One of the promising directions in creating dietary and medical supplements is the use of protein hydrolysates from marine algae (both wild and artificially cultivated), which contain various short peptides. The description and analysis of the mechanisms of action of such peptides are provided in a recent review by S. Bleakley & M. Hayes (2017). A distinctive feature of algae is their high protein content with a complete amino acid profile, including BCAAs (branched-chain amino acids), and efficient digestion in the human and animal gastrointestinal tract.
The process of obtaining short peptides from algae, such as Chlorella vulgaris, can be achieved through enzymatic hydrolysis, with the degree of hydrolysis determining the length of the amino acid chain in the peptides—ranging from two to 30 amino acids. These include di-, tri-, and tetrapeptides containing crucial amino acids for sports, such as leucine-arginine-tyrosine, valine-glutamine-glycine, valine-tyrosine, alanine-isoleucine-tyrosine-lysine, phenylalanine-tyrosine, isoleucine-tryptophan, alanine-glutamine-leucine (sic!), and others. Importantly, these short peptides are exclusively derived from natural sources, which has practical significance. Peptides with antioxidant properties have been isolated from microalgae such as Chlorella vulgaris, Navicula incerta, and Chlorella ellipsoidea and some marine brown algae.