Antihypertensive peptides from animal products, marine organisms, and plants.
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.
Department of Animal Science and Technology, Chung-Ang University, 4726 Seodong-daero, Daedeok-myeon, Anseong-si, Gyeonggi 17546, Republic of Korea.
Seung Yun
SY
Lee
Department of Animal Science and Technology, Chung-Ang University, 4726 Seodong-daero, Daedeok-myeon, Anseong-si, Gyeonggi 17546, Republic of Korea. Electronic address: hursj@cau.ac.kr.
Sun Jun
SJ
Hur
D000595:Amino Acid Sequence; D000806:Angiotensin-Converting Enzyme Inhibitors / Q000737:chemistry; D000818:Animals; D000959:Antihypertensive Agents / Q000737:chemistry*; D059001:Aquatic Organisms / Q000166:cytology* / Q000378:metabolism*; D010455:Peptides / Q000737:chemistry*
D000806:Angiotensin-Converting Enzyme Inhibitors; D000959:Antihypertensive Agents; D010455:Peptides
ACE-inhibitory peptide; Animal products; Enzymatic hydrolysis; Marine organisms; Peptide sequences; Plants