{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,28]],"date-time":"2026-09-28T18:19:17Z","timestamp":1790619557059,"version":"4.1.0"},"reference-count":123,"publisher":"MDPI AG","issue":"4","license":[{"start":{"date-parts":[[2017,3,23]],"date-time":"2017-03-23T00:00:00Z","timestamp":1490227200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Nutrients"],"abstract":"<jats:p>Hypertension is an important factor in cardiovascular diseases. Angiotensin-I-converting enzyme (ACE) inhibitors like synthetic drugs are widely used to control hypertension. ACE-inhibitory peptides from food origins could be a good alternative to synthetic drugs. A number of plant-based peptides have been investigated for their potential ACE inhibitor activities by using in vitro and in vivo assays. These plant-based peptides can be obtained by solvent extraction, enzymatic hydrolysis with or without novel food processing methods, and fermentation. ACE-inhibitory activities of peptides can be affected by their structural characteristics such as chain length, composition and sequence. ACE-inhibitory peptides should have gastrointestinal stability and reach the cardiovascular system to show their bioactivity. This paper reviews the current literature on plant-derived ACE-inhibitory peptides including their sources, production and structure, as well as their activity by in vitro and in vivo studies and their bioavailability.<\/jats:p>","DOI":"10.3390\/nu9040316","type":"journal-article","created":{"date-parts":[[2017,3,23]],"date-time":"2017-03-23T11:47:59Z","timestamp":1490269679000},"page":"316","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":326,"title":["Angiotensin-I-Converting Enzyme (ACE)-Inhibitory Peptides from Plants"],"prefix":"10.3390","volume":"9","author":[{"given":"Ceren","family":"Daskaya-Dikmen","sequence":"first","affiliation":[{"name":"Department of Food Engineering, Faculty of Chemical and Metallurgical Engineering, Istanbul Technical University, Maslak, Istanbul 34469, Turkey"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Aysun","family":"Yucetepe","sequence":"additional","affiliation":[{"name":"Department of Food Engineering, Faculty of Chemical and Metallurgical Engineering, Istanbul Technical University, Maslak, Istanbul 34469, Turkey"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Funda","family":"Karbancioglu-Guler","sequence":"additional","affiliation":[{"name":"Department of Food Engineering, Faculty of Chemical and Metallurgical Engineering, Istanbul Technical University, Maslak, Istanbul 34469, Turkey"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0155-1387","authenticated-orcid":false,"given":"Hayrettin","family":"Daskaya","sequence":"additional","affiliation":[{"name":"Department of Anesthesia and Reanimation, Bezmialem Vakif University Medical Faculty, Istanbul 34093, Turkey"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Beraat","family":"Ozcelik","sequence":"additional","affiliation":[{"name":"Department of Food Engineering, Faculty of Chemical and Metallurgical Engineering, Istanbul Technical University, Maslak, Istanbul 34469, Turkey"},{"name":"BIOACTIVE Research &amp; Innovation Food Manufacturing Industry Trade LTD Co., Maslak, Istanbul 34469, Turkey"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2017,3,23]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"4568","DOI":"10.1021\/jf060264q","article-title":"Angiotensin I-Converting Enzyme Inhibitory Peptide Derived from Glycinin, the 11S Globulin of Soybean (Glycine Max)","volume":"54","author":"Gouda","year":"2006","journal-title":"J. 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