Composition and properties of peptides that survive standardised in vitro gastro-pancreatic digestion of bovine milk

International Dairy Journal

Volumn 61, Issue , 2016, Pages 196-204

  Tagliazucchi, Davide ^a   Helal, Ahmed ^b   Verzelloni, Elena ^a   Bellesia, Andrea ^a   Conte, Angela ^a  

^a UNIVERSITY OF MODENA AND REGGIO EMILIA   (Italy)

^b DAMANHOUR UNIVERSITY   (Egypt)

Author keywords

[No Author keywords available]

Indexed keywords

MAMMALS; MASS SPECTROMETRY; MICROORGANISMS;

ACE-INHIBITORY ACTIVITY; ANTI-MICROBIAL ACTIVITY; ANTI-THROMBOTIC ACTIVITIES; BIOACTIVE PROTEINS; DISULPHIDE BONDS; EVOLUTIONARY PROCESS; IMMUNOMODULATORY; PROLINE RESIDUES;

PEPTIDES;

EID: 84978143573     PISSN: 09586946     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.idairyj.2016.06.002     Document Type: Article

References (43)

1. Adler-Nissen, J., Determination of the degree of hydrolysis of food protein hydrolysates by trinitrobenzensulfonic acid. Journal of Agricultural and Food Chemistry 27 (1979), 1256–1262.
2. Ashmarin, I.P., Karazeeva, E.P., Lyapina, L.A., Samonina, G.E., The simplest proline-containing peptides PG, GP, PGP, and GPGG: Regulatory activity and possible sources of biosynthesis. Biochemistry (Mosc) 63 (1998), 119–124.
3. Boutrou, R., Gaudichon, C., Dupont, D., Jardin, J., Airinei, G., Marsset-Baglieri, A., et al. Sequential release of milk protein-derived bioactive peptides in the jejunum in healthy humans. American Journal of Clinical Nutrition 97 (2013), 1314–1323.
4. Byun, H.G., Kim, S.K., Structure and activity of angiotensin I converting enzyme inhibitory peptides derived from Alaskan pollack skin. Journal of Biochemistry and Molecular Biology 35 (2002), 239–243.
5. Chabance, B., Marteau, P., Rambaud, J.C., Migliore-Samour, D., Boynard, M., Perrotin, P., et al. Casein peptide release and passage to the blood in humans during digestion of milk or yogurt. Biochimie 80 (1998), 155–165.
6. Choi, J., Sabikhi, L., Hassan, A., Anand, S., Bioactive peptides in dairy products. International Journal of Dairy Technology 65 (2012), 1–12.
7. Cieslinska, A., Kaminski, S., Kostyra, E., Sienkiewicz-Szlapka, E., Beta-casomorphin 7 in raw and hydrolyzed milk derived from cows of alternative beta-casein genotypes. Milchwissenschaft 62 (2007), 125–127.
8. Dahm, L.J., Jones, D.P., Secretion of cysteine and glutathione from mucosa to lumen in rat small intestine. American Journal of Physiology 267 (1994), G292–G300.
9. Daniel, H., Vohwinkel, M., Rehner, G., Effect of casein and β-casomorphins on gastrointestinal motility in rats. Journal of Nutrition 120 (1990), 252–257.
10. De Noni, I., Release of β-casomorphins 5 and 7 during simulated gastro-intestinal digestion of bovine β-casein variants and milk-based infant formulas. Food Chemistry 110 (2008), 897–903.
11. Dei Più, L., Tassoni, A., Serrazanetti, D.I., Ferri, M., Babini, E., Tagliazucchi, D., et al. Exploitation of starch industry liquid by-product to produce bioactive peptides from rice hydrolyzed proteins. Food Chemistry 155 (2014), 199–206.
12. Enari, J., Takahashi, Y., Kawarasaki, M., Tada, M., Tatsuta, K., Identification of angiotensin I-converting enzyme inhibitory peptides derived from salmon muscle and their antihypertensive effect. Fisheries Science 74 (2008), 911–920.
13. Fiat, A.M., Migliore-Samour, D., Jollès, P., Biologically active peptides from milk proteins with emphasis on two examples concerning antithrombotic and immunomodulating activities. Journal of Dairy Science 76 (1993), 301–310.
14. Gill, H.S., Doull, F., Rutherford, K.J., Cross, M.L., Immunoregolatory peptides in bovine milk. British Journal of Nutrition 84 (2000), S111–S117.
15. Harington, C.L., Pitt Rivers, R.R.V., The synthesis of cysteine- (cystine-) tyrosine peptides and the action thereon of crystalline pepsin. Biochemical Journal 38 (1944), 417–423.
16. Hernández-Ledesma, B., Recio, I., Amigo, L., Beta-lactoglobulin as source of bioactive peptides. Amino Acids 35 (2008), 257–265.
17. Jinsmaa, Y., Yoshikawa, M., Enzymatic release of neocasomorphin and β-casomorphin from bovine β-casein. Peptides 20 (1999), 957–962.
18. Juillerat-Jeanneret, L., Robert, M.C., Juillerat, M.A., Peptides from Lactobacillus hydrolysates of bovine milk caseins inhibit prolyl-peptidases of human colon cells. Journal of Agricultural and Food Chemistry 59 (2011), 370–377.
19. A receptors in mice. FEBS Letters 584 (2010), 599–604.
20. Kawasaki, K., Lafont, A.G., Sire, I.Y., The evolution of milk casein genes from tooth genes before the origin of mammals. Molecular Biology and Evolution 28 (2011), 2053–2061.
21. Kayser, H., Meisel, H., Stimulation of human peripheral blood lymphocytes by bioactive peptides derived from bovine milk proteins. FEBS Letters 383 (1996), 18–20.
22. Lawandi, J., Gerber-Lemaire, S., Juillerat-Jeanneret, L., Moitessier, N., Inhibitors of prolyl oligopeptidases for the therapy of human diseases: Defining diseases and inhibitors. Journal of Medicinal Chemistry 53 (2010), 3423–3438.
23. Lefèvre, C.M., Sharp, J.A., Nicholas, K.R., Evolution of lactation: Ancient origin and extreme adaptations of the lactation system. Annual Review Genomics Human Genetics 11 (2010), 219–238.
24. Maeno, M., Yamamoto, N., Takano, T., Identification of an antihypertensive peptide from casein hydrolysate produced by a proteinase from Lactobacillus helveticus CP790. Journal of Dairy Science 79 (1996), 1316–1321.
25. Meisel, H., Frister, H., Schlimme, E., Biologically active peptides in milk proteins. Zeitschrift für Ernährungswissenschaft 28 (1989), 267–278.
26. Minekus, M., Alminger, M., Alvito, P., Ballance, S., Bohn, T., Bourlieu, C., et al. A standardised static in vitro digestion method suitable for food – An international consensus. Food and Function 5 (2014), 1115–1124.
27. Morifuji, M., Koga, J., Kawanaka, K., Higuchi, M., Branched-chain amino acid-containing dipeptides, identified from whey protein hydrolysates, stimulate glucose uptake rate in L6 myotubes and isolated skeletal muscles. Journal of Nutritional Science and Vitaminology 55 (2009), 81–86.
28. Nagpal, R., Behare, P., Rana, R., Kumar, A., Kumar, M., Arora, S., et al. Bioactive peptides derived from milk proteins and their health beneficial potentials: An update. Food and Function 2 (2011), 18–27.
29. Nakahara, T., Sano, A., Yamaguchi, H., Sugimoto, K., Chikata, H., Kinoshita, E., et al. Antihypertensive effect of peptide-enriched soy sauce-like seasoning and identification of its angiotensin I-converting enzyme inhibitory substances. Journal of Agricultural and Food Chemistry 58 (2010), 821–827.
30. Nongonierma, A.B., Richard, J., FitzGerald, R.J., Dipeptidyl peptidase IV inhibitory and antioxidative properties of milk protein-derived dipeptides and hydrolysates. Peptides 39 (2013), 157–163.
31. Pan, D., Cao, J., Guo, H., Zhao, B., Studies on purification and the molecular mechanism of a novel ACE inhibitory peptide from whey protein hydrolysate. Food Chemistry 130 (2012), 121–126.
32. Picariello, G., Ferranti, P., Fierro, O., Mamone, G., Caira, S., Di Luccia, A., et al. Peptides surviving the simulated gastrointestinal digestion of milk proteins: Biological and toxicological implications. Journal of Chromatography B 878 (2010), 295–308.
33. Pihlanto-Leppälä, A., Rokka, T., Korhonen, H., Angiotensin I-converting enzyme inhibitory peptides derived from bovine milk proteins. International Dairy Journal 8 (1998), 525–531.
34. van Platerink, C.J., Janssen, H.G.M., Haverkamp, J., Application of at-line two-dimensional liquid chromatography-mass spectrometry for identification of small hydrophilic angiotensin I-inhibiting peptides in milk hydrolysates. Analytical and Bioanalytical Chemistry 391 (2008), 299–307.
35. Ricci-Cabello, I., Herrera, M.O., Artacho, R., Possible role of milk-derived bioactive peptides in the treatment and prevention of metabolic syndrome. Nutrition Review 70 (2012), 241–255.
36. Schmelzer, C.E.H., Schops, R., Reynell, L., Ulbrich-Hofmann, R., Neubert, R.H.H., Raith, K., Peptic digestion of β-casein. Time course and fate of possible bioactive peptides. Journal of Chromatography A 1166 (2007), 108–115.
37. Solieri, L., Rutella, G.S., Tagliazucchi, D., Impact of non-starter lactobacilli on release of peptides with angiotensin-converting enzyme inhibitory and antioxidant activities during bovine milk fermentation. Food Microbiology 51 (2015), 108–116.
38. Steen, H., Mann, M., The abc's (and xyz's) of peptide sequencing. Nature Review Molecular Cell Biology 5 (2004), 699–711.
39. Tagliazucchi, D., Shamsia, S., Conte, A., Release of angiotensin converting enzyme-inhibitory peptides during in vitro gastro-intestinal digestion of camel milk. International Dairy Journal 56 (2016), 119–128.
40. Tulipano, G., Sibilia, V., Caroli, A.M., Cocchi, D., Whey proteins as source of dipeptidyl dipeptidase IV (dipeptidyl peptidase-4) inhibitors. Peptides 32 (2011), 835–838.
41. Yin, H., Miao, J., Zhang, Y., Protective effect of β-casomorphin-7 on type 1 diabetes rats induced with streptozotocin. Peptides 31 (2010), 1725–1729.
42. Yoshimoto, T., Fischl, M., Orlowski, R.C., Walter, R., Post-proline cleaving enzyme and post-proline dipeptidyl aminopeptidase. Comparison of two peptidases with high specificity for proline residues. Journal of Biological Chemistry 253 (1978), 3708–3716.
43. Zoghbi, S., Trompette, A., Claustre, J., El Homsi, M., Garzón, J., Jourdan, G., et al. β-Casomorphin-7 regulates the secretion and expression of gastrointestinal mucins through a μ-opioid pathway. American Journal of Physiology Gastrointestinal Liver Physiology 290 (2006), G1105–G1113.