Antihypertensive peptides from animal products, marine organisms, and plants

•ACE-inhibitory activity is related to the degree of enzymatic hydrolysis and peptide sequence.•Optimal hydrolysis enzymes for animal products are pepsin, trypsin and chymotrypsin.•Optimal hydrolysis enzymes for marine organisms and plants are alcalase, neutrase and thermolysin.•ACE-inhibitory peptides are composed of hydrophobic amino acids at the N-terminus and proline.

Bioactive peptides from food proteins exert beneficial effects on human health, such as angiotensin-converting enzyme (ACE) inhibition and antihypertensive activity. Several studies have reported that ACE-inhibitory peptides can come from animal products, marine organisms, and plants-derived by hydrolyzing enzymes such as pepsin, chymotrypsin, and trypsin-and microbial enzymes such as alcalase, thermolysin, flavourzyme, and proteinase K. Different ACE-inhibitory effects are closely related with different peptide sequences and molecular weights. Sequences of ACE-inhibitory peptides are composed of hydrophobic (proline) and aliphatic amino acids (isoleucine and leucine) at the N-terminus. As result of this review, we assume that low molecular weight peptides have a greater ACE inhibition because lower molecular weight peptides have a higher absorbency in the body. Therefore, the ACE-inhibitory effect is closely related with the degree of enzymatic hydrolysis and the composition of the peptide sequence.