Molecular Localization of Health-Promoting Peptides Derived from Fish Protein Hydrolyzates on Fish Muscle Proteins

Abstract

The four previously reported health-promoting dipeptides, valine-tyrosine, lysine-tryptophan, methionine-phenylalanine, and arginine-isoleucine, found in the fish muscle hydrolyzates, were mainly located in the myosin subfragment-1 heavy chain, whereas the health-promoting tripeptide, alanine-lysine-lysine, was found in the fibrous rod consisting of the myosin subfragment-2 and light meromyosin with a regular coiled-coil structure of α-helix, irrespective of the fish species. Furthermore, the localization of these peptides either in the random coil, β-sheet, or α-helix was also examined in the three-dimensional image, showing no specific tendency. Surprisingly, the same trend was observed even for the mammalian rabbit fast muscle myosin heavy chain. Since a trade-off between myofibrillar ATPase and structural stability has been reported for fish living at low environmental temperatures, it is speculated that fish muscle proteins, when ingested, are easily digested by various proteases in the human digestive tract and provide various health-promoting peptides also in vivo. While fish actin contained only two dipeptides, methionine-phenylalanine and valine-tyrosine, glyceraldehyde 3-phosphate dehydrogenase, one of the major components of fish muscle water-soluble protein, contained all of the four dipeptides and one tripeptide mentioned above.