β-Casein hydrolysate generated by the cell envelope-associated proteinase of Lactobacillus delbrueckii ssp. lactis CRL 581 protects against trinitrobenzene sulfonic acid-induced colitis in mice

• Published in: Journal of dairy science 2012-03, Vol.95 (3), p.1108-1118
• Main Authors: Espeche Turbay, M.B., de Moreno de LeBlanc, A., Perdigón, G., Savoy de Giori, G., Hebert, E.M.
• Format: Article
• Language: English
• Subjects: animal models; Animal productions; Animals; anti-inflammatory activity; Antimutagenic Agents - pharmacology; beta-casein; beta-glucuronidase; bioactive peptide; Biological and medical sciences; casein hydrolysate; casein hydrolysates; Caseins - pharmacology; Caseins - therapeutic use; colitis; Colitis - chemically induced; Colitis - prevention & control; Crohn disease; Disease Models, Animal; Female; fermented dairy products; Food industries; Food microbiology; functional foods; Fundamental and applied biological sciences. Psychology; Glucuronidase - metabolism; hydrolysates; hydrolysis; inflammation; interferon-gamma; interleukin-10; lactic acid bacteria; Lactobacillus delbrueckii - metabolism; Lactobacillus delbrueckii subsp. lactis; liver; manufacturing; Mice; Mice, Inbred BALB C; mortality; mutagenesis; mutagenicity; Mutagenicity Tests; myeloperoxidase; peptides; Peroxidase - metabolism; Protein Hydrolysates - pharmacology; Protein Hydrolysates - therapeutic use; proteinase; proteinases; proteolysis; Salmonella typhimurium; starter cultures; sulfonic acid; Terrestrial animal productions; Trinitrobenzenesulfonic Acid - pharmacology; Vertebrates; weight loss
• ISSN: 0022-0302; 1525-3198
• DOI: 10.3168/jds.2011-4735

Lactobacillus delbrueckii ssp. lactis CRL 581, a thermophilic lactic acid bacterium used as a starter culture for the manufacture of several fermented dairy products, possesses an efficient proteolytic system that is able to release a series of potentially bioactive peptides (i.e., antihypertensive and phosphopeptides) from α- and β-caseins. Considering the potential beneficial health effects of the peptides released by L. delbrueckii ssp. lactis CRL 581 from milk proteins, the aim of this work was to analyze the anti-mutagenic and anti-inflammatory properties of the casein hydrolysates generated by the cell envelope-associated proteinase of this bacterium. The ability of α- and β-casein hydrolysates to suppress the mutagenesis of a direct-acting mutagen 4-nitroquinoline-N-oxide on Salmonella typhimurium TA 98 and TA 100 increased concomitantly with the time of casein hydrolysis. The anti-inflammatory effect of the β-casein hydrolysate was evaluated using a trinitrobenzene sulfonic acid (TNBS)-induced Crohn's disease murine model. The hydrolysate was administered to mice 10 d before the intrarectal inoculation of TNBS. The mice that received β-casein hydrolysate previously to TNBS showed decreased mortality rates, faster recovery of initial body weight loss, less microbial translocation to the liver, decreased β-glucuronidase and myeloperoxidase activities in the gut, and decreased colonic macroscopic and microscopic damage compared with the animals that did not receive this hydrolysate. In addition, β-casein hydrolysate exerted a beneficial effect on acute intestinal inflammation by increased interleukin 10 and decreased IFN-γ production in the gut. Our findings are consistent with the health-promoting attributes of the milk products fermented by L. delbrueckii ssp. lactis CRL 581 and open up new opportunities for developing novel functional foods.