{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,28]],"date-time":"2026-09-28T18:19:46Z","timestamp":1790619586097,"version":"4.1.0"},"reference-count":68,"publisher":"MDPI AG","issue":"6","license":[{"start":{"date-parts":[[2019,6,15]],"date-time":"2019-06-15T00:00:00Z","timestamp":1560556800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"the National Science Council, Taiwan","award":["NSC96-2313-B-019-012"],"award-info":[{"award-number":["NSC96-2313-B-019-012"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Nutrients"],"abstract":"<jats:p>This research focuses on cobia skin hydrolysates and their antihypertensive effects via the inhibitory activities of angiotensin I-converting enzyme (ACE). Marine fish Cobia (Rachycentron canadum) skin was hydrolysed for 5 h using Protamex and Protease N to obtain the cobia skin protein hydrolysates PX-5 and PN-5, respectively. The soluble protein and peptide contents of the PX-5 were 612 and 270 mg\/g, respectively, and for the PN-5, 531 and 400 mg\/g, respectively. The IC50 of PX-5 and PN-5 on ACE was 0.221 and 0.291 mg\/mL, respectively. Increasing the IC50 from 0.221 to 0.044 mg\/mL by simulated gastrointestinal digestion (PX-5G) reduced the ACE-inhibitory capacity of PX-5. Using gel filtration chromatography, the PX-5G was fractioned into eight fractions. The molecular weight of the fifth fraction from PX-5G was between 630 and 450 Da, and the highest inhibitory efficiency ratio on ACE was 1552.4%\/mg\/mL. We identified four peptide sequences: Trp-Ala-Ala, Ala-Trp-Trp, Ile-Trp-Trp, and Trp-Leu, with IC50 values for ACE of 118.50, 9.40, 0.51, and 26.80 \u03bcM, respectively. At a dose of 600 mg PX-5 powder\/kg body weight, in spontaneously hypertensive rats PX-5\u2019s antihypertensive effect significantly reduced systolic and diastolic blood pressure by 21.9 and 15.5 mm Hg, respectively, after 4 h of oral gavage.<\/jats:p>","DOI":"10.3390\/nu11061351","type":"journal-article","created":{"date-parts":[[2019,6,17]],"date-time":"2019-06-17T03:24:41Z","timestamp":1560741881000},"page":"1351","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":45,"title":["Preparation and Identification of Novel Antihypertensive Peptides from the In Vitro Gastrointestinal Digestion of Marine Cobia Skin Hydrolysates"],"prefix":"10.3390","volume":"11","author":[{"given":"Yu-Hsin","family":"Lin","sequence":"first","affiliation":[{"name":"Department of Food Technology and Marketing, Taipei University of Marine Technology, No. 212, Section 9, Yan Ping North Road, Taipei 111, Taiwan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chun-An","family":"Chen","sequence":"additional","affiliation":[{"name":"Department of Food Science, National Taiwan Ocean University, No. 2 Pei-Ning Road, Keelung 202, Taiwan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jenn-Shou","family":"Tsai","sequence":"additional","affiliation":[{"name":"Department of Food Science, National Taiwan Ocean University, No. 2 Pei-Ning Road, Keelung 202, Taiwan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3435-0725","authenticated-orcid":false,"given":"Guan-Wen","family":"Chen","sequence":"additional","affiliation":[{"name":"Department of Food Science, National Taiwan Ocean University, No. 2 Pei-Ning Road, Keelung 202, Taiwan"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2019,6,15]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"1241","DOI":"10.1038\/3218","article-title":"The global burden of disease, 1990\u20132020","volume":"4","author":"Lopez","year":"1998","journal-title":"Nat. Med."},{"key":"ref_2","unstructured":"Taylor, M.D., and Amidon, G.L. (1995). Oral absorption of angiotensin-converting enzyme inhibitors and peptide prodrugs. Peptide-Based Drug Design, American Chemistry Society, NW."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1177\/106002809603000110","article-title":"Adverse effects of the angiotensin-converting enzyme inhibitors","volume":"30","author":"Alderman","year":"1996","journal-title":"Ann. Pharmacother."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1159\/000013573","article-title":"Acute tubular necrosis due to captopril","volume":"20","author":"Raweily","year":"2000","journal-title":"Am. J. Nephrol."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"8106","DOI":"10.1021\/jf0508908","article-title":"ACE inhibitory peptides derived from enzymatic hydrolysates of animal muscle protein: A review","volume":"53","author":"Vercruysse","year":"2005","journal-title":"J. Agric. Food Chem."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"641","DOI":"10.1016\/j.idairyj.2006.07.004","article-title":"Purification of Angiotensin I-converting enzyme inhibitory peptides and antihypertensive effect of milk produced by protease-facilitated lactic fermentation","volume":"17","author":"Chen","year":"2007","journal-title":"Int. Dairy J."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"639","DOI":"10.1111\/j.1745-4514.2007.00135.x","article-title":"Cardiovascular effects of whey from prozyme 6-facilitated lactic acid bacteria fermentation of milk","volume":"31","author":"Chen","year":"2007","journal-title":"J. Food Biochem."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"552","DOI":"10.1016\/j.foodchem.2007.06.039","article-title":"Antihypertensive effect of bioactive peptides produced by protease-facilitated lactic acid fermentation of milk","volume":"106","author":"Tsai","year":"2008","journal-title":"Food Chem."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1046\/j.1444-2906.2002.00415.x","article-title":"Identification of antihypertensive peptides from peptic digest of the short-necked clam Tapes philippinarum and the pearl oyster Pinctada fucata martensii","volume":"68","author":"Suetsuna","year":"2002","journal-title":"Fisheries Sci."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"743","DOI":"10.1016\/j.procbio.2008.02.019","article-title":"ACE-inhibitory peptides identified from the muscle protein hydrolysate of hard clam (Meretrix lusoria)","volume":"43","author":"Tsai","year":"2008","journal-title":"Process Biochem."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"7432","DOI":"10.1021\/jf100977z","article-title":"Novel angiotensin-converting enzyme (ACE) inhibitory peptides derived from boneless chicken leg meat","volume":"58","author":"Terashima","year":"2010","journal-title":"J. Agric. Food Chem."},{"key":"ref_12","doi-asserted-by":"crossref","unstructured":"Jahandideh, F., Majumder, K., Chakrabarti, S., Morton, J.S., Panahi, S., Kaufman, S., Davidge, S.T., and Wu, J. (2014). Beneficial effects of simulated gastro-intestinal digests of fried egg and its fractions on blood pressure, plasma lipids and oxidative stress in spontaneously hypertensive rats. PLoS ONE, 9.","DOI":"10.1371\/journal.pone.0115006"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"667","DOI":"10.1016\/j.jff.2016.10.019","article-title":"Egg white protein hydrolysate reduces blood pressure, improves vascular relaxation and modifies aortic angiotensin II receptors expression in spontaneously hypertensive rats","volume":"27","author":"Jahandideh","year":"2016","journal-title":"J. Funct. Foods"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"1614","DOI":"10.1016\/j.foodchem.2010.12.039","article-title":"Purification and characterisation of angiotensin I converting enzyme (ACE) inhibitory peptides derived from enzymatic hydrolysate of ovotransferrin","volume":"126","author":"Majumder","year":"2011","journal-title":"Food Chem."},{"key":"ref_15","doi-asserted-by":"crossref","unstructured":"Majumder, K., Chakrabarti, S., Morton, J.S., Panahi, S., Kaufman, S., Davidge, S.T., and Wu, J. (2013). Egg-derived tri-peptide IRW exerts antihypertensive effects in spontaneously hypertensive rats. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0082829"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"50","DOI":"10.1016\/j.jff.2014.12.028","article-title":"Egg-derived ACE-inhibitory peptides IQW and LKP reduce blood pressure in spontaneously hypertensive rats","volume":"13","author":"Majumder","year":"2015","journal-title":"J. Funct. Foods"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"412","DOI":"10.1016\/j.foodchem.2011.01.010","article-title":"Characterisation of a new antihypertensiveangiotensin I-converting enzyme inhibitory peptide from Pleurotus cornucopiae","volume":"127","author":"Jang","year":"2011","journal-title":"Food Chem."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1007\/s10126-001-0012-7","article-title":"Identification of antihypertensive peptides from peptic digest of two microalgae, Chlorella vulgaris and Spirulina platensis","volume":"3","author":"Suetsuna","year":"2001","journal-title":"Mar. Biotechnol."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"1359","DOI":"10.1021\/acs.jafc.7b04294","article-title":"Antihypertensive effects, molecular docking study, and isothermal titration calorimetry assay of angiotensin I-converting enzyme inhibitory peptides from Chlorella vulgaris","volume":"66","author":"Xie","year":"2018","journal-title":"J. Agric. Food Chem."},{"key":"ref_20","doi-asserted-by":"crossref","unstructured":"Lin, Y.H., Chen, G.W., Yeh, C.H., Song, H., and Tsai, J.S. (2018). Purification and identification of angiotensin I-converting enzyme inhibitory peptides and the antihypertensive effect of Chlorella sorokiniana protein hydrolysates. Nutrients, 10.","DOI":"10.3390\/nu10101397"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"703","DOI":"10.1016\/j.foodres.2010.12.022","article-title":"Purification and identification of antihypertensive peptides from seaweed pipefish (Syngnathus schlegeli) muscle protein hydrolysate","volume":"44","author":"Wijesekara","year":"2011","journal-title":"Food Res. Int."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"1391666","DOI":"10.1080\/16546628.2017.1391666","article-title":"Antihypertensive properties of tilapia (Oreochromis spp.) frame and skin enzymatic protein hydrolysates","volume":"61","author":"Lin","year":"2018","journal-title":"Food Nutr. Res."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"1195","DOI":"10.1016\/S0032-9592(03)00223-1","article-title":"Production of angiotensin I converting enzyme inhibitory peptides from sea bream scales","volume":"39","author":"Fahmi","year":"2004","journal-title":"Process Biochem."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"1155","DOI":"10.1016\/S0032-9592(00)00297-1","article-title":"Purification and characterization of angiotensin I converting enzyme (ACE) inhibitory peptides from Alaska pollack (Theragra chalcogramma) skin","volume":"36","author":"Byun","year":"2001","journal-title":"Process Biochem."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1016\/j.foodchem.2011.08.064","article-title":"Angiotensin-I-converting enzyme (ACE)-inhibitory and antihypertensive properties of squid skin gelatin hydrolysates","volume":"131","author":"Lin","year":"2012","journal-title":"Food Chem."},{"key":"ref_26","first-page":"790","article-title":"Identification of ace-inhibitory peptides from squid skin collagen after in vitro gastrointestinal digestion","volume":"51","author":"Montero","year":"2013","journal-title":"Food Res. Int."},{"key":"ref_27","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_28","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1177\/1082013212442196","article-title":"Angiotensin I converting enzyme inhibitory activity and antihypertensive effect in spontaneously hypertensive rats of cobia (Rachycentron canadum) head papain hydrolysate","volume":"19","author":"Yang","year":"2012","journal-title":"Food Sci. Technol. Int."},{"key":"ref_29","first-page":"668","article-title":"Larval development, distribution, and ecology of cobia, Rachycentron canadum, (Family: Rachycentridae) in the northern Gulf of Mexico","volume":"90","author":"Ditty","year":"1992","journal-title":"Fish Bull"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1016\/j.aquaculture.2004.03.007","article-title":"Cobia culture in Taiwan: Currents status and problems","volume":"237","author":"Liao","year":"2004","journal-title":"Aquaculture"},{"key":"ref_31","first-page":"AOMB.MS.ID.000504","article-title":"Marine environmental management and development strategy for marine aquaculture in Taiwan: Cobia case study","volume":"1","author":"Shih","year":"2018","journal-title":"Ad. Oceanogr. Mar. Biol."},{"key":"ref_32","first-page":"158","article-title":"Evaluation of protein nutritional value in different tissues of cobia","volume":"35","author":"Liu","year":"2009","journal-title":"Food Sci. Technol."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"657","DOI":"10.1021\/jf990447v","article-title":"Biochemical and functional properties of Atlantic salmon (Salmo salar) muscle hydrolyzed with various alkaline proteases","volume":"48","author":"Kristinsson","year":"2000","journal-title":"J. Agric. Food Chem."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1016\/0308-8146(95)93934-J","article-title":"Production and characteristics of protein hydrolysates from capelin (Mallotus villosus)","volume":"53","author":"Shahidi","year":"1995","journal-title":"Food Chem."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"629","DOI":"10.1089\/jmf.2007.0114","article-title":"Purification and antioxidant properties of bigeye tuna (Thunnus obesus) dark muscle peptide on free radicalmediated oxidative systems","volume":"11","author":"Je","year":"2008","journal-title":"J. Med. Food"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"8398","DOI":"10.1021\/jf0710635","article-title":"Antihypertensive effect of angiotensin I converting enzyme-inhibitory peptide from hydrolysates of bigeye tuna dark muscle, Thunnus obesus","volume":"55","author":"Qian","year":"2007","journal-title":"J. Agric. Food Chem."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"840","DOI":"10.1016\/j.procbio.2007.02.006","article-title":"Purification and characterization of an antioxidant peptide obtained from tuna backbone protein by enzymatic hydrolysis","volume":"42","author":"Je","year":"2007","journal-title":"Process Biochem."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"1984","DOI":"10.1021\/jf000494j","article-title":"Isolation and characterization of antioxidative peptides from gelatin hydrolysate of Allaska Pollack skin","volume":"49","author":"Kim","year":"2001","journal-title":"J. Agric. Food Chem."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"96","DOI":"10.1016\/j.foodchem.2009.04.086","article-title":"A novel angiotensin I converting enzyme inhibitory peptides from tuna frame protein hydrolysate and its antihypertensive effect in spontaneously hypertensive rats","volume":"118","author":"Lee","year":"2010","journal-title":"Food Chem."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1016\/S0021-9258(19)52451-6","article-title":"Protein measurement with the folin phenol reagent","volume":"193","author":"Lowry","year":"1951","journal-title":"J. Biol. Chem."},{"key":"ref_41","unstructured":"Cooper, T.G. (1977). Spectrophotometry. The Tools of Biochemistry, Wiley-Interscience. [1st ed.]."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"1219","DOI":"10.3168\/jds.S0022-0302(83)81926-2","article-title":"Spectrophotometric assay using o-phthaldialdehyde for determination of proteolysis in milk and isolated milk proteins","volume":"66","author":"Church","year":"1983","journal-title":"J. Dairy Sci."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1016\/0003-2697(81)90175-5","article-title":"Modified colorimetric ninhydrin methods for peptidase assay","volume":"118","author":"Doi","year":"1981","journal-title":"Anal. Biochem."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"1637","DOI":"10.1016\/0006-2952(71)90292-9","article-title":"Spectrophotometric assay and properties of the angiotensin-converting enzyme of rabbit lung","volume":"20","author":"Cushman","year":"1971","journal-title":"Biochem. Parmacol."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"367","DOI":"10.1016\/S0963-9969(01)00131-4","article-title":"Characterization of inhibition and stability of soy-protein-derived angiotensin I-converting enzyme inhibitory peptides","volume":"35","author":"Wu","year":"2002","journal-title":"Food Res. Int."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"e12385","DOI":"10.1111\/jfbc.12385","article-title":"Purification and identification of hypocholesterolemic peptides from freshwater clam hydrolysate with in vitro gastrointestinal digestion","volume":"41","author":"Lin","year":"2017","journal-title":"J. Food Biochem."},{"key":"ref_47","unstructured":"(2019, January 01). UniProt Database. Available online: http:\/\/www.uniprot.org."},{"key":"ref_48","unstructured":"(2019, January 01). Pairwise Sequence Alignment Software. Available online: https:\/\/www.ebi.ac.uk\/Tools\/psa\/."},{"key":"ref_49","unstructured":"SAS Institute Inc. (2019). SAS\u00ae 9.4 TS1M5 User\u2019s Guide, SAS Institute Press."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"2276","DOI":"10.1016\/j.procbio.2006.05.023","article-title":"The inhibitory effects of freshwater clam (Corbicula fluminea, Muller) muscle protein hydrolysates on angiotensin I converting enzyme","volume":"41","author":"Tsai","year":"2006","journal-title":"Process Biochem."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"670","DOI":"10.1248\/jhs.50.670","article-title":"Antihypertensive and hypocholesterolem effects of tofuyo in spontaneously hypertensive rats","volume":"50","author":"Kuba","year":"2004","journal-title":"J. Health Sci."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1016\/j.idairyj.2015.09.004","article-title":"Tryptophan-containing dipeptides are bioavailable and inhibit plasma human angiotensin-converting enzyme in vivo","volume":"52","author":"Kaiser","year":"2016","journal-title":"Int. Dairy J."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"1075","DOI":"10.1016\/j.idairyj.2004.04.007","article-title":"Angiotensin converting enzyme inhibitory activity of peptides isolated from Manchego cheese. Stability under simulated gastrointestinal digestion","volume":"14","author":"Ruiz","year":"2004","journal-title":"Int. Dairy J."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"1536","DOI":"10.1016\/j.foodres.2011.04.006","article-title":"Angiotensin I-converting enzyme inhibitory activity of low-molecular-weight peptides from Atlantic salmon (Salmo salar L.) skin","volume":"44","author":"Gu","year":"2011","journal-title":"Food Res. Int."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1016\/j.jff.2014.01.021","article-title":"Antihypertensive effect of novel angiotensin I converting enzyme inhibitory peptide from chum salmon (Oncorhynchus keta) skin in spontaneously hypertensive rats","volume":"7","author":"Lee","year":"2014","journal-title":"J. Funct. Foods"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1016\/j.cis.2010.11.001","article-title":"Antihypertensive peptides: Production, bioavailability, and incorporation into foods","volume":"165","author":"Contreras","year":"2011","journal-title":"Adv. Coll. Interface Sci."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"513","DOI":"10.4327\/jsnfs.45.513","article-title":"Antihypertensive effects of tryptic hydrolysate of casein on normotensive and hypertensive volunteers","volume":"45","author":"Sekiya","year":"1992","journal-title":"J. Jpn. Soc. Nutr. Food Sci."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"1278","DOI":"10.1271\/bbb.67.1278","article-title":"Angiotensin I-converting enzyme inhibitory peptides isolated from tofuyo fermented soybean food","volume":"67","author":"Kuba","year":"2003","journal-title":"Biosci. Biotechnol. Biochem."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"383","DOI":"10.1111\/j.1365-2621.2005.01080.x","article-title":"Inhibition properties of dipeptides from salmon muscle hydrolysate on angiotensin I-converting enzyme","volume":"41","author":"Ono","year":"2006","journal-title":"Int. J. Food Sci. Technol."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1016\/j.compbiolchem.2018.10.001","article-title":"The potential peptides against angiotensin-I converting enzyme through a virtual tripeptide-constructing library","volume":"77","author":"Panyayai","year":"2018","journal-title":"Comput. Biol. Chem."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"10685","DOI":"10.1021\/jf403004e","article-title":"Measuring angiotensin-I converting enzyme inhibitory activity by microl plate assays: Comparison using marine cryptides and tentative threshold determinations with captopril and losartan","volume":"61","author":"Henda","year":"2013","journal-title":"J. Agric. Food Chem."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"171","DOI":"10.4172\/jpb.1000437","article-title":"Biopharmaceutical potential of ACE-inhibitory peptides","volume":"10","author":"Balgir","year":"2017","journal-title":"J. Proteom. Bioinform."},{"key":"ref_63","doi-asserted-by":"crossref","unstructured":"Daskaya-Dikmen, C., Yucetepe, A., Karbancioglu-Guler, F., Daskaya, H., and Ozcelik, B. (2017). Angiotensin-I-converting enzyme (ACE)-inhibitory peptides from plants. Nutrients, 9.","DOI":"10.3390\/nu9040316"},{"key":"ref_64","doi-asserted-by":"crossref","unstructured":"Mora, L., Gallego, M., and Toldr\u00e1, F. (2018). ACEI-inhibitory peptides naturally generated in meat and meat products and their health relevance. Nutrients, 10.","DOI":"10.3390\/nu10091259"},{"key":"ref_65","doi-asserted-by":"crossref","unstructured":"He, R., Ma, H., Zhao, W., Qu, W., Zhao, J., Luo, L., and Zhu, W. (2012). Modeling the QSAR of ACE-inhibitory peptides with ANN and its applied illustration. Int. J. Pept.","DOI":"10.1155\/2012\/620609"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"732","DOI":"10.1021\/jf051263l","article-title":"Structural requirements of angiotensin I-converting enzyme inhibitory peptides: Quantitative structure\u2212activity relationship study of di- and tripeptides","volume":"54","author":"Wu","year":"2006","journal-title":"J. Agric. Food Chem."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"469","DOI":"10.1016\/S0271-5317(04)00058-2","article-title":"Angiotensin-I-converting enzyme inhibitory peptides derived from food proteins and their physiological and pharmacological effects","volume":"24","author":"Li","year":"2004","journal-title":"Nutr. Res."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"401","DOI":"10.1016\/S0021-9258(19)86187-2","article-title":"Binding of peptide substrates and inhibitors of angiotensin-converting enzyme","volume":"255","author":"Cheung","year":"1980","journal-title":"J. Biol. Chem."}],"container-title":["Nutrients"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2072-6643\/11\/6\/1351\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T12:58:43Z","timestamp":1760187523000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2072-6643\/11\/6\/1351"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019,6,15]]},"references-count":68,"journal-issue":{"issue":"6","published-online":{"date-parts":[[2019,6]]}},"alternative-id":["nu11061351"],"URL":"https:\/\/doi.org\/10.3390\/nu11061351","relation":{},"ISSN":["2072-6643"],"issn-type":[{"value":"2072-6643","type":"electronic"}],"subject":[],"published":{"date-parts":[[2019,6,15]]}}}