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The major protein fractions in bovine milk include α-LA (lactalbumine), β-LG (lactoglobuline), caseins, immunoglobulins, lactoferrin, proteose-peptide fractions (heat-stable, acid soluble phosphoglycoproteins), and minor whey proteins such as transferrin and serum albumin.
It is well established that in vitro incubation of these milk proteins with gastrointestinal proteinase preparations enriched in pepsin, trypsin, and chymotrypsin activities results in the release numerous active peptides. Therefore it is likely that bioactive (antihypertensive and other physiologically active) peptides are generated during gastrointestinal transport.
Bacterial and plant proteinases can also be used to release active peptides. Therefore hydrolysates of whole milk protein, caseinates, whey proteins, and fractions enriched milk proteins are potentially good sources of bioactive peptides. There is considerable evidence that many bioactive peptides serve in multifunctional capacities and often share common structural features based on a defined, biospecific role.
Often, these peptides display multifunctional properties. Current knowledge on the identified physiological roles of functional peptides of milk makes it possible to distinguish six main effects:
• hypotensive,
• antithrombotic,
• calcium & minerals transport,
• immunomodulation,
• opioid like,
• antimicrobial.
These functions are detailed in the study as well as their market applications and their evaluation by industrial users.
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