Table of Contents Author Guidelines Submit a Manuscript
BioMed Research International
Volume 2014, Article ID 608979, 11 pages
http://dx.doi.org/10.1155/2014/608979
Review Article

Food-Derived Bioactive Peptides on Inflammation and Oxidative Stress

Department of Agricultural, Food & Nutritional Science, the Cardiovascular Research Centre, University of Alberta, 4-10 Ag/For Centre, Edmonton, AB, Canada T6G 2P5

Received 10 November 2013; Accepted 23 December 2013; Published 2 January 2014

Academic Editor: Blanca Hernández-Ledesma

Copyright © 2014 Subhadeep Chakrabarti et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. G. Danaei, G. M. Singh, C. J. Paciorek et al., “The global cardiovascular risk transition: associations of four metabolic risk factors with national income, urbanization, and Western diet in 1980 and 2008,” Circulation, vol. 127, no. 14, pp. 1493–1502, 2013. View at Publisher · View at Google Scholar
  2. B. M. Popkin, “Understanding global nutrition dynamics as a step towards controlling cancer incidence,” Nature Reviews Cancer, vol. 7, no. 1, pp. 61–67, 2007. View at Publisher · View at Google Scholar · View at Scopus
  3. R. O. Bonow, L. A. Smaha, S. C. Smith Jr., G. A. Mensah, and C. Lenfant, “World Heart Day 2002: the international burden of cardiovascular disease: responding to the emerging global epidemic,” Circulation, vol. 106, no. 13, pp. 1602–1605, 2002. View at Publisher · View at Google Scholar · View at Scopus
  4. A. D. Lopez and C. D. Mathers, “Measuring the global burden of disease and epidemiological transitions: 2002–2030,” Annals of Tropical Medicine and Parasitology, vol. 100, no. 5-6, pp. 481–499, 2006. View at Publisher · View at Google Scholar · View at Scopus
  5. M. Gutowski and S. Kowalczyk, “A study of free radical chemistry: their role and pathophysiological significance,” Acta Biochimica Polonica, vol. 60, no. 1, pp. 1–16, 2013. View at Google Scholar
  6. A. F. Ramos, M. B. de Fuccio, L. D. Moretzsohn et al., “Cystic fibrosis, gastroduodenal inflammation, duodenal ulcer, and H. pylori infection: the “cystic fibrosis paradox” revisited,” Journal of Cystic Fibrosis, vol. 12, no. 4, pp. 377–383, 2013. View at Google Scholar
  7. D. B. Vendramini-Costa and J. E. Carvalho, “Molecular link mechanisms between inflammation and cancer,” Current Pharmaceutical Design, vol. 18, no. 26, pp. 3831–3852, 2012. View at Google Scholar
  8. M. Yoshikawa, H. Fujita, N. Matoba et al., “Bioactive peptides derived from food proteins preventing lifestyle-related diseases,” BioFactors, vol. 12, no. 1–4, pp. 143–146, 2000. View at Google Scholar · View at Scopus
  9. D. D. Kitts and K. Weiler, “Bioactive proteins and peptides from food sources. Applications of bioprocesses used in isolation and recovery,” Current Pharmaceutical Design, vol. 9, no. 16, pp. 1309–1323, 2003. View at Publisher · View at Google Scholar · View at Scopus
  10. K. Erdmann, B. W. Y. Cheung, and H. Schröder, “The possible roles of food-derived bioactive peptides in reducing the risk of cardiovascular disease,” Journal of Nutritional Biochemistry, vol. 19, no. 10, pp. 643–654, 2008. View at Publisher · View at Google Scholar · View at Scopus
  11. R. Hartmann and H. Meisel, “Food-derived peptides with biological activity: from research to food applications,” Current Opinion in Biotechnology, vol. 18, no. 2, pp. 163–169, 2007. View at Publisher · View at Google Scholar · View at Scopus
  12. G. T. D. Sousa, F. S. Lira, J. C. Rosa et al., “Dietary whey protein lessens several risk factors for metabolic diseases: a review,” Lipids in Health and Disease, vol. 11, p. 67, 2012. View at Google Scholar
  13. A. J. Fitzgerald, P. S. Rai, T. Marchbank et al., “Reparative properties of a commercial fish protein hydrolysate preparation,” Gut, vol. 54, no. 6, pp. 775–781, 2005. View at Publisher · View at Google Scholar · View at Scopus
  14. K. Sato, Y. Egashira, S. Ono et al., “Identification of a hepatoprotective peptide in wheat gluten hydrolysate against D-galactosamine-induced acute hepatitis in rats,” Journal of Agricultural and Food Chemistry, vol. 61, no. 26, pp. 6304–6310, 2013. View at Google Scholar
  15. H. Izumi, S. Ishizuka, A. Inafune et al., “α-lactalbumin hydrolysate stimulates glucagon-like peptide-2 secretion and small intestinal growth in suckling rats,” Journal of Nutrition, vol. 139, no. 7, pp. 1322–1327, 2009. View at Publisher · View at Google Scholar · View at Scopus
  16. S. T. Davidge, “Prostaglandin H synthase and vascular function,” Circulation Research, vol. 89, no. 8, pp. 650–660, 2001. View at Google Scholar · View at Scopus
  17. S. Fiorucci, E. Distrutti, A. Mencarelli et al., “Cooperation between aspirin-triggered lipoxin and nitric oxide (NO) mediates antiadhesive properties of 2-(acetyloxy)benzoic acid 3-(nitrooxymethyl)phenyl ester (NCX-4016) (NO-aspirin) on neutrophil-endothelial cell adherence,” Journal of Pharmacology and Experimental Therapeutics, vol. 309, no. 3, pp. 1174–1182, 2004. View at Publisher · View at Google Scholar · View at Scopus
  18. N. R. Cook, I. M. Lee, S. M. Zhang, M. V. Moorthy, and J. E. Buring, “Alternate-day, low-dose aspirin and cancer risk: long-term observational follow-up of a randomized trial,” Annals of Internal Medicine, vol. 159, no. 2, pp. 77–85, 2013. View at Google Scholar
  19. A. Csiszar, M. Wang, E. G. Lakatta, and Z. Ungvari, “Inflammation and endothelial dysfunction during aging: role of NF-κB,” Journal of Applied Physiology, vol. 105, no. 4, pp. 1333–1341, 2008. View at Publisher · View at Google Scholar · View at Scopus
  20. M. Ruiz-Ortega, O. Lorenzo, and J. Egido, “Angiotensin III increases MCP-1 and activates NF-κB and AP-1 in cultured mesangial and mononuclear cells,” Kidney International, vol. 57, no. 6, pp. 2285–2298, 2000. View at Publisher · View at Google Scholar · View at Scopus
  21. T. Hirota, A. Nonaka, A. Matsushita et al., “Milk casein-derived tripeptides, VPP and IPP induced NO production in cultured endothelial cells and endothelium-dependent relaxation of isolated aortic rings,” Heart and Vessels, vol. 26, no. 5, pp. 549–556, 2011. View at Google Scholar · View at Scopus
  22. K. Aihara, H. Ishii, and M. Yoshida, “Casein-derived tripeptide, Val-Pro-Pro (VPP), modulates monocyte adhesion to vascular endothelium,” Journal of Atherosclerosis and Thrombosis, vol. 16, no. 5, pp. 594–603, 2009. View at Google Scholar · View at Scopus
  23. D. S. Nielsen, P. K. Theil, L. B. Larsen, and S. Purup, “Effect of milk hydrolysates on inflammation markers and drug-induced transcriptional alterations in cell-based models,” Journal of Animal Science, vol. 90, supplement 4, pp. 403–405, 2012. View at Google Scholar
  24. M. M. Iskandar, N. Dauletbaev, S. Kubow, N. Mawji, and L. C. Lands, “Whey protein hydrolysates decrease IL-8 secretion in lipopolysaccharide (LPS)-stimulated respiratory epithelial cells by affecting LPS binding to Toll-like receptor 4,” British Journal of Nutrition, vol. 110, no. 1, pp. 58–68, 2013. View at Google Scholar
  25. A. F. Piccolomini, M. M. Iskandar, L. C. Lands, and S. Kubow, “High hydrostatic pressure pre-treatment of whey proteins enhances whey protein hydrolysate inhibition of oxidative stress and IL-8 secretion in intestinal epithelial cells,” Food & Nutrition Research, vol. 56, 2012. View at Publisher · View at Google Scholar
  26. L. Håversen, B. G. Ohlsson, M. Hahn-Zoric, L. Å. Hanson, and I. Mattsby-Baltzer, “Lactoferrin down-regulates the LPS-induced cytokine production in monocytic cells via NF-κB,” Cellular Immunology, vol. 220, no. 2, pp. 83–95, 2002. View at Publisher · View at Google Scholar · View at Scopus
  27. D. Yan, D. Chen, J. Shen, G. Xiao, A. J. van Wijnen, and H. J. Im, “Bovine lactoferricin is anti-inflammatory and anti-catabolic in human articular cartilage and synovium,” Journal of Cellular Physiology, vol. 228, no. 2, pp. 447–456, 2013. View at Google Scholar
  28. J. S. Kim, M. B. Ellman, D. Yan et al., “Lactoferricin mediates anti-inflammatory and anti-catabolic effects via inhibition of IL-1 and LPS activity in the intervertebral disc,” Journal of Cellular Physiology, vol. 228, no. 9, pp. 1884–1896, 2013. View at Google Scholar
  29. K. J. Rutherfurd-Markwick, “Food proteins as a source of bioactive peptides with diverse functions,” British Journal of Nutrition, vol. 108, supplement 2, pp. S149–S157, 2012. View at Google Scholar
  30. Y. S. Kim, M. R. Young, G. Bobe, N. H. Colburn, and J. A. Milner, “Bioactive food components, inflammatory targets, and cancer prevention,” Cancer Prevention Research, vol. 2, no. 3, pp. 200–208, 2009. View at Publisher · View at Google Scholar · View at Scopus
  31. Y. Mine, “Egg proteins and peptides in human health-chemistry, bioactivity and production,” Current Pharmaceutical Design, vol. 13, no. 9, pp. 875–884, 2007. View at Publisher · View at Google Scholar · View at Scopus
  32. K. Majumder, S. Chakrabarti, S. T. Davidge, and J. Wu, “Structure and activity study of egg protein ovotransferrin derived peptides (IRW and IQW) on endothelial inflammatory response and oxidative stress,” Journal of Agricultural and Food Chemistry, vol. 61, no. 9, pp. 2120–2129, 2013. View at Publisher · View at Google Scholar
  33. W. Huang, S. Chakrabarti, K. Majumder, Y. Jiang, S. T. Davidge, and J. Wu, “Egg-derived peptide IRW inhibits TNF-α-induced inflammatory response and oxidative stress in endothelial cells,” Journal of Agricultural and Food Chemistry, vol. 58, no. 20, pp. 10840–10846, 2010. View at Publisher · View at Google Scholar · View at Scopus
  34. W. Huang, S. Shen, C. Nimalaratne, S. Li, K. Majumder, and J. Wu, “Effects of addition of egg ovotransferrin-derived peptides on the oxygen radical absorbance capacity of different teas,” Food Chemistry, vol. 135, no. 3, pp. 1600–1607, 2012. View at Google Scholar
  35. M. G. Vernaza, V. P. Dia, E. Gonzalez de Mejia, and Y. K. Chang, “Antioxidant and antiinflammatory properties of germinated and hydrolysed Brazilian soybean flours,” Food Chemistry, vol. 134, no. 4, pp. 2217–2225, 2012. View at Publisher · View at Google Scholar · View at Scopus
  36. J. S. Hwang, H. J. Yoo, H. J. Song et al., “Inflammation-related signaling pathways implicating TGFβ are revealed in the expression profiling of MCF7 cell treated with fermented soybean, Chungkookjang,” Nutrition and Cancer, vol. 63, no. 4, pp. 645–652, 2011. View at Publisher · View at Google Scholar · View at Scopus
  37. E. G. de Mejia and V. P. Dia, “Lunasin and lunasin-like peptides inhibit inflammation through suppression of NF-κB pathway in the macrophage,” Peptides, vol. 30, no. 12, pp. 2388–2398, 2009. View at Publisher · View at Google Scholar · View at Scopus
  38. B. Hernández-Ledesma, C.-C. Hsieh, and B. O. de Lumen, “Antioxidant and anti-inflammatory properties of cancer preventive peptide lunasin in RAW 264.7 macrophages,” Biochemical and Biophysical Research Communications, vol. 390, no. 3, pp. 803–808, 2009. View at Publisher · View at Google Scholar · View at Scopus
  39. A. Cam and E. G. de Mejia, “RGD-peptide lunasin inhibits Akt-mediated NF-κB activation in human macrophages through interaction with the αVβ3 integrin,” Molecular Nutrition & Food Research, vol. 56, no. 10, pp. 1569–1581, 2012. View at Publisher · View at Google Scholar
  40. D. E. Chatterton, D. N. Nguyen, S. B. Bering, and P. T. Sangild, “Anti-inflammatory mechanisms of bioactive milk proteins in the intestine of newborns,” The International Journal of Biochemistry & Cell Biology, vol. 45, no. 8, pp. 1730–1747, 2013. View at Google Scholar
  41. T. Nakamura, T. Hirota, K. Mizushima et al., “Milk-derived peptides, Val-Pro-Pro and Ile-Pro-Pro, attenuate atherosclerosis development in apolipoprotein e-deficient mice: a preliminary study,” Journal of Medicinal Food, vol. 16, no. 5, pp. 396–403, 2013. View at Google Scholar
  42. N. Shimizu, K. Dairiki, S. Ogawa, and T. Kaneko, “Dietary whey protein hydrolysate suppresses development of atopic dermatitis-like skin lesions induced by mite antigen in NC/Nga mice,” Allergology International, vol. 55, no. 2, pp. 185–189, 2006. View at Publisher · View at Google Scholar · View at Scopus
  43. M. Hatori, K. Ohki, S.-I. Hirano, X.-P. Yang, H. Kuboki, and C. Abe, “Effects of a casein hydrolysate prepared from Aspergillus oryzae protease on adjuvant arthritis in rats,” Bioscience, Biotechnology and Biochemistry, vol. 72, no. 8, pp. 1983–1991, 2008. View at Publisher · View at Google Scholar · View at Scopus
  44. M. Pescuma, M. B. Espeche Turbay, F. Mozzi, G. Font de Valdez, G. Savoy de Giori, and E. M. Hebert, “Diversity in proteinase specificity of thermophilic lactobacilli as revealed by hydrolysis of dairy and vegetable proteins,” Applied Microbiology and Biotechnology, vol. 97, no. 17, pp. 7831–7844, 2013. View at Google Scholar
  45. K. Majumder, S. Chakrabarti, J. S. Morton et al., “Egg-derived Tri-peptide IRW exerts antihypertensive effects in spontaneously hypertensive rats,” PLoS ONE, vol. 8, no. 11, Article ID e82829, 2013. View at Google Scholar
  46. T. Marchbank, G. Elia, and R. J. Playford, “Intestinal protective effect of a commercial fish protein hydrolysate preparation,” Regulatory Peptides, vol. 155, no. 1–3, pp. 105–109, 2009. View at Publisher · View at Google Scholar · View at Scopus
  47. T. Marchbank, J. K. Limdi, A. Mahmood, G. Elia, and R. J. Playford, “Clinical trial: protective effect of a commercial fish protein hydrolysate against indomethacin (NSAID)-induced small intestinal injury,” Alimentary Pharmacology and Therapeutics, vol. 28, no. 6, pp. 799–804, 2008. View at Publisher · View at Google Scholar · View at Scopus
  48. J. W. Hwang, S. J. Lee, Y. S. Kim et al., “Purification and characterization of a novel peptide with inhibitory effects on colitis induced mice by dextran sulfate sodium from enzymatic hydrolysates of Crassostrea gigas,” Fish & Shellfish Immunology, vol. 33, no. 4, pp. 993–999, 2012. View at Google Scholar
  49. B. Bjorndal, C. Berge, M. S. Ramsvik et al., “A fish protein hydrolysate alters fatty acid composition in liver and adipose tissue and increases plasma carnitine levels in a mouse model of chronic inflammation,” Lipids in Health and Disease, vol. 12, no. 1, p. 143, 2013. View at Google Scholar
  50. Y. Zhang, T. Kouguchi, K. Shimizu, M. Sato, Y. Takahata, and F. Morimatsu, “Chicken collagen hydrolysate reduces proinflammatory cytokine production in C57BL/6.KOR-ApoEsh1 mice,” Journal of Nutritional Science and Vitaminology, vol. 56, no. 3, pp. 208–210, 2010. View at Publisher · View at Google Scholar · View at Scopus
  51. Y. Zhang, T. Kouguchi, M. Shimizu, T. Ohmori, Y. Takahata, and F. Morimatsu, “Chicken collagen hydrolysate protects rats from hypertension and cardiovascular damage,” Journal of Medicinal Food, vol. 13, no. 2, pp. 399–405, 2010. View at Google Scholar · View at Scopus
  52. A. Saiga-Egusa, K. Iwai, T. Hayakawa, Y. Takahata, and F. Morimatsu, “Antihypertensive effects and endothelial progenitor cell activation by intake of chicken collagen hydrolysate in pre- and mild-hypertension,” Bioscience, Biotechnology and Biochemistry, vol. 73, no. 2, pp. 422–424, 2009. View at Publisher · View at Google Scholar · View at Scopus
  53. M. Mohammad Shahi, M.-R. Rashidi, S. Mahboob, F. Haidari, B. Rashidi, and J. Hanaee, “Protective effect of soy protein on collagen-induced arthritis in rat,” Rheumatology International, vol. 32, no. 8, pp. 2407–2414, 2012. View at Publisher · View at Google Scholar · View at Scopus
  54. S. Nagarajan, R. L. Burris, B. W. Stewart, J. E. Wilkerson, and T. M. Badger, “Dietary soy protein isolate ameliorates atherosclerotic lesions in apolipoprotein E-deficient mice potentially by inhibiting monocyte chemoattractant protein-1 expression,” Journal of Nutrition, vol. 138, no. 2, pp. 332–337, 2008. View at Google Scholar · View at Scopus
  55. J. Kovacs-Nolan, H. Zhang, M. Ibuki et al., “The PepT1-transportable soy tripeptide VPY reduces intestinal inflammation,” Biochim Biophys Acta, vol. 1820, no. 11, pp. 1753–1763, 2012. View at Google Scholar
  56. D. Young, M. Ibuki, T. Nakamori, M. Fan, and Y. Mine, “Soy-derived di-and tripeptides alleviate colon and ileum inflammation in pigs with dextran sodium sulfate-induced colitis,” Journal of Nutrition, vol. 142, no. 2, pp. 363–368, 2012. View at Publisher · View at Google Scholar · View at Scopus
  57. M. Mochizuki, H. Shigemura, and N. Hasegawa, “Anti-inflammatory effect of enzymatic hydrolysate of corn gluten in an experimental model of colitis,” Journal of Pharmacy and Pharmacology, vol. 62, no. 3, pp. 389–392, 2010. View at Publisher · View at Google Scholar · View at Scopus
  58. S. Wada, K. Sato, R. Ohta et al., “Ingestion of low dose pyroglutamyl leucine improves dextran sulfate sodium-induced colitis and intestinal microbiota in mice,” Journal of Agricultural and Food Chemistry, vol. 61, no. 37, pp. 8807–8813, 2013. View at Google Scholar
  59. J.-M. Lü, P. H. Lin, Q. Yao, and C. Chen, “Chemical and molecular mechanisms of antioxidants: experimental approaches and model systems,” Journal of Cellular and Molecular Medicine, vol. 14, no. 4, pp. 840–860, 2010. View at Publisher · View at Google Scholar · View at Scopus
  60. L. A. Pham-Huy, H. He, and C. Pham-Huy, “Free radicals, antioxidants in disease and health,” International Journal of Biomedical Science, vol. 4, no. 2, pp. 89–96, 2008. View at Google Scholar · View at Scopus
  61. G. Poli, G. Leonarduzzi, F. Biasi, and E. Chiarpotto, “Oxidative stress and cell signalling,” Current Medicinal Chemistry, vol. 11, no. 9, pp. 1163–1182, 2004. View at Google Scholar · View at Scopus
  62. T. P. A. Devasagayam, J. C. Tilak, K. K. Boloor, K. S. Sane, S. S. Ghaskadbi, and R. D. Lele, “Free radicals and antioxidants in human health: current status and future prospects,” Journal of Association of Physicians of India, vol. 52, pp. 794–804, 2004. View at Google Scholar · View at Scopus
  63. K. Brieger, S. Schiavone, F. J. Miller Jr., and K. H. Krause, “Reactive oxygen species: from health to disease,” Swiss Medical Weekly, vol. 142, p. w13659, 2012. View at Google Scholar
  64. H. Wiseman and B. Halliwell, “Damage to DNA by reactive oxygen and nitrogen species: role in inflammatory disease and progression to cancer,” Biochemical Journal, vol. 313, no. 1, pp. 17–29, 1996. View at Google Scholar · View at Scopus
  65. M. Valko, D. Leibfritz, J. Moncol, M. T. D. Cronin, M. Mazur, and J. Telser, “Free radicals and antioxidants in normal physiological functions and human disease,” International Journal of Biochemistry and Cell Biology, vol. 39, no. 1, pp. 44–84, 2007. View at Publisher · View at Google Scholar · View at Scopus
  66. E. R. Stadtman and R. L. Levine, “Free radical-mediated oxidation of free amino acids and amino acid residues in proteins,” Amino Acids, vol. 25, no. 3-4, pp. 207–218, 2003. View at Publisher · View at Google Scholar · View at Scopus
  67. U. Singh and I. Jialal, “Oxidative stress and atherosclerosis,” Pathophysiology, vol. 13, no. 3, pp. 129–142, 2006. View at Publisher · View at Google Scholar · View at Scopus
  68. M. A. Smith, C. A. Rottkamp, A. Nunomura, A. K. Raina, and G. Perry, “Oxidative stress in Alzheimer's disease,” Biochimica et Biophysica Acta, vol. 1502, no. 1, pp. 139–144, 2000. View at Publisher · View at Google Scholar · View at Scopus
  69. D.-H. Hyun, J. O. Hernandez, M. P. Mattson, and R. de Cabo, “The plasma membrane redox system in aging,” Ageing Research Reviews, vol. 5, no. 2, pp. 209–220, 2006. View at Publisher · View at Google Scholar · View at Scopus
  70. V. L. Kinnula and J. D. Crapo, “Superoxide dismutases in malignant cells and human tumors,” Free Radical Biology and Medicine, vol. 36, no. 6, pp. 718–744, 2004. View at Publisher · View at Google Scholar · View at Scopus
  71. E. Niki, “Assessment of antioxidant capacity of natural products,” Current Pharmaceutical Biotechnology, vol. 11, no. 8, pp. 801–809, 2010. View at Publisher · View at Google Scholar · View at Scopus
  72. M. Carocho and I. C. Ferreira, “A review on antioxidants, prooxidants and related controversy: natural and synthetic compounds, screening and analysis methodologies and future perspectives,” Food and Chemical Toxicology, vol. 51, pp. 15–25, 2013. View at Google Scholar
  73. T. Nagai, T. Egashira, Y. Yamanaka, and M. Kohno, “The protective effect of glycyrrhizin against injury of the liver caused by ischemia-reperfusion,” Archives of Environmental Contamination and Toxicology, vol. 20, no. 3, pp. 432–436, 1991. View at Google Scholar · View at Scopus
  74. C. Rousseau-Richards, C. Auclair, C. Richard, and R. Martin, “Free radical scavenging and cytotoxic properties in the ellipticine series,” Free Radical Biology and Medicine, vol. 8, no. 3, pp. 223–230, 1990. View at Publisher · View at Google Scholar · View at Scopus
  75. M. Saito, “Polychlorinated biphenyls-induced lipid peroxidation as measured by thiobarbituric acid-reactive substances in liver subcellular fractions of rats,” Biochimica et Biophysica Acta, vol. 1046, no. 3, pp. 301–308, 1990. View at Publisher · View at Google Scholar · View at Scopus
  76. R. C. Smith, J. C. Reeves, R. C. Dage, and R. A. Schnettler, “Antioxidant properties of 2-imidazolones and 2-imidazolthiones,” Biochemical Pharmacology, vol. 36, no. 9, pp. 1457–1460, 1987. View at Google Scholar · View at Scopus
  77. K. Harada, T. Maeda, Y. Hasegawa, T. Tokunaga, Y. Tamura, and T. Koizumi, “Antioxidant activity of fish sauces including puffer (Lagocephalus wheeleri) fish sauce measured by the oxygen radical absorbance capacity method,” Molecular Medicine Reports, vol. 3, no. 4, pp. 663–668, 2010. View at Publisher · View at Google Scholar · View at Scopus
  78. A. T. Girgih, C. C. Udenigwe, F. M. Hasan, T. A. Gill, and R. E. Aluko, “Antioxidant properties of Salmon (Salmo salar) protein hydrolysate and peptide fractions isolated by reverse-phase HPLC,” Food Research International, vol. 52, no. 1, pp. 315–322, 2013. View at Google Scholar
  79. J. Y. Ko, J. H. Lee, K. Samarakoon, J. S. Kim, and Y. J. Jeon, “Purification and determination of two novel antioxidant peptides from flounder fish (Paralichthys olivaceus) using digestive proteases,” Food and Chemical Toxicology, vol. 52, pp. 113–120, 2013. View at Google Scholar
  80. B. Wang, L. Li, C. F. Chi, J. H. Ma, H. Y. Luo, and Y. F. Xu, “Purification and characterisation of a novel antioxidant peptide derived from blue mussel (Mytilus edulis) protein hydrolysate,” Food Chemistry, vol. 138, no. 2-3, pp. 1713–1719, 2013. View at Google Scholar
  81. K. Suetsuna, H. Ukeda, and H. Ochi, “Isolation and characterization of free radical scavenging activities peptides derived from casein,” Journal of Nutritional Biochemistry, vol. 11, no. 3, pp. 128–131, 2000. View at Publisher · View at Google Scholar · View at Scopus
  82. M. D. M. Contreras, B. Hernández-Ledesma, L. Amigo, P. J. Martín-Álvarez, and I. Recio, “Production of antioxidant hydrolyzates from a whey protein concentrate with thermolysin: optimization by response surface methodology,” LWT-Food Science and Technology, vol. 44, no. 1, pp. 9–15, 2011. View at Publisher · View at Google Scholar · View at Scopus
  83. J. Á. Gómez-Ruiz, I. López-Expósito, A. Pihlanto, M. Ramos, and I. Recio, “Antioxidant activity of ovine casein hydrolysates: identification of active peptides by HPLC-MS/MS,” European Food Research and Technology, vol. 227, no. 4, pp. 1061–1067, 2008. View at Publisher · View at Google Scholar · View at Scopus
  84. Z. Li, A. Jiang, T. Yue, J. Wang, Y. Wang, and J. Su, “Purification and identification of five novel antioxidant peptides from goat milk casein hydrolysates,” Journal of Dairy Science, vol. 96, no. 7, pp. 4242–4251, 2013. View at Google Scholar
  85. K. Q. Zhou, S. Sun, and C. Canning, “Production and functional characterisation of antioxidative hydrolysates from corn protein via enzymatic hydrolysis and ultrafiltration,” Food Chemistry, vol. 135, no. 3, pp. 1192–1197, 2012. View at Google Scholar
  86. L. Zhang, J. Li, and K. Zhou, “Chelating and radical scavenging activities of soy protein hydrolysates prepared from microbial proteases and their effect on meat lipid peroxidation,” Bioresource Technology, vol. 101, no. 7, pp. 2084–2089, 2010. View at Publisher · View at Google Scholar · View at Scopus
  87. X. H. Kou, J. Gao, Z. H. Xue, Z. J. Zhang, H. Wang, and X. Wang, “Purification and identification of antioxidant peptides from chickpea (Cicer arietinum L.) albumin hydrolysates,” LWT-Food Science and Technology, vol. 50, no. 2, pp. 591–598, 2013. View at Google Scholar
  88. C. Lopez-Alarcon and A. Denicola, “Evaluating the antioxidant capacity of natural products: a review on chemical and cellular-based assays,” Analytica Chimica Acta, vol. 763, pp. 1–10, 2013. View at Google Scholar
  89. E. Niki, “Assessment of antioxidant capacity in vitro and in vivo,” Free Radical Biology and Medicine, vol. 49, no. 4, pp. 503–515, 2010. View at Publisher · View at Google Scholar · View at Scopus
  90. E. Mendis, N. Rajapakse, and S.-K. Kim, “Antioxidant properties of a radical-scavenging peptide purified from enzymatically prepared fish skin gelatin hydrolysate,” Journal of Agricultural and Food Chemistry, vol. 53, no. 3, pp. 581–587, 2005. View at Publisher · View at Google Scholar · View at Scopus
  91. R. Coda, C. G. Rizzello, D. Pinto, and M. Gobbetti, “Selected lactic acid bacteria synthesize antioxidant peptides during sourdough fermentation of cereal flours,” Applied and Environmental Microbiology, vol. 78, no. 4, pp. 1087–1096, 2012. View at Publisher · View at Google Scholar · View at Scopus
  92. R.-R. Lu, P. Qian, Z. Sun et al., “Hempseed protein derived antioxidative peptides: purification, identification and protection from hydrogen peroxide-induced apoptosis in PC12 cells,” Food Chemistry, vol. 123, no. 4, pp. 1210–1218, 2010. View at Publisher · View at Google Scholar · View at Scopus
  93. J. Zhang, H. Zhang, L. Wang, X. Guo, X. Wang, and H. Yao, “Isolation and identification of antioxidative peptides from rice endosperm protein enzymatic hydrolysate by consecutive chromatography and MALDI-TOF/TOF MS/MS,” Food Chemistry, vol. 119, no. 1, pp. 226–234, 2010. View at Publisher · View at Google Scholar · View at Scopus
  94. M. A. Manso, M. Miguel, J. Even, R. Hernández, A. Aleixandre, and R. López-Fandiño, “Effect of the long-term intake of an egg white hydrolysate on the oxidative status and blood lipid profile of spontaneously hypertensive rats,” Food Chemistry, vol. 109, no. 2, pp. 361–367, 2008. View at Publisher · View at Google Scholar · View at Scopus
  95. Z. Xue, W. Yu, Z. Liu, M. Wu, X. Kou, and J. Wang, “Preparation and antioxidative properties of a rapeseed (Brassica napus) protein hydrolysate and three peptide fractions,” Journal of Agricultural and Food Chemistry, vol. 57, no. 12, pp. 5287–5293, 2009. View at Publisher · View at Google Scholar · View at Scopus
  96. A. Cam and E. G. de Mejia, “Role of dietary proteins and peptides in cardiovascular disease,” Molecular Nutrition and Food Research, vol. 56, no. 1, pp. 53–66, 2012. View at Publisher · View at Google Scholar · View at Scopus
  97. A. Bast and G. R. M. M. Haenen, “The toxicity of antioxidants and their metabolites,” Environmental Toxicology and Pharmacology, vol. 11, no. 3-4, pp. 251–258, 2002. View at Publisher · View at Google Scholar · View at Scopus
  98. G. S. Omenn, G. E. Goodman, M. D. Thornquist et al., “Risk factors for lung cancer and for intervention effects in CARET, the beta-carotene and retinol efficacy trial,” Journal of the National Cancer Institute, vol. 88, no. 21, pp. 1550–1559, 1996. View at Publisher · View at Google Scholar · View at Scopus
  99. H. Akiyama, K. Sakata, Y. Yoshioka et al., “Profile analysis and immunoglobulin E reactivity of wheat protein hydrolysates,” International Archives of Allergy and Immunology, vol. 140, no. 1, pp. 36–42, 2006. View at Publisher · View at Google Scholar · View at Scopus
  100. P. Franck, D. A. Moneret Vautrin, B. Dousset et al., “The allergenicity of soybean-based products is modified by food technologies,” International Archives of Allergy and Immunology, vol. 128, no. 3, pp. 212–219, 2002. View at Publisher · View at Google Scholar · View at Scopus
  101. Y. Yamada, D. Yamauchi, H. Usui et al., “Hypotensive activity of novokinin, a potent analogue of ovokinin(2-7), is mediated by angiotensin AT2 receptor and prostaglandin IP receptor,” Peptides, vol. 29, no. 3, pp. 412–418, 2008. View at Publisher · View at Google Scholar · View at Scopus
  102. M. Yoshikawa, “Isolation and characterization of ovokinin, a bradykinin B1 agonist peptide derived from ovalbumin,” Peptides, vol. 16, no. 5, pp. 785–790, 1995. View at Publisher · View at Google Scholar · View at Scopus