Angiotensin Converting Enzyme Inhibitory Peptides Derived from Food Proteins: Biochemistry, Bioactivity and Production

Abstract

Food proteins contain latent biofunctional peptide sequences within their primary structures which may have the ability to exert a physiological response in vivo. A large range of biofunctional peptides have been isolated from food proteins including opioid, immunomodulatory, antimicrobial, mineral binding, growth and muscle stimulating, anti-cancer, proteinase and angiotensin converting enzyme (ACE, EC 3.4.15.1) inhibitory peptides. The biofunctional peptide activity currently most studied in food proteins appears to be those that inhibit ACE. ACE plays a central role in the regulation of blood pressure (BP) through the production of the potent vasoconstrictor, angiotensin (Ang) II , and the degradation of the vasodilator, bradykinin (BK). ACE inhibitory peptides may therefore have the ability to lower BP in vivo by limiting the vasoconstrictory effects of Ang II and by potentiating the vasodilatory effects of BK. These ACE inhibitory peptides can be enzymatically released from intact proteins in vitro and in vivo during food processing and gastrointestinal digestion, respectively. ACE inhibitory peptides may be generated in or incorporated into functional foods in the development of 'natural' beneficial health products. Several products are currently on the market or are in development that contain peptide sequences which have ACE inhibitory properties. Detailed human studies are required in order to demonstrate the efficacy of these bioactive peptides prior to their widespread utilisation as physiologically beneficial functional foods/food ingredients.

In silico analysis and antihypertensive effect of ACE-inhibitory peptides from smooth-hound viscera protein hydrolysate: Enzyme-peptide interaction study using molecular docking simulation

“…In addition, PRGPAGPHGPP contains the sequence GPP, previously identified as ACE inhibitor and antioxidant peptide [49,50].…”

Contribution of Leu and Hyp residues to antioxidant and ACE-inhibitory activities of peptide sequences isolated from squid gelatin hydrolysate

“…Although the structure-activity relationship of food derived ACE inhibitory peptides has not yet been fully established, correlation among different peptide inhibitors of ACE indicate that binding to this enzyme is strongly influenced by the C-terminal tripeptide sequence of the substrate or inhibitor. ACE appears to prefer substrates or competitive inhibitors that mainly have hydrophobic (aromatic or branched side chains) amino acid residues at the three Cterminal positions (Murray & FitzGerald, 2007). Therefore, the presence of Leu and Gly in peptide I at the second and third positions from carboxyl-terminus seems to play an important role in the ACE inhibitory activity.…”

“…Regarding the ACE-inhibitory activity, binding to ACE is strongly influenced by the C-terminal tripeptide sequence. Although the structure-activity relationship of food derived ACE inhibitory peptides has not yet been fully established, ACE prefers inhibitors containing hydrophobic amino acid residues at each of the three C-terminal positions (Murray & FitzGerald, 2007).…”

Blood pressure lowering effect of lactotripeptides assumed as functional foods: a meta-analysis of current available clinical trials

“…9 In particular, these peptides, that are encrypted within the primary structure of milk proteins and can be released by enzymatic hydrolysis either during gastrointestinal digestion or during food processing, have been reported to exert some angiotensin-converting enzyme inhibitory activity. 10 A detailed description of the individual milk proteins displaying in vitro angiotensin-converting enzyme-inhibitory activity is outside the purposes of this review and is reviewed elsewhere. 11 However, the best characterized peptides are those found in the fermented milk and bearing the aminoacid sequence isoleucine-proline-proline (IPP) and valine-proline-proline (VPP).…”