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ACE\u2010inhibitory peptides can be obtained from edible proteins and have the function of antihypertension. The amino acid sequences and the secondary structures of ACE\u2010inhibitory peptides determine the inhibitory activities and stability. The resistance of ACE\u2010inhibitory peptides to digestive enzymes and peptidase affect their antihypertensive bioactivity\n                    <jats:italic>in vivo<\/jats:italic>\n                    . In this paper, the mechanism of ACE\u2010inhibition, sources of the inhibitory peptides, structure\u2013activity relationships, stability during digestion, absorption and transportation of ACE\u2010inhibitory peptides, and consumption of ACE\u2010inhibitory peptides are reviewed, which provide guidance to the development of new functional foods and production of antihypertensive nutraceuticals and pharmaceuticals.\n                  <\/jats:p>","DOI":"10.1111\/1541-4337.12711","type":"journal-article","created":{"date-parts":[[2021,2,3]],"date-time":"2021-02-03T19:59:58Z","timestamp":1612382398000},"page":"1150-1187","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":160,"title":["Activity and bioavailability of food protein\u2010derived angiotensin\u2010I\u2010converting enzyme\u2013inhibitory peptides"],"prefix":"10.1111","volume":"20","author":[{"given":"Lu","family":"Xue","sequence":"first","affiliation":[{"name":"College of 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