{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,25]],"date-time":"2026-09-25T00:10:14Z","timestamp":1790295014370,"version":"4.1.0"},"reference-count":34,"publisher":"MDPI AG","issue":"7","license":[{"start":{"date-parts":[[2018,7,4]],"date-time":"2018-07-04T00:00:00Z","timestamp":1530662400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["41676129"],"award-info":[{"award-number":["41676129"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["41106149"],"award-info":[{"award-number":["41106149"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Scientific Research Foundation of the Third Institute of Oceanography, SOA","award":["2016007"],"award-info":[{"award-number":["2016007"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Marine Drugs"],"abstract":"<jats:p>Hypertension can cause coronary heart disease. Synthetic angiotensin-converting enzyme (ACE) inhibitors are effective antihypertensive drugs but often cause side effects. The aim of this study was to prepare potential ACE inhibitors from scales. Gelatin was extracted from lizardfish scales. Then, scale gelatin was enzymolyzed to prepare ACE inhibitory peptides using response surface methodology. Proteolytic conditions after optimization were as follows: pH 7.0, enzyme substrate ratio 3.2%, temperature 47 \u00b0C, and proteolysis lasting 2 h and 50 min. The experimental ACE inhibitory activity under optimal conditions was 86.0 \u00b1 0.4%. Among the 118 peptides identified from gelatin hydrolysates, 87.3% were hydrophilic and 93.22% had a molecular weight &lt;2000 Da. Gelatin peptides had high stability upon exposure to high temperature and pH as well as gastrointestinal tract enzymes. Gelatin peptides showed an antihypertensive effect in spontaneously hypertensive rats at a dosage of 2 g\/kg in the long-term experiments. A new ACE inhibitory peptide was isolated from gelatin hydrolysates, and was identified as AGPPGSDGQPGAK with an IC50 value of 420 \u00b1 20 \u03bcM. In this way, ACE inhibitory peptides derived from scale gelatin have the potential to be used as healthy ACE-inhibiting drug raw materials.<\/jats:p>","DOI":"10.3390\/md16070228","type":"journal-article","created":{"date-parts":[[2018,7,4]],"date-time":"2018-07-04T12:23:02Z","timestamp":1530706982000},"page":"228","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":37,"title":["Processing Optimization and Characterization of Angiotensin-\u0399-Converting Enzyme Inhibitory Peptides from Lizardfish (Synodus macrops) Scale Gelatin"],"prefix":"10.3390","volume":"16","author":[{"given":"Junde","family":"Chen","sequence":"first","affiliation":[{"name":"Marine Biological Resource Comprehensive Utilization Engineering Research Center of the State Oceanic Administration, the Third Institute of Oceanography of the State Oceanic Administration, Xiamen 361005, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ying","family":"Liu","sequence":"additional","affiliation":[{"name":"Marine Biological Resource Comprehensive Utilization Engineering Research Center of the State Oceanic Administration, the Third Institute of Oceanography of the State Oceanic Administration, Xiamen 361005, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Guangyu","family":"Wang","sequence":"additional","affiliation":[{"name":"Marine Biological Resource Comprehensive Utilization Engineering Research Center of the State Oceanic Administration, the Third Institute of Oceanography of the State Oceanic Administration, Xiamen 361005, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shanshan","family":"Sun","sequence":"additional","affiliation":[{"name":"Marine Biological Resource Comprehensive Utilization Engineering Research Center of the State Oceanic Administration, the Third Institute of Oceanography of the State Oceanic Administration, Xiamen 361005, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rui","family":"Liu","sequence":"additional","affiliation":[{"name":"Jiangsu Collaborative Innovation Center of Chinese Medicinal Resources Industrialization, and National and Local Collaborative Engineering Center of Chinese Medicinal Resources Industrialization and Formulae Innovative Medicine, Nanjing University of Chinese Medicine, Nanjing 210023, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bihong","family":"Hong","sequence":"additional","affiliation":[{"name":"Marine Biological Resource Comprehensive Utilization Engineering Research Center of the State Oceanic Administration, the Third Institute of Oceanography of the State Oceanic Administration, Xiamen 361005, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ran","family":"Gao","sequence":"additional","affiliation":[{"name":"Marine Biological Resource Comprehensive Utilization Engineering Research Center of the State Oceanic Administration, the Third Institute of Oceanography of the State Oceanic Administration, Xiamen 361005, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kaikai","family":"Bai","sequence":"additional","affiliation":[{"name":"Marine Biological Resource Comprehensive Utilization Engineering Research Center of the State Oceanic Administration, the Third Institute of Oceanography of the State Oceanic Administration, Xiamen 361005, China"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2018,7,4]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"506","DOI":"10.1016\/j.foodchem.2017.02.039","article-title":"Antihypertensive peptides from animal products, marine organisms, and plants","volume":"228","author":"Lee","year":"2017","journal-title":"Food Chem."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"8","DOI":"10.1016\/j.jprot.2015.06.016","article-title":"Bioactive peptides identified in thornback ray skin\u2019s gelatin hydrolysates by proteases from Bacillus subtilis and Bacillus amyloliquefaciens","volume":"128","author":"Lassoued","year":"2015","journal-title":"J. Proteom."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"72","DOI":"10.1016\/j.jff.2017.06.049","article-title":"Production and purification of glucosamine and angiotensin\u2014\u0406 converting enzyme (ACE) inhibitory peptides from mushroom hydrolysates","volume":"36","author":"Zhang","year":"2017","journal-title":"J. Funct. Foods"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1016\/j.foodres.2014.11.024","article-title":"Biological potential of protein hydrolysates and peptides from common bean (Phaseolus Vulgaris L.): A review","volume":"76","author":"Mojica","year":"2015","journal-title":"Food Res. Int."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"328","DOI":"10.1016\/j.talanta.2012.12.041","article-title":"Vegetable food: A cheap source of proteins and peptides with antihypertensive, antioxidant, and other less occurrence bioactivities","volume":"106","author":"Puchalska","year":"2013","journal-title":"Talanta"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1016\/j.jff.2014.03.002","article-title":"Mechanisms of food protein-derived antihypertensive peptides other than ACE inhibition","volume":"8C","author":"Udenigwe","year":"2014","journal-title":"J. Funct. Foods."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1016\/j.foodres.2017.06.018","article-title":"Novel bioactive peptides from enzymatic hydrolysate of Sardinelle (Sardinella aurita) muscle proteins hydrolysed by Bacillus subtilis A26 proteases","volume":"100","author":"Jemil","year":"2017","journal-title":"Food Res. Int."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1016\/j.foodres.2012.11.002","article-title":"Purification and characterization of angiotensin \u0406 converting enzyme inhibitory peptides from jellyfish Rhopilema esculentun","volume":"50","author":"Liu","year":"2013","journal-title":"Food Res. Int."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"1149","DOI":"10.1016\/S0271-5317(01)00333-5","article-title":"Effects of an ACE-inhibitory agent, katsuobushi oligopeptide, in the spontaneously hypertensive rat and in borderline and mildly hypertensive subjects","volume":"21","author":"Fujita","year":"2001","journal-title":"Nutr. Res."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"453","DOI":"10.1016\/j.lwt.2015.10.070","article-title":"Extraction and characterization of acid-soluble collagen from scales and skin of tilapia (Oreochromis niloticus)","volume":"66","author":"Chen","year":"2016","journal-title":"LWT-Food Sci. Technol."},{"key":"ref_11","doi-asserted-by":"crossref","unstructured":"Venkatesan, J., Anil, S., Kim, S.K., and Shim, M.S. (2017). Marine fish proteins and peptides for cosmeceuticals: A review. Mar. Drugs, 15.","DOI":"10.3390\/md15050143"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"708","DOI":"10.1016\/j.foodhyd.2014.07.025","article-title":"Isolation and characterization of collagen from the outer skin of squid (Doryteuthis Singhalensis)","volume":"43","author":"Veeruraj","year":"2015","journal-title":"Food Hydrocolloid."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"1179","DOI":"10.1016\/j.foodchem.2011.05.099","article-title":"Characteristics of acid soluble collagen and pepsin soluble collagen from scale of spotted golden goatfish (Parupeneus heptacanthus)","volume":"129","author":"Matmaroh","year":"2011","journal-title":"Food Chem."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"931","DOI":"10.1016\/j.foodhyd.2017.11.040","article-title":"Release kinetics of Tilapia scale \u0406 collagen peptides during tryptic hydrolysis","volume":"77","author":"Chen","year":"2018","journal-title":"Food Hydrocolloid."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1016\/j.foodchem.2017.10.087","article-title":"Immunomodulatory and anticancer protein hydrolysates (peptides) from food proteins: A review","volume":"245","author":"Chalamaiah","year":"2018","journal-title":"Food Chem."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"758","DOI":"10.1016\/j.lwt.2015.03.061","article-title":"Investigating the effect of roasting on functional properties of defatted hazelnut flour by response surface methodology (RSM)","volume":"63","author":"Turan","year":"2015","journal-title":"LWT-Food Sci. Technol."},{"key":"ref_17","first-page":"104","article-title":"Optimization of bromelain-aided production of angiotensin \u0406-coverting enzyme inhibitory hydrolysates from stone fish using response surface methodology","volume":"15","author":"Auwal","year":"2017","journal-title":"Mardrugs"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"676","DOI":"10.1016\/j.fbp.2012.04.001","article-title":"Optimization of antioxidant hydrolysate production from flying squid muscle protein using response surface methodology","volume":"90","author":"Fang","year":"2012","journal-title":"Food Bioprod. Process."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"328","DOI":"10.1016\/j.foodchem.2008.09.041","article-title":"Optimisation of hydrolysis conditions for the production of the angiotensin-\u0406 coverting enzyme (ACE) inhibitory peptides from whey protein using response surface methodology","volume":"114","author":"Guo","year":"2009","journal-title":"Food Chem."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"1066","DOI":"10.3390\/md10051066","article-title":"Optimization of hydrolysis conditions for the production of angiotensin \u0406-converting enzyme inhibitory peptides and isolation of a novel peptide from lizard fish (Saurida elongata) muscle protein hydrolysate","volume":"10","author":"Wu","year":"2012","journal-title":"Mar. Drugs"},{"key":"ref_21","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_22","doi-asserted-by":"crossref","first-page":"587","DOI":"10.1002\/jssc.201600821","article-title":"Peptidome characterization of the antipyretic fraction of Bubali Cornu aqueous extract by nano liquid chromatography with orbitrap mass spectrometry detection","volume":"40","author":"Liu","year":"2017","journal-title":"J. Sep. Sci."},{"key":"ref_23","doi-asserted-by":"crossref","unstructured":"Zhai, Y.J., Zhu, Z.H., Zhu, Y., Qian, D.W., Liu, R., Peng, Y.R., Ding, Y.H., Oiyang, Z., and Duan, J.A. (2017). Characterization of collagen peptides in Elaphuri Davidiani Cornu aqueous extract with proliferative activity on osteoblasts using nano-liquid chromatography in tandem with orbitrap mass spectrometry. Molecules, 22.","DOI":"10.3390\/molecules22010166"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"716","DOI":"10.1016\/j.jff.2015.02.037","article-title":"Functional and potential therapeutic ACE-inhibitory peptides derived from bromelain hydrolysis of trevally proteins","volume":"14","author":"Salampessy","year":"2015","journal-title":"J. Funct. Foods"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"471","DOI":"10.1016\/j.foodchem.2017.10.095","article-title":"Exploration of the molecular interactions between angiotensin\u2014\u0406-converting enzyme (ACE) and the inhibitory peptides derived from hazelnut (Corylus heterophylla Fisch.)","volume":"245","author":"Liu","year":"2018","journal-title":"Food Chem."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1017\/S0022029999003982","article-title":"Angiotensin\u2014I converting enzyme inhibitory properties of whey protein digests: Concentration and characterization of active peptides","volume":"67","author":"Koskinen","year":"2000","journal-title":"J. Dairy Res."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"761","DOI":"10.1016\/j.foodchem.2011.03.108","article-title":"Systemic screening of milk protein-derived ACE inhibitors through a chemically synthesised tripeptide library","volume":"128","author":"Ren","year":"2011","journal-title":"Food Chem."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.phymed.2017.09.013","article-title":"Identification and in silico characterization of a novel peptide inhibitor of angiotensin converting enzyme from pigeon pea (Cajanus cajan)","volume":"36","author":"Nawaz","year":"2017","journal-title":"Phytomedicine"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"924","DOI":"10.1016\/j.lwt.2015.09.024","article-title":"Characteristics and functional properties of gelatin extracted from squid (Loligo vulgaris) skin","volume":"65","author":"Abdelmalek","year":"2016","journal-title":"LWT-Food Sci. Technol."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"941","DOI":"10.1007\/s00217-011-1466-0","article-title":"Influence of the degree of hydrolysis (DH) on antioxidant properties and radical-scavenging activities of peanut peptides prepared from fermented peanut meal","volume":"232","author":"Zhang","year":"2011","journal-title":"Eur. Food Res. Technol."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"1256","DOI":"10.1021\/jf60226a042","article-title":"Determination of the degree of hydrolysis of food protein hydrolysates by trinitrobenzenesulfonic acid","volume":"27","year":"1979","journal-title":"J. Agric. Food Chem."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"1637","DOI":"10.1016\/0006-2952(71)90292-9","article-title":"Spectrophotometric assay and properties of the angiotensin \u0406-coverting enzyme of rabbit lung","volume":"20","author":"Cushman","year":"1971","journal-title":"Biochem. Pharmacol."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"302","DOI":"10.1016\/j.foodchem.2008.03.059","article-title":"Purification and identification of a ACE inhibitory peptide from oyster proteins hydrolysate and the antihypertensive effect of hydrolysate in spontaneously hypertensive rats","volume":"111","author":"Wang","year":"2008","journal-title":"Food Chem."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"482","DOI":"10.1016\/j.peptides.2009.05.029","article-title":"Ala-Val-Phe and Val-Phe: ACE inhibitory peptides derived from insect protein with antihypertensive activity in spontaneously hypertensive rats","volume":"31","author":"Vercruysse","year":"2010","journal-title":"Peptides"}],"container-title":["Marine Drugs"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1660-3397\/16\/7\/228\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T15:11:15Z","timestamp":1760195475000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1660-3397\/16\/7\/228"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2018,7,4]]},"references-count":34,"journal-issue":{"issue":"7","published-online":{"date-parts":[[2018,7]]}},"alternative-id":["md16070228"],"URL":"https:\/\/doi.org\/10.3390\/md16070228","relation":{},"ISSN":["1660-3397"],"issn-type":[{"value":"1660-3397","type":"electronic"}],"subject":[],"published":{"date-parts":[[2018,7,4]]}}}