The main milk proteins are caseins and whey proteins, some other minor proteins and peptides, are also found in milk. Proteins are vital ingredients for human because they provide all the essential amino acids needed for body and human health. Milk proteins are very important sources of bioactive peptides. The bioactive peptides are inactive within the sequence of the parent protein and can be released by proteolytic enzymes, during gastrointestinal digestion or during milk processing, for example the adding coagulation enzymes and starter culture. Once bioactive peptides are present in the body, these peptides may act as regulatory compounds with hormone-like activity. Furthermore, Bioactive peptides from milk proteins have many biological activities such as antimicrobial, antihypertensive, antithrombotic, antioxidant, mineral binding, and anti-diabetic. Bioactive peptides have potential health and have pharmaceutical applications. Antimicrobial peptides are recognized as an important component of innate immunity, particularly at mucosal surfaces such as the lungs and small intestine that are constantly exposed to a range of potential pathogens. The ability of protein hydrolysates to inhibit deleterious changes caused by lipid oxidation appears to be related to the nature and composition of the different peptide fractions. Milk protein hydrolysate possesses free-radical-scavenging and anti-inflammatory activities have many beneficial effects on the increase of the glucose-induced insulin secretion and reduction in postprandial glycemia. This article is tried through exposure in some detail to review characteristics of some milk protein peptides and its positive effects on human health.
| Published in | Advances in Biochemistry (Volume 7, Issue 1) |
| DOI | 10.11648/j.ab.20190701.15 |
| Page(s) | 22-33 |
| Creative Commons |
This is an Open Access article, distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium or format, provided the original work is properly cited. |
| Copyright |
Copyright © The Author(s), 2019. Published by Science Publishing Group |
Milk Proteins, Bioactive Peptides, Anti-diabetic, Antioxidant, Antimicrobial, Anti-hypertensive
| [1] | Swaisgood, H. E., 2003. Chemistry of the caseins. In Fox, P. F. and McSeeney, P. L. H. (Eds.), Advanced Dairy Chemistry, Vol. 1, Proteins, Part A (pp. 139–201). Kluwer Academic/Plenum Press. New York. USA. |
| [2] | Fox, P. F., 2003. Milk proteins: General and historical aspects. Fox, P. F. and McSeeney, P. L. H. (Eds.), Advanced Dairy Chemistry, Vol. 1, Proteins (pp. 1–48). Kluwer Academic/Plenum Press. New York. USA. |
| [3] | Dziuba, M., Dziuba, B., Iwaniak, A., 2009. Milk proteins as precursors of bioactive peptides. Acta Sci. Pol., Technol. Aliment, 8 (1): 71-90. |
| [4] | Korhonen, H., 2009a. Milk-derived bioactive peptides: From science to applications. Journal of Functional Foods, 1: 177 –187. |
| [5] | Korhonen, H., Pihlanto, A., 2003. Food-derived bioactive peptides opportunities for designing future foods. Current Pharmaceutical Design, 9: 1297–1308. |
| [6] | Hartmann, R., Meisel, H., 2007. Food-derived peptides with biological activity: from research to food applications. Curr. Opin. Biotechnol, 18: 163–169. |
| [7] | Hajirostamloo, B., 2010. Bioactive component in milk and dairy product. World academy of science, Engineering and Technology, 72: 162-166. |
| [8] | Plaisanciéa, P., Claustrec, J., Estiennea, M., Henryd, G., Boutroud, R., Paqueta, A., Léonild, J., 2013. A novel bioactive peptide from yoghurts modulates expression of the gel-forming MUC2 mucin as well as population of goblet cells and Paneth cells along the small intestin. Journal of Nutritional Biochemistry, 24: 213–221. |
| [9] | Kitts, D. D., Weiler, K., 2003. Bioactive proteins and peptides from Food sources. Applications of bioprocesses used in isolation and recovery. Current Pharmaceutical Design, 9: 1309–1323. |
| [10] | Atanasova, J., Ivanova, I., 2010. Antibacterial peptides from goat and sheep milk proteins. Biotechnol. & Biotechnol; 1799: 1803. |
| [11] | Vermeirssen, V., Van Camp, J., Verstraete, W., 2004. Bioavailability of angiotensin I-converting enzyme inhibitory peptides. British Journal of Nutrition, 92: 357–366. |
| [12] | Picariello, G., Ferranti, P., Fierroa O., Mamonea, G., Cairaa, S., Di Luccia, A., Monica, S., Addeon, F., 2010. Peptides surviving the simulated gastrointestinal digestion of milk proteins: Biological and toxicological implications. Journal of Chromatography; B 878: 295-308. |
| [13] | Phelan, M., Kerins, D., 2011. The potential role of milk-derived peptides in cardiovascular disease. Food Funct., 2: 153-167. |
| [14] | Phelan, M., Aherne, A., Fitzgerald, R. J., O'Brien, N. M., 2009. Casein- derived bioactive peptides: biological effects, industrial uses, safety aspects and regulatory status. International Dairy Journal, 19: 643-654. |
| [15] | Hernández-Ledesma. B., Contreras, M. M., Recio, I., 2011. Antihypertensive peptides: production, bioavailability and incorporation into foods. Advances in Colloid and Interface Science, 165: 23–35. |
| [16] | Wei, Q. and Zhimin, H. 2006. Enzymatic hydrolysis of protein: mechanism and kinetic model. Front. Chem. China, 3: 308−314. |
| [17] | Vanhoute, M., Froidevaux, R., Pierlot, C., Krier, F., Aubry, J. M., Guillochon, D., 2008. Advancement of foam separation of bioactive peptides using an aeration column with a bubbling-draining method. Separation and Purification Technology, 63: 460–465. |
| [18] | El-Sayed, M. I., 2013. Functional Properties of Goat and Buffalo Milk Proteins. pp 206- 235. Lampert Academic Publishing. Germany. |
| [19] | 19. FitzGerald, R. J., Murray, B. A., Walsh, D. J., 2004. Hypotensive peptides from milk proteins. Journal of Nutrition, 134: 980S–988S. |
| [20] | Gobbetti, M., Minervini, F., Rizzello, C. G. 2004. Angiotensin I-converting enzyme-inhibitory and antimicrobial bioactive peptides. International Journal of Dairy Technology, 57: 172–188. |
| [21] | Korhonen, H., Pihlanto, A., 2006. Bioactive peptides: Production and functionality. International Dairy Journal, 16: 945–960. |
| [22] | Meisel, H., FitzGerald, R. J., 2003. Biofunctional peptides from milk proteins: Mineral binding and cytomodulatory effects. Current Pharmaceutical Design, 9: 1289–1295. |
| [23] | Yamamoto, N., Ejiri, M., Mizuno, S., 2003. Biogenic peptides and their potential use. Current Pharmaceutical Design, 9: 1345–1355. |
| [24] | Gobbetti, M., Minervini, F., Rizzello, C. G., 2007. Bioactive Peptides in Dairy Products. In Y. H. Hui (Edt.), Handbook of food products manufacturing, pp. 489–517. Hoboken, New Jersey: John Wiley and Sons, Inc. |
| [25] | Kilara, A., Panyam, D., 2003. Peptides from milk proteins andtheir properties. Critical Reviews in Food Science and Nutrition, 43: 607–633. |
| [26] | Korhonen, H., 2008. Bioactive Components in Bovine Milk. In Park. Y. W (edt). Bioactive Components in Milk and Dairy Products. pp, 15: 42. Wiley-Blackwell. |
| [27] | Korhonen, H. J., 2009b. Bioactive milk proteins and peptides: from science to functional applications. The Australian Journal of Dairy Technology, 64: 16–25. |
| [28] | Morris, P. E., FitzGerald, R. J., 2008. Whey Proteins and Peptides in Human Health. In Whey Processing, Functionality and Health Benefits. Charles I. Onwulata _Peter J. Huth, Edt. Blackwell Publishing and the Institute of Food Technologists. pp 285-344. 2121 State Avenue, Ames, Iowa 50014-8300, USA. |
| [29] | Holder, A., Thienel, K., Klaiber, I., Pfannstiel, J., Weiss, J., Hinrichs J., 2014. Quantification of bio- and techno-functional peptides in tryptic bovine micellar casein and b-casein hydrolysates. Food Chemistry, 158: 118–124. |
| [30] | Kunji, E. R. S., Mierau, I., Hagting, A., Poolman, B., Konings, N., 1996. The proteolytic system of lactic acid bacteria. Antonie Leeuwenhoek 70: 187–221. |
| [31] | Christensen, J. E., Dudley, E. G., Pederson, J. A., Steele, J. L., 1999. Peptidases and amino acid catabolism in lactic acid bacteria. Antonie van Leeuwenhoek; 76: 217–246. |
| [32] | Nakamura, Y., Yamamoto, M., Sakai, K., Okubo, A., Yamazaki, S., Takano, T., 1995. Purification and characterization of angiotensin I converting enzyme inhibitors from sour milk. Journal of Dairy Science, 78, 777–783. |
| [33] | Sipola, M., Finkenberg, P., Korpela, R., Vapaatalo, H., Nurminen, M. L., 2002. Effect of long-term intake of milk products on blood pressure in hypertensive rats. Journal of Dairy Research, 69, 103–111. |
| [34] | Pessi, T., Isolauri, E., Sutas, Y., Kankaanranta, H., Moilanen, E., Hurme, M., 2001. Suppression of T-cell activation by Lactobacillus rhamnosus GG-degraded bovine casein. International Immunopharmacology, 1: 211–218. |
| [35] | Prioult, G., Pecquet, S., Fliss, I., 2004. Stimulation of interleukin-10 production by acidic β-lactoglobulin- derived peptides hydrolyzed with Lactobacillus paracasei NCC2461 peptidases. Clinical and Diagnostic Laboratory Immunology, 11, 266–271. |
| [36] | Donkor, O., Henriksson, A., Vasiljevic, T., Shah, N. P., 2007. Proteolytic activity of dairy lactic acid bacteria and probiotics as determinant of growth and in vitro angiotensin-converting enzyme inhibitory activity in fermented milk. Lait, 86: 21–38. |
| [37] | Silva, S. V., Malcata, F. X., 2005. Milk caseins as a source of bioactive peptides. International Dairy Journal, 15 (1): 1-15. |
| [38] | Iwaniak, A., Minkiewicz, P., 2007. Proteins as the source of physiologically and functionally active peptides. Acta Sci. Pol., Technol. Aliment. 6 (3), 5-15. |
| [39] | Tidona, F., Criscione, A., Guastella, A. M., Zuccaro, A., Bordonaro, S. and Marletta, D. 2009. Bioactive peptides in dairy products. Ital. J. Anim. Sci., 8: 315-340. |
| [40] | El-Sayed, M. I, Awad S, Wahba A, El Attar A, Yousef MI and Zedan M. 2016. In Vivo Anti-diabetic and Biological Activities of Milk Protein and Milk Protein Hydrolyaste. (2016). Advances in Dairy Research. Vol 4: 1-6. |
| [41] | Van Hooijdonk, A. C. M., Kussendrager, K. D., Steijns, J. M., 2000. In vivo antimicrobial and antiviral activity of components in bovine milk and colostrums involved in nonspecific defence. British Journal of Nutrition, 84: 127–134. |
| [42] | López-Expósito, I., Recio, I., 2008. Protective effect of milk peptides: Antibacterial and antitumor properties. In Bӧsze. Z (edt). Bioactive Components of Milk. Springer ScienceBusiness Media, New York, NY 10013, USA. |
| [43] | Jones, F. S., Simms, H. S., 1930. The bacterial growth inhibitor (lactenin) of milk. Journal of Experimental Medicine, 51: 327–339. |
| [44] | Hill, R. D., Lahov, E., Givol, D., 1974. A rennin-sensitive bond in alpha and beta casein. Journal of Dairy Research, 41: 147–153. |
| [45] | Lahov, E., Edelsten, D., Sode-Mogensen, M. T., Sofer, E., 1971. Properties of basic glycopeptides released from cow milk protein by heat. Milchwissenschaft, 26, 489–495. |
| [46] | Floris, R., Recio, I., Berkhout, B., Visser, S., 2003. Antibacterial and antiviral effects of milk proteins and derivatives thereof. Current Pharmaceutical Design, 9, 1257–1275. |
| [47] | Clare, D. A., Catignani, G. L., Swaisgood, H. E., 2003. Biodefense properties of milk: The role of antimicrobial proteins and peptides. Current Pharmaceutical Design, 9: 1239–1255. |
| [48] | Dashper. S. G., Liu. S. W., Reynolds. E. C., 2007. Antimicrobial Peptides and Their potential as oral therapeutic Agents. International Journal of Peptide Research and Therapeutics, 13 (4): 505–516. |
| [49] | Haque, E., Chand, R., 2008. Antihypertensive and antimicrobial bioactive peptides from milk proteins. Eur Food Res Technol 227: 7–15. |
| [50] | Brogden, K. A., 2005. Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?. Nat. Rev. Microbiol, 3: 238–250. |
| [51] | Benkerroum, N., 2010. Antimicrobial peptides generated from milk proteins: a survey and prospects for application in the food industry. International Journal of Dairy Technology, 63: 320-338. |
| [52] | Najafian, L., Babji, A. S., 2012. A review of fish-derived antioxidant and antimicrobial peptides: Their production, assessment, and applications. Peptides, 33: 178–185. |
| [53] | Seo, M., Won, D., Kim, H. S., Mishig-Ochir, J. H., Lee,. B. J., 2012. Antimicrobial Peptides for Therapeutic Applications: A Review. Molecules, 17: 12276-12286. |
| [54] | Teixeira, V., Feio, M. J., Bastos, M., 2012. Role of lipids in the interaction of antimicrobial peptides with membranes. Prog. Lipid Res., 51, 149–177. |
| [55] | El-Zahar, K., Sitohy, M., Choiset, Y., Métro, F., Haertle´, T., Chobert, J. M., 2004. Antimicrobial activity of ovine whey protein and their peptic hydrolysates. Milchwissenschaft; 59: 653–656. |
| [56] | Almaas, H., Holm, H., Langrud, T., Flengsrud, R., Vegarud, G. E., 2006. In vitro studies of the digestion of caprine whey proteins by human gastric and duodenal juice and the effects on selected microorganisms. British Journal of Nutrition; 96: 562–569. |
| [57] | Vogel, H. J., Schibli, D. J., Weiguo, J., Lohmeier-Vogel, E. M., Epand, R. F., Epand, R. M., 2002. Towards a structure-function analysis of bovine lactoferricin and related tryptophan and arginine containing peptides. Biochem. Cell Biol., 80, 49-63. |
| [58] | Farnaud, S., Evans, R. W., 2003. Lactoferrin- a multifunctional protein with antimicrobial properties. Mol Immunol, 40: 395-405. |
| [59] | Ulvatne, H., Samuelsen, O., Haukland, H. H., Kramer. M., Vorland, L. H., 2004. Lactoferricin B inhibits bacterial macromolecular synthesis in Escherichia coli and Bacillus subtilis. FEMS Microbiol. Lett. 237: 377-384. |
| [60] | Van der Kraan, M. I. A., Groenink, J., Nazmi, K., Veerman, E. C. I., Bolscher, J. G. M., Nieuw Amerongen, A. V. 2004. Lactoferrampin: A novel antimicrobial peptide in the N1-domain of bovine lactoferrin. Peptides, 25, 177–183. |
| [61] | Pellegrini, A., Thomas, U, Bramaz, N., Hunziker, P., Von Fellenberg, R., 1999. Isolation and identification of three bactericidal domains in the bovine α–lactalbumin molecule. Biochim. Biophys. Acta; 1426: 439–448. |
| [62] | Pellegrini, A., Dettling, C., Thomas, U., Hunziker, P., 2001. Isolation and characterization of four bactericidal domains in the bovine β-lactoglobulin. Biochim. Biophys. Acta, 1526: 131–140. |
| [63] | Théolier, J., Hammami, R., Labelle, P., Fliss, I., Jean, J., 2013. Isolation and identification of antimicrobial peptides derived by peptic cleavage of whey protein isolate. Journal of Functional Foods, 5: 706–714. |
| [64] | Lahov, E. and Regelson., W., 1996. Antibacterial and immunostimulating casein-derived substances from milk: casecidin, isracidin peptides. Food Chem. Toxicol, 34: 131–145. |
| [65] | Kayser, H., Meisel, H., 1996. Stimulation of human peripheral blood lymphocytes by bioactive peptides derived from bovine milk proteins. FEBS Letters 383: 18-20. |
| [66] | Kolb, A. F., 2001. The prospects of modifying the antimicrobial properties of milk. Biotechnology advances, 19: 299–316. |
| [67] | Hayes, M., Ross, R. P., Fitzgerald, G. F., Hill, C., Stanton C., 2005. Casein-derived antimicrobial peptides generated by lactobacillus acidophilus DPC6026. Appl. Environ. Microbiol. 72: 2260-2264. |
| [68] | Recio, I., Visser, S., 1999. Identification of two distinct antibacterial domains within the sequence of bovine αs2-casein. Biochim. Biophys. Acta 1428: 314-326. |
| [69] | McCann, K. B., Shiell, B. J., Michalski, W. P., Lee, A., Wan, J., Roginski, H., 2005. Isolation and characterisation of antibacterial peptides derived from the f (164–207) region of bovine αS2-casein. International Dairy Journal, 15: 133–143. |
| [70] | López-Expósito, I., Gómez-Ruiz, J. A., Amigo, L., Recio, I., 2006. Identification of antibacterial peptides from ovine as2-casein. Int. Dairy J. 16: 1072- 1080. |
| [71] | López-Expósito, I., 2007. Novel peptides with antibacterial activity derived from food proteins. Study of the mode of action and synergistic effect. Dissertation Tesis. Faculty of Science. Universidad Auto´ noma de Madrid. |
| [72] | Alvarez-Ordóñez, A., Begley, M., Clifford, T., Deasy, T., Considine, K., Hill. C. 2013. Structure-Activity Relationship of Variants of the Milk-Derived Antimicrobial Peptide αs2-Casein f (183–207). Appl. Environ. Microbiol; 79 (17): 5179-5185. |
| [73] | Liepke, C., Zucht, H. D., Forsmann, W. G. and Standker, L., 2001. Purification of novel peptide antibiotics from human milk. J. Chromatogr., 752: 369-377. |
| [74] | Malkoski, M., Dashper, S. G. O’Brien-Simpson, N. M., Talbo, G. H., Macris, M., Cross, K. J., Reynolds, E. C., 2001. Kappacin, a novel antibacterial peptide from bovine milk. Antimicrob. Agents. Chem., 45: 2309–2315. |
| [75] | López-Expósito, I., Recio, I., 2006. Antibacterial activity of peptides and folding variants from milk proteins. International Dairy Journal, 16: 1294–1305. |
| [76] | Thoma- Worringer, C., Sorensen, J., Lopez-Fandino, R., 2006. Health effects and technological features of caseinomacropeptide, Int Dairy J, 16: 1324-1333 |
| [77] | Seppo, L., Jauhiainen, T., Poussa, T. and Korpela, R. 2003. A fermented milk high in bioactive peptides has a blood pressure-lowering effect in hypertensive subjects. Am J Clin Nutr., 77: 326. |
| [78] | Yamamoto N, Takano T., 1999. Antihypertensive peptides derived from milk proteins. Nahrung43: 159–64. |
| [79] | Saito, T. 2008. Antihypertensive Peptides Derived from Bovine Casein and Whey Proteins. Z. Bösze (ed.), Bioactive Components of Milk. Springer. New York. |
| [80] | Abubakar, A., Saito, T., Kitazawa, H., Kawai, Y., Itoh, T. 1998. Structural analysis of new antihypertensive peptides derived from cheese whey protein by proteinase K digestion. Journal of Dairy Science, 81: 3131–3138. |
| [81] | Halliwell, B., 2001. Role of free radicals in the neurodegenerativediseases: Therapeutic implications for antioxidant treatment. DrugsAging, 18, 479–484. |
| [82] | Liu, Q., Raina, A., Smith, M., Sayre, L., Perry, G., 2003. Hydroxynonenal, toxic carbonyls, and Alzheimer disease. Molecular Aspects of Medicine, 24: 305–313. |
| [83] | Pihlanto, A., 2006. Antioxidative peptides derived from milk proteins. International Dairy Journal, 16: 1306–1314. |
| [84] | Sarmadi, B. H., Ismail, A., 2010. Antioxidative peptides from food proteins: A review. Peptides, 31: 1949–1956. |
| [85] | 85. Kamau, S. M., Lu, R. R., Chen, W., Liu, X. M., Tian, F. W., Shen, Y., Gao. T., 2010. Functional significance of bioactive peptides derived from milk proteins. Food Reviews International, 26: 386–401. |
| [86] | Awad S., El-Sayed MI., Wahba A., El Attar A., Yousef MI and Zedan M. 2016. Antioxidant activity of milk protein hydrolyaste in alloxan-induced diabetic rats. (2016). Journal of Dairy Science, 99: 8499–8510. |
| [87] | Wong, P. Y. Y. and Kitts, D. D., 2003. Chemistry of buttermilk solid antioxidant activity. Journal of Dairy Science, 86, 1541–1547. |
| [88] | Diaz, M., Dunn, C. M., McClements, D. J., Decker, E. A., 2003. Use of caseinophosphopeptides as natural antioxidants in oil-inwater emulsions. Journal of Agricultural and Food Chemistry, 51: 2365–2370. |
| [89] | Suetsuna, K., Ukeda, H., Ochi, H., 2000. Isolation and characterization of free radical scavenging activities peptides derived from casein. Journal of Nutritional Biochemistry, 11: 128–131. |
| [90] | Rival, S. G., Boeriu, C. G., Wichers, H. J., 2001a. Caseins and casein hydrolysates. 2. Antioxidative properties and relevance to lipoxygenase inhibition. Journal of Agricultural and Food Chemistry, 49: 295–302. |
| [91] | Rival, S. G., Fornaroli, S., Boeriu, C. G., Wichers, H. J., 2001b. Caseins and casein hydrolysates. 1. Lipoxygenase inhibitory properties. Journal of Agricultural and Food Chemistry, 49, 287–294. |
| [92] | Diaz, M., Decker, E. A., 2004. Antioxidant mechanisms of caseinophosphopeptides and casein hydrolysates and their application in ground beef. Journal of Agricultural and Food Chemistry, 52: 8208–8213. |
| [93] | Pritchard, S. R., Phillips, M., Kailasapathy, K., 2010. Identification of bioactive peptides in commercial Cheddar cheese. Food Research International, 43: 1545–1548. |
| [94] | Gómez-Ruiz, J. A., López-Expósito, I., Pihlanto, A., Ramos, M., Recio, I., 2008. Antioxidant activity of ovine casein hydrolysates: identification of active peptides by HPLC–MS/MS. Eur. Food. Res. Technol, 227: 1061–1067. |
| [95] | Laparra, J. M., Alegrı´a, A., Barbera´, R., Farre´, R., 2008. Antioxidant effect of casein phosphopeptides compared with fruit beverages supplemented with skimmed milk against H2O2-induced oxidative stress in Caco-2 cells. Food Research International, 41: 773–779. |
| [96] | Mao, X., Cheng, X., Wang, X., Wu, S., 2011. Free-radical-scavenging and anti-inflammatory effect of yak milk casein before and after enzymatic hydrolysis. Food Chemistry, 126: 484–490. |
| [97] | Chang, O. K., Seol, K. H., Jeong, S. G., Oh, M. H., Park, B. Y., Perrin, C., Ham, J. S., 2013. Casein hydrolysis by Bifidobacterium longum KACC91563 and antioxidant activities of peptides derived therefrom. J. Dairy Sci; 96: 1–12. |
| [98] | Gad, A., Khadrawy, Y., El-Nekeety, A. A., Mohamed, S. R., Hassan, N. S., Abdel-Wahhab, M. A., 2011. Antioxidant activity and hepatoprotective effects of whey protein and spirulina in rats. Nutrition; 27 (5): 582–589. |
| [99] | Phelan, M., Aherne-Bruce, S. A., O’Sullivan, D., FitzGerald, R. J., O’Brien, N. M., 2009b. Potential bioactive effects of casein hydrolysates on human cultured cells. International Dairy Journal; 19, 279–285. |
| [100] | Nongonierma, A. B., FitzGerald. R. J., 2013. Dipeptidyl peptidase IV inhibitory and antioxidative properties of milk protein-derived dipeptides and hydrolysates. Peptides; 39: 157–163. |
| [101] | Peng, X., Xiong, Y. and Kong, B., 2009. Antioxidant activity of peptide fractions from whey protein hydrolysates as measured by electron spin resonance. Food Chem., 113 (1): 196 –201. |
| [102] | Hernández-Ledesma, B., Dávalos, A., Bartolomé, B., Amigo, L., 2005. Preparation of antioxidant enzymatic hydrolysates from α-lactalbumin and β-lactoglobulin. Identification of active peptides by HPLC-MS/ MS. Journal of Agricultural and Food Chemistry, 53: 588–593. |
| [103] | Timón, M. L., Parra, V., Otte, J., Broncano, J. M., Petrón, M. J. 2014. Identification of radical scavenging peptides (< 3 kDa) from Burgos-type cheese. LWT - Food Science and Technology, 57: 359-365. |
| [104] | WHO, 2006. Definition and diagnosis of diabetes mellitus and intermediate hyperglycemia: report of a WHO/IDF consultation. |
| [105] | 105. Schrezenmeir, J. and Jagla, A. 2000. Milk and diabetes. Journal of the American College of Nutrition, Vol. 19, No. 2: 176S–190S. |
| [106] | WHO., 2011. Global status report on noncommunicable diseases 2010. World Health Organization, WHO Press. |
| [107] | IDF. (2017). IDF diabetes atlas, 8th ed. Brussels: International Diabetes Federation. |
| [108] | 108. Bailey, C. J., Flatt, P. R., 1995. Development of antidiabetic drugs. In: Ioannides, C., Flatt, P. R. (Eds.), Drugs, Diet and Disease: Mechanistic Approaches toDiabetes. Ellis Horwood, London, pp. 279–326. |
| [109] | Tamrakara, A. K., Jaiswala, N., Yadavb, P. P., Mauryab, R. and Srivastavaa, A. K. 2011. Pongamol from Pongamiapinnata stimulates glucose uptake by increasing surface GLUT4 level in skeletal muscle. Molecular and Cellular Endocrinology, 339: 98–104. |
| [110] | Baynes, J. W., 1991. Role of oxidative stress in development of complications in diabetes. Diabetes, 40: 405. |
| [111] | Nilsson, M., Holst, JJ., Bjorck IM., 2007. Metabolic effects of amino acid mixtures and whey protein in healthy subjects: studies using glucose-equivalent drinks. Am. J. Clin. Nutr., 85: 996–1004. |
| [112] | Power, O., Hallihan, A., Jakeman, P., 2009. Human insulinotropic response to oral ingestion of native and hydrolysed whey protein. Amino Acids, 37, 333e339. |
| [113] | Tulipano, G., Sibilia, V., Caroli, A. M., Cocchi, D., 2011. Whey proteins as source of dipeptidyl dipeptidase IV (dipeptidyl peptidase- 4) inhibitors. Peptides, 32 (4), 835–838. |
| [114] | Jakubowicz, D., Froy, O., 2013. Biochemical and metabolic mechanisms by which dietary whey protein may combat obesity and Type 2 diabetes. Journal of Nutritional Biochemistry, 24: 1–5. |
| [115] | Han, D. N., Dong-Hui Zhang, D. H., Wang, L. P., Zhang. Y. S., 2013. Protective effect of _-casomorphin-7 on cardiomyopathy of streptozotocin-induced diabetic rats via inhibition of hyperglycemia and oxidative stress. Peptides, 44: 120–126. |
| [116] | Drucker, DJ., 2006. Enhancing the action of incretin hormones: a new whey forward. Endocrinology, 147: 3171–2. |
| [117] | Yan, J., Zhao, J., Yang, R & Zhao, W., 2019. Bioactive peptides with antidiabetic properties: a review. International Journal of Food Science and Technology, 1: 11. doi: 10.1111/ijfs.14090 |
| [118] | Bjelke, J. R., Christensen, J., Nielsen, P. F., Branner, S., Kanstrup, A. B., Wagtmann, N., 2006. Dipeptidyl peptidases 8 and 9: Specificity and molecular characterization compared with dipeptidyl peptidase IV. Biochemistry Journal; 396: 391–399. |
| [119] | Nauck, M. A., Vilsboll, T., Gallwitz, B., Garber, A. and Madsbad, S., 2009. Incretin-based therapies: viewpoints on the way to consensus. Diabetes Care; 32 Suppl. 2: S223-231. |
| [120] | Portha, B., Tourrel-Cuzin, C., Movassat, J., 2011. Activation of the GLP-1 receptor signaling pathway: a relevant strategy to repair a deficient beta-cell mass. Exp. Diabetes Res., 376509. |
| [121] | Uchida, M., Ohshiba, Y., Mogami, O., 2011. Novel dipeptidyl peptidase- 4-inhibiting peptide derived from β-lactoglobulin. Journal Pharmacological Science, 117: 37–63. |
| [122] | Uenishi, H., Kabuki, T., Seto, Y., Serizawa, A., Nakajima, H., 2012. Isolation and identification of casein-derived dipeptidyl-peptidase 4 (DPP-4)-inhibitory peptide LPQNIPPL from gouda-type cheese and its effect on plasma glucose in rats. International Dairy Journal, 22: 24–30. |
| [123] | Lacroix, I. M. E. and Li-Chan, E. C. Y., 2012. Dipeptidyl peptidase-IV inhibitory activity of dairy protein hydrolysates. International Dairy Journal, 25 (2): 97–102. |
| [124] | Nongonierma, A. B., Mooney, C., Shields, D. C., FitzGerald. R. J., 2013. Inhibition of dipeptidyl peptidase IV and xanthine oxidase by amino acids and dipeptides. Food Chemistry, 141: 644–653. |
| [125] | Silveira, S. T., Martínez-Maqueda, D., Recio, I., Hernandez-Ledesma, B., 2013. Dipeptidyl peptidase-IV inhibitory peptides generated by tryptic hydrolysis of a whey protein concentrate rich in b-lactoglobulin. Food Chemistry, 141: 1072–1077. |
APA Style
Mahmoud El-Sayed, Sameh Awad. (2019). Milk Bioactive Peptides: Antioxidant, Antimicrobial and Anti-Diabetic Activities. Advances in Biochemistry, 7(1), 22-33. https://doi.org/10.11648/j.ab.20190701.15
ACS Style
Mahmoud El-Sayed; Sameh Awad. Milk Bioactive Peptides: Antioxidant, Antimicrobial and Anti-Diabetic Activities. Adv. Biochem. 2019, 7(1), 22-33. doi: 10.11648/j.ab.20190701.15
AMA Style
Mahmoud El-Sayed, Sameh Awad. Milk Bioactive Peptides: Antioxidant, Antimicrobial and Anti-Diabetic Activities. Adv Biochem. 2019;7(1):22-33. doi: 10.11648/j.ab.20190701.15
Share This Article
Twitter
Linked In
Facebook
Copy
Download@article{10.11648/j.ab.20190701.15,
author = {Mahmoud El-Sayed and Sameh Awad},
title = {Milk Bioactive Peptides: Antioxidant, Antimicrobial and Anti-Diabetic Activities},
journal = {Advances in Biochemistry},
volume = {7},
number = {1},
pages = {22-33},
doi = {10.11648/j.ab.20190701.15},
url = {https://doi.org/10.11648/j.ab.20190701.15},
eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.ab.20190701.15},
abstract = {The main milk proteins are caseins and whey proteins, some other minor proteins and peptides, are also found in milk. Proteins are vital ingredients for human because they provide all the essential amino acids needed for body and human health. Milk proteins are very important sources of bioactive peptides. The bioactive peptides are inactive within the sequence of the parent protein and can be released by proteolytic enzymes, during gastrointestinal digestion or during milk processing, for example the adding coagulation enzymes and starter culture. Once bioactive peptides are present in the body, these peptides may act as regulatory compounds with hormone-like activity. Furthermore, Bioactive peptides from milk proteins have many biological activities such as antimicrobial, antihypertensive, antithrombotic, antioxidant, mineral binding, and anti-diabetic. Bioactive peptides have potential health and have pharmaceutical applications. Antimicrobial peptides are recognized as an important component of innate immunity, particularly at mucosal surfaces such as the lungs and small intestine that are constantly exposed to a range of potential pathogens. The ability of protein hydrolysates to inhibit deleterious changes caused by lipid oxidation appears to be related to the nature and composition of the different peptide fractions. Milk protein hydrolysate possesses free-radical-scavenging and anti-inflammatory activities have many beneficial effects on the increase of the glucose-induced insulin secretion and reduction in postprandial glycemia. This article is tried through exposure in some detail to review characteristics of some milk protein peptides and its positive effects on human health.},
year = {2019}
}
TY - JOUR T1 - Milk Bioactive Peptides: Antioxidant, Antimicrobial and Anti-Diabetic Activities AU - Mahmoud El-Sayed AU - Sameh Awad Y1 - 2019/06/17 PY - 2019 N1 - https://doi.org/10.11648/j.ab.20190701.15 DO - 10.11648/j.ab.20190701.15 T2 - Advances in Biochemistry JF - Advances in Biochemistry JO - Advances in Biochemistry SP - 22 EP - 33 PB - Science Publishing Group SN - 2329-0862 UR - https://doi.org/10.11648/j.ab.20190701.15 AB - The main milk proteins are caseins and whey proteins, some other minor proteins and peptides, are also found in milk. Proteins are vital ingredients for human because they provide all the essential amino acids needed for body and human health. Milk proteins are very important sources of bioactive peptides. The bioactive peptides are inactive within the sequence of the parent protein and can be released by proteolytic enzymes, during gastrointestinal digestion or during milk processing, for example the adding coagulation enzymes and starter culture. Once bioactive peptides are present in the body, these peptides may act as regulatory compounds with hormone-like activity. Furthermore, Bioactive peptides from milk proteins have many biological activities such as antimicrobial, antihypertensive, antithrombotic, antioxidant, mineral binding, and anti-diabetic. Bioactive peptides have potential health and have pharmaceutical applications. Antimicrobial peptides are recognized as an important component of innate immunity, particularly at mucosal surfaces such as the lungs and small intestine that are constantly exposed to a range of potential pathogens. The ability of protein hydrolysates to inhibit deleterious changes caused by lipid oxidation appears to be related to the nature and composition of the different peptide fractions. Milk protein hydrolysate possesses free-radical-scavenging and anti-inflammatory activities have many beneficial effects on the increase of the glucose-induced insulin secretion and reduction in postprandial glycemia. This article is tried through exposure in some detail to review characteristics of some milk protein peptides and its positive effects on human health. VL - 7 IS - 1 ER -
Information
Email: