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This study aimed to verify the following research hypothesis: ACE inhibitors and antioxidant peptides can be released from salmon and carp proteins during simulated <jats:italic>in silico<\/jats:italic> human-like gastrointestinal digestion. The potential to release biopeptides was evaluated using the BIOPEP-UWM quantitative criteria including the profile of biological activity, frequency of the occurrence (A)\/release (A<jats:sub>E<\/jats:sub>) of fragments with an ACE inhibitory or antioxidant activity by selected enzymes, and relative frequency of release of bioactive fragments with a given activity by selected enzymes (W). Salmon collagen and myofibrillar proteins of carp turned out to be the best potential source of the searched peptides\u2013ACE inhibitors and antioxidant peptides. Nonetheless, after digestion, the highest numbers of ACE inhibitors and antioxidant peptides were potentially released from the myofibrillar proteins of salmon and carp. Peptide Ranker Score, Pepsite2, and ADMETlab platform were applied to evaluate peptides\u2019 bioactivity potential, their safety and drug-like properties. Among the 63 sequences obtained after the simulated digestion of salmon and carp proteins, 30 were considered potential biopeptides. The amino acid sequences of ACE-inhibiting and antioxidant peptides were predominated by P, G, F, W, R, and L. The predicted high probability of absorption of most analyzed peptides and their low toxicity should be considered as their advantage.<\/jats:p>","DOI":"10.1371\/journal.pone.0255969","type":"journal-article","created":{"date-parts":[[2021,8,10]],"date-time":"2021-08-10T17:24:42Z","timestamp":1628616282000},"page":"e0255969","update-policy":"https:\/\/doi.org\/10.1371\/journal.pone.corrections_policy","source":"Crossref","is-referenced-by-count":19,"title":["Properties of peptides released from salmon and carp via simulated human-like gastrointestinal digestion described applying quantitative parameters"],"prefix":"10.1371","volume":"16","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-4322-9211","authenticated-orcid":true,"given":"Justyna","family":"Borawska-Dziadkiewicz","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6084-1985","authenticated-orcid":true,"given":"Ma\u0142gorzata","family":"Darewicz","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anna Sylwia","family":"Tarczy\u0144ska","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"340","published-online":{"date-parts":[[2021,8,10]]},"reference":[{"key":"pone.0255969.ref001","doi-asserted-by":"crossref","first-page":"e121","DOI":"10.1161\/STROKEAHA.115.008097","article-title":"Organizational update: the world health organization global status report on noncommunicable diseases 2014; one more landmark step in the combat against stroke and vascular disease","volume":"46","author":"S Mendis","year":"2015","journal-title":"Stroke"},{"key":"pone.0255969.ref002","doi-asserted-by":"crossref","first-page":"334","DOI":"10.1016\/j.jff.2015.04.038","article-title":"Chemometrics and cheminformatics in the analysis of biologically active peptides from food sources","volume":"16","author":"A Iwaniak","year":"2015","journal-title":"J Funct Foods"},{"key":"pone.0255969.ref003","doi-asserted-by":"crossref","first-page":"863","DOI":"10.1007\/s00394-015-0974-2","article-title":"Food protein-derived bioactive peptides in management of type 2 diabetes","volume":"54","author":"P Patil","year":"2015","journal-title":"Eur J Nutr"},{"key":"pone.0255969.ref004","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1016\/j.cofs.2014.09.005","article-title":"Bioactive peptides and protein hydrolysates: Research trends and challenges for application as nutraceuticals and functional food ingredients","volume":"1","author":"ECY Li-Chan","year":"2015","journal-title":"Curr Opin Food Sci"},{"key":"pone.0255969.ref005","article-title":"Recent Progress in Enzymatic Release of Peptides in Foods of Animal Origin and Assessment of Bioactivity","author":"F Toldr\u00e1","year":"2020","journal-title":"J Agric Food Chem"},{"key":"pone.0255969.ref006","first-page":"506","volume-title":"Food Chemistry","author":"SY Lee","year":"2017"},{"key":"pone.0255969.ref007","doi-asserted-by":"crossref","first-page":"114","DOI":"10.1111\/1541-4337.12051","article-title":"Food-originating ACE inhibitors, including antihypertensive peptides, as preventive food components in blood pressure reduction","volume":"13","author":"A Iwaniak","year":"2014","journal-title":"Compr Rev Food Sci Food Saf."},{"key":"pone.0255969.ref008","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":"JK Lee","year":"2014","journal-title":"J Funct Foods"},{"key":"pone.0255969.ref009","first-page":"1","volume-title":"Analytica Chimica Acta","author":"C L\u00f3pez-Alarc\u00f3n","year":"2013"},{"key":"pone.0255969.ref010","first-page":"28","article-title":"Globalny rynek \u0142ososia 2007\/08","volume":"2","author":"T. Kulikowski","year":"2008","journal-title":"Mag Przem Rybn"},{"key":"pone.0255969.ref011","unstructured":"FAO. http:\/\/www.fao.org\/state-of-fisheries-aquaculture. In: The State of World Fisheries and Aquaculture 2020. 2020."},{"key":"pone.0255969.ref012","doi-asserted-by":"crossref","first-page":"78","DOI":"10.1016\/j.foodchem.2010.10.080","article-title":"Marine and farmed fish in the Polish market: Comparison of the nutritional value","volume":"126","author":"Z Usydus","year":"2011","journal-title":"Food Chem"},{"key":"pone.0255969.ref013","doi-asserted-by":"crossref","first-page":"14077","DOI":"10.3390\/ijms150814077","article-title":"Angiotensin I-converting enzyme (ACE) inhibitory activity and ace inhibitory peptides of salmon (Salmo salar) protein hydrolysates obtained by human and porcine gastrointestinal enzymes","volume":"15","author":"M Darewicz","year":"2014","journal-title":"Int J Mol Sci"},{"key":"pone.0255969.ref014","doi-asserted-by":"crossref","first-page":"1","DOI":"10.2174\/0929866524666161117115441","article-title":"European Carp (Cyprinus carpi L.) Protein-Derived Ex Vivo Digests and In Vitro Hydrolysates Differ in the ACE I Inhibitory Activity and Composition of Released ACE Inhibitory Peptides","volume":"24","author":"M Darewicz","year":"2017","journal-title":"Protein Pept Lett"},{"key":"pone.0255969.ref015","doi-asserted-by":"crossref","first-page":"111","DOI":"10.17221\/300\/2015-CJFS","article-title":"Carp proteins as a source of bioactive peptides\u2014An in Silico approach","volume":"34","author":"M Darewicz","year":"2016","journal-title":"Czech J Food Sci"},{"key":"pone.0255969.ref016","doi-asserted-by":"crossref","first-page":"3463","DOI":"10.1007\/s00216-018-0974-1","article-title":"Bioinformatics and peptidomics approaches to the discovery and analysis of food-derived bioactive peptides","volume":"410","author":"D Agyei","year":"2018","journal-title":"Anal Bioanal Chem"},{"key":"pone.0255969.ref017","doi-asserted-by":"crossref","first-page":"5978","DOI":"10.3390\/ijms20235978","article-title":"BIOPEP-UWM database of bioactive peptides: Current opportunities","volume":"20","author":"P Minkiewicz","year":"2019","journal-title":"Int J Mol Sci"},{"key":"pone.0255969.ref018","doi-asserted-by":"crossref","first-page":"109616","DOI":"10.1016\/j.lwt.2020.109616","article-title":"An in silico model to predict and estimate digestion-resistant and bioactive peptide content of dairy products: A primarily study of a time-saving and affordable method for practical research purposes","volume":"130","author":"M Barati","year":"2020","journal-title":"LWT"},{"key":"pone.0255969.ref019","article-title":"Biologically active peptides from food proteins: In silico, in vitro and in vivo studies, application aspects, and safety evaluation","volume":"22","author":"P Minkiewicz","year":"2015","journal-title":"Zywn Nauk Technol Jakosc\/Food Sci Technol Qual"},{"key":"pone.0255969.ref020","doi-asserted-by":"crossref","first-page":"103486","DOI":"10.1016\/j.jff.2019.103486","article-title":"Elucidation of the role of in 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Dziuba","year":"2007","journal-title":"Food Sci Technol Int"},{"key":"pone.0255969.ref024","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1177\/1082013210368461","article-title":"Bovine meat proteins as potential precursors of biologically active peptides\u2014a computational study based on the BIOPEP database","volume":"17","author":"P Minkiewicz","year":"2011","journal-title":"Food Sci Technol Int"},{"key":"pone.0255969.ref025","doi-asserted-by":"crossref","first-page":"e73957","DOI":"10.1371\/journal.pone.0073957","article-title":"In Silico Approach for Predicting Toxicity of Peptides and Proteins","volume":"8","author":"S Gupta","year":"2013","journal-title":"PLoS One"},{"key":"pone.0255969.ref026","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0045012","article-title":"Towards the Improved Discovery and Design of Functional Peptides: Common Features of Diverse Classes Permit Generalized Prediction of Bioactivity","volume":"7","author":"C Mooney","year":"2012","journal-title":"PLoS One"},{"key":"pone.0255969.ref027","doi-asserted-by":"crossref","first-page":"423","DOI":"10.1093\/nar\/gks398","article-title":"PepSite: Prediction of peptide-binding sites from protein surfaces","volume":"40","author":"LG Trabuco","year":"2012","journal-title":"Nucleic Acids Res"},{"key":"pone.0255969.ref028","doi-asserted-by":"crossref","first-page":"103618","DOI":"10.1016\/j.jff.2019.103618","article-title":"Dual-function peptides derived from egg white ovalbumin: Bioinformatics identification with validation using in vitro assay","volume":"64","author":"MAS Mohd Salim","year":"2020","journal-title":"J Funct Foods"},{"key":"pone.0255969.ref029","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/s13321-018-0283-x","article-title":"Admetlab: A platform for systematic ADMET evaluation based on a comprehensively collected ADMET database","volume":"10","author":"J Dong","year":"2018","journal-title":"J Cheminform"},{"key":"pone.0255969.ref030","doi-asserted-by":"crossref","first-page":"W357","DOI":"10.1093\/nar\/gkz382","article-title":"SwissTargetPrediction: updated data and new features for efficient prediction of protein targets of small molecules","volume":"47","author":"A Daina","year":"2019","journal-title":"Nucleic Acids Res"},{"key":"pone.0255969.ref031","doi-asserted-by":"crossref","first-page":"e45012","DOI":"10.1371\/journal.pone.0045012","article-title":"Towards the improved discovery and design of functional peptides: common features of diverse classes permit generalized prediction of bioactivity","volume":"7","author":"C Mooney","year":"2012","journal-title":"PLoS One"},{"key":"pone.0255969.ref032","first-page":"13","article-title":"Identification and Functional Mechanism of Novel Angiotensin i Converting Enzyme Inhibitory Dipeptides from Xerocomus badius Cultured in Shrimp Processing Waste Medium","volume":"2018","author":"X Gao","year":"2018","journal-title":"Biomed Res Int"},{"key":"pone.0255969.ref033","doi-asserted-by":"crossref","first-page":"6635","DOI":"10.1021\/jp400974n","article-title":"Catalytic mechanism of angiotensin-converting enzyme and effects of the chloride ion","volume":"117","author":"C Zhang","year":"2013","journal-title":"J Phys Chem B"},{"key":"pone.0255969.ref034","doi-asserted-by":"crossref","first-page":"434","DOI":"10.1111\/j.1365-2621.2002.tb11424.x","article-title":"Antihypertensive activities of peptides derived from porcine skeletal muscle myosin in spontaneously hypertensive rats","volume":"67","author":"Y Nakashima","year":"2002","journal-title":"J Food Sci"},{"key":"pone.0255969.ref035","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":"Y Saito","year":"1994","journal-title":"Biosci Biotechnol Biochem"},{"key":"pone.0255969.ref036","doi-asserted-by":"crossref","first-page":"502","DOI":"10.1046\/j.1432-1327.1999.00885.x","article-title":"Decisive structural determinants for the interaction of proline derivatives with the intestinal H+\/peptide symporter","volume":"266","author":"M Brandsch","year":"1999","journal-title":"Eur J Biochem"},{"key":"pone.0255969.ref037","doi-asserted-by":"crossref","first-page":"415","DOI":"10.1016\/S0955-2863(98)00036-9","article-title":"characterization of angiotensin I-converting enzyme inhibitor dipeptides derived from Allium sativum L (garlic).","volume":"9","author":"Suetsuna K. Isolation","year":"1998","journal-title":"J Nutr Biochem"},{"key":"pone.0255969.ref038","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":"A Fahmi","year":"2004","journal-title":"Process Biochem"},{"key":"pone.0255969.ref039","doi-asserted-by":"crossref","first-page":"812","DOI":"10.1271\/bbb.58.812","article-title":",Antihypertensive Effects of Peptide in Sake and Its By-products on Spontaneously Hypertensive Rats","volume":"58","author":"Y Saito","year":"1994","journal-title":"Biosci Biotechnol Biochem"},{"key":"pone.0255969.ref040","doi-asserted-by":"crossref","first-page":"303","DOI":"10.1016\/j.jff.2017.05.053","article-title":"Transport of angiotensin converting enzyme and renin dual inhibitory peptides LY, RALP and TF across Caco-2 cell monolayers","volume":"35","author":"YJ Yang","year":"2017","journal-title":"J Funct Foods"},{"key":"pone.0255969.ref041","doi-asserted-by":"crossref","first-page":"1611","DOI":"10.1111\/j.1365-2621.2003.tb12300.x","article-title":"Isolation of peptides with angiotensin I-converting enzyme inhibitory effect derived from hydrolysate of upstream chum salmon muscle","volume":"68","author":"S Ono","year":"2003","journal-title":"J Food Sci"},{"key":"pone.0255969.ref042","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":"S Kaiser","year":"2016","journal-title":"Int Dairy J"},{"key":"pone.0255969.ref043","doi-asserted-by":"crossref","first-page":"1398","DOI":"10.1271\/bbb.59.1398","article-title":"Antihypertensive Effects of Angiotensin Fragments in SHR","volume":"59","author":"H Matsufuji","year":"1995","journal-title":"Biosci Biotechnol Biochem"},{"key":"pone.0255969.ref044","first-page":"303","volume-title":"International Dairy Journal","author":"J. Bleiel","year":"2010"},{"key":"pone.0255969.ref045","first-page":"843","volume-title":"Food Chemistry","author":"A Santini","year":"2013"},{"key":"pone.0255969.ref046","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1080\/87559129.2013.818011","article-title":"Biological and Chemical Databases for Research into the Composition of Animal Source Foods","volume":"29","author":"P Minkiewicz","year":"2013","journal-title":"Food Rev Int"},{"key":"pone.0255969.ref047","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1016\/j.tifs.2014.02.004","article-title":"Bioinformatics approaches, prospects and challenges of food bioactive peptide research","volume":"36","author":"CC Udenigwe","year":"2014","journal-title":"Trends Food Sci Technol"},{"key":"pone.0255969.ref048","first-page":"1021","article-title":"Meat proteome as source of functional biopeptides.","volume":"54","author":"CC Udenigwe","year":"2013","journal-title":"FRIN"},{"key":"pone.0255969.ref049","author":"M Geirsd\u00f3ttir","year":"2009","journal-title":"Isolation, purification and investigation of peptides from fish proteins with blood pressure decreasing properties"},{"key":"pone.0255969.ref050","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1016\/j.jprot.2012.11.016","article-title":"The sarcoplasmic fish proteome: Pathways, metabolic networks and potential bioactive peptides for nutritional inferences","volume":"78","author":"M Carrera","year":"2013","journal-title":"J Proteomics"},{"key":"pone.0255969.ref051","doi-asserted-by":"crossref","first-page":"304","DOI":"10.1016\/j.ijbiomac.2017.03.061","article-title":"Physico-chemical characteristics and fibril-forming capacity of carp swim bladder collagens and exploration of their potential bioactive peptides by in silico approaches","volume":"101","author":"GK Pal","year":"2017","journal-title":"Int J Biol Macromol"},{"key":"pone.0255969.ref052","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1016\/j.jchromb.2018.06.056","article-title":"Isolation and identification of a novel algicidal peptide from mackerel muscle hydrolysate","volume":"1093\u20131094","author":"JY Cho","year":"2018","journal-title":"J Chromatogr B Anal Technol Biomed Life Sci"},{"key":"pone.0255969.ref053","doi-asserted-by":"crossref","first-page":"724","DOI":"10.1016\/j.foodchem.2018.08.004","article-title":"An in vitro and in silico study on the antioxidant and cell culture-based study on the chemoprotective activities of fish muscle protein hydrolysates obtained from European seabass and gilthead seabream","volume":"271","author":"C Alt\u0131nelataman","year":"2019","journal-title":"Food Chem"},{"key":"pone.0255969.ref054","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1556\/AAlim.34.2005.4.9","article-title":"The BIOPEP database\u2014A tool for the in silico method of classification of food proteins as the source of peptides with antihypertensive activity","volume":"34","author":"A Iwaniak","year":"2005","journal-title":"Acta Aliment"},{"key":"pone.0255969.ref055","first-page":"1","article-title":"High throughput identification of antihypertensive peptides from fish proteome datasets","volume":"16","author":"Y Yi","year":"2018","journal-title":"Mar Drugs"},{"key":"pone.0255969.ref056","doi-asserted-by":"crossref","first-page":"3642","DOI":"10.1021\/pr200271w","article-title":"Structural determinants of limited proteolysis","volume":"10","author":"MD Kazanov","year":"2011","journal-title":"J Proteome Res"},{"key":"pone.0255969.ref057","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/j.idairyj.2012.12.002","article-title":"Demasking rate constants for tryptic hydrolysis of \u03b2-casein","volume":"30","author":"MM Vorob\u2019ev","year":"2013","journal-title":"Int Dairy J"},{"key":"pone.0255969.ref058","doi-asserted-by":"crossref","first-page":"575","DOI":"10.1016\/j.peptides.2008.06.027","article-title":"Critical evaluation of the use of bioinformatics as a theoretical tool to find high-potential sources of ACE inhibitory peptides","volume":"30","author":"L Vercruysse","year":"2009","journal-title":"Peptides"},{"key":"pone.0255969.ref059","doi-asserted-by":"crossref","first-page":"911","DOI":"10.1111\/j.1444-2906.2008.01606.x","article-title":"Identification of angiotensin I-converting enzyme inhibitory peptides derived from salmon muscle and their antihypertensive effect","volume":"74","author":"H Enari","year":"2008","journal-title":"Fish Sci"},{"key":"pone.0255969.ref060","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":"RZ Gu","year":"2011","journal-title":"Food Res Int"},{"key":"pone.0255969.ref061","doi-asserted-by":"crossref","first-page":"72","DOI":"10.3390\/molecules21010072","article-title":"The Structure-Activity Relationship of the Antioxidant Peptides from Natural Proteins","volume":"21","author":"T-B Zou","year":"2016","journal-title":"Molecules"},{"key":"pone.0255969.ref062","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1002\/psc.800","article-title":"Quantitative structure-activity relationship study of bitter di- and tri-peptides including relationship with angiotensin I-converting enzyme inhibitory activity","volume":"13","author":"J Wu","year":"2007","journal-title":"J Pept Sci"},{"key":"pone.0255969.ref063","doi-asserted-by":"crossref","first-page":"950","DOI":"10.3390\/molecules24050950","article-title":"Structure-activity prediction of ACE inhibitory\/bitter dipeptides\u2014a chemometric approach based on stepwise regression","volume":"24","author":"M Hrynkiewicz","year":"2019","journal-title":"Molecules"},{"key":"pone.0255969.ref064","doi-asserted-by":"crossref","DOI":"10.1038\/srep29809","article-title":"Structural and thermodynamic basis of proline-induced transmembrane complex stabilization","volume":"6","author":"T Schmidt","year":"2016","journal-title":"Sci Rep"},{"key":"pone.0255969.ref065","first-page":"23","volume-title":"Advances in Colloid and Interface Science","author":"B Hern\u00e1ndez-Ledesma","year":"2011"},{"key":"pone.0255969.ref066","doi-asserted-by":"crossref","first-page":"1974","DOI":"10.1002\/jsfa.5570","article-title":"Angiotensin-converting enzyme inhibitory and antioxidative activities and functional characterization of protein hydrolysates of hard-to-cook chickpeas","volume":"92","author":"S Medina-Godoy","year":"2012","journal-title":"J Sci Food Agric"},{"key":"pone.0255969.ref067","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":"BH Sarmadi","year":"2010","journal-title":"Peptides"},{"key":"pone.0255969.ref068","doi-asserted-by":"crossref","first-page":"3661","DOI":"10.1021\/jf021156g","article-title":"Antioxidant activity of peptides obtained from porcine myofibrillar proteins by protease treatment","volume":"51","author":"A Saiga","year":"2003","journal-title":"J Agric Food Chem"},{"key":"pone.0255969.ref069","doi-asserted-by":"crossref","first-page":"581","DOI":"10.1021\/jf048877v","article-title":"Antioxidant properties of a radical-scavenging peptide purified from enzymatically prepared fish skin gelatin hydrolysate","volume":"53","author":"E Mendis","year":"2005","journal-title":"J Agric Food Chem"},{"key":"pone.0255969.ref070","doi-asserted-by":"crossref","first-page":"2619","DOI":"10.1021\/jf950833m","article-title":"Antioxidant Activity of Designed Peptides Based on the Antioxidative Peptide Isolated from Digests of a Soybean Protein","volume":"44","author":"HM Chen","year":"1996","journal-title":"J Agric Food Chem"},{"key":"pone.0255969.ref071","first-page":"319","volume":"57","author":"K Arihara","year":"2001","journal-title":"Peptide inhibitors for angiotensin I-converting enzyme from enzymatic hydrolysates of porcine skeletal muscle proteins"},{"key":"pone.0255969.ref072","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":"M Terashima","year":"2010","journal-title":"J Agric Food Chem"},{"key":"pone.0255969.ref073","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1002\/biot.200700045","article-title":"Putting microbes to work: Diary fermentation, cell factories and bioactive peptides. Part II: Bioactive peptide functions","volume":"2","author":"M Hayes","year":"2007","journal-title":"Biotechnol J"},{"key":"pone.0255969.ref074","first-page":"239","article-title":"Structure and activity of angiotensin I converting enzyme inhibitory peptides derived from alaskan pollack skin","volume":"35","author":"HG Byun","year":"2002","journal-title":"J Biochem Mol Biol"},{"key":"pone.0255969.ref075","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":"H Matsufuji","year":"1994","journal-title":"Biosci Biotechnol Biochem"},{"key":"pone.0255969.ref076","doi-asserted-by":"crossref","first-page":"106","DOI":"10.1016\/j.niox.2010.04.006","article-title":"Tryptic amaranth glutelin digests induce endothelial nitric oxide production through inhibition of ACE: Antihypertensive role of amaranth peptides","volume":"23","author":"AP Barba de la Rosa","year":"2010","journal-title":"Nitric Oxide\u2014Biol Chem"},{"key":"pone.0255969.ref077","doi-asserted-by":"crossref","first-page":"403","DOI":"10.1016\/j.jff.2012.01.008","article-title":"Evaluation of the potential of dietary proteins as precursors of dipeptidyl peptidase (DPP)-IV inhibitors by an in silico approach.","volume":"4","author":"IME Lacroix","year":"2012","journal-title":"J Funct Foods."},{"key":"pone.0255969.ref078","doi-asserted-by":"crossref","first-page":"582","DOI":"10.1016\/j.foodchem.2009.05.024","article-title":"Fractionation and evaluation of radical scavenging peptides from in vitro digests of buckwheat protein","volume":"118","author":"Y Ma","year":"2010","journal-title":"Food Chem"},{"key":"pone.0255969.ref079","doi-asserted-by":"crossref","first-page":"357","DOI":"10.3136\/fstr.8.357","article-title":"Antioxidative Activity of Peptides Prepared from Okara Protein","volume":"8","author":"A Yokomizo","year":"2002","journal-title":"Food Sci Technol Res"},{"key":"pone.0255969.ref080","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3389\/fphar.2019.00835","article-title":"Reliable target prediction of bioactive molecules based on chemical similarity without employing statistical methods","volume":"10","author":"A Forouzesh","year":"2019","journal-title":"Front Pharmacol"},{"key":"pone.0255969.ref081","doi-asserted-by":"crossref","first-page":"1942","DOI":"10.1111\/ijfs.14048","article-title":"Intestinal absorption of small peptides: a review","volume":"54","author":"W Shen","year":"2019","journal-title":"Int J Food Sci Technol"},{"key":"pone.0255969.ref082","doi-asserted-by":"crossref","first-page":"399","DOI":"10.1016\/j.tifs.2019.02.050","article-title":"Bioavailability of bioactive peptides derived from food proteins across the intestinal epithelial membrane: A review","volume":"86","author":"Q Xu","year":"2019","journal-title":"Trends Food Sci Technol"},{"key":"pone.0255969.ref083","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1016\/j.peptides.2007.09.023","article-title":"Antihypertensive mechanism of the dipeptide Val-Tyr in rat aorta","volume":"29","author":"L Vercruysse","year":"2008","journal-title":"Peptides"},{"key":"pone.0255969.ref084","doi-asserted-by":"crossref","first-page":"709","DOI":"10.1007\/s00217-009-1103-3","article-title":"Antioxidant activities of the rice endosperm protein hydrolysate: Identification of the active peptide","volume":"229","author":"J Zhang","year":"2009","journal-title":"Eur Food Res Technol"},{"key":"pone.0255969.ref085","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1016\/j.ab.2011.02.037","article-title":"Application of 13C stable isotope labeling liquid chromatography-multiple reaction monitoring-tandem mass spectrometry method for determining intact absorption of bioactive dipeptides in rats","volume":"414","author":"EMN Nakashima","year":"2011","journal-title":"Anal Biochem"}],"container-title":["PLOS ONE"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.pone.0255969","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,8,10]],"date-time":"2021-08-10T17:26:12Z","timestamp":1628616372000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.pone.0255969"}},"subtitle":[],"editor":[{"given":"Dulce Elena","family":"Casarini","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"editor"}]}],"short-title":[],"issued":{"date-parts":[[2021,8,10]]},"references-count":85,"journal-issue":{"issue":"8","published-online":{"date-parts":[[2021,8,10]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.pone.0255969","relation":{},"ISSN":["1932-6203"],"issn-type":[{"value":"1932-6203","type":"electronic"}],"subject":[],"published":{"date-parts":[[2021,8,10]]}}}