An overview of “omic” analytical methods applied in bioactive peptide studies

- Dietary proteins are a rich source of hidden bioactive peptides.
- Bioactive peptides can be produced during digestion or food processing.
- Lactic acid bacteria with technological properties might release bioactive peptides.
- The complexity and peptide abundance challenge the actual detection methodologies.
- New omic analytical methods will improve our knowledge on food-derived peptides.

Nowadays, there is an increased interest in health-promoting functional foods, whereby consumers hold higher expectations of health-promoting benefits beyond basic nutrition. Dietary proteins provide a rich source of bioactive peptides, which are hidden in a latent state within the native protein, requiring enzymatic proteolysis for their release. Bioactive peptides can be produced during in vivo gastrointestinal digestion and/or food processing. Lactic acid bacteria are among the most widely microorganisms used as starter cultures for the production of fermented foods, and through their proteolytic system, they contribute to the release of bioactive peptides from dietary proteins. In vitro and in vivo studies demonstrated several biological functions attributed to bioactive peptides, such as antimicrobial, immunomodulatory, enhancement of mineral absorption, antithrombotic, antihypertensive, opioid and antioxidant activities. The great complexity and the wide dynamic range of relative peptide abundance in these products severely challenge the capabilities of existing analytical methodologies. However, functional and comparative genomic studies as well as proteomic approaches provide a wealth of knowledge in the way in which these lactic acid bacteria can use food proteins releasing bioactive peptides.