{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,28]],"date-time":"2026-04-28T14:09:17Z","timestamp":1777385357879,"version":"3.51.4"},"reference-count":69,"publisher":"MDPI AG","issue":"7","license":[{"start":{"date-parts":[[2024,6,29]],"date-time":"2024-06-29T00:00:00Z","timestamp":1719619200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"National Science Foundation of China","award":["U2006205"],"award-info":[{"award-number":["U2006205"]}]},{"name":"National Science Foundation of China","award":["32330001"],"award-info":[{"award-number":["32330001"]}]},{"name":"National Science Foundation of China","award":["2022QNLM030004-3"],"award-info":[{"award-number":["2022QNLM030004-3"]}]},{"name":"National Science Foundation of China","award":["SKLMTFCP-2023-06"],"award-info":[{"award-number":["SKLMTFCP-2023-06"]}]},{"name":"Marine S&amp;T Fund of Shandong Province for Qingdao Marine Science and Technology Center","award":["U2006205"],"award-info":[{"award-number":["U2006205"]}]},{"name":"Marine S&amp;T Fund of Shandong Province for Qingdao Marine Science and Technology Center","award":["32330001"],"award-info":[{"award-number":["32330001"]}]},{"name":"Marine S&amp;T Fund of Shandong Province for Qingdao Marine Science and Technology Center","award":["2022QNLM030004-3"],"award-info":[{"award-number":["2022QNLM030004-3"]}]},{"name":"Marine S&amp;T Fund of Shandong Province for Qingdao Marine Science and Technology Center","award":["SKLMTFCP-2023-06"],"award-info":[{"award-number":["SKLMTFCP-2023-06"]}]},{"name":"SKLMT Frontiers and Challenges Project","award":["U2006205"],"award-info":[{"award-number":["U2006205"]}]},{"name":"SKLMT Frontiers and Challenges Project","award":["32330001"],"award-info":[{"award-number":["32330001"]}]},{"name":"SKLMT Frontiers and Challenges Project","award":["2022QNLM030004-3"],"award-info":[{"award-number":["2022QNLM030004-3"]}]},{"name":"SKLMT Frontiers and Challenges Project","award":["SKLMTFCP-2023-06"],"award-info":[{"award-number":["SKLMTFCP-2023-06"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Marine Drugs"],"abstract":"<jats:p>Marine bacterial proteases have rarely been used to produce bioactive peptides, although many have been reported. This study aims to evaluate the potential of the marine bacterial metalloprotease A69 from recombinant Bacillus subtilis in the preparation of peanut peptides (PPs) with antioxidant activity and angiotensin-converting enzyme (ACE)-inhibitory activity. Based on the optimization of the hydrolysis parameters of protease A69, a process for PPs preparation was set up in which the peanut protein was hydrolyzed by A69 at 3000 U g\u22121 and 60 \u00b0C, pH 7.0 for 4 h. The prepared PPs exhibited a high content of peptides with molecular weights lower than 1000 Da (&gt;80%) and 3000 Da (&gt;95%) and contained 17 kinds of amino acids. Moreover, the PPs displayed elevated scavenging of hydroxyl radical and 1,1-diphenyl-2-picryl-hydrazyl radical, with IC50 values of 1.50 mg mL\u22121 and 1.66 mg mL\u22121, respectively, indicating the good antioxidant activity of the PPs. The PPs also showed remarkable ACE-inhibitory activity, with an IC50 value of 0.71 mg mL\u22121. By liquid chromatography mass spectrometry analysis, the sequences of 19 ACE inhibitory peptides and 15 antioxidant peptides were identified from the PPs. These results indicate that the prepared PPs have a good nutritional value, as well as good antioxidant and antihypertensive effects, and that the marine bacterial metalloprotease A69 has promising potential in relation to the preparation of bioactive peptides from peanut protein.<\/jats:p>","DOI":"10.3390\/md22070305","type":"journal-article","created":{"date-parts":[[2024,7,1]],"date-time":"2024-07-01T08:17:29Z","timestamp":1719821849000},"page":"305","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":4,"title":["Potential of Marine Bacterial Metalloprotease A69 in the Preparation of Peanut Peptides with Angiotensin-Converting Enzyme (ACE)-Inhibitory and Antioxidant Properties"],"prefix":"10.3390","volume":"22","author":[{"given":"Wen-Jie","family":"Cao","sequence":"first","affiliation":[{"name":"State Key Laboratory of Microbial Technology, Marine Biotechnology Research Center, Shandong University, Qingdao 266237, China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Rui","family":"Liu","sequence":"additional","affiliation":[{"name":"State Key Laboratory of Microbial Technology, Marine Biotechnology Research Center, Shandong University, Qingdao 266237, China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Wen-Xiao","family":"Zhao","sequence":"additional","affiliation":[{"name":"State Key Laboratory of Microbial Technology, Marine Biotechnology Research Center, Shandong University, Qingdao 266237, China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jian","family":"Li","sequence":"additional","affiliation":[{"name":"State Key Laboratory of Microbial Technology, Marine Biotechnology Research Center, Shandong University, Qingdao 266237, China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yan","family":"Wang","sequence":"additional","affiliation":[{"name":"State Key Laboratory of Microbial Technology, Marine Biotechnology Research Center, Shandong University, Qingdao 266237, China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Xiao-Jie","family":"Yuan","sequence":"additional","affiliation":[{"name":"State Key Laboratory of Microbial Technology, Marine Biotechnology Research Center, Shandong University, Qingdao 266237, China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Hui-Lin","family":"Wang","sequence":"additional","affiliation":[{"name":"State Key Laboratory of Microbial Technology, Marine Biotechnology Research Center, Shandong University, Qingdao 266237, China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2017-1005","authenticated-orcid":false,"given":"Yu-Zhong","family":"Zhang","sequence":"additional","affiliation":[{"name":"State Key Laboratory of Microbial Technology, Marine Biotechnology Research Center, Shandong University, Qingdao 266237, China"},{"name":"Frontiers Science Center for Deep Ocean Multispheres and Earth System, College of Marine Life Sciences, Ocean University of China, Qingdao 266003, China"},{"name":"Joint Research Center for Marine Microbial Science and Technology of Shandong University and Ocean University of China, Qingdao 266237, China"},{"name":"Laboratory for Marine Biology and Biotechnology, Qingdao Marine Science and Technology Center, Qingdao 266237, China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2991-3631","authenticated-orcid":false,"given":"Xiu-Lan","family":"Chen","sequence":"additional","affiliation":[{"name":"State Key Laboratory of Microbial Technology, Marine Biotechnology Research Center, Shandong University, Qingdao 266237, China"},{"name":"Joint Research Center for Marine Microbial Science and Technology of Shandong University and Ocean University of China, Qingdao 266237, China"},{"name":"Laboratory for Marine Biology and Biotechnology, Qingdao Marine Science and Technology Center, Qingdao 266237, China"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yu-Qiang","family":"Zhang","sequence":"additional","affiliation":[{"name":"State Key Laboratory of Microbial Technology, Marine Biotechnology Research Center, Shandong University, Qingdao 266237, China"},{"name":"Joint Research Center for Marine Microbial Science and Technology of Shandong University and Ocean University of China, Qingdao 266237, China"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2024,6,29]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"224","DOI":"10.1007\/s12393-012-9058-8","article-title":"Use of Proteomics and Peptidomics Methods in Food Bioactive Peptide Science and Engineering","volume":"4","year":"2012","journal-title":"Food Eng. Rev."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1016\/j.foodres.2015.05.013","article-title":"Biologically active peptides: Processes for their generation, purification and identification and applications as natural additives in the food and pharmaceutical industries","volume":"74","author":"Sato","year":"2015","journal-title":"Food Res. Int."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"1905","DOI":"10.2174\/0929867054546618","article-title":"Biochemical Properties of Peptides Encrypted in Bovine Milk Proteins","volume":"12","author":"Meisel","year":"2005","journal-title":"Curr. Med. Chem."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1111\/j.1471-0307.2004.00139.x","article-title":"Angiotensin I-converting-enzyme-inhibitory and antimicrobial bioactive peptides","volume":"57","author":"Gobbetti","year":"2004","journal-title":"Int. J. Dairy Technol."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"493","DOI":"10.1002\/mnfr.201200252","article-title":"Antioxidant capacities of fractionated barley hordein hydrolysates in relation to peptide structures","volume":"57","author":"Bamdad","year":"2013","journal-title":"Mol. Nutr. Food Res."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"4403","DOI":"10.1039\/D0FO00151A","article-title":"The milk macromolecular peptide: Preparation and evaluation of antihypertensive activity in rats","volume":"11","author":"Cui","year":"2020","journal-title":"Food Funct."},{"key":"ref_7","doi-asserted-by":"crossref","unstructured":"Cheng, J.-H., Zhang, X.-Y., Wang, Z., Zhang, X., Liu, S.-C., Song, X.-Y., Zhang, Y.-Z., Ding, J.-M., Chen, X.-L., and Xu, F. (2021). Potential of Thermolysin-like Protease A69 in Preparation of Bovine Collagen Peptides with Moisture-Retention Ability and Antioxidative Activity. Mar. Drugs, 19.","DOI":"10.3390\/md19120676"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"7153","DOI":"10.1002\/jsfa.12797","article-title":"Production of marine bacterial metalloprotease A69 and evaluation of its potential in preparing soybean peptides with angiotensin-converting enzyme-inhibitory activity","volume":"103","author":"Zhang","year":"2023","journal-title":"J. Sci. Food Agric."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1007\/BF01087919","article-title":"Effects of dry heat treatments to peanut kernels on the functional properties of the defatted meal","volume":"43","author":"Patil","year":"1993","journal-title":"Plant Foods Hum. Nutr."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1007\/BF02193772","article-title":"Effects of roasting and storage on proteins and oil in peanut kernels","volume":"40","author":"Damame","year":"1990","journal-title":"Plant Foods Hum. Nutr."},{"key":"ref_11","doi-asserted-by":"crossref","unstructured":"Tang, L., Sun, J., Zhang, H.C., Zhang, C.S., Yu, L.N., Bi, J., Zhu, F., Liu, S.F., and Yang, Q.L. (2012). Evaluation of Physicochemical and Antioxidant Properties of Peanut Protein Hydrolysate. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0037863"},{"key":"ref_12","first-page":"6039","article-title":"Purification and Identification of Novel Antioxidant Peptides from Hydrolysates of Peanuts (Arachis hypogaea) and Their Neuroprotective Activities","volume":"71","author":"Ma","year":"2023","journal-title":"J. Agric. Food Chem."},{"key":"ref_13","first-page":"698","article-title":"Bioactive Peptides from Low Denatured Peanut Dregs: Production and Antihypertensive Activity","volume":"343\u2013344","author":"Zhang","year":"2011","journal-title":"Adv. Mater. Res."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"10102","DOI":"10.1021\/jf901787e","article-title":"Purification, Activity and Sequence of Angiotensin I Converting Enzyme Inhibitory Peptide from Alcalase Hydrolysate of Peanut Flour","volume":"57","author":"Guang","year":"2009","journal-title":"J. Agric. Food Chem."},{"key":"ref_15","first-page":"66","article-title":"Identification and in vitro Characterization of Novel Antidiabetic Peptides Released Enzymatically from Peanut Protein","volume":"79","author":"Li","year":"2023","journal-title":"Plant Foods Hum. Nutr."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"732","DOI":"10.1021\/jf051263l","article-title":"Structural Requirements of Angiotensin I-Converting Enzyme Inhibitory Peptides:\u2009 Quantitative Structure\u2212Activity Relationship Study of Di- and Tripeptides","volume":"54","author":"Wu","year":"2006","journal-title":"J. Agric. Food Chem."},{"key":"ref_17","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_18","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1016\/j.jff.2011.05.006","article-title":"Food-derived peptidic antioxidants: A review of their production, assessment, and potential applications","volume":"3","author":"Samaranayaka","year":"2011","journal-title":"J. Funct. Foods"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"1949","DOI":"10.1016\/j.peptides.2010.06.020","article-title":"Antioxidative peptides from food proteins: A review","volume":"31","author":"Sarmadi","year":"2010","journal-title":"Peptides"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"2342","DOI":"10.1007\/s11947-011-0606-7","article-title":"Comparisons on the Functional Properties and Antioxidant Activity of Spray-Dried and Freeze-Dried Egg White Protein Hydrolysate","volume":"5","author":"Chen","year":"2011","journal-title":"Food Bioprocess Technol."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"210","DOI":"10.1039\/C4FO00621F","article-title":"Ex vivo digestion of carp muscle tissue\u2014ACE inhibitory and antioxidant activities of the obtained hydrolysates","volume":"6","author":"Borawska","year":"2015","journal-title":"Food Funct."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"226","DOI":"10.1016\/j.foodchem.2009.06.015","article-title":"Isolation and identification of antioxidative peptides from rice endosperm protein enzymatic hydrolysate by consecutive chromatography and MALDI-TOF\/TOF MS\/MS","volume":"119","author":"Zhang","year":"2010","journal-title":"Food Chem."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"662","DOI":"10.1016\/j.foodchem.2014.07.117","article-title":"Purification and characterization of three antioxidant peptides from protein hydrolyzate of croceine croaker (Pseudosciaena crocea) muscle","volume":"168","author":"Chi","year":"2015","journal-title":"Food Chem."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"991","DOI":"10.1016\/j.foodchem.2013.08.099","article-title":"Novel antioxidative peptides from the protein hydrolysate of oysters (Crassostrea talienwhanensis)","volume":"145","author":"Wang","year":"2014","journal-title":"Food Chem."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"78","DOI":"10.1016\/j.foodchem.2013.09.136","article-title":"Purification and antioxidant properties of octapeptide from salmon byproduct protein hydrolysate by gastrointestinal digestion","volume":"147","author":"Ahn","year":"2014","journal-title":"Food Chem."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"34","DOI":"10.1016\/j.foodchem.2013.07.076","article-title":"ACE-inhibitory activity of enzymatic protein hydrolysates from lupin and other legumes","volume":"145","author":"Boschin","year":"2014","journal-title":"Food Chem."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"773","DOI":"10.2174\/138161207780363068","article-title":"Angiotensin Converting Enzyme Inhibitory Peptides Derived from Food Proteins: Biochemistry, Bioactivity and Production","volume":"13","author":"Murray","year":"2007","journal-title":"Curr. Pharm. Des."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"412","DOI":"10.1016\/j.foodchem.2011.01.010","article-title":"Characterisation of a new antihypertensive angiotensin I-converting enzyme inhibitory peptide from Pleurotus cornucopiae","volume":"127","author":"Jang","year":"2011","journal-title":"Food Chem."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"341","DOI":"10.2337\/diabetes.55.02.06.db05-0885","article-title":"ACE Inhibitor or Angiotensin II Receptor Antagonist Attenuates Diabetic Neuropathy in Streptozotocin-Induced Diabetic Rats","volume":"55","author":"Coppey","year":"2006","journal-title":"Diabetes"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"2682","DOI":"10.1016\/j.foodchem.2013.04.064","article-title":"LC\u2013MS\/MS coupled with QSAR modeling in characterising of angiotensin I-converting enzyme inhibitory peptides from soybean proteins","volume":"141","author":"Gu","year":"2013","journal-title":"Food Chem."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"4897","DOI":"10.1021\/jf026186y","article-title":"Isolation and Antihypertensive Effect of Angiotensin I-Converting Enzyme (ACE) Inhibitory Peptides from Spinach Rubisco","volume":"51","author":"Yang","year":"2003","journal-title":"J. Agric. Food Chem."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"1653","DOI":"10.1016\/j.foodchem.2010.11.171","article-title":"Inhibition of angiotensin I-converting enzyme by wheat gliadin hydrolysates","volume":"127","author":"Thewissen","year":"2011","journal-title":"Food Chem."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"424","DOI":"10.1016\/j.jprot.2015.08.018","article-title":"Screening, discovery, and characterization of angiotensin-I converting enzyme inhibitory peptides derived from proteolytic hydrolysate of bitter melon seed proteins","volume":"128","author":"Priyanto","year":"2015","journal-title":"J. Proteom."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"106027","DOI":"10.1016\/j.pep.2021.106027","article-title":"Separation and identification of ACE inhibitory peptides from lizard fish proteins hydrolysates by metal affinity-immobilized magnetic liposome","volume":"191","author":"Lu","year":"2022","journal-title":"Protein Expr. Purif."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"2455","DOI":"10.15252\/embj.201796750","article-title":"Protease cleavage site fingerprinting by label-free in-gel degradomics reveals pH-dependent specificity switch of legumain","volume":"36","author":"Vidmar","year":"2017","journal-title":"EMBO J."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"2864","DOI":"10.1016\/S0021-9258(18)49927-9","article-title":"Three-dimensional structure of the elastase of Pseudomonas aeruginosa at 1.5-A resolution","volume":"266","author":"Thayer","year":"1991","journal-title":"J. Biol. Chem."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1002\/(SICI)1097-0282(1997)43:2<119::AID-BIP4>3.0.CO;2-Y","article-title":"Biochemical properties of regulatory peptides derived from mil proteins","volume":"43","author":"Meisel","year":"1997","journal-title":"Biopolymers"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"564","DOI":"10.1111\/j.1365-2621.2000.tb16049.x","article-title":"Classification and Antihypertensive Activity of Angiotensin I-Converting Enzyme Inhibitory Peptides Derived from Food Proteins","volume":"65","author":"Iroyukifujita","year":"2008","journal-title":"J. Food Sci."},{"key":"ref_39","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. Importance of the COOH-terminal dipeptide sequence","volume":"255","author":"Cheung","year":"1980","journal-title":"J. Biol. Chem."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1016\/j.jtbi.2012.10.029","article-title":"Characterization of structure\u2013antioxidant activity relationship of peptides in free radical systems using QSAR models: Key sequence positions and their amino acid properties","volume":"318","author":"Li","year":"2013","journal-title":"J. Theor. Biol."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"3020","DOI":"10.1016\/j.foodchem.2012.06.100","article-title":"Fish protein hydrolysates: Proximate composition, amino acid composition, antioxidant activities and applications: A review","volume":"135","author":"Chalamaiah","year":"2012","journal-title":"Food Chem."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"3329","DOI":"10.1016\/j.foodchem.2013.06.048","article-title":"Comparison of analytical methods to assay inhibitors of angiotensin I-converting enzyme","volume":"141","author":"Chen","year":"2013","journal-title":"Food Chem."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"1165","DOI":"10.1016\/j.peptides.2010.02.022","article-title":"Arachin derived peptides as selective angiotensin I-converting enzyme (ACE) inhibitors: Structure\u2013activity relationship","volume":"31","author":"Jimsheena","year":"2010","journal-title":"Peptides"},{"key":"ref_44","doi-asserted-by":"crossref","unstructured":"Motta, A., Shi, A., Liu, H., Liu, L., Hu, H., Wang, Q., and Adhikari, B. (2014). Isolation, Purification and Molecular Mechanism of a Peanut Protein-Derived ACE-Inhibitory Peptide. PLoS ONE, 9.","DOI":"10.1371\/journal.pone.0111188"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1007\/s00217-009-1136-7","article-title":"Detection of an angiotensin converting enzyme inhibitory peptide from peanut protein isolate and peanut polypeptides by western blot and dot blot hybridization","volume":"230","author":"Liu","year":"2009","journal-title":"Eur. Food Res. Technol."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"148","DOI":"10.1016\/j.foodchem.2014.04.010","article-title":"Purification and identification of antioxidant peptides from peanut protein isolate hydrolysates using UHR-Q-TOF mass spectrometer","volume":"161","author":"Ji","year":"2014","journal-title":"Food Chem."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"5431","DOI":"10.1021\/jf3017173","article-title":"Isolation and Characterization of an Oxygen Radical Absorbance Activity Peptide from Defatted Peanut Meal Hydrolysate and Its Antioxidant Properties","volume":"60","author":"Zheng","year":"2012","journal-title":"J. Agric. Food Chem."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"364","DOI":"10.1111\/1541-4337.12017","article-title":"Identification of Bioactive Peptides from Cereal Storage Proteins and Their Potential Role in Prevention of Chronic Diseases","volume":"12","author":"Cavazos","year":"2013","journal-title":"Compr. Rev. Food Sci. Food Saf."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1016\/j.jprot.2013.06.023","article-title":"Peptides with angiotensin I converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne Lactobacillus","volume":"89","author":"Castellano","year":"2013","journal-title":"J. Proteom."},{"key":"ref_50","first-page":"71","article-title":"Milk proteins as precursors of bioactive peptides","volume":"8","author":"Dziuba","year":"2009","journal-title":"Acta Sci. Pol. Technol. Aliment."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"521","DOI":"10.1080\/10408398.2012.664829","article-title":"Isolation and Characterization of Peptides with Antihypertensive Activity in Foodstuffs","volume":"55","author":"Puchalska","year":"2014","journal-title":"Crit. Rev. Food Sci. Nutr."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"2244","DOI":"10.1271\/bbb.58.2244","article-title":"Angiotensin I-converting Enzyme Inhibitory Peptides in an Alkaline Protease Hydrolyzate Derived from Sardine Muscle","volume":"58","author":"Matsufuji","year":"2014","journal-title":"Biosci. Biotechnol. Biochem."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1016\/j.jnutbio.2003.11.004","article-title":"Antihypertensive effects of Undaria pinnatifida (wakame) peptide on blood pressure in spontaneously hypertensive rats","volume":"15","author":"Suetsuna","year":"2004","journal-title":"J. Nutr. Biochem."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"11234","DOI":"10.1021\/jf202902r","article-title":"Inhibition Strength of Short Peptides Derived from an ACE Inhibitory Peptide","volume":"59","author":"Terashima","year":"2011","journal-title":"J. Agric. Food Chem."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"239","DOI":"10.5483\/BMBRep.2002.35.2.239","article-title":"Structure and Activity of Angiotensin I Converting Enzyme Inhibitory Peptides Derived from Alaskan Pollack Skin","volume":"35","author":"Byun","year":"2002","journal-title":"BMB Rep."},{"key":"ref_56","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"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1080\/87559129.2012.692137","article-title":"Bioactive Peptides of Buffalo, Camel, Goat, Sheep, Mare, and Yak Milks and Milk Products","volume":"29","year":"2013","journal-title":"Food Rev. Int."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"5297","DOI":"10.1128\/AEM.69.9.5297-5305.2003","article-title":"Angiotensin I-Converting-Enzyme-Inhibitory and Antibacterial Peptides from Lactobacillus helveticus PR4 Proteinase-Hydrolyzed Caseins of Milk from Six Species","volume":"69","author":"Minervini","year":"2003","journal-title":"Appl. Environ. Microbiol."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"1767","DOI":"10.1271\/bbb.58.1767","article-title":"Structure and Activity of Angiotensin I Converting Enzyme Inhibitory Peptides from Sake and Sake Lees","volume":"58","author":"Saito","year":"2014","journal-title":"Biosci. Biotechnol. Biochem."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"738","DOI":"10.1007\/s12010-012-0024-y","article-title":"Review on the Angiotensin-I-Converting Enzyme (ACE) Inhibitor Peptides from Marine Proteins","volume":"169","author":"He","year":"2012","journal-title":"Appl. Biochem. Biotechnol."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"197","DOI":"10.2174\/1568016033477496","article-title":"Design of a Genetically Modified Soybean Protein Preventing Hypertension Based on an Anti-Hypertensive Peptide Derived from Ovalbumin","volume":"1","author":"Matoba","year":"2003","journal-title":"Curr. Med. Chem. Cardiovasc. Hematol. Agents"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"3668","DOI":"10.1021\/jf021191n","article-title":"Antioxidative Properties of Tripeptide Libraries Prepared by the Combinatorial Chemistry","volume":"51","author":"Saito","year":"2003","journal-title":"J. Agric. Food Chem."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"8825","DOI":"10.1021\/jf101556n","article-title":"Chromatographic Separation and Tandem MS Identification of Active Peptides in Potato Protein Hydrolysate That Inhibit Autoxidation of Soybean Oil-in-Water Emulsions","volume":"58","author":"Cheng","year":"2010","journal-title":"J. Agric. Food Chem."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"214","DOI":"10.1016\/j.idairyj.2010.11.011","article-title":"Isolation and identification of antioxidative peptides from bovine \u03b1-lactalbumin","volume":"21","author":"Sadat","year":"2011","journal-title":"Int. Dairy J."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"194","DOI":"10.1016\/j.foodchem.2015.02.046","article-title":"Identification and characterization of antioxidant peptides from chickpea protein hydrolysates","volume":"180","author":"Contreras","year":"2015","journal-title":"Food Chem."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"451","DOI":"10.1007\/s13594-015-0226-5","article-title":"Structure-activity relationship of a series of antioxidant tripeptides derived from \u03b2-Lactoglobulin using QSAR modeling","volume":"95","author":"Tian","year":"2015","journal-title":"Dairy Sci. Technol."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"989","DOI":"10.1007\/s00227-003-1128-2","article-title":"Two different proteases produced by a deep-sea psychrotrophic bacterial strain, Pseudoaltermonas sp. SM9913","volume":"143","author":"Chen","year":"2003","journal-title":"Mar. Biol."},{"key":"ref_68","unstructured":"(2016). Determination of Protein in Foods (Standard No. GB 5009.168-2016)."},{"key":"ref_69","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."}],"container-title":["Marine Drugs"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1660-3397\/22\/7\/305\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T15:07:55Z","timestamp":1760108875000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1660-3397\/22\/7\/305"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,6,29]]},"references-count":69,"journal-issue":{"issue":"7","published-online":{"date-parts":[[2024,7]]}},"alternative-id":["md22070305"],"URL":"https:\/\/doi.org\/10.3390\/md22070305","relation":{},"ISSN":["1660-3397"],"issn-type":[{"value":"1660-3397","type":"electronic"}],"subject":[],"published":{"date-parts":[[2024,6,29]]}}}