Bioactive peptides derived from casein and whey proteins

HEBERT, E.M.; SAAVEDRA, L.; FERRANTI, P.

Biotechnology of Lactic Acid Bacteria: Novel Applications

Wiley-Blackwell

Lugar: Iowa; Año: 2010; p. 233 - 249

Milk proteins have attracted more attention in the biological and medical research community not only because of their nutrient value but as substances which constantly supply the organisms with bioactive compounds. Bioactive peptides are hidden in a latent state within the primary sequences of casein and whey proteins, requiring enzymatic proteolysis for their release. Bioactive peptides can be produced during in vivo gastrointestinal digestion or food processing. Therefore, peptides with physiological effects are largely found in fermented milks and cheeses. The proteolytic system of lactic acid bacteria used as starter cultures in the manufacture of yoghurt, fermented milk and cheeses contributes to the release of bioactive peptides or precursor thereof. Antimicrobial, immunomodulatory, antithrombotic, opioid and antioxidant activities, enhancement of mineral absorption and/or bioavailability and a blood pressure-lowering (ACE inhibitory) effect are some of the biological activities attributed to milk derived peptides. Certain milk-derived peptides are commercially produced and these peptides are being used for its application as dietary supplementation in functional foods, personal products or drugs. The great complexity and the wide dynamic range of relative peptide abundance in these products severely challenge the capabilities of existing analytical methodologies. A major step forward in this field has been achieved by combining the biochemical and biological approach with the tools of proteomics technology. In this review, the most recent achievements will be presented, leading to a deeper definition of the structure-activity relationship in these complex peptide systems.