Recent trends in the analysis of bioactive peptides in milk and dairy products

Abstract

Food-derived constituents represent important sources of several classes of bioactive compounds. Among them peptides have gained great attention in the last two decades thanks to the scientific evidence of their beneficial effects on health in addition to their established nutritional value. Several functionalities for bioactive peptides have been described, including antioxidative, antihypertensive, anti-inflammatory, immunomodulatory, and antimicrobial activity. They are now considered as novel and potential dietary ingredients to promote human health, though in some cases they may also have detrimental effects on health. Bioactive peptides can be naturally occurring, produced in vitro by enzymatic hydrolysis, and formed in vivo during gastrointestinal digestion of proteins. Thus, the need to gain a better understanding of the positive health effects of food peptides has prompted the development of analytical strategies for their isolation, separation, and identification in complex food matrices. Dairy products and milk are potential sources of bioactive peptides: several of them possess extra-nutritional physiological functions that qualify them to be classified under the functional food label. In this trends article we briefly describe the state-of-the-art of peptidomics methods for the identification and discovery of bioactive peptides, also considering recent progress in their analysis and highlighting the difficulty in the analysis of short amino acid sequences and endogenous peptides

Learnings from quantitative structure–activity relationship (QSAR) studies with respect to food protein-derived bioactive peptides: a review

“…[5][6][7] However, advances in mass spectrometric (MS) analysis have allowed greater capability in the identication of peptides within complex mixtures and also identication of a large number of peptide sequences in an automated manner, for reviews, see: ref. [8][9][10][11]. Nevertheless, challenges such as the reliable identication of short peptide sequences (<5 amino acid residues) are still an issue for a more comprehensive understanding of dietary BAP structures.…”

Bioactive hydrolysates from casein: generation, identification, and in silico toxicity and allergenicity prediction of peptides

“…Casein is widely used as a functional ingredient in food products owing to its nutritional merits. [4][5][6] Casein has been considered to be a natural vehicle for bioactivities in drug delivery systems because of its particular structure and physicochemical properties. 7,8 Moreover, casein releases bioactive peptides with multiple activities of promoting health and preventing disease, such as antioxidant, antibacterial, anticoagulant, immunomodulatory, and angiotensin-converting-enzyme (ACE) inhibitory (ACEI) activity, through enzymatic hydrolysis, microbial fermentation, and other combined mechanisms.…”

Bioactive Peptides in Milk: From Encrypted Sequences to Nutraceutical Aspects

“…Processing techniques in laboratory and on industrial scale are now being developed for the extraction, fractionation and isolation of main proteins from milk [54][55][56][57], with particular attention to modern non-thermal, clean and green methodologies [58]. It is worth stressing, as already demonstrated by several studies, that each time a nutraceutical with potential health benefits is needed for a functional food, a specific enzymatic hydrolysis of milk proteins should be planned [59,60].…”