HEBERT Elvira Maria
congresos y reuniones científicas
ANTIMUTAGENIC EFFECT OF CASEIN HYDROLYSATES GENERATED BY THE CELL ENVELOPE PROTEINASE OF Lactobacillus delbrueckii subsp lactis CRL 581
ESPECHE TURBAY, B.; SAVOY DE GIORI, G.; HEBERT, E.M.
Egmond aan Zee, The Netherland
Simposio; NINETH SYMPOSIUM ON LACTIC ACID BACTERIA. GENETICS, METABOLISM AND APPLICATIONS.; 2008
Milk proteins are source of a wide range of biological activities that influence digestion, metabolic responses, growth and development of specific organs, and resistance to disease. Bioactive peptides are latent within the precursor protein, and can be released through proteolytic enzymes of lactic acid bacteria. Several small peptides with specific bioactivity have been found in hydrolysates of milk proteins. Among the different groups of bioactive peptides, antimutagenic peptides are receiving special attention due to their beneficial effects related to the high incidence of cancer in developed countries. The aim of this study was to investigate the potential release of antimutagenic peptides from a- and b-casein hydrolysates generated by the cell envelope associated proteinase of the cheese starter strain Lactobacillus delbrueckii subsp. lactis CRL 581. Non-proliferating cells of this microorganism were incubated with ¥á- and ¥â-caseins for 15 to 240 min at 40¨¬C. The suppression of a- and b- casein hydrolysates against the mutagenesis induced by 4-nitroquinoline-N-oxide (4-NQO), a direct-acting mutagen, on Salmonella typhimurium TA 98 and TA 100 (Ames test), was investigated. The inhibition percentage of mutagenesis was about 59% and 4% for ¥á- and ¥â-casein hydrolysates, respectively, after 30 min of incubation. The highest inhibition values (98%) for both casein hydrolysates were observed after 240 min of incubation. The antimutagenic and anti-hypertensive properties exhibited by L. delbrueckii subsp. lactis CRL 581, together to its optimal technological performance, make this strain an excellent candidate for manufacturing functional foods.