de la Recherche et de l'Innovation
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This study found that peptides released from the surface proteins of Streptococcus thermophilus have anti-inflammatory activity by decreasing the secretion of pro-inflammatory cytokines and reducing the expression levels of inflammation-related proteins. These findings suggest that this bacterium may have potential anti-inflammatory effects and could help prevent low-grade inflammation.
Streptococcus thermophilus, a lactic acid bacterium widely used in the dairy industry, is consumed regularly by a significant proportion of the population. Some strains show in vitro anti-inflammatory activity which is not fully understood. We hypothesized that peptides released from the surface proteins of this bacterium during digestion could be implied in this activity. Consequently, we prepared a peptide hydrolysate by shaving and hydrolysis of surface proteins using trypsin, and the origin of peptides was checked by liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis. Most of the identified peptides originated from bacterial cell surface proteins. The anti-inflammatory activity of peptide hydrolysate was investigated under inflammatory conditions in two cell models. Peptide hydrolysate significantly decreased secretion of pro-inflammatory cytokine IL-8 in lipopolysaccharide (LPS)-stimulated human colon epithelial HT-29 cells. It also reduced the production of pro-inflammatory cytokines IL-8, IL-1 beta and the protein expression levels of Pro-IL-1 beta and COX-2 in LPS-stimulated THP-1 macrophages. The results showed that peptides released from bacterial surface proteins by a pancreatic protease could therefore participate in an anti-inflammatory activity of S. thermophilus LMD-9 and could prevent low-grade inflammation.
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