Plant food-derived Angiotensin I converting enzyme inhibitory peptides

J Agric Food Chem. 2009 Jun 24;57(12):5113-20. doi: 10.1021/jf900494d.


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.

Publication types

  • Review

MeSH terms

  • Angiotensin-Converting Enzyme Inhibitors / chemistry
  • Angiotensin-Converting Enzyme Inhibitors / isolation & purification
  • Angiotensin-Converting Enzyme Inhibitors / pharmacology*
  • Animals
  • Antihypertensive Agents / chemistry
  • Antihypertensive Agents / isolation & purification
  • Antihypertensive Agents / pharmacology*
  • Food Analysis*
  • Humans
  • Hypertension / drug therapy*
  • Peptides / chemistry
  • Peptides / isolation & purification
  • Peptides / pharmacology
  • Peptidyl-Dipeptidase A / metabolism
  • Plants / chemistry*


  • Angiotensin-Converting Enzyme Inhibitors
  • Antihypertensive Agents
  • Peptides
  • Peptidyl-Dipeptidase A