Plant food-derived Angiotensin I converting enzyme inhibitory peptides.
Hypertension is one of the most common worldwide diseases that afflict humans. Angiotensin I converting enzyme (ACE) catalyzes the formation of vasoconstrictor, angiotensin II, and the inactivation of vasodilator, bradykinin. The influences of ACE on blood pressure make it an ideal target clinically and nutritionally in the treatment of hypertension. A number of animal food-derived peptides have been reviewed about their in vitro and in vivo ACE inhibitory activities. The aim of this review is to discuss the plant food-derived angiotensin I converting enzyme (ACE) inhibitory peptides from sources, production, purification, and structure to in vitro and in vivo activities.
Guang
Cuie
C
Department of Food Science and Technology, University of Georgia, Griffin, Georgia 30223-1797, USA.
Phillips
Robert D
RD
D000806:Angiotensin-Converting Enzyme Inhibitors / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology*; D000818:Animals; D000959:Antihypertensive Agents / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology*; D005504:Food Analysis; D006801:Humans; D006973:Hypertension / Q000188:drug therapy*; D010455:Peptides / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology; D007703:Peptidyl-Dipeptidase A / Q000378:metabolism; D010944:Plants / Q000737:chemistry*
D000806:Angiotensin-Converting Enzyme Inhibitors; D000959:Antihypertensive Agents; D010455:Peptides; D007703:Peptidyl-Dipeptidase A