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Antihypertensive Peptides from Animal Proteins

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Book cover Bioactive Molecules in Food

Part of the book series: Reference Series in Phytochemistry ((RSP))

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Abstract

Hypertension is considered a major health problem throughout the world among adults, adolescents, as well as children and several preventive and therapeutic interventions are available. In addition to the pharmaceutical drugs and lifestyle changes, significant milestones have been achieved in the past decades in the identification of bioactive peptides from animal proteins with useful antihypertensive activities. The antihypertensive properties of these peptides are attributed to several mechanisms ranging from mineral-binding, opioid-like and antithrombotic properties to inhibition of ACE (angiotensin-converting enzyme). ACE-inhibitory peptides are the most widely studied bioactive peptides with promising potential in hypertension management. In addition to milk and dairy products, which are the major sources of antihypertensive peptides, a remarkable increase has been observed in the documentation of peptides from other animal proteins, such as meat, with demonstrated in vitro and in vivo antihypertensive properties. Numerous opportunities exist in the global market for the development of novel food products and additives based on these antihypertensive peptides for the dietary management of hypertension. This chapter reviews the antihypertensive peptides derived from meat proteins and examines their possible role as a functional ingredient in foods for the management of hypertension.

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References

  1. Knowlin L, Reid T, Williams F, Cairns B, Charles A (2017) Burn mortality in patients with pre-existing cardiovascular disease. Burns 43:949–955. https://doi.org/10.1016/j.burns.2017.01.026

    Article  PubMed  PubMed Central  Google Scholar 

  2. Mozaffarian D, Benjamin EJ, Go AS, Arnett DK, Blaha MJ, Cushman M, de Ferranti S, Després JP, Fullerton HJ, Howard VJ, Huffman MD, Judd SE, Kissela BM, Lackland DT, Lichtman JH, Lisabeth LD, Liu S, Mackey RH, Matchar DB, McGuire DK, Mohler ER 3rd, Moy CS, Muntner P, Mussolino ME, Nasir K, Neumar RW, Nichol G, Palaniappan L, Pandey DK, Reeves MJ, Rodriguez CJ, Sorlie PD, Stein J, Towfighi A, Turan TN, Virani SS, Willey JZ, Woo D, Yeh RW, Turner MB (2015) Heart disease and stroke statistics-2015 update: a report from the American heart association. Circulation 131:e29–322. https://doi.org/10.1161/CIR.0000000000000152

    Article  PubMed  Google Scholar 

  3. Roth GA, Moran AE, Barber R, Nguyen G, Feigin VL, Naghavi M, Mensah GA, Murray CJL (2015) Demographic and epidemiologic drivers of global cardiovascular mortality. N Engl J Med 372:1333–1341. https://doi.org/10.1056/NEJMoa1406656

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  4. Humphries KH, Izadnegahdar M, Sedlak T, Saw J, Johnston N, Schenck-Gustafsson K, Shah RU, Regitz-Zagrosek V, Grewal J, Vaccarino V, Wei J, Merz BCN (2017) Sex differences in cardiovascular disease-Impact on care and outcomes. Front Neuroendocrinol 46:46–47. https://doi.org/10.1016/j.atherosclerosis.2015.01.027

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  5. Perk J, De Backer G, Gohlke H, Graham I, Reiner Z, Verschuren M, Albus C, Benlian P, Boysen G, Cifkova R, Deaton C, Ebrahim S, Fisher M, Germano G, Hobbs R, Hoes A, Karadeniz S, Mezzani A, Prescott E, Ryden L, Scherer M, Syvänne M, Scholte op Reimer WJ, Vrints C, Wood D, Zamorano JL, Zannad F (2012) European guidelines on cardiovascular disease prevention in clinical practice (version 2012): The fifth joint task force of the European society of cardiology and other societies on cardiovascular disease prevention in clinical practice. Eur Heart J 33:1635–1701. https://doi.org/10.1093/eurheartj/ehs092

    Article  CAS  PubMed  Google Scholar 

  6. Rosendorff C, Lackland DT, Allison M, Aronow WS, Black HR, Blumenthal RS, Cannon CP, de Lemos JA, Elliott WJ, Findeiss L, Gersh BJ, Gore JM, Levy D, Long JB, O'Connor CM, O’Gara PT, Ogedegbe G, Oparil S, White WB (2015) Treatment of hypertension in patients with coronary artery disease: a scientific statement from the American heart association, American college of cardiology, and American society of hypertension. Circulation 131:e435–e470. https://doi.org/10.1161/CIR.0000000000000207

    Article  PubMed  PubMed Central  Google Scholar 

  7. Mills KT, Bundy JD, Kelly TN, Reed JE, Kearney PM, Reynolds K, Chen J, He J (2016) Global disparities of hypertension prevalence and control: a systematic analysis of population-based studies from 90 countries. Circulation 134:441–450. https://doi.org/10.1161/circulationaha.115.018912

    Article  PubMed  PubMed Central  Google Scholar 

  8. Gasowski J, Piotrowicz K (2017) Hypertension in the elderly: change of, or new implications within the existing, paradigm? Eur Geriatric Med. https://doi.org/10.1016/j.eurger.2017.05.002

  9. Campbell NRC, Lackland DT, Niebylski ML (2014) High blood pressure: why prevention and control are urgent and important – a 2014 fact sheet from the world hypertension league and the international society of hypertension. J Clin Hypertens 16:551–553. https://doi.org/10.1111/jch.12372

    Article  Google Scholar 

  10. Garfinkle MA (2017) Salt and essential hypertension: pathophysiology and implications for treatment. J Am Soc Hypertens 11:385–391. https://doi.org/10.1016/j.jash.2017.04.006

    Article  CAS  PubMed  Google Scholar 

  11. Campbell NR, Lackland DT, Lisheng L, Niebylski ML, Nilsson PM, Zhang XH (2015) Using the global burden of disease study to assist development of nation-specific fact sheets to promote prevention and control of hypertension and reduction in dietary salt: a resource from the world hypertension league. J Clin Hypertens 17:165–167. https://doi.org/10.1111/jch.12479

    Article  Google Scholar 

  12. Danaei G, Ding EL, Mozaffarian D, Taylor B, Rehm J, Murray CJ, Ezzati M (2009) The preventable causes of death in the United States: comparative risk assessment of dietary, lifestyle, and metabolic risk factors. PLoS Med 6(4):e1000058. https://doi.org/10.1371/journal.pmed.1000058

    Article  PubMed  PubMed Central  Google Scholar 

  13. IFPMA (2016) Hypertension: putting the pressure on the silent killer. https://www.ifpma.org/wp-content/uploads/2016/05/2016-Hypertension-putting-the-pressure-on-the-silent-killer.pdf

  14. Karatzi K, Protogerou AD, Moschonis G, Tsirimiagou C, Androutsos O, Chrousos GP, Lionis C, Manios Y (2017) Prevalence of hypertension and hypertension phenotypes by age and gender among school children in Greece: the healthy growth study. Atherosclerosis 259:128–133. https://doi.org/10.1016/j.atherosclerosis.2017.01.027

    Article  CAS  PubMed  Google Scholar 

  15. Beckie TM (2017) Ethnic and racial disparities in hypertension management among women. Semin Perinatol. https://doi.org/10.1053/j.semperi.2017.04.004

  16. Chobanian AV (2015) Time to reassess blood-pressure goals. N Engl J Med 373:2093–2095. https://doi.org/10.1056/nejmp1513290

    Article  CAS  PubMed  Google Scholar 

  17. O’Shea PM, Griffin TP, Fitzgibbon M (2017) Hypertension: the role of biochemistry in the diagnosis and management. Clin Chim Acta 465:131–143. https://doi.org/10.1016/j.cca.2016.12.014

    Article  CAS  PubMed  Google Scholar 

  18. Kearney PM, Whelton M, Reynolds K, Whelton PK, He J (2004) Worldwide prevalence of hypertension: a systematic review. J Hypertens 22:11–19. https://doi.org/10.1097/01.hjh.0000098149.7095679

    Article  CAS  PubMed  Google Scholar 

  19. Mancia G, Fagard R, Narkiewicz K, Redon J, Zanchetti A, Böhm M, Christiaens T, Cifkova R, De Backer G, Dominiczak A, Galderisi M, Grobbee DE, Jaarsma T, Kirchhof P, Kjeldsen SE, Laurent S, Manolis AJ, Nilsson PM, Ruilope LM, Schmieder RE, Sirnes PA, Sleight P, Viigimaa M, Waeber B, Zannad F, Redon J, Dominiczak A, Narkiewicz K, Nilsson PM, Burnier M, Viigimaa M, Ambrosioni E, Caufield M, Coca A, Olsen MH, Schmieder RE, Tsioufis C, van de Borne P, Zamorano JL, Achenbach S, Baumgartner H, Bax JJ, Bueno H, Dean V, Deaton C, Erol C, Fagard R, Ferrari R, Hasdai D, Hoes AW, Kirchhof P, Knuuti J, Kolh P, Lancellotti P, Linhart A, Nihoyannopoulos P, Piepoli MF, Ponikowski P, Sirnes PA, Tamargo JL, Tendera M, Torbicki A, Wijns W, Windecker S, Clement DL, Coca A, Gillebert TC, Tendera M, Rosei EA, Ambrosioni E, Anker SD, Bauersachs J, Hitij JB, Caulfield M, De Buyzere M, De Geest S, Derumeaux GA, Erdine S, Farsang C, Funck-Brentano C, Gerc V, Germano G, Gielen S, Haller H, Hoes AW, Jordan J, Kahan T, Komajda M, Lovic D, Mahrholdt H, Olsen MH, Ostergren J, Parati G, Perk J, Polonia J, Popescu BA, Reiner Z, Rydén L, Sirenko Y, Stanton A, Struijker-Boudier H, Tsioufis C, van de Borne P, Vlachopoulos C, Volpe M, Wood DA (2013) ESH/ESC guidelines for the management of arterial hypertension: the task force for the management of arterial hypertension of the European society of hypertension (ESH) and of the European society of cardiology (ESC). Eur Heart J 34:2159–2219. https://doi.org/10.1093/eurheartj/eht151

    Article  PubMed  Google Scholar 

  20. Heredia-Blonval K, Blanco-Metzler A, Montero-Campos M, Dunford EK (2014) The salt content of products from popular fast-food chains in Costa Rica. Appetite 83:173–177. https://doi.org/10.1016/j.appet.2014.08.027

    Article  PubMed  Google Scholar 

  21. Bazzano LA, Green T, Harrison TN, Reynolds K (2013) Dietary approaches to prevent hypertension. Curr Hypertens Rep 15:694–702. https://doi.org/10.1007/s11906-013-0390-z

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  22. Campbell N, Jilliian J, Campbell T (2012) Sodium consumption: and individual’s choice? Int J Hypertens 2012:1–6. https://doi.org/10.1155/2012/860954

    Article  Google Scholar 

  23. Dunford E (2012) International collaborative project to compare and track the nutritional composition of fast foods. BMC Public Health 12:559. https://doi.org/10.1186/1471-2458-12-559

    Article  Google Scholar 

  24. McDonough AA, Veiras LC, Guevara CA, Ralph DL (2017) Cardiovascular benefits associated with higher dietary K vs. lower dietary Na evidence from population and mechanistic studies. Am J Physiol Endocrinol Metab 312:E348. https://doi.org/10.1152/ajpendo.00453.2016

    Article  PubMed  PubMed Central  Google Scholar 

  25. Wu L, Sun D, He Y (2016a) Fruit and vegetables consumption and incident hypertension: dose–response meta-analysis of prospective cohort studies. J Human Hypertens 30:573–580. https://doi.org/10.1038/jhh.2016.44

    Article  CAS  Google Scholar 

  26. Aluko RE (2015) Antihypertensive peptides from food proteins. Annual Rev Food Sci Technol 6:235–262. https://doi.org/10.1146/annurev-food-022814-015520

    Article  CAS  Google Scholar 

  27. Vercruysse L, Van Camp J, Smagghe G (2005) ACE inhibitory peptides derived from enzymatic hydrolysates of animal muscle protein: a review. J Agric Food Chem 53:8106–8115. https://doi.org/10.1021/jf0508908

    Article  CAS  PubMed  Google Scholar 

  28. Fu Y, Young JF, Therkildsen M (2017) Bioactive peptides in beef: endogenous generation through postmortem aging. Meat Sci 123:134–142. https://doi.org/10.1016/j.meatsci.2016.09.015

    Article  CAS  PubMed  Google Scholar 

  29. Lee SY, Hur SJ (2017) Antihypertensive peptides from animal products, marine organisms, and plants. Food Chem 228:506–517. https://doi.org/10.1016/j.foodchem.2017.02.039

    Article  CAS  PubMed  Google Scholar 

  30. Norris R, Fitzgerald RJ (2013) Antihypertensive peptides from food proteins. In: Hernandez-Ledesma B, Hsieh CC (eds) Bioactive food peptides in health and disease. InTech, Rijeka. https://doi.org/10.5772/51710

    Chapter  Google Scholar 

  31. Bah CSF, Bekhit AEDA, Carne A, McConnell MA (2013) Slaughterhouse blood: an emerging source of bioactive compounds. Compr Rev Food Sci Food Saf 12:314–331. https://doi.org/10.1111/1541-4337.12013

    Article  CAS  Google Scholar 

  32. Ryder K, Bekhit AED, McConnell M, Carne A (2016) Towards generation of bioactive peptides from meat industry waste proteins: generation of peptides using commercial microbial proteases. Food Chem 208:42–50. https://doi.org/10.1016/j.foodchem.2016.03.121

    Article  CAS  PubMed  Google Scholar 

  33. Murray BA, FitzGerald RJ (2007) Angiotensin converting enzyme inhibitory peptides derived from proteins: biochemistry, bioactivity, and production. Curr Pharm Des 13:773–791

    Article  CAS  PubMed  Google Scholar 

  34. Ko JY, Kang N, Lee JH, Kim JS, Kim WS, Park SJ, Yong-Tae Kim YT, Jeo YJ (2016) Angiotensin I-converting enzyme inhibitory peptides from an enzymatic hydrolysate of flounder fish (Paralichthys olivaceus) muscle as a potent anti-hypertensive agent. Process Biochem 51:535–541. https://doi.org/10.1016/j.procbio.2016.01.009

    Article  CAS  Google Scholar 

  35. Tagliazucchi D, Shamsia S, Helal A, Conte A (2016) Release of angiotensin converting enzyme-inhibitory peptides during in vitro gastro-intestinal digestion of camel milk. Int Dairy J 56:119–128. https://doi.org/10.1016/j.idairyj.2016.01.009

    Article  CAS  Google Scholar 

  36. Mahmoud AH, Jeanette O, Cristian DG, Ali O, Essam H (2017) Angiotensin I-converting enzyme inhibitory activity and antioxidant capacity of bioactive peptides derived from enzymatic hydrolysis of buffalo milk proteins. Int Dairy J 66:91–98. https://doi.org/10.1016/j.idairyj.2016.11.006

    Article  CAS  Google Scholar 

  37. Wu S, Feng X, Lan X, Xu Y, Liao D (2015) Purification and identification of angiotensin-I converting enzyme (ACE) inhibitory peptide from lizard fish (Saurida elongata) hydrolysate. J Funct Foods 13:295–299. https://doi.org/10.1016/j.jff.2014.12.051

    Article  CAS  Google Scholar 

  38. Corrêa APF, Daroit DJ, Fontoura R, Meira SMM, Segalin J, Brandelli A (2014) Hydrolysates of sheep cheese whey as a source of bioactive peptides with antioxidant and angiotensin-converting enzyme inhibitory activities. Peptides 61:48–55. https://doi.org/10.1016/j.peptides.2014.09.001

    Article  CAS  PubMed  Google Scholar 

  39. Pokora M, Zambrowicz A, Da browska A, Eckert E, Setner B, Szołtysik M, Chrzanowska J (2014) An attractive way of egg white protein by-product use for producing of novel anti-hypertensive peptides. Food Chem 151:500–505. https://doi.org/10.1016/j.foodchem.2013.11.111

    Article  CAS  PubMed  Google Scholar 

  40. Ngo D-H, Vo T-S, Ryu B-M, Kim S-K (2016) Angiotensin-I-converting enzyme (ACE) inhibitory peptides from Pacific cod skin gelatine using ultrafiltration membranes. Process Biochem 51:1622–1628. https://doi.org/10.1016/j.procbio.2016.07.006

    Article  CAS  Google Scholar 

  41. Lee JK, Jeon JK, Byun HG (2014) Antihypertensive effect of novel angiotensin I converting enzyme inhibitory peptide from chum salmon (Oncorhynchusketa) skin in spontaneously hypertensive rats. J Funct Foods 7:381–389. https://doi.org/10.1016/j.jff.2014.01.021

    Article  CAS  Google Scholar 

  42. Salampessy J, Reddy N, Phillips M, Kailasapathy K (2017) Isolation and characterization of nutraceutically potential ACE-Inhibitory peptides from leatherjacket (Meuchenia sp.) protein hydrolysates. LWT-Food Sci Technol 80:430–436. https://doi.org/10.1016/j.lwt.2017.03.004

    Article  CAS  Google Scholar 

  43. Stuknytè M, Cattaneo S, Masotti F, De Noni I (2015) Occurrence and fate of ACE-inhibitor peptides in cheeses and in their digestates following in vitro static gastrointestinal digestion. Food Chem 168:27–33. https://doi.org/10.1016/j.foodchem.2014.07.045

    Article  CAS  PubMed  Google Scholar 

  44. Majumder K, Chakrabarti S, Morton JS, Panahi S, Kaufman S, Davidge ST, Jianping WU (2015) Egg-derived ACE-inhibitory peptides IQW and LKP reduce blood pressure in spontaneously hypertensive rats. J Funct Foods 13:50–60. https://doi.org/10.1016/j.jff.2014.12.028

    Article  CAS  Google Scholar 

  45. Majumder K, Jianping W (2010) A new approach for identification of novel antihypertensive peptides from egg proteins by QSAR and bioinformatics. Food Res Int 43:1371–1378. https://doi.org/10.1016/j.foodres.2010.04.027

    Article  CAS  Google Scholar 

  46. Tagliazucchi D, Shamsia S, Helal A, Conte A (2017) Angiotensin-converting enzyme inhibitory peptides from goats' milk released by in vitro gastro-intestinal digestion. Int Dairy J 71:6–16. https://doi.org/10.1016/j.idairyj.2017.03.001

    Article  CAS  Google Scholar 

  47. Corrons MA, Liggieri CS, Trejo SA, Bruno MA (2017) ACE-inhibitory peptides from bovine caseins released with peptidases from Maclura pomifera latex. Food Res Int 93:8–15. https://doi.org/10.1016/j.foodres.2017.01.003

    Article  CAS  PubMed  Google Scholar 

  48. Ibrahim HR, Ahmed AS, Miyata T (2017) Novel angiotensin-converting enzyme inhibitory peptides from caseins and whey proteins of goat milk. J Adv Res 8(1):63–71. https://doi.org/10.1016/j.jare.2016.12.002

    Article  CAS  PubMed  Google Scholar 

  49. Norris R, O’Keeffe MB, Poyarkov A, FitzGerald RJ (2015) Peptide identification and angiotensin converting enzyme (ACE) inhibitory activity in prolyl endoproteinase digests of bovine αs-casein. Food Chem 188:210–217. https://doi.org/10.1016/j.foodchem.2015.04.130

    Article  CAS  PubMed  Google Scholar 

  50. Li Y, Sadiq FA, Liu T-J, Chen J-C, He G-Q (2015) Purification and identification of novel peptides with inhibitory effect against angiotensin I-converting enzyme and optimization of process conditions in milk fermented with the yeast Kluyveromyces marxianus. J Funct Foods 16:278–288. https://doi.org/10.1016/j.jff.2015.04.043

    Article  CAS  Google Scholar 

  51. Paul M, Phillips JG, Renye JA Jr (2016) Measuring the angiotensin-converting enzyme inhibitory activity of an 8-amino acid (8mer) fragment of the C12 antihypertensive peptide. J Dairy Sci 99:3263–3266. https://doi.org/10.3168/jds.2015-10437

    Article  CAS  PubMed  Google Scholar 

  52. Asoodeh A, Homayouni-Tabrizi M, Shabestarian H, Emtenani S, Emtenani S (2016) Biochemical characterization of a novel antioxidant and angiotensin I-converting enzyme inhibitory peptide from Struthio camelus egg white protein hydrolysis. J Food Drug Analysis 24:332–342. https://doi.org/10.1016/j.jfda.2015.11.010

    Article  CAS  Google Scholar 

  53. Chen Y, Wang Z, Chen X, Liu Y, Zhang H, Sun T (2010) Identification of angiotensin I-converting enzyme inhibitory peptides from koumiss, a traditional fermented mare’s milk. J Dairy Sci 93:884–892. https://doi.org/10.3168/jds.2009-2672

    Article  CAS  PubMed  Google Scholar 

  54. Quiro A, Ramos M, Muguerza B, Delgado MA, Miguel M, Aleixandre A, Recio I (2007) Identification of novel antihypertensive peptides in milk fermented with Enterococcus faecalis. Int Dairy J 17:33–41. https://doi.org/10.1016/j.idairyj.2005.12.011

    Article  CAS  Google Scholar 

  55. Geerlings A, Villar IC, Zarco FH, Sanchez M, Vera RA, Gomez Z, Boza J, Duarte J (2006) Identification and characterization of novel angiotensin-converting enzyme inhibitors obtained from goat milk. J Dairy Sci 89:3326–3335. https://doi.org/10.3168/jds.S0022-0302(06)72369-4

    Article  CAS  PubMed  Google Scholar 

  56. Contreras MDM, Carrón R, Montero MJ, Ramos M, Recio I (2009) Novel casein-derived peptides with antihypertensive activity. Int Dairy J 19:566–573. https://doi.org/10.1016/j.idairyj.2009.05.004

    Article  CAS  Google Scholar 

  57. Garcés-Rimón M, López-Expósito I, López-Fandiño R, Miguel M (2016) Egg white hydrolysates with in vitro biological multiactivities to control complications associated with the metabolic syndrome. Eur Food Res Technol 242:61–69. https://doi.org/10.1007/s00217-015-2518-7

    Article  CAS  Google Scholar 

  58. Sarmadi BH, Ismail A (2010) Antioxidative peptides from food proteins: a review. Peptides 31:1949–1956. https://doi.org/10.1016/j.peptides.2010.06.020

    Article  CAS  PubMed  Google Scholar 

  59. Wu J, Aluko RE, Nakai S (2006) Structural requirements of angiotensin I-converting enzyme inhibitory peptides: Quantitative structure - Activity relationship study of di- and tripeptides. J Agric Food Chem 54:732–738. https://doi.org/10.1021/jf051263l

    Article  CAS  PubMed  Google Scholar 

  60. Ferreira LAF, Galle A, Raida M, Schrader M, Lebrun I, Habermehl G (1998) Isolation, analysis and properties of three bradykinin-potentiating peptides (BPP-II, BPPIII, and BPP-V) From Bothrops neuwiedi venom. J Protein Chem 17:285–289

    Article  CAS  PubMed  Google Scholar 

  61. Norris R, Casey F, FitzGerald RJ, Shields D, Mooney C (2012) Predictive modelling of angiotensin converting enzyme inhibitory dipeptides. Food Chem 133:1349–1354. https://doi.org/10.1016/j.foodchem.2012.02.023

    Article  CAS  Google Scholar 

  62. Gobbetti M, Minervini F, Rizzello CG (2004) Angiotensin I-converting enzyme-inhibitory and antimicrobial bioactive peptides. Int J Dairy Technol 57:173–188. https://doi.org/10.1111/j.1471-0307.2004.00139

    Article  CAS  Google Scholar 

  63. De Gobba C, Tompa G, Otte J (2014) Bioactive peptides from caseins released by cold active proteolytic enzymes from Arsukibacterium ikkense. Food Chem 165:205–215. https://doi.org/10.1016/j.foodchem.2014.05.082

    Article  CAS  PubMed  Google Scholar 

  64. Hernández-Ledesma B, Miralles B, Amigo L, Ramos M, Recio I (2005) Identification of antioxidant and ACE-inhibitory peptides in fermented milk. J Sci Food Agric 85:1041–1048. https://doi.org/10.1002/jsfa.2063

    Article  CAS  Google Scholar 

  65. Wu J, Liao W, Udenigwe CC (2017) Revisiting the mechanisms of ACE inhibitory peptides from food proteins. Trends Food Sci Technol. https://doi.org/10.1016/j.tifs.2017.07.011

  66. Hall JE, Granger JP, do Carmo JM, da Silva AA, Dubinion J, George E, Hamza S, Speed J, Hall ME (2012) Hypertension: physiology and pathophysiology. J Compr Physiol 2:2393–2442. https://doi.org/10.1002/cphy.c110058.

    Article  Google Scholar 

  67. Udenigwe CC, Mohan A (2014) Mechanisms of food protein-derived antihypertensive peptides other than ACE inhibition. J Funct Foods 8:45–52. https://doi.org/10.1016/j.jff.2014.03.002

    Article  CAS  Google Scholar 

  68. Majumder K, Wu J (2014) Molecular targets of antihypertensive peptides: understanding the mechanisms of action based on the pathophysiology of hypertension. Int J Mol Sci 16(1):256–283. https://doi.org/10.3390/ijms16010256

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  69. Saadi S, Saari N, Anwar F, Hamid AA, Ghazali MH (2015) Recent advances in food biopeptides: production, biological functionalities and therapeutic applications. Biotechnol Adv 33:80–116. https://doi.org/10.1016/j.biotechadv.2014.12.00

    Article  CAS  PubMed  Google Scholar 

  70. Elavarasan K, Shamasundar BA, Badii F, Howell N (2016) Angiotensin I-converting enzyme (ACE) inhibitory activity and structural properties of oven and freeze-dried protein hydrolysate from fresh water fish (Cirrhinus mrigala). Food Chem 206:210–216. https://doi.org/10.1016/j.foodchem.2016.03.047

    Article  CAS  PubMed  Google Scholar 

  71. Deniz E, Mora L, Aristoy MC, Candoğan K, Toldrá F (2016) Free amino acids and bioactive peptides profile of Pastırma during its processing. Food Res Int 89:194–201. https://doi.org/10.1016/j.foodres.2016.07.025

    Article  CAS  PubMed  Google Scholar 

  72. Lafargaa T, O’Connorb P, Hayes M (2014) Identification of novel dipeptidyl peptidase-IV and angiotensin-I-converting enzyme inhibitory peptides from meat proteins using in silico analysis. Peptides 59:53–62. https://doi.org/10.1016/j.peptides.2014.07.005

    Article  CAS  Google Scholar 

  73. Nejati F, Rizzello CG, Di Cagno R, Sheikh-Zeinoddin M, Diviccaro A, Minervini F, Gobbetti M (2013) Manufacture of a functional fermented milk enriched of angiotensin-I-converting enzyme (ACE)-inhibitory peptides and g-amino butyric acid (GABA). LWT-Food Sci Technol 51:183–189. https://doi.org/10.1016/j.lwt.2012.09.017

    Article  CAS  Google Scholar 

  74. Mirzaei M, Mirdamadi S, Ehsani MR, Aminlari M, Hosseini E (2015) Purification and identification of antioxidant and ACE-inhibitory peptide from Saccharomyces cerevisiae protein hydrolysate. J Functional Foods 19:259–268. https://doi.org/10.1016/j.jff.2015.09.031

    Article  CAS  Google Scholar 

  75. Wu Q, Du J, Jia J, Kuang C (2016) Production of ACE inhibitory peptides from sweet sorghum grain protein using alcalase: hydrolysis kinetic, purification and molecular docking study. Food Chem 199:140–149. https://doi.org/10.1016/j.foodchem.2015.12.012

    Article  CAS  PubMed  Google Scholar 

  76. Nasri M (2017) Protein hydrolysates and biopeptides: production, biological activities, and applications in foods and health benefits. A review. In: Toldra, F. (Ed.), Advances in food and nutrition research, vol 81. ISSN 1043–4526, Elsevier Publications. https://doi.org/10.1016/bs.afnr.2016.10.003

  77. Toopcham T, Roytrakul S, Yongsawatdigul J (2015) Characterization and identification of angiotensin I-converting enzyme (ACE) inhibitory peptides derived from tilapia using Virgibacillus halodenitrificans SK1-3-7 proteinases. J Funct Foods 14:435–444. https://doi.org/10.1016/j.foodchem.2016.09.183

    Article  CAS  Google Scholar 

  78. Kim SK, Wijesekara I (2010) Development and biological activities of marine-derived bioactive peptides: a review. J Funct Foods 2:1–9. https://doi.org/10.1016/j.jff.2010.01.003

    Article  CAS  Google Scholar 

  79. Castellano P, Aristoy MC, Sentandreu MA, Vignolo G, Toldra F (2013) Peptides with angiotensin I-converting enzyme (ACE) inhibitory activity generated from porcine skeletal muscle proteins by the action of meat-borne lactobacillus. J Proteome 89:183–190. https://doi.org/10.1016/j.jprot.2013.06.023

    Article  CAS  Google Scholar 

  80. Fakhfakh N, Ktari N, Siala R, Nasri M (2013) Wool-waste valorization: production of protein hydrolysates with high antioxidative potential by fermentation with a new keratinolytic bacterium, Bacillus pumilus A1. J Applied Microbiol 115:424–433. https://doi.org/10.1111/jam.12246

    Article  CAS  Google Scholar 

  81. Jemil I, Jridi M, Nasri R, Ktari N, Slama-Ben Salem RB, Mehiri M, Hajji M, Nasri M (2014) Functional, antioxidant and antibacterial properties of protein hydrolysates prepared from fish meat fermented by Bacillus subtilis. Process Biochem 49:963–972. https://doi.org/10.1016/j.procbio.2014.03.004

    Article  CAS  Google Scholar 

  82. Balakrishnan B, Prasad B, Rai AK, Narayan B (2011) In vitro antioxidant and antibacterial properties of hydrolysed proteins of delimed tannery fleshings: comparison of acid hydrolysis and fermentation methods. Biodegradation 22:287–295. https://doi.org/10.1007/s10532-010-9398-0

    Article  CAS  PubMed  Google Scholar 

  83. Hernández-Ledesma B, Contreras MDM, Recio I (2011) Antihypertensive peptides: production, bioavailability and incorporation into foods. Adv Colloid Interf Sci 165:23–35. https://doi.org/10.1016/j.cis.2010.11.001

    Article  CAS  Google Scholar 

  84. Rao S, Su Y, Junhua Li XZ, Yang Y (2009) Design and expression of recombinant antihypertensive peptide multimer gene in Escherichia coli BL21. J Microbiol Biotechnol 19(12):1620–1627. https://doi.org/10.4014/jmb.0905.05055

    Article  CAS  PubMed  Google Scholar 

  85. Bhat ZF, Kumar S, Bhat HF (2017) Antihypertensive peptides of animal origin: a review. Crit Rev Food Sci Nutr 57:566–578. https://doi.org/10.1080/10408398.2014.898241

    Article  CAS  PubMed  Google Scholar 

  86. Dziuba B, Dziuba M (2014) Milk proteins-derived bioactive peptides in dairy products: molecular, biological and methodological aspects. Acta Sci Pol Technol Aliment 13(1):5–25. 10.17306/J.AFS.2014.1.1

    Article  CAS  PubMed  Google Scholar 

  87. Fosgerau K, Hoffmann T (2015) Peptide therapeutics: current status and future directions. Drug Discov Today 20(1):122–128. https://doi.org/10.1016/j.drudis.2014.10.003

    Article  CAS  PubMed  Google Scholar 

  88. Mora L, Gallego M, Reig M, Toldra F (2017) Challenges in the quantitation of naturally generated bioactive peptides in processed meats. Trends Food Sci Technol. https://doi.org/10.1016/j.tifs.2017.04.011

  89. Khan RS, Grigor J, Winger R, Win A (2013) Functional food product development-opportunities and challenges for food manufacturers. Trends Food Sci Technol 30:27–23. https://doi.org/10.1016/j.tifs.2012.11.004

    Article  CAS  Google Scholar 

  90. Contreras MM, Sevilla MA, Monroy-Ruix J, Amigo L, Gómez-Sala B, Molina E, Ramos M, Recio I (2011) Food-grade production of an antihypertensive casein hydrolysate and resistance of active peptides to drying and storage. Int Dairy J 21:470–476. https://doi.org/10.1016/j.idairyj.2011.02.004

    Article  CAS  Google Scholar 

  91. Jang A, Jo C, Lee M (2007) Storage stability of the synthetic angiotensin converting enzyme (ACE) inhibitory peptides separated from beef sarcoplasmic protein extracts at different pH, temperature, and gastric digestion. Food Sci Biotechnol 16:572

    CAS  Google Scholar 

  92. Bouglé D, Bouhallab S (2017) Dietary bioactive peptides: human studies. Crit Rev Food Sci Nutr 57:335–343. https://doi.org/10.1080/10408398.2013.873766

    Article  CAS  PubMed  Google Scholar 

  93. Leo FD, Panarese S, Gallerani R, Ceci LR (2009) Angiotensin converting enzyme (ACE) inhibitory peptides: production and implementation of functional food. Curr Pharm Des 15:3622–3643. https://doi.org/10.2174/138161209789271834

    Article  PubMed  Google Scholar 

  94. Daskaya-Dikmen C, Yucetepe A, Karbancioglu-Guler F, Daskaya H, Ozcelik B (2017) Angiotensin-I-converting enzyme (ace)-inhibitory peptides from plants. Forum Nutr 9(4):316. https://doi.org/10.3390/nu9040316

    Article  CAS  Google Scholar 

  95. Balti R, Bougatef A, Sila A, Guillochon D, Dhulster P, Nedjar-Arroume N (2015) Nine novel angiotensin I-converting enzyme (ACE) inhibitory peptides from cuttlefish (Sepia officinalis) muscle protein hydrolysates and antihypertensive effect of the potent active peptide in spontaneously hypertensive rats. Food Chem 170:519–525. https://doi.org/10.1016/j.foodchem.2013.03.091

    Article  CAS  PubMed  Google Scholar 

  96. Turpeinen AM, Kumpu M, Seppo RL, Kautiainen T, Jauhiainen H, Korpela VR (2009) Antihypertensive and cholesterol-lowering effects of a spread containing bioactive peptides IPP and VPP and plant sterols. J Funct Foods 1:260–265. https://doi.org/10.1016/j.jff.2009.03.001

    Article  CAS  Google Scholar 

  97. Lafarga T, Hayes M (2014) Bioactive peptides from meat muscle and by-products: generation, functionality and application as functional ingredients. Meat Sci 98:227–239. https://doi.org/10.1016/j.meatsci.2014.05.036

    Article  CAS  PubMed  Google Scholar 

  98. Fujita H, Yokohama K, Yoshikawa M (2000) Classification and antihypertensive activity of angiotensin I-converting enzyme inhibitory peptides derived from food proteins. J Food Chem 65:564–569. https://doi.org/10.1111/j.1365-2621.2000.tb16049.x

    Article  CAS  Google Scholar 

  99. Katayama K, Jamhari Mori T, Kawahara S, Miake K, Kodama Y, Sugiyama M, Kawamura Y, Nakayama T, Muruyama M, Muguruma M (2007) Angiotensin-I converting enzyme inhibitory peptide derived from porcine skeletal muscle myosin and its antihypertensive activity in spontaneously hypertensive rats. J Food Sci 9:S702–S706. https://doi.org/10.1111/j.1750-3841.2007.00571.x

    Article  CAS  Google Scholar 

  100. Jang A, Jo C, Kang KS, Lee M (2008) Antimicrobial and human cancer cell cytotoxic effect of synthetic angiotensin-converting enzyme (ACE) inhibitory peptides. Food Chem 107:327–336. https://doi.org/10.1016/j.foodchem.2007.08.036

    Article  CAS  Google Scholar 

  101. Ahhmed AM, Muguruma M (2010) A review of meat protein hydrolysates and hypertension. Meat Sci 86(1):110–118. https://doi.org/10.1016/j.meatsci.2010.04.032

    Article  CAS  PubMed  Google Scholar 

  102. Iwaniak A, Minkiewicz P, Darewicz M (2014) Food originating ACE inhibitors, including antihypertensive peptides, as preventive food components in blood pressure reduction. Compr Rev Food Sci Food Saf 13:114–134. https://doi.org/10.1111/1541-4337.12051

    Article  CAS  PubMed  Google Scholar 

  103. Katayama K, Anggraeni HE, Mori T, Ahhmed AM, Kawahara S, Sugiyama M, Nakayama T, Maruyama M, Muguruma M (2008) Porcine skeletal muscle troponin is a good source of peptides with angiotensin-I converting enzyme inhibitory activity and antihypertensive effects in spontaneously hypertensive rats. J Agric Food Chem 56:355–360. https://doi.org/10.1021/jf071408j

    Article  CAS  PubMed  Google Scholar 

  104. Saiga A, Okumura T, Makihara T, Katsuta S, Shimizu T, Yamada R, Nishimura TF (2003) Angiotensin I-converting enzyme inhibitory peptides in a hydrolyzed chicken breast muscle extract. J Agric Food Chem 51:1741–1745. https://doi.org/10.1021/jf020604h

    Article  CAS  PubMed  Google Scholar 

  105. Stadnik J, Kęska P (2015) Meat and fermented meat products as a source of bioactive peptides. Acta Sci Pol Technol Aliment 14:181–190. https://doi.org/10.17306/J.AFS.2015.3.19.

    Article  PubMed  Google Scholar 

  106. Gomez-Guillen MC, Gimenez B, Lopez-Caballero ME, Montero MP (2011) Functional and bioactive properties of collagen and gelatin from alternative sources: a review. Food Hydrocol 25:1813–1827. https://doi.org/10.1016/j.foodhyd.2011.02.007

    Article  CAS  Google Scholar 

  107. Atsuta SHK, Himizu TSS, Amada RYY, Ishimura TON (2003) Angiotensin I-converting enzyme inhibitory peptides in a hydrolyzed chicken breast muscle extract. Blood Press 18:1741–1745. https://doi.org/10.1021/jf020604h

    Article  CAS  Google Scholar 

  108. Arihara K, Nakashima Y, Mukai T, Ishikawa S, Itoh M (2001) Peptide inhibitors for angiotensin I-converting enzyme from enzymatic hydrolysates of porcine skeletal muscle proteins. Meat Sci 57:319–324. https://doi.org/10.1016/S0309-1740(00)00108-X

    Article  CAS  PubMed  Google Scholar 

  109. Arihara K (2006) Strategies for designing novel functional meat products. Meat Sci 74:219–229. https://doi.org/10.1016/j.meatsci.2006.04.028

    Article  CAS  PubMed  Google Scholar 

  110. Nakashima Y, Arihara K, Sasaki A, Mio H, Ishikawa S, Itoh M (2002) Antihypertensive activities of peptides derived from porcine skeletal muscle myosin in spontaneously hypertensive rats. J Food Sci 67:434–437. https://doi.org/10.1111/j.1365-2621.2002.tb11424.x

    Article  CAS  Google Scholar 

  111. Muguruma M, Ahhmed AM, Katayama K, Kawahara S, Maruyama M, Nakamura T (2009) Identification of pro-drug type ACE inhibitory peptide sourced from porcine myosin B: evaluation of its antihypertensive effects in vivo. Food Chem 114:516–522. https://doi.org/10.1016/j.foodchem.2008.09.081

    Article  CAS  Google Scholar 

  112. Ukeda H, Matsuda H, Osajima K, Matsufuji H, Matsui T, Osajima Y (1992) Peptides from peptidic hydrolysate of heated sardine meat that inhibit angiotensin I-converting enzyme. Nippon Nogei Kaishi 66:25–29

    Article  CAS  Google Scholar 

  113. Saiga A, Okumura T, Makihara T, Katsuda S-I, Morimatsu F, Nishimura T (2006) Action mechanism of an angiotensin I-converting enzyme inhibitory peptide derived from chicken breast muscle. J Agric Food Chem 54:942–945. https://doi.org/10.1021/jf0508201

    Article  CAS  PubMed  Google Scholar 

  114. Ryan JT, Ross RP, Bolton D, Fitzgerald GF, Stanton C (2011) Bioactive peptides from muscle sources: meat and fish. Forum Nutr 3(9):765–791. https://doi.org/10.3390/nu3090765

    Article  CAS  Google Scholar 

  115. Toldrá F, Reig M, Aristoy MC, Mora L (2017) Generation of bioactive peptides during food processing. Food Chem. https://doi.org/10.1016/j.foodchem.2017.06.119

  116. Fernández M, Benito MH, Martín A, Casquete R, Córdoba JJ, Córdoba MG (2016) Influence of starter culture and a protease on the generation of ACE-inhibitory and antioxidant bioactive nitrogen compounds in Iberian dry-fermented sausage ‘salchichón’. Heliyon 2(3):e00093. https://doi.org/10.1016/j.heliyon.2016.e00093

    Article  PubMed  PubMed Central  Google Scholar 

  117. Gu Y, Majumder K, Wu J (2011) QSAR-aided in silico approach in evaluation of food proteins as precursors of ACE inhibitory peptides. Food Res Int 44:2465–2474. https://doi.org/10.1016/j.foodres.2011.01.051

    Article  CAS  Google Scholar 

  118. Terashima M, Baba T, Ikemoto N, Katayama M, Morimoto T, Matsumura S (2010) Novel angiotensin-converting enzyme (ACE) inhibitory peptides derived from boneless chicken leg meat. J Agric Food Chem 58(12):7432–7436. https://doi.org/10.1021/jf100977z

    Article  CAS  PubMed  Google Scholar 

  119. R-Z G, Liu WY, Lin F, Jin ZT, Chen L, Yi WX, Lu J, Cai MY (2012) Antioxidant and angiotensin I-converting enzyme inhibitory properties of oligopeptides derived from black-bone silky fowl (Gallus gallus domesticus Brisson) muscle. Food Res Int 49:326–333. https://doi.org/10.1016/j.foodres.2012.07.009

    Article  CAS  Google Scholar 

  120. Katayama K, Tomatsu M, Fuchu H, Sugiyama M, Kawahara S, Yamauchi K, Muguruma M (2003) Purification and characterization of an angiotensin I-converting enzyme inhibitory peptide derived from porcine troponin C. Anim Sci J 74:53–58. https://doi.org/10.1046/j.1344-3941.2003.00086.x

    Article  CAS  Google Scholar 

  121. Escudero E, Sentandreu MA, Arihara K, Toldrá F (2010) Angiotensin I-converting enzyme inhibitory peptides generated from in vitro gastrointestinal digestion of pork meat. J Agric Food Chem 58:2895–2901. https://doi.org/10.1021/jf904204n.

    Article  CAS  PubMed  Google Scholar 

  122. Escudero E, Toldrá F, Sentandreu MA, Nishimura H, Arihara K (2012b) Antihypertensive activity of peptides identified in the in vitro gastrointestinal digest of pork meat. Meat Sci 91:382–384. https://doi.org/10.1016/j.meatsci.2012.02.007

    Article  CAS  PubMed  Google Scholar 

  123. Jang A, Lee M (2005) Purification and identification of angiotensin converting enzyme inhibitory peptides from beef hydrolysates. Meat Sci 69:653–661. https://doi.org/10.1016/j.meatsci.2004.10.014

    Article  CAS  PubMed  Google Scholar 

  124. Jang A, Cho YJ, Lee JI, Shin JH, Kim IS, Lee M (2004) The effect of beef peptide on blood pressure and serum lipid concentration of spontaneously hypertensive rat (SHR). J Anim Sci Technol 46:107–114. https://doi.org/10.5187/JAST.2004.46.1.107

    Article  CAS  Google Scholar 

  125. Bernardini RD, Mullen AM, Bolton D, Kerry J, O'Neill E, Hayes M (2012) Assessment of the angiotensin-I-converting enzyme (ACE-I) inhibitory and antioxidant activities of hydrolysates of bovine brisket sarcoplasmic proteins produced by papain and characterisation of associated bioactive peptidic fractions. Meat Sci 90:226–235. https://doi.org/10.1016/j.meatsci.2011.07.008

    Article  CAS  PubMed  Google Scholar 

  126. Sakanaka S, Tachibana Y, Ishihara N, Juneja LR (2005) Antioxidant properties of casein calcium peptides and their effects on lipid oxidation in beef homogenates. Food Chem 53:464–468. https://doi.org/10.1021/jf0487699

    Article  CAS  Google Scholar 

  127. Díaz M, Decker EA (2004) Antioxidant mechanisms of caseinophosphopeptidases and casein hydrolysates and their application in ground beef. J Agric Food Chem 52:8208–8213. https://doi.org/10.1021/jf048869e

    Article  CAS  PubMed  Google Scholar 

  128. Peña-Ramos EA, Xiong YL (2003) Whey and soy hydrolysates inhibit lipid oxidation in cooked pork patties. Meat Sci 64:259–263. https://doi.org/10.1016/S0309-1740(02)00187-0

    Article  CAS  PubMed  Google Scholar 

  129. Minkiewicz P, Dziuba J, Michalska J (2011) Bovine meat proteins as potential precursors of biologically active peptides – a computational study based on the BIOPEP database. Food Sci Technol Int 17:39–45. https://doi.org/10.1177/1082013210368461.

    Article  CAS  PubMed  Google Scholar 

  130. Fu Y, Young JF, Løkke MM, Lametsch R, Aluko RE, Therkildsen M (2016) Revalorisation of bovine collagen as a potential precursor of angiotensin I-converting enzyme (ACE) inhibitory peptides based on in silico and in vitro protein digestions. J Funct Foods 24:196–206. https://doi.org/10.1016/j.jff.2016.03.026

    Article  CAS  Google Scholar 

  131. Fu Y, Young JF, Rasmussen MK, Dalsgaard TK, Lametsch R, Aluko RE, Therkildsen M (2016) Angiotensin I-Converting enzyme–inhibitory peptides from bovine collagen: insights into inhibitory mechanism and transepithelial transport. Food Res Int 89:373–381. https://doi.org/10.1016/j.foodres.2016.08.037

    Article  CAS  PubMed  Google Scholar 

  132. Fu Y, Young JF, Dalsgaard TK, Therkildsen M (2015) Separation of angiotensin I converting enzyme inhibitory peptides from bovine connective tissue and their stability towards temperature, pH and digestive enzymes. Int J Food Sci Technol 50:1234–1243. https://doi.org/10.1111/ijfs.12771

    Article  CAS  Google Scholar 

  133. Banerjee P, Shanthi C (2012) Isolation of novel bioactive regions from bovine Achilles tendon collagen having angiotensin I-converting enzyme-inhibitory properties. Process Biochem 47:2335–2346. https://doi.org/10.1016/j.procbio.2012.09.012

    Article  CAS  Google Scholar 

  134. O’Keeffe MB, Norris R, Alashi MA, Aluko RE, FitzGerald RJ (2017) Peptide identification in a porcine gelatin prolyl endoproteinase hydrolysate with angiotensin converting enzyme (ACE) inhibitory and hypotensive activity. J Funct Foods 34:77–88. https://doi.org/10.1016/j.jff.2017.04.018

    Article  CAS  Google Scholar 

  135. Ngo DH, Kang KH, Ryu B, Vo TS, Jung WK, Byun HG, Kim SK (2015) Angiotensin-I converting enzyme inhibitory peptides from antihypertensive skate (Okamejei kenojei) skin gelatin hydrolysate in spontaneously hypertensive rats. Food Chem 174:37–43. https://doi.org/10.1016/j.foodchem.2014.11.013

    Article  CAS  PubMed  Google Scholar 

  136. Lin L, Lv S, Li B (2012) Angiotensin-I-converting enzyme (ACE)-inhibitory and antihypertensive properties of squid skin gelatin hydrolysates. Food Chem 131:225–230. https://doi.org/10.1016/j.foodchem.2011.08.064

    Article  CAS  Google Scholar 

  137. Zhuang Y, Sun L, Zhang Y, Liu G (2012) Antihypertensive effect of long-term oral administration of jellyfish (Rhopilema esculentum) collagen peptides on renovascular hypertension. Mar Drugs 10:417. https://doi.org/10.3390/md10020417.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  138. Herregods G, Van Camp J, Morel N, Ghesquière B, Gevaert K, Vercruysse L, Smagghe G (2011) Angiotensin I-converting enzyme inhibitory activity of gelatin hydrolysates and identification of bioactive peptides. J Agric Food Chem 59:552–558. https://doi.org/10.1021/jf1037823

    Article  CAS  PubMed  Google Scholar 

  139. Ichimura T, Yamanaka A, Otsuka T, Yamashita E, Maruyama S (2009) Antihypertensive effect of enzymatic hydrolysate of collagen and Gly-Pro in spontaneously hypertensive rats. Biosci Biotechnol Biochem 73:2317–2319. https://doi.org/10.1271/bbb.90197

    Article  CAS  PubMed  Google Scholar 

  140. Faria M, da Costa EL, Gontijo JAR, Netto FM (2008) Evaluation of the hypotensive potential of bovine and porcine collagen hydrolysates. J Med Food 11:560–567. https://doi.org/10.1089/jmf.2007.0573.

    Article  CAS  PubMed  Google Scholar 

  141. Saiga A, Iwai K, Hayakawa T, Takahata Y, Kitamura S, Nishimura T, Morimatsu F (2008) Angiotensin I-converting enzyme-inhibitory peptides obtained from chicken collagen hydrolysate. J Agric Food Chem 56:9586–9591. https://doi.org/10.1021/jf072669w

    Article  CAS  PubMed  Google Scholar 

  142. Taga Y, Kusubata M, Ogawa-Goto K, Hattori S (2016) Efficient absorption of X-hydroxyproline (Hyp)-Gly after oral administration of a novel gelatine hydrolysate prepared using ginger protease. J Agric Food Chem 64:2962–2970. https://doi.org/10.1021/acs.jafc.6b00609

    Article  CAS  PubMed  Google Scholar 

  143. Iwai K, Hasegawa T, Taguchi Y, Morimatsu F, Sato K, Nakamura Y, Ohtsuki K (2005) Identification of food-derived collagen peptides in human blood after oral ingestion of gelatin hydrolysates. J Agric Food Chem 53:6531–6536. https://doi.org/10.1021/acs.jafc.6b00609

    Article  CAS  PubMed  Google Scholar 

  144. Inoue N, Hamasaki A, Hidaka S, Miura N, Fukahori M, Maruyama M, Kawahara S, Ohta K, Muguruma M (2013) Analysis of the components of porcine liver hydrolysate and examination of the antioxidant activity and angiotensin converting enzyme (ACE)-inhibiting activity. Yakugaku Zasshi 133(1):107–115. https://doi.org/10.1248/yakushi.y110184

    Article  CAS  PubMed  Google Scholar 

  145. Wu H, He HL, Chen XL, Sun CY, Zhang YZ, Zhou BC (2008) Purification and identification of novel angiotensin-I-converting enzyme inhibitory peptides from shark meat hydrolysate. Process Biochem 43:457–461. https://doi.org/10.1016/j.procbio.2008.01.018

    Article  CAS  Google Scholar 

  146. Van Platerink CJ, Janssen HGM, Haverkamp J (2008) Application of at-line two-dimensional liquid chromatography-mass spectrometry for identification of small hydrophilic angiotensin I-inhibiting peptides in milk hydrolysates. Anal Bioanal Chem 391:299–307. https://doi.org/10.1007/s00216-008-1990-3

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  147. Yu Y, Hu J, Miyaguchi Y, Bai X, Du Y, Lin B (2006) Isolation and characterisation of angiotensin I-converting enzyme inhibitory peptides derived from porcine haemoglobin. Peptides 27:2950–2956. https://doi.org/10.1016/j.peptides.2006.05.025

    Article  CAS  PubMed  Google Scholar 

  148. Kim SK, Byun HG, Park PJ, Shahidi F (2001) Angiotensin I converting enzyme inhibitory peptides purified from bovine skin gelatin hydrolysate. J Agric Food Chem 49:2992–2997

    Article  CAS  PubMed  Google Scholar 

  149. Ferranti P, Nitride C, Nicolai MA, Mamone G, Picariello G, Bordoni A, Valli V, Nunzio MD, Babini E, Marcolini E, Capozzi F (2014) In vitro digestion of Bresaola proteins and release of potential bioactive peptides. Food Res Int 63:157–169. https://doi.org/10.1016/j.foodres.2014.02.008

    Article  CAS  Google Scholar 

  150. Gallego M, Mora L, Fraser PD, Aristoy MC, Toldrá F (2014) Degradation of LIM domain-binding protein three during processing of Spanish dry-cured ham. Food Chem 149:121–128. https://doi.org/10.1016/j.foodchem.2013.10.076

    Article  CAS  PubMed  Google Scholar 

  151. Christensen L, Ertbjerg P, Løje H, Risbo J, van den Berg FW, Christensen M (2013) Relationship between meat toughness and properties of connective tissue from cows and young bulls heat treated at low temperatures for prolonged times. Meat Sci 93:787–795. https://doi.org/10.1016/j.meatsci.2012.12.001

    Article  PubMed  Google Scholar 

  152. Fogle DR, Plimpton RF, Ockerman HW, Jarenback L, Persson T (1982) Tenderization of beef: effect of enzyme, enzyme level, and cooking method. J Food Sci 47:1113–1118

    Article  CAS  Google Scholar 

  153. Escudero E, Mora L, Fraser PD, Aristoy MC, Arihara K, Toldrá F (2013) Purification and identification of antihypertensive peptides in Spanish dry-cured ham. J Proteome 78:499–507. https://doi.org/10.1016/j.jprot.2012.10.019

    Article  CAS  Google Scholar 

  154. Liu D, Chen X, Huang J, Huang M, Zhou G (2017) Generation of bioactive peptides from duck meat during post-mortem aging. Food Chem 237:408–415. https://doi.org/10.1016/j.foodchem.2017.05.094

    Article  CAS  PubMed  Google Scholar 

  155. Sangsawad P, Roytrakul S, Yongsawatdigul J (2017) Angiotensin converting enzyme (ACE) inhibitory peptides derived from the simulated in vitro gastrointestinal digestion of cooked chicken breast. J Funct Foods 29:77–83. https://doi.org/10.1016/j.jff.2016.12.005

    Article  CAS  Google Scholar 

  156. Darewicz M, Borawska J, Vegarud GE, Minkiewicz P, Iwaniak A (2014) Angiotensin I-converting enzyme (ACE) inhibitory activity and ACE inhibitory peptides of salmon (Salmo salar) protein hydrolysates obtained by human and porcine gastrointestinal enzymes. Int J Mol Sci 15:14077–14101. https://doi.org/10.3390/ijms150814077

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  157. Natesh R, Schwager SL, Sturrock ED, Acharya KR (2003) Crystal structure of the human angiotensin-converting enzyme-lisinopril complex. Nature 421:551–554. https://doi.org/10.1038/nature01370

    Article  CAS  PubMed  Google Scholar 

  158. Soladoye O, Juárez M, Aalhus J, Shand P, Estévez M (2015) Protein oxidation in processed meat: mechanisms and potential implications on human health. Compr Rev Food Sci Food Saf 14:106–122. https://doi.org/10.1111/1541-4337.12127

    Article  CAS  PubMed  Google Scholar 

  159. Estévez M (2011) Protein carbonyls in meat systems: a review. Meat Sci 89:259–279. https://doi.org/10.1016/j.meatsci.2011.04.025

    Article  CAS  PubMed  Google Scholar 

  160. Katayama K, Tomatsu M, Kawahara S, Yamauchi K, Fuchu H, Kodama Y, Kawamura Y, Muguruma M (2004) Inhibitory profile of nanopeptide derived from porcine troponin C against angiotensin I-converting enzyme. J Agric Food Chem 52:771–775. https://doi.org/10.1021/jf0350865

    Article  CAS  PubMed  Google Scholar 

  161. Mirdhayati I, Hermanianto J, Wijaya CH, Sajuthi D, Arihara K (2016) Angiotensin converting enzyme (ACE) inhibitory and antihypertensive activities of protein hydrolysate from meat of Kacang goat (Capra aegagrus hircus). J Sci Food Agric 96:3536–3542. https://doi.org/10.1002/jsfa.7538

    Article  CAS  PubMed  Google Scholar 

  162. Mora L, Aristoy M, Toldrá F (2016) Bioactive peptides in foods. In: Caballero B, Finglas PM, Toldrá F (eds) Encyclopedia of food and health, vol vol 1. Academic Press/Elsevier Science Ltd, London, pp 395–400

    Chapter  Google Scholar 

  163. Escudero E, Aristoy MC, Nishimura H, Arihara K, Toldrá F (2012) Antihypertensive effect and antioxidant activity of peptide fractions extracted from Spanish dry cured ham. Meat Sci 91:306–311. https://doi.org/10.1016/j.meatsci.2012.02.008

    Article  CAS  PubMed  Google Scholar 

  164. Arihara K, Ohata M (2008) Bioactive compounds in meat. In: Meat biotechnology, Springer, pp 231–249, Toldrá, F (Edn), ISBN: 978-0-387-79381-8 (Print), 978-0-387-79382-5 (Online).

    Google Scholar 

  165. Escudero E, Mora L, Toldrá F (2014) Stability of ACE inhibitory ham peptides against heat treatment and in vitro digestion. Food Chem 161:305–311. https://doi.org/10.1016/j.foodchem.2014.03.117

    Article  CAS  PubMed  Google Scholar 

  166. Mora L, Escudero E, Arihara K, Toldrá F (2015) Antihypertensive effect of peptides naturally generated during Iberian dry-cured ham processing. Food Res Int 78:71–78. https://doi.org/10.1016/j.foodres.2015.11.005

    Article  CAS  PubMed  Google Scholar 

  167. Dellafiora L, Paolella S, Dall'Asta C, Dossena A, Cozzini P, Galaverna G (2015) Hybrid in silico/in vitro approach for the identification of angiotensin I converting enzyme inhibitory peptides from Parma dry-cured ham. J Agric Food Chem 63(28):6366–6375. https://doi.org/10.1021/acs.jafc.5b02303

    Article  CAS  PubMed  Google Scholar 

  168. Paolella S, Falavigna C, Faccini A, Virgili R, Sforza S, Dall'Asta C, Dossena A, Galaverna G (2015) Effect of dry-cured ham maturation time on simulated gastrointestinal digestion: characterization of the released peptide fraction. Food Res Int 67:136–144. https://doi.org/10.1016/j.foodres.2014.10.026

    Article  CAS  Google Scholar 

  169. Sentandreu MA, Toldrá F (2007) Evaluation of ACE inhibitory activity of dipeptides generated by the action of porcine muscle dipeptidyl peptidases. Food Chem 102:511–515. https://doi.org/10.1016/j.foodchem.2006.04.018

    Article  CAS  Google Scholar 

  170. Vaštag Ž, Popović L, Popović S, Petrović L, Peričin D (2010) Antioxidant and angiotensin-I converting enzyme inhibitory activity in the water-soluble protein extract from Petrovac Sausage (Petrovská Kolbasá). Food Control 21:1298–1302. https://doi.org/10.1016/j.foodcont.2010.03.004

    Article  CAS  Google Scholar 

  171. Gallego M, Grootaert C, Mora L, Aristoy MC, Camp JV, Toldrá F (2016) Transepithelial transport of dry-cured ham peptides with ACE inhibitory activity through a Caco-2 cell monolayer. J Funct Foods 21:388–395. https://doi.org/10.1016/j.jff.2015.11.046

    Article  CAS  Google Scholar 

  172. Mora L, Escudero E, Toldrá F (2016) Characterization of the peptide profile in Spanish Teruel, Italian Parma and Belgian dry-cured hams and its potential bioactivity. Food Res Int 89:638–646. https://doi.org/10.1016/j.foodres.2016.09.016

    Article  CAS  PubMed  Google Scholar 

  173. Benito MJ, Connerton IF, Cordoba JJ (2006) Genetic characterization and expression of the novel fungal protease: EPg222 active in dry-cured meat products. Appl Microbiol Biot 73:356–365. https://doi.org/10.1007/s00253-006-0498-z

    Article  CAS  Google Scholar 

  174. Mejri L, Romy VV, Hassouna MN, Marina ML, García MC (2017) Identification of peptides with antioxidant and antihypertensive capacities by RP-HPLC-Q-TOF-MS in dry fermented camel sausages inoculated with different starter cultures and ripening times. Food Res Int. https://doi.org/10.1016/j.foodres.2017.07.072

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Bhat, Z.F., Mason, S., Morton, J.D., Bekhit, A.ED.A., Bhat, H.F. (2019). Antihypertensive Peptides from Animal Proteins. In: Mérillon, JM., Ramawat, K.G. (eds) Bioactive Molecules in Food. Reference Series in Phytochemistry. Springer, Cham. https://doi.org/10.1007/978-3-319-78030-6_18

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