{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,9]],"date-time":"2026-05-09T20:20:41Z","timestamp":1778358041667,"version":"3.51.4"},"reference-count":214,"publisher":"MDPI AG","issue":"10","license":[{"start":{"date-parts":[[2025,5,8]],"date-time":"2025-05-08T00:00:00Z","timestamp":1746662400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Research in Veterinary Medicine Unit (I-MVET), of the Faculty of Veterinary Medicine, Lus\u00f3fona University"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Nutrients"],"abstract":"<jats:p>The growing threat of antimicrobial resistance has intensified the search for alternative strategies to conventional antibiotics and preservatives. Casein-derived antimicrobial peptides (CDAMPs), generated through proteolysis, exhibit potent activity against a broad spectrum of pathogens, including antibiotic-resistant strains, revealing strong potential as natural preservatives and therapeutic agents in food and medical applications. Furthermore, casein can be an ideal source for peptide production in these sectors due to its abundance, disordered structure, which enhances enzymatic cleavage, and its amino acid profile, which favors bioactivity. Nonetheless, there is limited literature addressing real-life applications in veterinary medicine, food safety, and public health. This review provides a structured synthesis of current knowledge on the antibacterial properties of CDPs. We classify the main types of these peptides, describe their production methods, and summarize their mechanisms of action against Gram-positive and Gram-negative bacteria. Furthermore, we examine their potential applications in clinical, veterinary, and food-related contexts, and discuss key aspects related to delivery systems, safety, and regulatory considerations. Overall, our findings highlight the potential of CDPs in addressing antimicrobial resistance, reducing antibiotic use in livestock and humans, and contributing to sustainable food safety and functional food production.<\/jats:p>","DOI":"10.3390\/nu17101615","type":"journal-article","created":{"date-parts":[[2025,5,8]],"date-time":"2025-05-08T09:58:09Z","timestamp":1746698289000},"page":"1615","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":16,"title":["Casein and Casein-Derived Peptides: Antibacterial Activities and Applications in Health and Food Systems"],"prefix":"10.3390","volume":"17","author":[{"ORCID":"https:\/\/orcid.org\/0009-0002-4191-1997","authenticated-orcid":false,"given":"Tom\u00e1s","family":"Moita","sequence":"first","affiliation":[{"name":"Research in Veterinary Medicine (I-MVET), Faculty of Veterinary Medicine, Lus\u00f3fona University, Lisbon University Centre, Campo Grande, 376, 1749-024 Lisbon, Portugal"}]},{"given":"Laurentina","family":"Pedroso","sequence":"additional","affiliation":[{"name":"Research in Veterinary Medicine (I-MVET), Faculty of Veterinary Medicine, Lus\u00f3fona University, Lisbon University Centre, Campo Grande, 376, 1749-024 Lisbon, Portugal"},{"name":"Veterinary and Animal Research Centre (CECAV), Faculty of Veterinary Medicine, Lus\u00f3fona University, Lisbon University Centre, 1749-024 Lisbon, Portugal"},{"name":"IPLUSO\u2014Polytechnic Institute of Lusofonia, School of Health, Protection and Animal Welfare, Campo Grande 400, 1700-098 Lisbon, Portugal"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9421-9315","authenticated-orcid":false,"given":"Isabel","family":"Santos","sequence":"additional","affiliation":[{"name":"Research in Veterinary Medicine (I-MVET), Faculty of Veterinary Medicine, Lus\u00f3fona University, Lisbon University Centre, Campo Grande, 376, 1749-024 Lisbon, Portugal"},{"name":"Veterinary and Animal Research Centre (CECAV), Faculty of Veterinary Medicine, Lus\u00f3fona University, Lisbon University Centre, 1749-024 Lisbon, Portugal"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8251-6286","authenticated-orcid":false,"given":"Ana","family":"Lima","sequence":"additional","affiliation":[{"name":"Research in Veterinary Medicine (I-MVET), Faculty of Veterinary Medicine, Lus\u00f3fona University, Lisbon University Centre, Campo Grande, 376, 1749-024 Lisbon, Portugal"},{"name":"Veterinary and Animal Research Centre (CECAV), Faculty of Veterinary Medicine, Lus\u00f3fona University, Lisbon University Centre, 1749-024 Lisbon, Portugal"},{"name":"IPLUSO\u2014Polytechnic Institute of Lusofonia, School of Health, Protection and Animal Welfare, Campo Grande 400, 1700-098 Lisbon, Portugal"}]}],"member":"1968","published-online":{"date-parts":[[2025,5,8]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","unstructured":"Runthala, A., Mbye, M., Ayyash, M., Xu, Y., and Kamal-Eldin, A. (2023). Caseins: Versatility of Their Micellar Organization in Relation to the Functional and Nutritional Properties of Milk. Molecules, 28.","DOI":"10.3390\/molecules28052023"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1093\/nutrit\/nuab097","article-title":"Dairy bioactive proteins and peptides: A narrative review","volume":"79","author":"Auestad","year":"2021","journal-title":"Nutr. Rev."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"6","DOI":"10.20463\/pan.2020.0009","article-title":"Pre-sleep casein protein ingestion: New paradigm in post-exercise recovery nutrition","volume":"24","author":"Kim","year":"2020","journal-title":"Phys. Act. Nutr."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"141829","DOI":"10.1016\/j.foodchem.2024.141829","article-title":"Unveiling the slow digestion and peptide profiles of polymerised whey gel via heat and TGase crosslinking: An in vitro\/vivo perspective","volume":"464","author":"Leng","year":"2025","journal-title":"Food Chem."},{"key":"ref_5","doi-asserted-by":"crossref","unstructured":"Jim\u00e9nez-Barrios, P., S\u00e1nchez-Rivera, L., Mart\u00ednez-Maqueda, D., Gouar, Y.L., Dupont, D., Miralles, B., and Recio, I. (2023). Peptidomic Characterization and Amino Acid Availability after Intake of Casein vs. a Casein Hydrolysate in a Pig Model. Nutrients, 15.","DOI":"10.3390\/nu15051065"},{"key":"ref_6","unstructured":"Walter, L., and Hurley, W.L. (2012). Alpha-Casein as a Molecular Chaperone. Milk Protein, InTech."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"139369","DOI":"10.1016\/j.foodchem.2024.139369","article-title":"Stabilizing interactions of casein microparticles after a thermal post-treatment","volume":"450","author":"Gebhardt","year":"2024","journal-title":"Food Chem."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"837","DOI":"10.1080\/10942912.2015.1048356","article-title":"Milk derived antimicrobial bioactive peptides: A review","volume":"19","author":"Mohanty","year":"2016","journal-title":"Int. J. Food Prop."},{"key":"ref_9","doi-asserted-by":"crossref","unstructured":"Hou, J., Liu, Z., Cao, S., Wang, H., Jiang, C., Hussain, M.A., and Pang, S. (2018). Broad-Spectrum antimicrobial activity and low cytotoxicity against human cells of a peptide derived from bovine \u03b1S1-casein. Molecules, 23.","DOI":"10.3390\/molecules23051220"},{"key":"ref_10","doi-asserted-by":"crossref","unstructured":"Daliri, E.B.-M., Oh, D.H., and Lee, B.H. (2017). Bioactive peptides. Foods, 6.","DOI":"10.3390\/foods6050032"},{"key":"ref_11","doi-asserted-by":"crossref","unstructured":"Aslam, B., Khurshid, M., Arshad, M.I., Muzammil, S., Rasool, M., Yasmeen, N., Shah, T., Chaudhry, T.H., Rasool, M.H., and Shahid, A. (2021). Antibiotic Resistance: One Health One World Outlook. Front. Cell. Infect. Microbiol., 11.","DOI":"10.3389\/fcimb.2021.771510"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"116072","DOI":"10.1016\/j.ejmech.2023.116072","article-title":"Antimicrobial peptides: An alternative to traditional antibiotics","volume":"265","author":"Ji","year":"2024","journal-title":"Eur. J. Med. Chem."},{"key":"ref_13","doi-asserted-by":"crossref","unstructured":"Luo, Y., and Song, Y. (2021). Mechanism of antimicrobial peptides: Antimicrobial, anti-inflammatory and antibiofilm activities. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms222111401"},{"key":"ref_14","first-page":"48","article-title":"Antimicrobial peptides: Mechanism of action, activity and clinical potential","volume":"8","author":"Zhang","year":"2021","journal-title":"Mil. Med. Res."},{"key":"ref_15","doi-asserted-by":"crossref","unstructured":"Wang, S., Zeng, X., Yang, Q., and Qiao, S. (2016). Antimicrobial peptides as potential alternatives to antibiotics in food animal industry. Int. J. Mol. Sci., 17.","DOI":"10.3390\/ijms17050603"},{"key":"ref_16","doi-asserted-by":"crossref","unstructured":"Chakrabarti, S., Guha, S., and Majumder, K. (2018). Food-derived bioactive peptides in human health: Challenges and opportunities. Nutrients, 10.","DOI":"10.3390\/nu10111738"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1016\/j.tifs.2020.09.012","article-title":"Dairy and plant proteins as natural food emulsifiers","volume":"105","author":"Kim","year":"2020","journal-title":"Trends Food Sci. Technol."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"451","DOI":"10.1002\/jobm.201100590","article-title":"Optimization of media components for chitinase production by chickpea rhizosphere associated Lysinibacillus fusiformis B-CM18","volume":"53","author":"Singh","year":"2013","journal-title":"J. Basic Microbiol."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"178","DOI":"10.1016\/j.tifs.2016.10.005","article-title":"Utilizing unique properties of caseins and the casein micelle for delivery of sensitive food ingredients and bioactives","volume":"57","author":"Ranadheera","year":"2016","journal-title":"Trends Food Sci. Technol."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1007\/s41061-017-0158-z","article-title":"Potential of Casein as a Carrier for Biologically Active Agents","volume":"375","year":"2017","journal-title":"Top. Curr. Chem."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1024\/0300-9831\/a000418","article-title":"Health Implications of Bioactive Peptides: A Review","volume":"88","author":"Nourmohammadi","year":"2018","journal-title":"Int. J. Vitam. Nutr. Res."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"e0209","DOI":"10.15275\/rusomj.2022.0209","article-title":"Structure and biological functions of milk caseins","volume":"11","author":"Petrova","year":"2022","journal-title":"Russ. Open Med. J."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1007\/s12602-022-10004-y","article-title":"Milk-Derived Antimicrobial Peptides: Overview, Applications, and Future Perspectives","volume":"15","author":"Singh","year":"2022","journal-title":"Probiotics Antimicrob. Proteins"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"4897","DOI":"10.1021\/acs.jafc.9b00204","article-title":"Chemical Composition of Commercial Cow\u2019s Milk","volume":"67","author":"Foroutan","year":"2019","journal-title":"J. Agric. Food Chem."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"2","DOI":"10.1186\/s43014-020-00045-7","article-title":"A comprehensive review on bioactive peptides derived from milk and milk products of minor dairy species","volume":"3","author":"Guha","year":"2021","journal-title":"Food Prod. Process Nutr."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"2","DOI":"10.1016\/j.idairyj.2016.01.004","article-title":"Casein and casein micelle structures, functions and diversity in 20 species","volume":"60","author":"Holt","year":"2016","journal-title":"Int. Dairy J."},{"key":"ref_27","unstructured":"Yada, R.Y. (2018). The caseins: Structure, stability, and functionality. Proteins in Food Processing, Elsevier. [2nd ed.]."},{"key":"ref_28","doi-asserted-by":"crossref","unstructured":"Fox, P.F., and McSweeney, P.L.H. (2003). Casein Micelle Structure, Functions and Interactions. Advanced Dairy Chemistry\u20141 Proteins, Springer Science + Business Media. [3rd ed.].","DOI":"10.1007\/978-1-4419-8602-3"},{"key":"ref_29","unstructured":"Caballero, B., Finglas, P., and Toldra, F. (2016). Milk: Sources and Composition. Encyclopedia of Food and Health, Elsevier."},{"key":"ref_30","unstructured":"(2025). The UniProt Consortium, UniProt: The Universal Protein Knowledgebase in 2025. Nucleic Acids Res., 53, D609\u2013D617."},{"key":"ref_31","doi-asserted-by":"crossref","unstructured":"Minkiewicz, P., Iwaniak, A., and Darewicz, M. (2019). BIOPEP-UWM Database of Bioactive Peptides: Current Opportunities. Int. J. Mol. Sci., 20.","DOI":"10.3390\/ijms20235978"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"8368","DOI":"10.3168\/jds.2023-23456","article-title":"Novel details on the dissociation of casein micelle suspensions as a function of pH and temperature","volume":"106","author":"Moller","year":"2023","journal-title":"J. Dairy Sci."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1016\/j.idairyj.2016.11.010","article-title":"Bovine \u03b2-casein: Isolation, properties and functionality. A review","volume":"66","author":"Atamer","year":"2016","journal-title":"Int. Dairy J."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"118","DOI":"10.1111\/j.1471-0307.2006.00250.x","article-title":"Bioactive Peptides and Lactic Fermentations","volume":"59","author":"Fitzgerald","year":"2006","journal-title":"Int. J. Dairy Technol."},{"key":"ref_35","doi-asserted-by":"crossref","unstructured":"Kanekanian, A. (2014). Bioactive Peptides from Casein and Whey Proteins. Milk and Dairy Products as Functional Foods, Wiley Blackwell.","DOI":"10.1002\/9781118635056"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"11510","DOI":"10.1080\/10408398.2023.2240396","article-title":"Bioactive milk peptides: An updated comprehensive overview and database","volume":"64","author":"Nielsen","year":"2023","journal-title":"Crit. Rev. Food Sci. Nutr."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"643","DOI":"10.1016\/j.idairyj.2009.06.001","article-title":"Casein-derived bioactive peptides: Biological effects, industrial uses, safety aspects and regulatory status","volume":"19","author":"Phelan","year":"2009","journal-title":"Int. Dairy J."},{"key":"ref_38","doi-asserted-by":"crossref","unstructured":"Zhou, S., Xu, T., Zhang, X., Luo, J., An, P., and Luo, Y. (2022). Effect of casein hydrolysate on Cardiovascular Risk Factors: A Systematic Review and Meta-Analysis of Randomized Controlled Trials. Nutrients, 14.","DOI":"10.3390\/nu14194207"},{"key":"ref_39","doi-asserted-by":"crossref","unstructured":"De Vasconcelos, M.L., Oliveira, L.M.F.S., Hill, J.P., and Vidal, A.M.C. (2023). Difficulties in Establishing the Adverse Effects of \u03b2-Casomorphin-7 Released from \u03b2-Casein Variants\u2014A Review. Foods, 12.","DOI":"10.3390\/foods12173151"},{"key":"ref_40","doi-asserted-by":"crossref","unstructured":"Liu, H., Zhang, L., Yu, J., and Shao, S. (2024). Advances in the application and mechanism of bioactive peptides in the treatment of inflammation. Front. Immunol., 15.","DOI":"10.3389\/fimmu.2024.1413179"},{"key":"ref_41","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_42","doi-asserted-by":"crossref","first-page":"1331","DOI":"10.2174\/1381612033454856","article-title":"Opioid receptor ligands derived from food proteins","volume":"9","author":"Teschemacher","year":"2003","journal-title":"Curr. Pharm. Des."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"777","DOI":"10.3168\/jds.S0022-0302(95)76689-9","article-title":"Purification and characterization of angiotensin-converting enzyme inhibitors from sour milk","volume":"78","author":"Nakamura","year":"1995","journal-title":"J. Dairy Sci."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1002\/(SICI)1521-3803(19990601)43:3<159::AID-FOOD159>3.0.CO;2-R","article-title":"Antihypertensive peptides derived from milk proteins","volume":"43","author":"Yamamoto","year":"1999","journal-title":"Food\/Nahrung"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"1225","DOI":"10.2174\/1381612033454865","article-title":"Antimicrobial Peptides from Food Proteins","volume":"9","author":"Pellegrini","year":"2003","journal-title":"Curr. Pharm. Des."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1016\/j.idairyj.2004.06.008","article-title":"Isolation and characterisation of antibacterial peptides derived from the f(164-207) region of bovine \u03b1S2-casein","volume":"15","author":"McCann","year":"2005","journal-title":"Int. Dairy J."},{"key":"ref_47","doi-asserted-by":"crossref","unstructured":"Benoit, S., Chaumontet, C., Violle, N., Boulier, A., Hafeez, Z., Cakir-Kiefer, C., Tom\u00e9, D., Schwarz, J., and Miclo, L. (2022). The Anxiolytic-like Properties of a Tryptic Hydrolysate of Bovine \u03b1s1 Casein Containing \u03b1-Casozepine Rely on GABAA Receptor Benzodiazepine Binding Sites but Not the Vagus Nerve. Nutrients, 14.","DOI":"10.3390\/nu14112212"},{"key":"ref_48","doi-asserted-by":"crossref","unstructured":"Freret, T., Largilliere, S., N\u00e9e, G., Coolzaet, M., Corvaisier, S., and Boulouard, M. (2021). Fast Anxiolytic-Like Effect Observed in the Rat Conditioned Defensive Burying Test, after a Single Oral Dose of Natural Protein Extract Products. Nutrients, 13.","DOI":"10.3390\/nu13072445"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"726","DOI":"10.1080\/10408398.2016.1217825","article-title":"Antioxidative and antibacterial peptides derived from bovine milk proteins","volume":"58","author":"Sah","year":"2016","journal-title":"Crit. Rev. Food Sci. Nutr."},{"key":"ref_50","doi-asserted-by":"crossref","unstructured":"Abril, A.G., Pazos, M., Villa, T.G., Calo-Mata, P., Barros-Vel\u00e1zquez, J., and Carrera, M. (2022). Proteomics Characterization of Food-Derived Bioactive Peptides with Anti-Allergic and Anti-Inflammatory Properties. Nutrients, 14.","DOI":"10.3390\/nu14204400"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"945","DOI":"10.1016\/j.idairyj.2005.10.012","article-title":"Bioactive peptides: Production and functionality","volume":"16","author":"Korhonen","year":"2006","journal-title":"Int. Dairy J."},{"key":"ref_52","doi-asserted-by":"crossref","unstructured":"Bamdad, F., Bark, S., Kwon, C.H., Suh, J.W., and Sunwoo, H. (2017). Anti-inflammatory and antioxidant properties of peptides released from \u03b2-lactoglobulin by high hydrostatic pressure-assisted enzymatic hydrolysis. Molecules, 22.","DOI":"10.3390\/molecules22060949"},{"key":"ref_53","doi-asserted-by":"crossref","unstructured":"Liu, M., Khani, A., Eghbalpour, S., and Uversky, V.N. (2022). Bioactive Peptides: Synthesis, Sources, Applications, and Proposed Mechanisms of Action. Int. J. Mol. Sci., 23.","DOI":"10.3390\/ijms23031445"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"315","DOI":"10.1007\/s00726-012-1379-7","article-title":"Manufacturing of peptides exhibiting biological activity","volume":"44","author":"Zambrowicz","year":"2013","journal-title":"Amino Acids"},{"key":"ref_55","doi-asserted-by":"crossref","unstructured":"Santos, I., Silva, M., Gr\u00e1cio, M., Pedroso, L., and Lima, A. (2024). Milk Antiviral Proteins and Derived Peptides against Zoonoses. Int. J. Mol. Sci., 25.","DOI":"10.3390\/ijms25031842"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"401","DOI":"10.1016\/j.foodcont.2010.09.010","article-title":"Isolation and screening of lactic acid bacteria from Thai traditional fermented fish (Plasom) and production of Plasom from selected strains","volume":"22","author":"Hwanhlem","year":"2011","journal-title":"Food Control"},{"key":"ref_57","doi-asserted-by":"crossref","unstructured":"Abdul Hakim, B.N., Xuan, N.J., and Oslan, S.N.H. (2023). A Comprehensive Review of Bioactive Compounds from Lactic Acid Bacteria: Potential Functions as Functional Food in Dietetics and the Food Industry. Foods, 12.","DOI":"10.3390\/foods12152850"},{"key":"ref_58","doi-asserted-by":"crossref","unstructured":"Mokoena, M.P. (2017). Lactic acid bacteria and their bacteriocins: Classification, biosynthesis and applications against uropathogens: A mini\u2013review. Molecules, 22.","DOI":"10.3390\/molecules22081255"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1016\/j.foodcont.2014.06.034","article-title":"Antibacterial mechanism of lactic acid on physiological and morphological properties of Salmonella Enteritidis, Escherichia coli and Listeria monocytogenes","volume":"47","author":"Wang","year":"2015","journal-title":"Food Control"},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1016\/j.tifs.2020.12.002","article-title":"Novel technologies for the production of bioactive peptides","volume":"108","author":"Ulug","year":"2020","journal-title":"Trends Food Sci. Technol."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"1417","DOI":"10.1002\/fsn3.976","article-title":"Effects of combined high pressure and enzymatic treatments on physicochemical and antioxidant properties of peanut proteins","volume":"7","author":"Dong","year":"2019","journal-title":"Food Sci. Nutr."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1016\/j.foodchem.2018.01.133","article-title":"Changes on antioxidant activity of microwave-treated protein hydrolysates after simulated gastrointestinal digestion: Purification and identification","volume":"254","author":"Ketnawa","year":"2018","journal-title":"Food Chem."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1016\/j.foodchem.2015.10.116","article-title":"Peptidomic analysis reveals proteolytic activity of kefir microorganisms on bovine milk proteins","volume":"197","author":"Dallas","year":"2015","journal-title":"Food Chem."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"554","DOI":"10.1021\/jf202176d","article-title":"Variability of Hydrolysis of \u03b2-, \u03b1s1- and \u03b1s2-Caseins by 10 Strains of Streptococcus thermophilus and Resulting Bioactive Peptides","volume":"60","author":"Miclo","year":"2011","journal-title":"J. Agric. Food Chem."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"3514","DOI":"10.3168\/jds.2011-5046","article-title":"Cheese peptidomics: A detailed study on the evolution of the oligopeptide fraction in Parmigiano-Reggiano cheese from curd to 24 months of aging","volume":"95","author":"Sforza","year":"2012","journal-title":"J. Dairy Sci."},{"key":"ref_66","first-page":"396","article-title":"Identification of antioxidant peptides in cheddar cheese made with adjunct culture Lactobacillus casei ssp. casei 300","volume":"65","author":"Gupta","year":"2010","journal-title":"Milchwissenschaft"},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"2795","DOI":"10.1021\/jf7036533","article-title":"Sensomics mapping and identification of the key bitter metabolites in gouda cheese","volume":"56","author":"Toelstede","year":"2008","journal-title":"J. Agric. Food Chem."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"553","DOI":"10.1111\/j.1365-2621.2002.tb10637.x","article-title":"Isolation and Identification of Low-Molecular-Weight Peptides from Emmentaler Cheese","volume":"67","author":"Combes","year":"2002","journal-title":"J. Food Sci."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1016\/j.cofs.2018.01.005","article-title":"New approaches based on comparative proteomics for the assessment of food quality","volume":"22","author":"Mora","year":"2018","journal-title":"Curr. Opin. Food Sci."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"1626","DOI":"10.1080\/10942912.2019.1666137","article-title":"Lactoferrin (LF): A natural antimicrobial protein","volume":"22","author":"Niaz","year":"2019","journal-title":"Int. J. Food Prop."},{"key":"ref_71","doi-asserted-by":"crossref","unstructured":"Khan, M.U., Pirzadeh, M., F\u00f6rster, C.Y., Shityakov, S., and Shariati, M.A. (2018). Role of milk-derived antibacterial peptides in modern food biotechnology: Their synthesis, applications and future perspectives. Biomolecules, 8.","DOI":"10.3390\/biom8040110"},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"1469","DOI":"10.1128\/IAI.69.3.1469-1476.2001","article-title":"Human lactoferrin and peptides derived from its N terminus are highly effective against infections with antibiotic-resistant bacteria","volume":"69","author":"Nibbering","year":"2001","journal-title":"Infect. Immun."},{"key":"ref_73","first-page":"273","article-title":"rRNA Probes Used to Quantify the Effects of Glycomacropeptide and-Lactalbumin Supplementation on the Predominant Groups of Intestinal Bacteria of Infant Rhesus Monkeys Challenged with Enteropathogenic Escherichia coli","volume":"37","author":"Kelleher","year":"2003","journal-title":"J. Pediatr. Gastroenterol. Nutr."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"2291","DOI":"10.1039\/C9FO02813G","article-title":"A novel endogenous antimicrobial peptide CAMP211-225 derived from casein in human milk","volume":"11","author":"Wang","year":"2020","journal-title":"Food Funct."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"2243","DOI":"10.1002\/mnfr.201500182","article-title":"Virtual screening of a milk peptide database for the identification of food-derived antimicrobial peptides","volume":"59","author":"Liu","year":"2015","journal-title":"Mol. Nutr. Food Res."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"2260","DOI":"10.1128\/AEM.72.3.2260-2264.2006","article-title":"Casein-Derived Antimicrobial Peptides Generated by Lactobacillus acidophilus DPC6026","volume":"72","author":"Hayes","year":"2006","journal-title":"Appl. Environ. Microbiol."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1111\/j.1472-765X.2012.03271.x","article-title":"Production of the antimicrobial peptides Caseicin A and B by Bacillus isolates growing on sodium caseinate","volume":"55","author":"Kent","year":"2012","journal-title":"Lett. Appl. Microbiol."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"2353","DOI":"10.1128\/AEM.07312-11","article-title":"Extensive manipulation of caseicins A and B highlights the tolerance of these antimicrobial peptides to change","volume":"78","author":"Norberg","year":"2012","journal-title":"Appl. Environ. Microbiol."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"443","DOI":"10.1016\/j.foodchem.2013.09.094","article-title":"Antimicrobial activity of antihypertensive food-derived peptides and selected alanine analogues","volume":"146","author":"McClean","year":"2013","journal-title":"Food Chem."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1016\/0278-6915(95)00097-6","article-title":"Antibacterial and immunostimulating casein-derived substances from milk: Casecidin, isracidin peptides","volume":"34","author":"Lahov","year":"1996","journal-title":"Food Chem. Toxicol."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1111\/j.1365-2672.2008.03996.x","article-title":"Antimicrobial activity of two peptides casecidin 15 and 17, found naturally in bovine colostrum","volume":"106","author":"Birkemo","year":"2008","journal-title":"J. Appl. Microbiol."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"2348","DOI":"10.3168\/jds.S0022-0302(05)72913-1","article-title":"Antibacterial Activities of Peptides from the Water-Soluble Extracts of Italian Cheese Varieties","volume":"88","author":"Rizzello","year":"2005","journal-title":"J. Dairy Sci."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"316","DOI":"10.1016\/j.idairyj.2005.05.005","article-title":"Isolation and characterisation of a novel antibacterial peptide from bovine \u03b1S1-casein","volume":"16","author":"McCann","year":"2005","journal-title":"Int. Dairy J."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"413","DOI":"10.1016\/j.foodcont.2014.09.030","article-title":"An antimicrobial peptide screened from casein hydrolyzate by Saccharomyces cerevisiae cell membrane affinity method","volume":"50","author":"Tang","year":"2014","journal-title":"Food Control"},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1002\/biof.1023","article-title":"Identification of novel antibacterial peptides isolated from a commercially available casein hydrolysate by autofocusing technique","volume":"38","author":"Elbarbary","year":"2012","journal-title":"BioFactors"},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"1072","DOI":"10.1016\/j.idairyj.2005.10.006","article-title":"Identification of antibacterial peptides from ovine \u03b1s2-casein","volume":"16","author":"Amigo","year":"2006","journal-title":"Int. Dairy J."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"5179","DOI":"10.1128\/AEM.01394-13","article-title":"Structure-Activity Relationship of Synthetic Variants of the Milk-Derived Antimicrobial Peptide \u03b1 s2 -Casein f(183\u2013207)","volume":"79","author":"Begley","year":"2013","journal-title":"Appl. Environ. Microbiol."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"314","DOI":"10.1016\/S0304-4165(99)00079-3","article-title":"Identification of two distinct antibacterial domains within the sequence of bovine \u03b1s2-casein","volume":"1428","author":"Recio","year":"1999","journal-title":"Biochim. Biophys. Acta Gen. Subj."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"2444","DOI":"10.1016\/j.bbamem.2008.06.018","article-title":"Identification of the initial binding sites of \u03b1s2-casein f(183\u2013207) and effect on bacterial membranes and cell morphology","volume":"1778","author":"Amigo","year":"2008","journal-title":"Biochim. Biophys. Acta Biomembr."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"2184","DOI":"10.3168\/jds.2007-0037","article-title":"Synergistic effect between different Milk-Derived peptides and proteins","volume":"91","author":"Pellegrini","year":"2008","journal-title":"Int. Dairy J."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1007\/s11010-013-1778-4","article-title":"Structure\u2013activity relationships of \u03b1s-casein peptides with multifunctional biological activities","volume":"384","author":"Sistla","year":"2013","journal-title":"Mol. Cell. Biochem."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1016\/0014-5793(95)00974-E","article-title":"Casocidin-I: A casein-\u03b1s2 derived peptide exhibits antibacterial activity","volume":"372","author":"Zucht","year":"1995","journal-title":"FEBS Lett."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1016\/j.jff.2017.02.026","article-title":"Antibacterial activity of new peptide from bovine casein hydrolyzed by a serine metalloprotease of Lactococcus lactis subsp lactis BR16","volume":"32","author":"Bougherra","year":"2017","journal-title":"J. Funct. Foods"},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"104651","DOI":"10.1016\/j.idairyj.2020.104651","article-title":"Inhibitory effect of milk-derived peptide \u03b1S2-casein151-181 against spore-forming bacteria","volume":"104","author":"Liu","year":"2020","journal-title":"Int. Dairy J."},{"key":"ref_95","doi-asserted-by":"crossref","unstructured":"Ouertani, A., Chaabouni, I., Mosbah, A., Long, J., Barakat, M., Mansuelle, P., Mghirbi, O., Najjari, A., Ouzari, H., and Masmoudi, A.S. (2018). Two New Secreted Proteases Generate a Casein-Derived Antimicrobial Peptide in Bacillus cereus Food Born Isolate Leading to Bacterial Competition in Milk. Front. Microbiol., 9.","DOI":"10.3389\/fmicb.2018.01148"},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1016\/j.lwt.2015.12.019","article-title":"Isolation and identification of some antibacterial peptides in the plasmin-digest of \u03b2-casein","volume":"68","author":"Sedaghati","year":"2015","journal-title":"LWT"},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"2992","DOI":"10.4315\/0362-028X-69.12.2992","article-title":"Identification of Antibacterial Peptides from Bovine \u03ba-Casein","volume":"69","author":"Minervini","year":"2006","journal-title":"J. Food Prot."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1016\/S0304-4165(01)00116-7","article-title":"Isolation and characterization of four bactericidal domains in the bovine \u03b2-lactoglobulin","volume":"1526","author":"Pellegrini","year":"2001","journal-title":"Biochim. Biophys. Acta Gen. Subj."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"218","DOI":"10.1080\/09540105.2014.893998","article-title":"Plasmin-digest of \u03b2-lactoglobulin with antibacterial properties","volume":"26","author":"Sedaghati","year":"2014","journal-title":"Food Agric. Immunol."},{"key":"ref_100","first-page":"94","article-title":"Antibacterial activity of peptides extracted from tryptic hydrolyzate of whey protein by nanofiltration","volume":"28","author":"Gauthier","year":"2012","journal-title":"Int. Dairy J."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"706","DOI":"10.1016\/j.jff.2013.01.014","article-title":"Isolation and identification of antimicrobial peptides derived by peptic cleavage of whey protein isolate","volume":"5","author":"Hammami","year":"2013","journal-title":"J. Funct. Foods"},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1111\/j.1834-7819.2012.01711.x","article-title":"Antibacterial efficacy of casein-derived peptides against Enterococcus faecalis","volume":"57","author":"Liu","year":"2012","journal-title":"Aust. Dent. J."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"2309","DOI":"10.1128\/AAC.45.8.2309-2315.2001","article-title":"Kappacin, a Novel Antibacterial Peptide from Bovine Milk","volume":"45","author":"Malkoski","year":"2001","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1017\/S0022029914000120","article-title":"Plasmin digest of \u03ba-casein as a source of antibacterial peptides","volume":"81","author":"Sedaghati","year":"2014","journal-title":"J. Dairy Res."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3168\/jds.2010-4142","article-title":"Effect of pepsin-treated bovine and goat caseinomacropeptide on Escherichia coli and Lactobacillus rhamnosus in acidic conditions","volume":"95","author":"Robitaille","year":"2011","journal-title":"J. Dairy Sci."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"88","DOI":"10.18683\/germs.2021.1244","article-title":"Salmonella spp. Infection\u2014A continuous threat worldwide","volume":"15","author":"Popa","year":"2021","journal-title":"Germs"},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"811","DOI":"10.1016\/j.tim.2021.01.008","article-title":"Making Sense of the Biodiversity and Virulence of Listeria monocytogenes","volume":"29","author":"Disson","year":"2021","journal-title":"Trends Microbiol."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"4645","DOI":"10.2147\/IDR.S365269","article-title":"Review of Escherichia coli O157:H7 Prevalence, Pathogenicity, Heavy Metal and Antimicrobial Resistance, African Perspective","volume":"15","author":"Gambushe","year":"2022","journal-title":"Infect. Drug Resist."},{"key":"ref_109","doi-asserted-by":"crossref","unstructured":"Romano, A., Carrella, S., Rezza, S., Nia, Y., Hennekinne, J., Bianchi, D., Martucci, F., Zuccon, F., Gulino, M., and Mari, C. (2023). First report of food poisoning due to staphylococcal enterotoxin type B in d\u00f6ner kebab (Italy). Pathogens, 12.","DOI":"10.3390\/pathogens12091139"},{"key":"ref_110","doi-asserted-by":"crossref","unstructured":"Yang, K., Shi, Y., Li, Y., Wei, G., Zhao, Q., and Huang, A. (2022). iTRAQ-based quantitative proteomic analysis of antibacterial mechanism of milk-derived peptide BCp12 against Escherichia coli. Foods, 11.","DOI":"10.3390\/foods11050672"},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"136454","DOI":"10.1016\/j.foodchem.2023.136454","article-title":"Novel casein antimicrobial peptides for the inhibition of oral pathogenic bacteria","volume":"425","author":"Qi","year":"2023","journal-title":"Food Chem."},{"key":"ref_112","doi-asserted-by":"crossref","unstructured":"Sansi, M.S., Iram, D., Zanab, S., Vij, S., Puniya, A.K., Singh, A., and Meena, S. (2022). Antimicrobial bioactive peptides from goat Milk proteins: In silico prediction and analysis. J. Food Biochem., 46.","DOI":"10.1111\/jfbc.14311"},{"key":"ref_113","doi-asserted-by":"crossref","unstructured":"Tomazou, M., Oulas, A., Anagnostopoulos, A.K., Tsangaris, G.T., and Spyrou, G.M. (2019). In Silico Identification of Antimicrobial Peptides in the Proteomes of Goat and Sheep Milk and Feta Cheese. Proteomes, 7.","DOI":"10.3390\/proteomes7040032"},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"3416","DOI":"10.1002\/jsfa.8854","article-title":"Bioactive hydrolysates from casein: Generation, identification, and in silico toxicity and allergenicity prediction of peptides","volume":"98","author":"Tu","year":"2017","journal-title":"J. Sci. Food Agric."},{"key":"ref_115","first-page":"100494","article-title":"Fundamentals on the molecular mechanism of action of antimicrobial peptides","volume":"8","author":"Evangelista","year":"2019","journal-title":"Acta Mater."},{"key":"ref_116","doi-asserted-by":"crossref","unstructured":"Saubenova, M., Oleinikova, Y., Rapoport, A., Maksimovich, S., Yermekbay, Z., and Khamedova, E. (2024). Bioactive peptides derived from whey proteins for health and functional beverages. Fermentation, 10.","DOI":"10.3390\/fermentation10070359"},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"4037","DOI":"10.1007\/s00284-021-02665-9","article-title":"An alternative to antibiotics: Selected methods to combat zoonotic foodborne bacterial infections","volume":"78","author":"Sakowicz","year":"2021","journal-title":"Curr. Microbiol."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"597","DOI":"10.1128\/AAC.00828-06","article-title":"Length effects in antimicrobial peptides of the (RW)n series","volume":"51","author":"Liu","year":"2007","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_119","doi-asserted-by":"crossref","unstructured":"Bin Hafeez, A., Jiang, X., Bergen, P.J., and Zhu, Y. (2021). Antimicrobial peptides: An update on classifications and databases. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms222111691"},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"132","DOI":"10.1016\/j.bbrc.2017.01.059","article-title":"Antimicrobial activity and mechanism of PDC213, an endogenous peptide from human milk","volume":"484","author":"Sun","year":"2017","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"3779","DOI":"10.3168\/jds.2022-22823","article-title":"Identification and molecular mechanism of action of antibacterial peptides from Flavourzyme-hydrolyzed yak casein against Staphylococcus aureus","volume":"106","author":"Zhang","year":"2023","journal-title":"J. Dairy Sci."},{"key":"ref_122","doi-asserted-by":"crossref","unstructured":"Talapko, J., Me\u0161trovi\u0107, T., Juzba\u0161i\u0107, M., Tomas, M., Eri\u0107, S., Aleksijevi\u0107, L., Beki\u0107, S., Schwarz, D., Mati\u0107, S., and Neuberg, M. (2022). Antimicrobial peptides\u2014Mechanisms of action, antimicrobial effects and clinical applications. Antibiotics, 11.","DOI":"10.3390\/antibiotics11101417"},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"3428","DOI":"10.3168\/jds.2024-26090","article-title":"Milk-derived antimicrobial peptide GMp7: Disrupting protein networks for multi-target antibacterial inhibition and enhanced dairy preservation","volume":"108","author":"He","year":"2025","journal-title":"J. Dairy Sci."},{"key":"ref_124","doi-asserted-by":"crossref","unstructured":"Amiri, E.O., Farmani, J., Amiri, Z.R., Dehestani, A., and Mohseni, M. (2021). Antimicrobial activity, environmental sensitivity, mechanism of action, and food application of \u03b1s165-181 peptide. Int. J. Food Microbiol., 358.","DOI":"10.1016\/j.ijfoodmicro.2021.109403"},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"1878","DOI":"10.3168\/jds.2021-20944","article-title":"Cow and camel milk-derived whey and casein protein hydrolysates demonstrated effective antifungal properties against selected Candida species","volume":"105","author":"Mudgil","year":"2021","journal-title":"J. Dairy Sci."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"105249","DOI":"10.1016\/j.arabjc.2023.105249","article-title":"Antifungal activity and identification of bioactive peptide from Etawa crossbreed goat (Capra hircus) milk protein hydrolyzed using trypsin enzyme","volume":"16","author":"Ningsih","year":"2023","journal-title":"Arab. J. Chem."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"100781","DOI":"10.1016\/j.colcom.2024.100781","article-title":"Reuse of waste casein peptides to capture Cu (II) for long-term antibacterial reutilization","volume":"60","author":"Qu","year":"2024","journal-title":"Colloid Interface Sci. Commun."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"74","DOI":"10.1002\/1097-0282(2000)55:1<74::AID-BIP70>3.0.CO;2-S","article-title":"Combinatorial libraries: A tool to design antimicrobial and antifungal peptide analogues having lytic specificities for structure-activity relationship studies","volume":"55","author":"Blondelle","year":"2000","journal-title":"Biopolymers"},{"key":"ref_129","first-page":"83","article-title":"Bioactive peptides from milk proteins: A perspective for consumers and producers","volume":"56","author":"Meisel","year":"2001","journal-title":"Aust. J. Dairy Technol."},{"key":"ref_130","unstructured":"(2025, February 20). Milk Protein Market Size, Share & Trends Analysis Report by Product (Concentrates, Isolates, Hydrolyzed), by Form (Powder, Liquid), by Application (Food & Beverages, Dietary Supplements), by Region, and Segment Forecasts, 2025\u20132030. Available online: https:\/\/www.grandviewresearch.com\/industry-analysis\/milk-protein-market-report."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"431","DOI":"10.1080\/10408399309527643","article-title":"Whey protein concentrates and isolates: Processing and functional properties","volume":"33","author":"Morr","year":"1993","journal-title":"Crit. Rev. Food Sci. Nutr."},{"key":"ref_132","doi-asserted-by":"crossref","unstructured":"Samtiya, M., Samtiya, S., Badgujar, P.C., Puniya, A.K., Dhewa, T., and Aluko, R.E. (2022). Health-Promoting and Therapeutic Attributes of Milk-Derived Bioactive Peptides. Nutrients, 14.","DOI":"10.3390\/nu14153001"},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"4426","DOI":"10.1111\/1541-4337.12795","article-title":"Progress in micellar casein concentrate: Production and applications","volume":"20","author":"Hammam","year":"2021","journal-title":"Compr. Rev. Food Sci. Food Saf."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"108434","DOI":"10.1016\/j.lwt.2019.108434","article-title":"Protective effects of \u03b1-casein or \u03b2-casein on the stability and antioxidant capacity of blueberry anthocyanins and their interaction mechanism","volume":"115","author":"Lang","year":"2019","journal-title":"Lebensm. Wiss. Technol."},{"key":"ref_135","first-page":"1852","article-title":"Preparation and potential applications of casein\u2013polysaccharide conjugates: A review","volume":"100","year":"2019","journal-title":"J. Sci. Food Agric."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"134","DOI":"10.1080\/87559129.2014.896017","article-title":"Antimicrobial Peptides of Dairy Proteins: From Fundamental to Applications","volume":"30","author":"Fliss","year":"2014","journal-title":"Food Rev. Int."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1007\/s00253-009-2433-6","article-title":"Enzymatic fragmentation of the antimicrobial peptides casocidin and isracidin by Streptococcus thermophilus and Lactobacillus delbrueckii ssp. bulgaricus","volume":"87","author":"Somkuti","year":"2010","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"11116","DOI":"10.3168\/jds.2020-18577","article-title":"Characterization of a novel antimicrobial peptide from buffalo casein hydrolysate based on live bacteria adsorption","volume":"103","author":"Zhao","year":"2020","journal-title":"J. Dairy Sci."},{"key":"ref_139","first-page":"204","article-title":"Antioxidant and antimicrobial peptides derived from casein: Current trends in food preservation","volume":"121","author":"Ribeiro","year":"2019","journal-title":"Food Res. Int."},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"9901018","DOI":"10.1155\/2022\/9901018","article-title":"Potentials of Natural preservatives to Enhance food Safety and shelf life: A review","volume":"2022","author":"Teshome","year":"2022","journal-title":"Sci. World J."},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"136","DOI":"10.1016\/j.tifs.2018.07.003","article-title":"Bioactive peptides as natural antioxidants in food products\u2014A review","volume":"79","author":"Lorenzo","year":"2018","journal-title":"Trends Food Sci. Technol."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1016\/j.meatsci.2018.10.016","article-title":"Natural antioxidants used in meat products: A brief review","volume":"148","author":"Ribeiro","year":"2018","journal-title":"Meat Sci."},{"key":"ref_143","doi-asserted-by":"crossref","unstructured":"L\u00f3pez-Garc\u00eda, G., Dublan-Garc\u00eda, O., Arizmendi-Cotero, D., and G\u00f3mez Oliv\u00e1n, L.M. (2022). Antioxidant and Antimicrobial Peptides Derived from Food Proteins. Molecules, 27.","DOI":"10.3390\/molecules27041343"},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"12369","DOI":"10.1021\/acs.jafc.1c04020","article-title":"Bioactive peptides: A promising alternative to chemical preservatives for food preservation","volume":"69","author":"Zhang","year":"2021","journal-title":"J. Agric. Food Chem."},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"276","DOI":"10.1016\/j.foodqual.2018.10.014","article-title":"Using rejection thresholds to determine acceptability of novel bioactive compounds added to milk-based beverages","volume":"73","author":"Murray","year":"2019","journal-title":"Food Qual. Prefer."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.idairyj.2015.04.001","article-title":"Generation of the antimicrobial peptide caseicin A from casein by hydrolysis with thermolysin enzymes","volume":"49","author":"Guinane","year":"2015","journal-title":"Int. Dairy J."},{"key":"ref_147","doi-asserted-by":"crossref","unstructured":"Zhang, R., Wang, B., Zhang, F., Zheng, K., and Liu, Y. (2024). Milk-derived antimicrobial peptides incorporated whey protein film as active coating to improve microbial stability of refrigerated soft cheese. Int. J. Food Microbiol., 419.","DOI":"10.1016\/j.ijfoodmicro.2024.110751"},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"R125","DOI":"10.1111\/j.1750-3841.2006.00175.x","article-title":"Eukaryotic antimicrobial peptides: Promises and premises in food safety","volume":"71","author":"Rydlo","year":"2006","journal-title":"J. Food Sci."},{"key":"ref_149","doi-asserted-by":"crossref","unstructured":"Gogliettino, M., Balestrieri, M., Ambrosio, R.L., Anastasio, A., Smaldone, G., Proroga, Y.T.R., Moretta, R., Rea, I., De Stefano, L., and Agrillo, B. (2020). Extending the Shelf-Life of meat and dairy products via PET-Modified packaging activated with the antimicrobial peptide MTP1. Front. Microbiol., 10.","DOI":"10.3389\/fmicb.2019.02963"},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"298","DOI":"10.1016\/j.tifs.2020.10.022","article-title":"Peptides and protein hydrolysates as food preservatives and bioactive components of edible films and coatings\u2014A review","volume":"106","author":"Tkaczewska","year":"2020","journal-title":"Trends Food Sci. Technol."},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1016\/j.ifset.2018.06.008","article-title":"Nisin and other antimicrobial peptides: Production, mechanisms of action, and application in active food packaging","volume":"48","author":"Santos","year":"2018","journal-title":"Innov. Food Sci. Emerg. Technol."},{"key":"ref_152","doi-asserted-by":"crossref","unstructured":"Khan, M.R., Volpe, S., Valentino, M., Miele, N.A., Cavella, S., and Torrieri, E. (2021). Active Casein Coatings and Films for Perishable Foods: Structural Properties and Shelf-Life Extension. Coatings, 11.","DOI":"10.3390\/coatings11080899"},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"1253","DOI":"10.3168\/jds.S0022-0302(95)76745-5","article-title":"Antihypertensive Effect of Sour Milk and Peptides Isolated from It That are Inhibitors to Angiotensin I-Converting Enzyme","volume":"78","author":"Nakamura","year":"1995","journal-title":"J. Dairy Sci."},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"1434","DOI":"10.3168\/jds.S0022-0302(00)75013-2","article-title":"Isolation and structural analysis of antihypertensive peptides that exist naturally in Gouda cheese","volume":"83","author":"Saito","year":"2000","journal-title":"J. Dairy Sci."},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"4402","DOI":"10.1021\/jf000895z","article-title":"Peptides identified during Emmental cheese ripening: Origin and proteolytic systems involved","volume":"49","author":"Gagnaire","year":"2001","journal-title":"J. Agric. Food Chem."},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"511","DOI":"10.1016\/S0958-6946(02)00042-0","article-title":"23 Microbiological, compositional, biochemical and textural characterisation of Caciocavallo Pugliese cheese during ripening","volume":"12","author":"Gobbetti","year":"2002","journal-title":"Int. Dairy J."},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1023\/A:1002063805780","article-title":"Bioactive peptides encrypted in milk proteins: Proteolytic activation and thropo-functional properties","volume":"76","author":"Meisel","year":"1999","journal-title":"Antonie Van Leeuwenhoek"},{"key":"ref_158","first-page":"307","article-title":"ACE inhibitory activities in milk products","volume":"52","author":"Meisel","year":"1997","journal-title":"Milchwissenschaft"},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"1684","DOI":"10.1002\/jsfa.11509","article-title":"Nanoencapsulation of CDP within electrospun nanofibres","volume":"102","author":"Rajanna","year":"2022","journal-title":"J. Sci. Food Agric."},{"key":"ref_160","doi-asserted-by":"crossref","first-page":"303","DOI":"10.1016\/j.cis.2003.10.023","article-title":"Formation and stability of nano-emulsions","volume":"108\u2013109","author":"Tadros","year":"2004","journal-title":"Adv. Colloid Interface Sci."},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"1947","DOI":"10.3168\/jds.S0022-0302(05)72870-8","article-title":"Partial Identification of Water-Soluble Peptides Released at Early Stages of Proteolysis in Sterilized Ovine Cheese-Like Systems: Influence of Type of Coagulant and Starter","volume":"88","author":"Silva","year":"2005","journal-title":"J. Dairy Sci."},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"156","DOI":"10.1016\/j.fshw.2019.03.010","article-title":"Isolation and identification of novel casein-derived bioactive peptides and potential functions in fermented casein with Lactobacillus helveticus","volume":"8","author":"Fan","year":"2019","journal-title":"Food Sci. Hum. Wellness"},{"key":"ref_163","doi-asserted-by":"crossref","unstructured":"Coscueta, E.R., Batista, P., Gomes, J.E.G., da Silva, R., and Pintado, M.M. (2022). Screening of Novel Bioactive Peptides from Goat Casein: In Silico to In Vitro Validation. Int. J. Mol. Sci., 23.","DOI":"10.3390\/ijms23052439"},{"key":"ref_164","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1016\/j.fshw.2020.08.014","article-title":"In vitro and in silico analysis of dual-function peptides derived from casein hydrolysate","volume":"10","author":"Tu","year":"2020","journal-title":"Food Sci. Hum. Wellness"},{"key":"ref_165","doi-asserted-by":"crossref","first-page":"126063","DOI":"10.1016\/j.foodchem.2019.126063","article-title":"Casein-based hydrogels: A mini\u2013review","volume":"314","author":"Nascimento","year":"2019","journal-title":"Food Chem."},{"key":"ref_166","doi-asserted-by":"crossref","first-page":"176","DOI":"10.1016\/j.tifs.2021.07.018","article-title":"Industrial production of spirulina as a protein source for bioactive peptide generation","volume":"116","author":"Lafarga","year":"2021","journal-title":"Trends Food Sci. Technol."},{"key":"ref_167","first-page":"79","article-title":"Peptides and proteins","volume":"2021","author":"Montfort","year":"2021","journal-title":"Bioact. Compd. Health Dis."},{"key":"ref_168","doi-asserted-by":"crossref","first-page":"505","DOI":"10.1007\/s10989-007-9094-z","article-title":"Antimicrobial peptides and their potential as oral therapeutic agents","volume":"13","author":"Dashper","year":"2007","journal-title":"Int. J. Pept. Res. Ther."},{"key":"ref_169","unstructured":"Reynolds, E.C., Dashper, S.G., O\u2019Brien-Simpson, N.M., Talbo, G.H., and Malkoski, M. (2007). Antimicrobial Peptides. (EP1032592B1), European Patent, Available online: https:\/\/patents.google.com\/patent\/EP1032592B1\/en."},{"key":"ref_170","unstructured":"Reynolds, E.C., Dashper, S.G., and Paolini, R.A. (2013). Antimicrobial Composition. (AU2010224414B2), Australian Patent, Available online: https:\/\/patents.google.com\/patent\/AU2010224414B2\/en."},{"key":"ref_171","doi-asserted-by":"crossref","first-page":"391","DOI":"10.1016\/j.tifs.2020.01.027","article-title":"Casein and pectin: Structures, interactions, and applications","volume":"97","author":"Wusigale","year":"2020","journal-title":"Trends Food Sci. Technol."},{"key":"ref_172","doi-asserted-by":"crossref","unstructured":"Sarode, A., Sawale, P., Khedkar, C., Kalyankar, S., and Pawshe, R. (2015). Casein and Caseinate: Methods of Manufacture, Elsevier.","DOI":"10.1016\/B978-0-12-384947-2.00122-7"},{"key":"ref_173","doi-asserted-by":"crossref","first-page":"276","DOI":"10.25518\/1780-4507.13692","article-title":"Cow milk coagulation: Process description, variation factors and evaluation methodologies. A review","volume":"21","author":"Troch","year":"2017","journal-title":"BASE"},{"key":"ref_174","first-page":"981","article-title":"Chemical interactions among caseins during rennet coagulation of milk","volume":"105","author":"Olivas","year":"2021","journal-title":"J. Dairy Sci."},{"key":"ref_175","doi-asserted-by":"crossref","first-page":"3233","DOI":"10.1021\/jf960879v","article-title":"Rennet coagulation of milk subjected to high pressures","volume":"45","author":"Ramos","year":"1997","journal-title":"J. Agric. Food Chem."},{"key":"ref_176","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1016\/j.idairyj.2012.03.014","article-title":"Effect of calcium chelators on heat coagulation and heat-induced changes of concentrated micellar casein solutions: The role of calcium-ion activity and micellar integrity","volume":"26","author":"Minor","year":"2012","journal-title":"Int. Dairy J."},{"key":"ref_177","doi-asserted-by":"crossref","first-page":"378","DOI":"10.3168\/jds.S0022-0302(00)74892-2","article-title":"The Two-Stage coagulation of milk proteins in the minimum of the heat coagulation Time-PH profile of milk: Effect of Casein micelle size","volume":"83","author":"Fox","year":"2000","journal-title":"J. Dairy Sci."},{"key":"ref_178","doi-asserted-by":"crossref","first-page":"2465","DOI":"10.3168\/jds.2020-18811","article-title":"Invited review: Microfiltration-derived casein and whey proteins from milk","volume":"104","author":"Carter","year":"2021","journal-title":"J. Dairy Sci."},{"key":"ref_179","doi-asserted-by":"crossref","first-page":"405","DOI":"10.1016\/S0260-8774(97)00053-8","article-title":"A continuous process for casein production using high-pressure carbon dioxide","volume":"33","author":"Tomasula","year":"1997","journal-title":"J. Food Eng."},{"key":"ref_180","doi-asserted-by":"crossref","first-page":"3590","DOI":"10.3168\/jds.S0022-0302(04)73497-9","article-title":"Impact of Milk Preacidification with CO2 on the Aging and Proteolysis of Cheddar Cheese","volume":"87","author":"Nelson","year":"2004","journal-title":"J. Dairy Sci."},{"key":"ref_181","doi-asserted-by":"crossref","first-page":"5236","DOI":"10.1039\/C4AY00895B","article-title":"HPLC separation of casein components on a diol-bonded silica column with MALDI TOF\/TOF MS identification","volume":"6","author":"Pomastowski","year":"2014","journal-title":"Anal. Methods"},{"key":"ref_182","doi-asserted-by":"crossref","first-page":"1725","DOI":"10.3168\/jds.S0022-0302(71)86106-4","article-title":"Chromatographic Separation of milk Proteins: A review","volume":"54","author":"Yaguchi","year":"1971","journal-title":"J. Dairy Sci."},{"key":"ref_183","doi-asserted-by":"crossref","first-page":"7697","DOI":"10.1007\/s13197-015-1840-1","article-title":"Enzymatic hydrolysis of whey and casein protein- effect on functional, rheological, textural and sensory properties of breads","volume":"52","author":"Gani","year":"2015","journal-title":"J. Food Sci. Technol."},{"key":"ref_184","doi-asserted-by":"crossref","first-page":"2830","DOI":"10.1111\/ijfs.15622","article-title":"Mechanisms and applications of milk-derived bioactive peptides in Food for Special Medical Purposes","volume":"57","author":"Wang","year":"2022","journal-title":"Int. J. Food Sci. Technol."},{"key":"ref_185","doi-asserted-by":"crossref","first-page":"334","DOI":"10.1016\/j.foodres.2013.03.036","article-title":"Stability and antioxidative activities of casein peptide fractions during simulated gastrointestinal digestion in vitro: Charge properties of peptides affect digestive stability","volume":"52","author":"Ao","year":"2013","journal-title":"Food Res. Int."},{"key":"ref_186","doi-asserted-by":"crossref","first-page":"188","DOI":"10.1016\/j.foodres.2015.12.013","article-title":"Bioavailability of peptides from casein hydrolysate in vitro: Amino acid compositions of peptides affect the antioxidant efficacy and resistance to intestinal peptidases","volume":"81","author":"Wang","year":"2015","journal-title":"Food Res. Int."},{"key":"ref_187","first-page":"101628","article-title":"Recent advances in the application of novel carriers for peptide delivery","volume":"19","author":"Wang","year":"2025","journal-title":"J. Agric. Food Res."},{"key":"ref_188","doi-asserted-by":"crossref","unstructured":"Omidian, H., Wilson, R.L., and Castejon, A.M. (2025). Recent Advances in Peptide-Loaded PLGA Nanocarriers for Drug Delivery and Regenerative Medicine. Pharmaceuticals, 18.","DOI":"10.3390\/ph18010127"},{"key":"ref_189","doi-asserted-by":"crossref","first-page":"953","DOI":"10.1016\/j.jconrel.2023.03.050","article-title":"Particle carriers for controlled release of peptides","volume":"360","author":"Jiang","year":"2023","journal-title":"J. Control. Release"},{"key":"ref_190","doi-asserted-by":"crossref","unstructured":"Oliveira, C.B.P., Gomes, V., Ferreira, P.M.T., Martins, J.A., and Jervis, P.J. (2022). Peptide-Based Supramolecular Hydrogels as Drug Delivery Agents: Recent Advances. Gels, 8.","DOI":"10.3390\/gels8110706"},{"key":"ref_191","doi-asserted-by":"crossref","first-page":"101229","DOI":"10.1016\/j.nantod.2021.101229","article-title":"Design, optimization, and nanotechnology of antimicrobial peptides: From exploration to applications","volume":"39","author":"Peng","year":"2021","journal-title":"Nanotoday"},{"key":"ref_192","doi-asserted-by":"crossref","first-page":"26388","DOI":"10.1039\/D4RA02626H","article-title":"Design and characterisation of casein coated and drug loaded magnetic nanoparticles for theranostic applications","volume":"14","author":"Wenck","year":"2024","journal-title":"RSC Adv."},{"key":"ref_193","doi-asserted-by":"crossref","unstructured":"Lombardi, L., Li, J., and Williams, D.R. (2024). Peptide-Based Biomaterials for Combatting Infections and Improving Drug Delivery. Pharmaceutics, 16.","DOI":"10.20944\/preprints202410.1104.v1"},{"key":"ref_194","doi-asserted-by":"crossref","first-page":"471","DOI":"10.1016\/j.tifs.2021.04.019","article-title":"Antimicrobial peptides and their application in food packaging","volume":"112","author":"Liu","year":"2021","journal-title":"Trends Food Sci. Technol."},{"key":"ref_195","doi-asserted-by":"crossref","unstructured":"Duda-Chodak, A., Tarko, T., and Petka-Poniatowska, K. (2023). Antimicrobial Compounds in Food Packaging. Int. J. Mol. Sci., 24.","DOI":"10.3390\/ijms24032457"},{"key":"ref_196","doi-asserted-by":"crossref","unstructured":"Fahimirad, S., Abtahi, H., Razavi, S.H., Alizadeh, H., and Ghorbanpour, M. (2017). Production of recombinant antimicrobial polymeric protein beta casein-E 50-52 and its antimicrobial synergistic effects assessment with thymol. Molecules, 22.","DOI":"10.3390\/molecules22060822"},{"key":"ref_197","doi-asserted-by":"crossref","first-page":"2104165","DOI":"10.1002\/advs.202104165","article-title":"Self-Assembling Peptide-Based hydrogels for wound tissue repair","volume":"9","author":"Guan","year":"2022","journal-title":"Adv. Sci."},{"key":"ref_198","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1016\/j.actbio.2019.12.025","article-title":"Topical antimicrobial peptide formulations for wound healing: Current developments and future prospects","volume":"103","author":"Thapa","year":"2019","journal-title":"Acta Biomater."},{"key":"ref_199","doi-asserted-by":"crossref","unstructured":"Patel, H.R., Patel, G.N., and Patel, R.K. (2017). Formulation and evaluation of oral mucosal casein salt film for the anti-diabetic activity. Polym. Sci., 03.","DOI":"10.4172\/2471-9935-C1-002"},{"key":"ref_200","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1016\/j.colsurfb.2019.02.019","article-title":"Fabrication of novel casein gel with controlled release property via acidification, spray drying and tableting approach","volume":"177","author":"Tan","year":"2019","journal-title":"Colloids Surf. B Biointerfaces"},{"key":"ref_201","doi-asserted-by":"crossref","first-page":"116","DOI":"10.1016\/j.ijbiomac.2020.04.179","article-title":"Drug polarity effect over the controlled release in casein and chondroitin sulfate-based hydrogels","volume":"158","author":"Fragal","year":"2020","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_202","doi-asserted-by":"crossref","first-page":"302","DOI":"10.1016\/j.ijbiomac.2020.01.093","article-title":"pH-responsive hybrid hydrogels: Chondroitin sulfate\/casein trapped silica nanospheres for controlled drug release","volume":"148","author":"Fragal","year":"2020","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_203","doi-asserted-by":"crossref","first-page":"287","DOI":"10.1016\/j.msec.2013.12.025","article-title":"Using casein and oxidized hyaluronic acid to form biocompatible composite hydrogels for controlled drug release","volume":"36","author":"Li","year":"2014","journal-title":"Mater. Sci. Eng. C Mater. Biol. Appl."},{"key":"ref_204","doi-asserted-by":"crossref","first-page":"515","DOI":"10.1007\/s11095-021-03017-9","article-title":"Enhancement of the Mechanical and Drug-Releasing Properties of Poloxamer 407 Hydrogels with Casein","volume":"38","author":"Tundisi","year":"2021","journal-title":"Pharm. Res."},{"key":"ref_205","first-page":"1137","article-title":"Mathematical Modeling and Release Kinetics of Green Tea Polyphenols Released from Casein Nanoparticles","volume":"18","author":"Upputuri","year":"2019","journal-title":"Iran. J. Pharm. Res."},{"key":"ref_206","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1080\/10915810500259556","article-title":"Studies of the Toxicological Potential of Tripeptides (L-Valyl-L-prolyl-L-proline and L-lsoleucyl-L-prolyl-L-proline): III. Single- and\/or Repeated-Dose Toxicity of Tripeptides-Containing Lactobacillus helveticus-Fermented Milk Powder and Casein Hydrolysate in Rats","volume":"24","author":"Maeno","year":"2005","journal-title":"Int. J. Toxicol."},{"key":"ref_207","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1080\/10915810500259606","article-title":"Studies of the toxicological potential of tripeptides (L-Valyl-L-prolyl-L-proline and L-lsoleucyl-L-prolyl-L-proline): V. A 13-Week toxicity Study of Tripeptides-Containing Casein Hydrolysate in male and female rats","volume":"24","author":"Mizuno","year":"2005","journal-title":"Int. J. Toxicol."},{"key":"ref_208","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1080\/10915810500259630","article-title":"Studies of the Toxicological Potential of Tripeptides (L-Valyl-L-prolyl-L-proline and L-lsoleucyl-L-prolyl-L-proline): VI. Effects of Lactobacillus helveticus-fermented Milk Powder on Fertility and Reproductive Performance of Rats","volume":"24","author":"Kurosaki","year":"2005","journal-title":"Int. J. Toxicol."},{"key":"ref_209","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1016\/j.fct.2008.10.001","article-title":"Safety evaluation of an IPP tripeptide-containing milk protein hydrolysate","volume":"47","author":"Doorten","year":"2008","journal-title":"Food Chem. Toxicol."},{"key":"ref_210","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":"Matsufuji","year":"1995","journal-title":"Biosci. Biotechnol. Biochem."},{"key":"ref_211","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1079\/BJN2000206","article-title":"The effect of casein phosphopeptides on calcium absorption from calcium-fortified milk in growing rats","volume":"85","author":"Tsuchita","year":"2001","journal-title":"Br. J. Nutr."},{"key":"ref_212","doi-asserted-by":"crossref","unstructured":"(1999). Scientific Concepts of Functional Foods in Europe Consensus Document. Br. J. Nutr., 81, 1\u201327.","DOI":"10.1017\/S0007114599000471"},{"key":"ref_213","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1002\/biof.552210114","article-title":"Caseinophosphopeptides and their cell modulating potential","volume":"21","author":"Hartmann","year":"2004","journal-title":"BioFactors"},{"key":"ref_214","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1177\/1082013211398801","article-title":"Review: Production and functionality of active peptides from milk","volume":"17","author":"Urista","year":"2011","journal-title":"Food Sci. Technol. Int."}],"container-title":["Nutrients"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2072-6643\/17\/10\/1615\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,9]],"date-time":"2025-10-09T17:29:37Z","timestamp":1760030977000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2072-6643\/17\/10\/1615"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,5,8]]},"references-count":214,"journal-issue":{"issue":"10","published-online":{"date-parts":[[2025,5]]}},"alternative-id":["nu17101615"],"URL":"https:\/\/doi.org\/10.3390\/nu17101615","relation":{},"ISSN":["2072-6643"],"issn-type":[{"value":"2072-6643","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,5,8]]}}}