{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,9]],"date-time":"2026-07-09T04:44:11Z","timestamp":1783572251839,"version":"3.55.0"},"reference-count":41,"publisher":"Wiley","issue":"10","license":[{"start":{"date-parts":[[2017,8,23]],"date-time":"2017-08-23T00:00:00Z","timestamp":1503446400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/501100008798","name":"Ministry of Science, Research and Technology","doi-asserted-by":"crossref","id":[{"id":"10.13039\/501100008798","id-type":"DOI","asserted-by":"crossref"}]},{"name":"Research Council of University of Tehran"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal of Food Science"],"published-print":{"date-parts":[[2017,10]]},"abstract":"<jats:sec>\n                    <jats:title>Abstract<\/jats:title>\n                    <jats:p>\n                      In this study, the production, fractionation, purification and identification of ACE (angiotensin\u2010I\u2010converting enzyme) inhibitory peptides from wild almond (\n                      <jats:italic>Amygdalus scoparia<\/jats:italic>\n                      ) proteins were investigated. Wild almond proteins were hydrolyzed using 5 different enzymes (pepsin, trypsin, chymotrypsin, alcalase and flavourzyme) and assayed for their ACE inhibitory activities. The degree of ACE inhibiting activity obtained after hydrolysis was found to be in the following order: alcalase &gt; chymotrypsin &gt; trypsin\/pepsin &gt; flavourzyme. The hydrolysates obtained from alcalase (IC\n                      <jats:sub>50<\/jats:sub>\n                      = 0.8 mg\/mL) were fractionated by sequential ultrafiltration at 10 and 3 kDa cutoff values and the most active fraction (&lt;3 kDa) was further separated using reversed phase high\u2010performance liquid chromatography (RP\u2010HPLC). Peptide sequence identifications were carried out on highly potential fractions obtained from RP\u2010HPLC by means of liquid chromatography coupled to electrospray ionization and tandem mass spectrometry (LC\u2010ESI\u2010MS\/MS). Sequencing of ACE inhibitory peptides present in the fraction 26 of RP\u2010HPLC resulted in the identification of 3 peptide sequences (VVNE, VVTR, and VVGVD) not reported previously in the literature. Sequence identification of fractions 40 and 42 from RP\u2010HPLC, which showed the highest ACE inhibitory activities (84.1% and 86.9%, respectively), resulted in the identification of more than 40 potential ACE inhibitory sequences. The results indicate that wild almond protein is a rich source of potential antihypertensive peptides and can be suggested for applications in functional foods and drinks with respect to hindrance and mitigation of hypertension after\n                      <jats:italic>in vivo<\/jats:italic>\n                      assessment.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Practical Application<\/jats:title>\n                    <jats:p>This study has shown the potential of wild almond proteins as good sources for producing ACE\u2010inhibitory active peptides. According to this finding, peptides with higher ACE inhibitory activities could be released during the gastrointestinal digestion and contribute to the health\u2010 promoting activities of this natural protein source.<\/jats:p>\n                  <\/jats:sec>","DOI":"10.1111\/1750-3841.13840","type":"journal-article","created":{"date-parts":[[2017,8,23]],"date-time":"2017-08-23T06:52:42Z","timestamp":1503471162000},"page":"2421-2431","source":"Crossref","is-referenced-by-count":51,"title":["Identification of Potent ACE Inhibitory Peptides from Wild Almond Proteins"],"prefix":"10.1111","volume":"82","author":[{"given":"Mozhgan","family":"Mirzapour","sequence":"first","affiliation":[{"name":"Dept. of Food Science, Engineering and Technology Univ. of Tehran  Karaj 31587\u201377871 Iran"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3503-0659","authenticated-orcid":false,"given":"Karamatollah","family":"Rezaei","sequence":"additional","affiliation":[{"name":"Dept. of Food Science, Engineering and Technology Univ. of Tehran  Karaj 31587\u201377871 Iran"},{"name":"Center of Excellence for Application of Modern Technologies for Producing Functional Foods and Drinks Univ. of Tehran  Karaj 31587\u201377871 Iran"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Miguel Angel","family":"Sentandreu","sequence":"additional","affiliation":[{"name":"Inst. de Agroqu\u00edmica y Tecnolog\u00eda de Alimentos (CSIC)  Avd. 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