{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,28]],"date-time":"2026-03-28T07:24:09Z","timestamp":1774682649050,"version":"3.50.1"},"reference-count":39,"publisher":"MDPI AG","issue":"24","license":[{"start":{"date-parts":[[2022,12,12]],"date-time":"2022-12-12T00:00:00Z","timestamp":1670803200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Evaluation of characteristic and advantageous agricultural products in Gansu Province","award":["2021HXKFSWXY012"],"award-info":[{"award-number":["2021HXKFSWXY012"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecules"],"abstract":"<jats:p>Angiotensin-I-converting enzyme (ACE) inhibitors are used extensively to control hypertension. In this study, a computer-assisted experimental approach was used to screen ACE-inhibiting peptides from X. sorbifolum seed meal (XSM). The process conditions for XSM hydrolysis were optimized through the orthogonal experimental method combined with a database. The optimal conditions for ACE inhibition included an alkaline protease dose of 5%, 45 \u00b0C, 15 min and pH 9.5. The hydrolysate was analyzed by LC-MS\/MS, and 10 optimal peptides were screened. Molecular docking results revealed four peptides (GGLPGFDPA, IMAVLAIVL, ETYFIVR, and INPILLPK) with ACE inhibitory potential. At 0.1 mg\/mL, the synthetic peptides GGLPGFDPA, ETYFIVR, and INPILLPK provided ACE inhibition rates of 24.89%, 67.02%, and 4.19%, respectively. GGLPGFDPA and ETYFIVR maintained high inhibitory activities during in vitro digestions. Therefore, the XSM protein may be a suitable material for preparing ACE inhibitory peptides, and computer-assisted experimental screening is an effective, accurate and promising method for discovering new active peptides.<\/jats:p>","DOI":"10.3390\/molecules27248792","type":"journal-article","created":{"date-parts":[[2022,12,12]],"date-time":"2022-12-12T05:10:19Z","timestamp":1670821819000},"page":"8792","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":4,"title":["Screening and Mechanism of Novel Angiotensin-I-Converting Enzyme Inhibitory Peptides in X. sorbifolia Seed Meal: A Computer-Assisted Experimental Study Method"],"prefix":"10.3390","volume":"27","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-9062-4914","authenticated-orcid":false,"given":"Yihan","family":"Mu","sequence":"first","affiliation":[{"name":"College of Biological Sciences and Biotechnology, Beijing Forestry University, Beijing 100083, China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Dongwei","family":"Liu","sequence":"additional","affiliation":[{"name":"College of Biological Sciences and Biotechnology, Beijing Forestry University, Beijing 100083, China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Huaping","family":"Xie","sequence":"additional","affiliation":[{"name":"Urban and Rural Development Research Center, Beijing 100835, China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Xinyu","family":"Zhang","sequence":"additional","affiliation":[{"name":"College of Biological Sciences and Biotechnology, Beijing Forestry University, Beijing 100083, China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Xue","family":"Han","sequence":"additional","affiliation":[{"name":"College of Biological Sciences and Biotechnology, Beijing Forestry University, Beijing 100083, China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Zhaolin","family":"Lv","sequence":"additional","affiliation":[{"name":"College of Biological Sciences and Biotechnology, Beijing Forestry University, Beijing 100083, China"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2022,12,12]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"1622","DOI":"10.1016\/j.procbio.2016.07.006","article-title":"Angiotensin-i-converting enzyme (ace) inhibitory peptides from pacific cod skin gelatin using ultrafiltration membranes","volume":"51","author":"Ngo","year":"2016","journal-title":"Process Biochem."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"98","DOI":"10.1016\/j.foodchem.2018.02.107","article-title":"Identification of a novel ACE-inhibitory peptide from casein and evaluation of the inhibitory mechanisms","volume":"256","author":"Tu","year":"2018","journal-title":"Food Chem."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"423","DOI":"10.1016\/j.foodchem.2016.05.087","article-title":"Purification and characterisation of a novel angiotensin-I converting enzyme (ACE)-inhibitory peptide derived from the enzymatic hydrolysate of Enteromorpha clathrata protein","volume":"211","author":"Pan","year":"2016","journal-title":"Food Chem."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"350","DOI":"10.1016\/j.foodchem.2008.03.074","article-title":"Angiotensin I-converting enzyme (ACE) inhibitory activities of sardinelle (Sardinella aurita) by-products protein hydrolysates obtained by treatment with microbial and visceral fish serine proteases","volume":"111","author":"Bougatef","year":"2008","journal-title":"Food Chem."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"870","DOI":"10.1016\/j.foodchem.2009.05.080","article-title":"A HPLC-UV method for the determination of angiotensin I-converting enzyme (ACE) inhibitory activity","volume":"118","author":"Karine","year":"2010","journal-title":"Food Chem."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1016\/j.idairyj.2006.06.023","article-title":"Preparation of ingredients containing an ace-inhibitory peptide by tryptic hydrolysis of whey protein concentrates","volume":"17","author":"Ferreira","year":"2007","journal-title":"Int. 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