Relevance of Peptides Bioactivity in Foods

Chapter
Part of the Food Microbiology and Food Safety book series (FMFS, volume 2)

Abstract

Food protein-derived bioactive peptides are a group of functional food components. Enzymatic hydrolysis of food proteins generates various peptides with physiological functions, such as antihypertensive, opioid, immunostimulating, antimicrobial, antithrombotic, hypocholesterolemic, and antioxidative activities. This chapter includes an overview of bioactive peptides generated from food proteins. Also, utilization of modern nutrigenomics techniques for such peptides is discussed. Nutrigenomics has been rapidly applied to the field of nutrition and health. Although application of this strategy for studying food protein-derived bioactive peptides is still limited, it offers a great possibility for understanding and utilizing bioactive peptides.

Keywords

Cholesterol Fatigue Fermentation Proline Angiotensin 

References

  1. Affolter M, Raymond F, Kussmann M (2009) Omics in nutrition and health research. In: Mine Y, Miyashita K, Shahidi F (eds) Nutrigenomics and proteomics in health and disease. Wiley-Blackwell, Ames, pp 11–29CrossRefGoogle Scholar
  2. Aguilar MI (2004) Reversed-phase high-performance liquid chromatography. In: Aguilar MI (ed) HPLC of peptides and proteins. Humana Press, Totowa, pp 9–22Google Scholar
  3. Aito-Inoue M, Lackeyram D, Fan MZ, Sato K, Mine Y (2007) Transport of tripeptide, Gly-Pro-Hyp, across the intestinal brush border membrane of porcine. J Peptide Sci 13:468–474CrossRefGoogle Scholar
  4. Akimoto M, Namioka S, Arihara K, Tomita K, Ishikawa S, Itoh M (2007) Novel stress-biomarker and its application. Japan Patent (No. 2007–93597)Google Scholar
  5. Aleixandre A, Miguel M (2012) Food proteins and peptide as bioactive agents. In: Hettiarachchy NS, Sato K, Marshall MR, Kannan A (eds) Bioactive food proteins and peptides, applications in human health. CRC Press, Boca Raton, pp 131–180Google Scholar
  6. Arihara K (2006) Functional properties of bioactive peptides derived from meat proteins. In: Nollet LML, Toldrá F (eds) Advanced technologies for meat processing. CRC Press, Boca Raton, pp 247–273Google Scholar
  7. Arihara K (2012) Meat-based bioactive compounds and functional meat products. Food Sci Technol 26:26–28Google Scholar
  8. Arihara K, Ohata M (2011) Functional meat products. In: Saarela M (ed) Functional foods: concept to products, 2nd edn. Woodhead, Cambridge, pp 512–533CrossRefGoogle Scholar
  9. 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 67:434–437Google Scholar
  10. Arihara K, Ishikawa S, Itoh M (2011a)Bifidobacteriumgrowth promoting peptides derived from meat proteins. Japan Patent (No. 4726129)Google Scholar
  11. Arihara K, Tomita K, Ishikawa S, Itoh M, Akimoto M, Sameshima T (2011b) Anti-fatigue peptides derived from meat proteins. Japan Patent (No. 4828890)Google Scholar
  12. Astley S, Penn L (2009) Design of human nutrigenomics studies. Wageningen Academic, WageningenGoogle Scholar
  13. Bagchi D, Lau FC, Bagchi M (2010) Genomics, proteomics and metabolomics in nutraceuticals and functional foods. Wiley-Blackwell, AmesCrossRefGoogle Scholar
  14. Bidlack WR, Rodriguez RL (2012) Nutritional genomics, the impact of dietary regulation of gene function on human disease. CRC Press, Boca RatonGoogle Scholar
  15. Boonen K (2009) Peptidomics of the mouse, unraveling the role of bioactive peptides in intercellular signaling. Lambert Academic, SaarbrückenGoogle Scholar
  16. Brody EP (2000) Biological activities of bovine glycomacropeptide. Br J Nutr 84:S39–S46CrossRefGoogle Scholar
  17. Bütikofer U, Meyer J, Sieber R, Walther B, Wechsler D (2008) Occurrence of the angiotensin-converting enzyme-inhibiting tripeptides Val-Pro-Pro and Ile-Pro-Pro in different cheese varieties of Swiss origin. J Dairy Sci 91:29–38CrossRefGoogle Scholar
  18. Chen H-M, Muramoto K, Yamauchi F (1995) Antioxidative activity of designed peptides based on the antioxidative peptide isolated from digests of a soybean protein. J Agric Food Chem 44:2619–2623CrossRefGoogle Scholar
  19. Chiba H, Yoshikawa M (1986) Biologically functional peptides from food proteins: new opioid peptides from milk proteins. In: Feeney RE, Whitaker JR (eds) Protein tailoring for food and medical users. Marcel Dekker, New York, pp 123–153Google Scholar
  20. Cushman DW, Cheung HS (1971) Spectrophotometric assay and properties of the angiotensin converting enzyme of rabbit lung. Biochem Pharmacol 20:1637–1648CrossRefGoogle Scholar
  21. Dainty R, Blom H (1995) Flavor chemistry of fermented sausages. In: Campbell-Platt G, Cook PE (eds) Fermented meats. Blackie Academic & Professional, Glasgow, pp 176–193Google Scholar
  22. Fiat A-M, Migliore-Samour D, Jolles P, Drout L, Collier C, Caen J (1993) Biologically active peptides from milk proteins with emphasis on two examples concerning antithrombotic and immunomodulating activities. J Dairy Sci 76:301–310CrossRefGoogle Scholar
  23. Fuchs D, Winkelmann I, Johnson IT, Mariman E, Wenzel U, Daniel H (2005) Proteomics in nutrition research: principles, technologies and applications. Br J Nutr 94:302–314CrossRefGoogle Scholar
  24. Fujita H, Yokoyama K, Yoshikawa M (2000) Classification and antihypertensive activity of ­angiotensin I-converting enzyme inhibitory peptides derived from food proteins. J Food Sci 65:564–569CrossRefGoogle Scholar
  25. Gagnaire V, Molle D, Herrouin M, Leonil J (2001) Peptides identified during emmental cheese ripening: origin and proteolytic systems involved. J Agric Food Chem 49:4402–4413CrossRefGoogle Scholar
  26. Ghassem M, Arihara K, Babji AS, Said M, Ibrahim S (2011) Purification and identification of ACE inhibitory peptides from Haruan (Channa striatus) myofibrillar protein hydrolysate using HPLC-ESI-TOF MS/MS. Food Chem 129:1770–1777CrossRefGoogle Scholar
  27. Gobbetti M, Ferranti P, Smacchi E, Goffredi F, Addeo F (2000) Production of angiotensin-I converting-enzyme-inhibitory peptides in fermented milks started byLactobacillus delbrueckiisubsp.bulgaricusSS1 andLactococcus lactissubsp.cremorisFT4. Appl Environ Microbiol 66:3898–3904CrossRefGoogle Scholar
  28. Gobbetti M, Minervini F, Rizzello CG (2007) Bioactive peptides in dairy products. In: Hui YH (ed) Handbook of food products manufacturing: health, meat, milk, poultry, seafood, and vegetables. Wiley, Hoboken, pp 489–517Google Scholar
  29. Gomez-Ruiz JA, Ramos M, Recio I (2002) Angiotensin-converting enzyme-inhibitory peptides in Manchego cheeses manufactured with different starter cultures. Int Dairy J 12:697–706CrossRefGoogle Scholar
  30. Hammes WP, Haller D, Gänzle MG (2003) Fermented meat. In: Farnworth ER (ed) Handbook of fermented functional foods. CRC Press, Boca Raton, pp 251–275Google Scholar
  31. Hernändez-Ledesma B, Amigo L, Ramos M, Recio I (2004) Angiotensin converting enzyme inhibitory activity in commercial fermented products. J Agric Food Chem 52:1504–1510CrossRefGoogle Scholar
  32. Hertog MGL (1996) Epidemiological evidence on potential health properties of flavonoids. Proc Nutr Soc 55:385–387CrossRefGoogle Scholar
  33. Hettiarachchy NS, Sato K, Marshall MR, Kannan A (2012) Bioactive food proteins and peptides, application in human health. CRC Press, Boca RatonGoogle Scholar
  34. Hipkiss AR, Brownson CA (2000) A possible new role for the anti-aging peptide carnosine. Cell Mol Life Sci 57:747–753CrossRefGoogle Scholar
  35. Huttunen MM, Pekkinen M, Ahlstrom MEB, Lamberg-Allardt CJE (2007) Effects of bioactive peptides isoleucine-proline-proline (IPP), valine-proline-proline (VPP) and leucine-lysine-proline (LKP) on gene expression of osteoblasts differentiated from human mesenchymal stem cell. Br J Nutr 98:780–788CrossRefGoogle Scholar
  36. Ibrahim HR, Sugimoto Y, Aoki T (2000) Ovotransferrin antimicrobial peptide (OTAP-92) kills bacteria through a membrane damage mechanism. Biochim Biophys Acta 1523:196–205CrossRefGoogle Scholar
  37. Kannan A, Hettiarachchy N, Marshall M (2012) Food proteins and peptide as bioactive agents. In: Hettiarachchy NS, Sato K, Marshall MR, Kannan A (eds) Bioactive food proteins and peptides, applications in human health. CRC Press, Boca Raton, pp 1–28Google Scholar
  38. Kaput J (2007) Developing the promise of nutrigenomics through complete science and international collaborations. Forum Nutr 60:209–223CrossRefGoogle Scholar
  39. Kim S-K, Wijesekara I, Park EY, Matsumura Y, Nakamura Y, Sato K (2012) Proteins and peptide as antioxidants. In: Hettiarachchy NS, Sato K, Marshall MR, Kannan A (eds) Bioactive food proteins and peptides, applications in human health. CRC Press, Boca Raton, pp 97–115Google Scholar
  40. Koohmaraie M (1994) Muscle proteinases and meat aging. Meat Sci 36:93–104CrossRefGoogle Scholar
  41. Korhonen H, Pihlanto A (2007) Bioactive peptides from food proteins. In: Hui YH (ed) Handbook of food products manufacturing: health, meat, milk, poultry, seafood, and vegetables. Wiley, Hoboken, pp 5–38Google Scholar
  42. Li GH, Le GW, Shi YH, Shrestha S (2004) Angiotensin I-converting enzyme inhibitory peptides derived from food proteins and their physiological and pharmacological effects. Nutr Res 24:469–486Google Scholar
  43. Lottspeich F (1979) Novel opioid peptides derived from casein (b-Casomorphins) I. Isolation from bovine casein peptone. Hoppe-Seyler’s Z Physiol Chem 360:1211–1216CrossRefGoogle Scholar
  44. Mano H, Shimizu J, Wada M (2009) Microarrays: a powerful tool for studying the functions of food and its nutrients. In: Mine Y, Miyashita K, Shahidi F (eds) Nutrigenomics and proteomics in health and disease. Wiley-Blackwell, Ames, pp 341–349Google Scholar
  45. Masotti A, Sacco LD, Bottazzo GF, Alisi A (2010) Microarray technology: a promising tool in nutrigenomics. Crit Rev Food Sci Nutr 50:693–698CrossRefGoogle Scholar
  46. Meisel H, Walsh DJ, Murry B, FitzGerald RJ (2005) ACE inhibitory peptides. In: Mine Y, Shahidi F (eds) Nutraceutical proteins and peptides in health and disease. CRC Press, Boca Raton, pp 269–315Google Scholar
  47. Mellander O (1950) The physiological importance of the casein phosphopeptide calcium salts II: Peroral calcium dosage in infants. Acta Soc Med Uppsala 55:247–255Google Scholar
  48. Mine Y (2009) Peptidomics. In: Mine Y, Miyashita K, Shahidi F (eds) Nutrigenomics and proteomics in health and disease. Wiley-Blackwell, Ames, pp 375–386CrossRefGoogle Scholar
  49. Mine Y, Miyashita K, Shahidi F (2009) Nutrigenomics and proteomics in health and disease. Wiley-Blackwell, AmesCrossRefGoogle Scholar
  50. Nagaoka S (2012) Peptide-lipid interactions and functionalities. In: Hettiarachchy NS, Sato K, Marshall MR, Kannan A (eds) Food proteins and peptides: chemistry, functionality, interactions and commercialization. CRC Press, Boca Raton, pp 263–276CrossRefGoogle Scholar
  51. Nagaoka S, Futamura Y, Miwa K, Awano T, Yamauchi K, Kanamaru Y, Kojima T, Kuwata T (2001) Identification of novel hypocholesterolemic peptides derived from bovine b-lactoglobulin. Biochem Biophys Res Commun 281:11–17CrossRefGoogle Scholar
  52. Nakamura Y, Yamamoto N, Sakai K, Takano T (1995) Antihypertensive effect of sour milk and peptides isolated from it that are inhibitors to angiotensin I-converting enzyme. J Dairy Sci 78:1253–1257CrossRefGoogle Scholar
  53. Nakashima Y, Arihara K, Sasaki A, Ishikawa S, Itoh M (2002) Antihypertensive activities of peptides derived from porcine skeletal muscle myosin in spontaneously hypertensive rats. J Food Sci 67:434–437CrossRefGoogle Scholar
  54. Nishimura T, Rhue MR, Okitani A, Kato H (1988) Components contributing to the improvement of meat taste during storage. Agric Biol Chem 52:2323–2330CrossRefGoogle Scholar
  55. Nurminen M-L, Sipola M, Kaarto H, Pihlanto-Leppälä A, Piiola K, Korpela R, Tossavainen O, Korhonen H, Vapaatalo H (2000) a-Lactophin lowers blood pressure via radiotelemetry in normotensive and spontaneously hypertensive rats. Life Sci 66:1535–1543CrossRefGoogle Scholar
  56. Oshima G, Shimabukuro H, Nagasawa K (1979) Peptide inhibitors of angiotensin I-converting enzyme in digests of gelatin by bacterial collagenase. Biochim Biophys Acta 566:128–137CrossRefGoogle Scholar
  57. Otani H, Hata I (1995) Inhibition of proliferative responses of mouse spleen lymphocytes and rabbit Peyer’s patch cells by bovine milk caseins and their digests. J Dairy Res 62:339–348CrossRefGoogle Scholar
  58. Owusu-Aspenten R (2010) Bioactive peptides, application for improving nutrition and health. CRC Press, Boca RatonGoogle Scholar
  59. Pihlanto A, Korhonen H (2003) Bioactive peptides and proteins. Adv Food Nutr Res 47:175–276CrossRefGoogle Scholar
  60. Pouliot Y, Gauthier SF, Groleau PE (2006) Membrane-based fractionation and purification strategies for bioactive peptides. In: Mine Y, Shahidi F (eds) Nutraceutical proteins and peptides in health and disease. CRC Press, Boca Raton, pp 639–658Google Scholar
  61. Saarela M (2011) Functional foods, concept to product, 2nd edn. Woodhead, CambridgeCrossRefGoogle Scholar
  62. Saiga A, Tanabe S, Nishimura T (2003) Antioxidant activity of peptides obtained from porcine myofibrillar proteins by protease treatment. J Agric Food Chem 51:3661–3667CrossRefGoogle Scholar
  63. Saito T, Nakamura T, Kitazawa H, Kawai Y, Itoh T (2000) Isolation and structural analysis of antihypertensive peptides that exist naturally in Gouda cheese. J Dairy Sci 83:1434–1440CrossRefGoogle Scholar
  64. Sato K, Hashimoto K (2012) Large-scale fractionation of biopeptides. In: Hettiarachchy NS, Sato K, Marshall MR, Kannan A (eds) Food proteins and peptides: chemistry, functionality, interactions and commercialization. CRC Press, Boca Raton, pp 395–408CrossRefGoogle Scholar
  65. Shen TL, Noon KR (2004) Liquid chromatography-mass spectrometry and tandem mass spectrometry of peptides and proteins. In: Aguilar MI (ed) HPLC of peptides and proteins. Humana Press, Totowa, pp 111–139Google Scholar
  66. Thomson-Smith LD (2010) Nutrigenomics, nutrition and DNA could go hand in hand. Fastbook, Beau Bassin/ MauritiusGoogle Scholar
  67. Toldrá F (2004) Dry. In: Jensen WK, Devine C, Dikeman M (eds) Encyclopedia of meat sciences. Elsevier, Oxford, pp 360–365CrossRefGoogle Scholar
  68. Tomita M, Takase M, Bellamy WR, Shimamura S (1994) A review, the active peptide of lactoferrin. Acta Paediatr Japan 36:585–591CrossRefGoogle Scholar
  69. Vegarud GE, Langsrud T, Svening C (2000) Mineral-binding milk proteins and peptides; occurrence, biochemical and technological characteristics. Br J Nutr 84:91–98CrossRefGoogle Scholar
  70. Webster NR (1998) Opioid and immune system. Br J Anesth 81:835–836CrossRefGoogle Scholar
  71. Whitfield P, Kirwan J (2010) Metabolomics: an emerging postgenomic tool for nutrition. In: Bagchi D, Lau FC, Bagchi M (eds) Genomics, proteomics and metabolomics in nutraceuticals and functional foods. Wiley-Blackwell, Ames, pp 271–285CrossRefGoogle Scholar
  72. Yamaji T, Kume H (2008) Hepatoprotective effects of whey protein and whey peptides on hepatitis. Milk Sci 56:115–118Google Scholar
  73. Yasumatsu H, Tanabe S (2010) The casein peptide Asn-Pro-Trp-Asp-Gln enforces the intestinal tight junction partly by increasing occludin expression in Caco-2 cells. Br J Nutr 104:951–956CrossRefGoogle Scholar
  74. Young D, Mine Y (2009) Functional bioactive proteins and peptides in nutrigenomics. In: Mine Y, Miyashita K, Shahidi F (eds) Nutrigenomics and proteomics in health and disease. Wiley-Blackwell, Ames, pp 129–144CrossRefGoogle Scholar
  75. Zhang X, Wang W, Xiao K (2010) Novel omics technologies in nutraceutical and functional food research. In: Bagchi D, Lau FC, Bagchi M (eds) Genomics, proteomics and metabolomics in nutraceuticals and functional foods. Wiley-Blackwell, Ames, pp 11–22CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 2013

Authors and Affiliations

  1. 1.Department of Animal ScienceKitasato UniversityTowada-shiJapan

Personalised recommendations