Antioxidative and antibacterial peptides derived from bovine milk proteins

References

• Agyei, D. and Danquah, M. K. (2011). Industrial-scale manufacturing of pharmaceutical-grade bioactive peptides. Biotechnol. Adv. 29(3):272–277. doi: 10.1016/j.biotechadv.2011.01.001
   PubMed Web of Science ®Google Scholar
• Agyei, D. and Danquah, M. K. (2012). Rethinking food-derived bioactive peptides for antimicrobial and immunomodulatory activities. Trends Food Sci. Technol. 23(2):62–69. doi: 10.1016/j.tifs.2011.08.010
   Web of Science ®Google Scholar
• Alvarez-Ordóñez, A., Begley, M., Clifford, T., Deasy, T., Considine, K. and Hill, C. (2013). Structure-activity relationship of synthetic variants of the milk-derived antimicrobial peptide αS2-casein f(183–207). Appl. Environ. Microbiol. 79(17):5179–5185. doi: 10.1128/AEM.01394-13
   PubMed Web of Science ®Google Scholar
• Antolovich, M., Prenzler, P. D., Patsalides, E., McDonald, S. and Robards, K. (2002). Methods for testing antioxidant activity. Analyst. 127(1):183–198. doi: 10.1039/b009171p
   PubMed Web of Science ®Google Scholar
• Ao, J. and Li, B. (2013). Stability and antioxidative activities of casein peptide fractions during simulated gastrointestinal digestion in vitro: Charge properties of peptides affect digestive stability. Food Res. Int. 52(1):334–341. doi: 10.1016/j.foodres.2013.03.036
   Web of Science ®Google Scholar
• Appendini, P. and Hotchkiss, J. H. (2002). Review of antimicrobial food packaging. Innov. Food Sci. Emerg. Technol. 3(2):113–126. doi: 10.1016/S1466-8564(02)00012-7
   Google Scholar
• Azarkan, M., Matagne, A., Wattiez, R., Bolle, L., Vandenameele, J. and Baeyens-Volant, D. (2011). Selective and reversible thiol-pegylation, an effective approach for purification and characterization of five fully active ficin (iso)forms from Ficus carica latex. Phytochemistry. 72(14–15):1718–1731. doi: 10.1016/j.phytochem.2011.05.009
   PubMed Web of Science ®Google Scholar
• Bahar, A. A. and Ren, D. (2013). Antimicrobial Peptides. Pharmaceuticals. 6(12):1543–1575. doi: 10.3390/ph6121543
   Google Scholar
• Barbosa, C. M. S., Morais, H. A., Delvivo, F. M., Mansur, H. S., De Oliveira, M. C. and Silvestre, M. P. C. (2004). Papain hydrolysates of casein: Molecular weight profile and encapsulation in lipospheres. J. Sci. Food Agric. 84(14):1891–1900. doi: 10.1002/jsfa.1855
   Web of Science ®Google Scholar
• Bargeman, G., Koops, G. H., Houwing, J., Breebaart, I., Van Der Horst, H. C. and Wessling, M. (2002). The development of electro-membrane filtration for the isolation of bioactive peptides: The effect of membrane selection and operating parameters on the transport rate. Desalination. 149(1–3):369–374. doi: 10.1016/S0011-9164(02)00824-X
   Web of Science ®Google Scholar
• Bechinger, B., Zasloff, M. and Opella, S. J. (1993). Structure and orientation of the antibiotic peptide magainin in membranes by solid-state nuclear magnetic resonance spectroscopy. Protein Sci. 2(12):2077–2084. doi: 10.1002/pro.5560021208
   PubMed Web of Science ®Google Scholar
• Benkerroum, N. (2010). Antimicrobial peptides generated from milk proteins: A survey and prospects for application in the food industry. A review. Int. J. Dairy Technol. 63(3):320–338. doi: 10.1111/j.1471-0307.2010.00584.x
   Web of Science ®Google Scholar
• Brogden, K. A. (2005). Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria? Nat. Rev. Microbiol. 3(3):238–250. doi: 10.1038/nrmicro1098
   PubMed Web of Science ®Google Scholar
• Butnariu, M. and Grozea, L. (2012). Antioxidant (antiradical) compounds. J. Bioequivalence Bioavailab. 4(6):xvii–xix. doi: 10.4172/jbb.10000e18
   Google Scholar
• Calkins, M. J., Manczak, M. and Reddy, P. H. (2012). Mitochondria-targeted antioxidant SS31 prevents amyloid beta-induced mitochondrial abnormalities and synaptic degeneration in Alzheimer's disease. Pharmaceuticals. 5(10):1103–1119. doi: 10.3390/ph5101103
   Google Scholar
• Chen, H. M., Muramoto, K. and Yamauchi, F. (1995). Structural analysis of antioxidative peptides from soybean β-conglycinin. J. Agric. Food. Chem. 43(3):574–578. doi: 10.1021/jf00051a004
   Web of Science ®Google Scholar
• Chen, H. M., Muramoto, K., Yamauchi, F. and Nokihara, K. (1996). Antioxidant activity of designed peptides based on the antioxidative peptide isolated from digests of a soybean protein. J. Agric. Food. Chem. 44(9):2619–2623.
   Web of Science ®Google Scholar
• Chen, M. and Li, B. (2012). The effect of molecular weights on the survivability of casein-derived antioxidant peptides after the simulated gastrointestinal digestion. Innov. Food Sci. Emerg. Technol. 16:341–348.doi: 10.1016/j.ifset.2012.07.009
   Web of Science ®Google Scholar
• Choudhari, S. K., Chaudhary, M., Gadbail, A. R., Sharma, A. and Tekade, S. (2014). Oxidative and antioxidative mechanisms in oral cancer and precancer: A review. Oral Oncol. 50(1):10–18. doi: 10.1016/j.oraloncology.2013.09.011
   PubMed Web of Science ®Google Scholar
• Christensen, J. E., Dudley, E. G., Pederson, J. A. and Steele, J. L. (1999). Peptidases and amino acid catabolism in lactic acid bacteria. Antonie Van Leeuwenhoek. 76(1–4):217–246. doi: 10.1023/A:1002001919720
   PubMed Web of Science ®Google Scholar
• Contreras, M. D. M., Hernández-Ledesma, B., Amigo, L., Martín-Álvarez, P. J. and Recio, I. (2011). Production of antioxidant hydrolyzates from a whey protein concentrate with thermolysin: Optimization by response surface methodology. LWT–Food Sci. Technol. 44(1):9–15. doi: 10.1016/j.lwt.2010.06.017
   Web of Science ®Google Scholar
• da Silva Jr, A., and Teschke, O. (2003). Effects of the antimicrobial peptide PGLa on live Escherichia coli. Biochim. Biophys. Acta. 1643(1–3):95–103. doi: 10.1016/j.bbamcr.2003.10.001
   PubMed Web of Science ®Google Scholar
• Demers-Mathieu, V., Gauthier, S. F., Britten, M., Fliss, I., Robitaille, G. and Jean, J. (2013). Antibacterial activity of peptides extracted from tryptic hydrolyzate of whey protein by nanofiltration. Int. Dairy J. 28(2):94–101. doi: 10.1016/j.idairyj.2012.09.003
   Web of Science ®Google Scholar
• Devasagayam, T. P. A., Tilak, J. C., Boloor, K. K., Sane, K. S., Ghaskadbi, S. S. and Lele, R. D. (2004). Free radicals and antioxidants in human health: Current status and future prospects. J. Assoc. Physicians India. 52(OCT):794–804.
   PubMedGoogle Scholar
• Di Pierro, G., O'Keeffe, M. B., Poyarkov, A., Lomolino, G. and Fitzgerald, R. J. (2014). Antioxidant activity of bovine casein hydrolysates produced by Ficus carica L.-derived proteinase. Food Chem. 156:305–311.doi: 10.1016/j.foodchem.2014.01.080
   PubMed Web of Science ®Google Scholar
• Díaz, M. and Decker, E. A. (2004). Antioxidant mechanisms of caseinophosphopeptides and casein hydrolysates and their application in ground beef. J. Agric. Food. Chem. 52(26):8208–8213. doi: 10.1021/jf048869e
   PubMed Web of Science ®Google Scholar
• Dionysius, D. A. and Milne, J. M. (1997). Antibacterial peptides of bovine lactoferrin: Purification and characterization. J. Dairy Sci. 80(4):667–674. doi: 10.3168/jds.S0022-0302(97)75985-X
   PubMed Web of Science ®Google Scholar
• Dziuba, B. and Dziuba, M. (2014). New milk protein-derived peptides with potential antimicrobial activity: An approach based on bioinformatic studies. Int. J. Mol. Sci. 15(8):14531–14545. doi: 10.3390/ijms150814531
   PubMed Web of Science ®Google Scholar
• Elbarbary, H. A., Abdou, A. M., Nakamura, Y., Park, E. Y., Mohamed, H. A. and Sato, K. (2012). Identification of novel antibacterial peptides isolated from a commercially available casein hydrolysate by autofocusing technique. Bio Factors. 38(4):309–315. doi: 10.1002/biof.1023
   PubMed Web of Science ®Google Scholar
• Elfahri, K. R., Vasiljevic, T., Yeager, T. and Donkor, O. N. (2016). Anti-colon cancer and antioxidant activities of bovine skim milk fermented by selected Lactobacillus helveticus strains. J. Dairy Sci. 99(1):31–40. doi: 10.3168/jds.2015-10160
   PubMed Web of Science ®Google Scholar
• Elias, R. J., Kellerby, S. S. and Decker, E. A. (2008). Antioxidant activity of proteins and peptides. Crit. Rev. Food Sci. Nutr. 48(5):430–441. doi: 10.1080/10408390701425615
   PubMed Web of Science ®Google Scholar
• Ellegård, K. H., Gammelgård-Larsen, C., Sørensen, E. S. and Fedosov, S. (1999). Process scale chromatographic isolation, characterization and identification of tryptic bioactive casein phosphopeptides. Int. Dairy J. 9(9):639–652. doi: 10.1016/S0958-6946(99)00135-1
   Web of Science ®Google Scholar
• Faist, V., Drusch, S., Kiesner, C., Elmadfa, I. and Erbersdobler, H. F. (2000). Determination of lysinoalanine in foods containing milk protein by high-performance chromatography after derivatisation with dansyl chloride. Int. Dairy J. 10(5–6):339–346. doi: 10.1016/S0958-6946(00)00075-3
   Web of Science ®Google Scholar
• Farvin, K. H. S., Baron, C. P., Nielsen, N. S., Otte, J. and Jacobsen, C. (2010). Antioxidant activity of yoghurt peptides: Part 2–Characterisation of peptide fractions. Food Chem. 123(4):1090–1097. doi: 10.1016/j.foodchem.2010.05.029
   Web of Science ®Google Scholar
• Favaro-Trindade, C. S., Santana, A. S., Monterrey-Quintero, E. S., Trindade, M. A. and Netto, F. M. (2010). The use of spray drying technology to reduce bitter taste of casein hydrolysate. Food Hydrocoll. 24(4):336–340. doi: 10.1016/j.foodhyd.2009.10.012
   Web of Science ®Google Scholar
• FitzGerald, R. J. (1998). Potential uses of caseinophosphopeptides. Int. Dairy J. 8(5–6):451–457. doi: 10.1016/S0958-6946(98)00068-5
   Web of Science ®Google Scholar
• Furukawa, T., Akutagawa, T., Funatani, H., Uchida, T., Hotta, Y., Niwa, M., and Takaya, Y. (2012). Cyclic dipeptides exhibit potency for scavenging radicals. Bioorg. Med. Chem. 20(6):2002–2009. doi: 10.1016/j.bmc.2012.01.050
   PubMed Web of Science ®Google Scholar
• Giangaspero, A., Sandri, L. and Tossi, A. (2001). Amphipathic α helical antimicrobial peptides: A systematic study of the effects of structural and physical properties on biological activity. Eur. J. Biochem. 268(21):5589–5600. doi: 10.1046/j.0014-2956.2001.02494.x
   PubMedGoogle Scholar
• Gill, I., López-Fandiño, R., Jorba, X. and Vulfson, E. N. (1996). Biologically active peptides and enzymatic approaches to their production. Enzyme Microb. Technol. 18(3):163–183. doi: 10.1016/0141-0229(95)00097-6
   PubMed Web of Science ®Google Scholar
• Hancock, R. E. W. and Rozek, A. (2002). Role of membranes in the activities of antimicrobial cationic peptides. FEMS Microbiol. Lett. 206(2):143–149. doi: 10.1016/S0378-1097(01)00480-3
   PubMed Web of Science ®Google Scholar
• Hancock, R. E. W. and Sahl, H. G. (2006). Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies. Nat. Biotechnol. 24(12):1551–1557. doi: 10.1038/nbt1267
   PubMed Web of Science ®Google Scholar
• Hernández-Ledesma, B., Contreras, M. M. and Recio, I. (2011). Antihypertensive peptides: Production, bioavailability and incorporation into foods. Adv. Colloid Interface Sci. 165(1):23–35. doi: 10.1016/j.cis.2010.11.001
   PubMed Web of Science ®Google Scholar
• Hernández-Ledesma, B., Dávalos, A., Bartolomé, B. and Amigo, L. (2005). Preparation of antioxidant enzymatic hydrolysates from α-lactalbumin and β-lactoglobulln. Identification of active peptides by HPLC-MS/MS. J. Agric. Food. Chem. 53(3):588–593. doi: 10.1021/jf048626m
   PubMed Web of Science ®Google Scholar
• Hogan, S., Zhang, L., Li, J., Wang, H. and Zhou, K. (2009). Development of antioxidant rich peptides from milk protein by microbial proteases and analysis of their effects on lipid peroxidation in cooked beef. Food Chem. 117(3):438–443. doi: 10.1016/j.foodchem.2009.04.040
   Web of Science ®Google Scholar
• Huang, D., Boxin, O. U. and Prior, R. L. (2005). The chemistry behind antioxidant capacity assays. J. Agric. Food. Chem. 53(6):1841–1856. doi: 10.1021/jf030723c
   PubMed Web of Science ®Google Scholar
• Ibraheem, D., Elaissari, A. and Fessi, H. (2014). Administration strategies for proteins and peptides. Int. J. Pharm. 477(1–2):578–589. doi: 10.1016/j.ijpharm.2014.10.059
   PubMed Web of Science ®Google Scholar
• Ji, N., Sun, C., Zhao, Y., Xiong, L. and Sun, Q. (2014). Purification and identification of antioxidant peptides from peanut protein isolate hydrolysates using UHR-Q-TOF mass spectrometer. Food Chem. 161:148–154.doi: 10.1016/j.foodchem.2014.04.010
   PubMed Web of Science ®Google Scholar
• Johansen, J. S., Harris, A. K., Rychly, D. J. and Ergul, A. (2005). Oxidative stress and the use of antioxidants in diabetes: Linking basic science to clinical practice. Cardiovasc. Diabetol. 4:5–15. doi: 10.1186/1475-2840-4-5
   PubMed Web of Science ®Google Scholar
• Jones, F. S., Simms, H. S. and Maaroufi, A. (1930). The bacterial growth inhibitor (lactenin) of milk: I. The preparation in concentrated form. J. Exp. Med. 51(2):327–339.
   PubMedGoogle Scholar
• Juillard, V., Laan, H., Kunji, E. R. S., Jeronimus-Stratingh, C. M., Bruins, A. P. and Konings, W. N. (1995). The extracellular PI-type proteinase of Lactococcus lactis hydrolyzes β-casein into more than one hundred different oligopeptides. J. Bacteriol. 177(12):3472–3478.
   PubMed Web of Science ®Google Scholar
• Jun, S. Y., Park, P. J., Jung, W. K. and Kim, S. K. (2004). Purification and characterization of an antioxidative peptide from enzymatic hydrolysate of yellowfin sole (Limanda aspera) frame protein. Eur. Food Res. Technol. 219(1):20–26. doi: 10.1007/s00217-004-0882-9
   Web of Science ®Google Scholar
• Kopf-Bolanz, K. A., Schwander, F., Gijs, M., Vergéres, G., Portmann, R. and Egger, L. (2012). Validation of an in vitro digestive system for studying macronutrient decomposition in humans. J. Nutr. 142(2):245–250. doi: 10.3945/jn.111.148635
   PubMed Web of Science ®Google Scholar
• Kopf-Bolanz, K. A., Schwander, F., Gijs, M., Vergères, G., Portmann, R. and Egger, L. (2014). Impact of milk processing on the generation of peptides during digestion. Int. Dairy J. 35(2):130–138. doi: 10.1016/j.idairyj.2013.10.012
   Web of Science ®Google Scholar
• Korhonen, H. (2009). Milk-derived bioactive peptides: From science to applications. J. Funct. Foods. 1(2):177–187. doi: 10.1016/j.jff.2009.01.007
   Web of Science ®Google Scholar
• Korhonen, H. and Pihlanto, A. (2003). Food-derived bioactive peptides—Opportunities for designing future foods. Curr. Pharm. Des. 9(16):1297–1308. doi: 10.2174/1381612033454892
   PubMed Web of Science ®Google Scholar
• Korhonen, H. and Pihlanto, A. (2006). Bioactive peptides: production and functionality. Int. Dairy J. 16(9):945–960. doi: 10.1016/j.idairyj.2005.10.012
   Web of Science ®Google Scholar
• Korhonen, H. and Pihlanto, A. (2007). Technological options for the production of health-promoting proteins and peptides derived from milk and colostrum. Curr. Pharm. Des. 13(8):829–843. doi: 10.2174/138161207780363112
   PubMed Web of Science ®Google Scholar
• Kudoh, Y., Matsuda, S., Igoshi, K. and Oki, T. (2001). Antioxidative peptide from milk fermented with Lactobacillus delbrueckii subsp. bulgaricus IFO13953. J. Jpn Soc Food Sci. 48(1):44–50.
   Web of Science ®Google Scholar
• Kunji, E. R. S., Mierau, I., Poolman, B. and Konings, W. N. (1996). The proteolytic systems of lactic acid bacteria. Antonie van Leeuwenhoek, Int. J. Gen. Mol. Microbiol. 70(2–4):187–221.
   PubMed Web of Science ®Google Scholar
• Lahov, E. and Regelson, W. (1996). Antibacterial and immunostimulating casein-derived substances from milk: Casecidin, isracidin peptides. Food Chem. Toxicol. 34(1):131–145. doi: 10.1016/0278-6915(95)00097-6
   PubMed Web of Science ®Google Scholar
• Lee, H. J. (2002). Protein drug oral delivery: The recent progress. Arch. Pharmacol. Res. 25(5):572–584. doi: 10.1007/BF02976925
   PubMed Web of Science ®Google Scholar
• Lee, K. D., Lo, C. G. and Warthesen, J. J. (1996). Removal of bitterness from the bitter peptides extracted from Cheddar cheese with peptidases from Lactococcus lactis ssp. cremoris SK11. J. Dairy Sci. 79(9):1521–1528. doi: 10.3168/jds.S0022-0302(96)76512-8
   Web of Science ®Google Scholar
• Li, Y. W., Li, B., He, J. and Qian, P. (2011). Quantitative structure–activity relationship study of antioxidative peptide by using different sets of amino acids descriptors. J. Mol. Struct. 998(1–3):53–61. doi: 10.1016/j.molstruc.2011.05.011
   Web of Science ®Google Scholar
• López-Expósito, I., Amigo, L. and Recio, I. (2008). Identification of the initial binding sites of αS2-casein f(183–207) and effect on bacterial membranes and cell morphology. Biochim. Biophys. Acta Biomembr. 1778(10):2444–2449. doi: 10.1016/j.bbamem.2008.06.018
   PubMed Web of Science ®Google Scholar
• López-Expósito, I., Gómez-Ruiz, J. A., Amigo, L. and Recio, I. (2006a). Identification of antibacterial peptides from ovine αS2-casein. Int. Dairy J. 16(9):1072–1080. doi: 10.1016/j.idairyj.2005.10.006
   Web of Science ®Google Scholar
• López-Expósito, I., Minervini, F., Amigo, L. and Recio, I. (2006b). Identification of antibacterial peptides from bovine κ-casein. J. Food Prot. 69(12):2992–2997.
   PubMed Web of Science ®Google Scholar
• López-Expósito, I., Quirós, A., Amigo, L. and Recio, I. (2007). Casein hydrolysates as a source of antimicrobial, antioxidant and antihypertensive peptides. Lait. 87(4–5):241–249. doi: 10.1051/lait:2007019
   Google Scholar
• López-Fandiño, R., Otte, J. and van Camp, J. (2006). Physiological, chemical and technological aspects of milk-protein-derived peptides with antihypertensive and ACE-inhibitory activity. Int. Dairy J. 16(11):1277–1293. doi: 10.1016/j.idairyj.2006.06.004
   Web of Science ®Google Scholar
• Maehashi, K., Matano, M., Wang, H., Vo, L. A., Yamamoto, Y. and Huang, L. (2008). Bitter peptides activate hTAS2Rs, the human bitter receptors. Biochem. Biophys. Res. Commun. 365(4):851–855. doi: 10.1016/j.bbrc.2007.11.070
   PubMed Web of Science ®Google Scholar
• Malkoski, M., Dashper, S. G., O'Brien-Simpson, N. M., Talbo, G. H., Macris, M., Cross, K. J. and Reynolds, E. C. (2001). Kappacin, a novel antibacterial peptide from bovine milk. Antimicrob. Agents Chemother. 45(8):2309–2315. doi: 10.1128/AAC.45.8.2309-2315.2001
   PubMed Web of Science ®Google Scholar
• McCann, K. B., Shiell, B. J., Michalski, W. P., Lee, A., Wan, J., Roginski, H. and Coventry, M. J. (2005). Isolation and characterisation of antibacterial peptides derived from the f(164–207) region of bovine αS2-casein. Int. Dairy J. 15(2):133–143. doi: 10.1016/j.idairyj.2004.06.008
   Web of Science ®Google Scholar
• Mehra, T., Köberle, M., Braunsdorf, C., Mailänder-Sanchez, D., Borelli, C. and Schaller, M. (2012). Alternative approaches to antifungal therapies. Exp. Dermatol. 21(10):778–782. doi: 10.1111/exd.12004
   PubMed Web of Science ®Google Scholar
• Meisel, H. and FitzGerald, R. J. (2003). Biofunctional peptides from milk proteins: Mineral binding and cytomodulatory effects. Curr. Pharm. Des. 9(16):1289–1295.
   PubMed Web of Science ®Google Scholar
• Mellander, O. (1950). The physiological importance of the casein phosphopeptide calcium salts. II. Peroral calcium dosage of infants. Acta Soc. Med. Ups. 55(5–6):247–255.
   PubMedGoogle Scholar
• Mendanha, D. V., Ortiz, S. E. M., Favaro-Trindade, C. S., Mauri, A., Monterrey-Quintero, E. S. and Thomazini, M. (2009). Microencapsulation of casein hydrolysate by complex coacervation with SPI/pectin. Food Res. Int. 42(8):1099–1104. doi: 10.1016/j.foodres.2009.05.007
   Web of Science ®Google Scholar
• Mielnik, M. B., Aaby, K. and Skrede, G. (2003). Commercial antioxidants control lipid oxidation in mechanically deboned turkey meat. Meat Sci. 65(3):1147–1155. doi: 10.1016/S0309-1740(02)00345-5
   PubMed Web of Science ®Google Scholar
• Mills, S., Ross, R. P., Hill, C., Fitzgerald, G. F. and Stanton, C. (2011). Milk intelligence: Mining milk for bioactive substances associated with human health. Int. Dairy J. 21(6):377–401. doi: 10.1016/j.idairyj.2010.12.011
   Web of Science ®Google Scholar
• Minkiewicz, P., Dziuba, J., Iwaniak, A., Dziuba, M. and Darewicz, M. (2008). BIOPEP database and other programs for processing bioactive peptide sequences. J. AOAC Int. 91(4):965–980.
   PubMed Web of Science ®Google Scholar
• Neklyudov, A. D., Ivankin, A. N. and Berdutina, A. V. (2000). Production and purification of protein hydrolysates (review). Appl. Biochem. Microbiol. 36(4):317–324. doi: 10.1007/BF02738038
   Web of Science ®Google Scholar
• Ney, K. H. (1971). Prediction of bitterness of peptides from their amino acid composition. Z. Lebensm. Unters. Forsch. 147(2):64–68. doi: 10.1007/BF01879606
   Google Scholar
• Nguyen, L. T., Haney, E. F. and Vogel, H. J. (2011). The expanding scope of antimicrobial peptide structures and their modes of action. Trends Biotechnol. 29(9):464–472. doi: 10.1016/j.tibtech.2011.05.001
   PubMed Web of Science ®Google Scholar
• Oren, Z., Hong, J. and Shai, Y. (1997). A repertoire of novel antibacterial diastereomeric peptides with selective cytolytic activity. J. Biol. Chem. 272(23):14643–14649. doi: 10.1074/jbc.272.23.14643
   PubMed Web of Science ®Google Scholar
• Otoni, C. G., Espitia, P. J. P., Avena-Bustillos, R. J. and McHugh, T. H. (2016). Trends in antimicrobial food packaging systems: Emitting sachets and absorbent pads. Food Res. Int. 83:60–73.doi: 10.1016/j.foodres.2016.02.018
   Web of Science ®Google Scholar
• Pathak, N., Salas-Auvert, R., Ruche, G., Janna, M. H., McCarthy, D. and Harrison, R. G. (1995). Comparison of the effects of hydrophobicity, amphiphilicity, and α-helicity on the activities of antimicrobial peptides. Proteins: Struct. Funct. Genet. 22(2):182–186. doi: 10.1002/prot.340220210
   PubMed Web of Science ®Google Scholar
• Pellegrini, A., Dettling, C., Thomas, U. and Hunziker, P. (2001). Isolation and characterization of four bactericidal domains in the bovine β-lactoglobulin. Biochim. Biophys. Acta, Gen. Subj. 1526(2):131–140. doi: 10.1016/S0304-4165(01)00116-7
   PubMed Web of Science ®Google Scholar
• Pellegrini, A., Thomas, U., Bramaz, N., Hunziker, P. and Von Fellenberg, R. (1999). Isolation and identification of three bactericidal domains in the bovine α-lactalbumin molecule. Biochim. Biophys. Acta Gen. Subj. 1426(3):439–448. doi: 10.1016/S0304-4165(98)00165-2
   PubMed Web of Science ®Google Scholar
• Peng, X., Kong, B., Xia, X. and Liu, Q. (2010). Reducing and radical-scavenging activities of whey protein hydrolysates prepared with Alcalase. Int. Dairy J. 20(5):360–365. doi: 10.1016/j.idairyj.2009.11.019
   Web of Science ®Google Scholar
• Peng, X., Xiong, Y. L. 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. doi: 10.1016/j.foodchem.2008.07.068
   Web of Science ®Google Scholar
• Pescuma, M., Hébert, E. M., Haertlé, T., Chobert, J. M., Mozzi, F. and Font De Valdez, G. (2015). Lactobacillus delbrueckii subsp. bulgaricus CRL 454 cleaves allergenic peptides of β-lactoglobulin. Food Chem. 170:407–414.doi: 10.1016/j.foodchem.2014.08.086
   PubMed Web of Science ®Google Scholar
• Phanturat, P., Benjakul, S., Visessanguan, W. and Roytrakul, S. (2010). Use of pyloric caeca extract from bigeye snapper (Priacanthus macracanthus) for the production of gelatin hydrolysate with antioxidative activity. LWT–Food Sci. Technol. 43(1):86–97. doi: 10.1016/j.lwt.2009.06.010
   Web of Science ®Google Scholar
• Pichereau, C. and Allary, C. (2005). Therapeutic peptides under the spotlight. EBR Eur. Biopharm. Rev. (WINTER):88–93.
   Google Scholar
• Pihlanto-Leppälä, A. (2000). Bioactive peptides derived from bovine whey proteins: Opioid and ace-inhibitory peptides. Trends Food Sci. Technol. 11(9–10):347–356. doi: 10.1016/S0924-2244(01)00003-6
   Web of Science ®Google Scholar
• Pihlanto, A. (2006). Antioxidative peptides derived from milk proteins. Int. Dairy J. 16(11):1306–1314. doi: 10.1016/j.idairyj.2006.06.005
   Web of Science ®Google Scholar
• Qian, B., Xing, M., Cui, L., Deng, Y., Xu, Y., Huang, M. and Zhang, S. (2011). Antioxidant, antihypertensive, and immunomodulatory activities of peptide fractions from fermented skim milk with Lactobacillus delbrueckii ssp. bulgaricus LB340. J. Dairy Res. 78(1):72–79.
   PubMed Web of Science ®Google Scholar
• Rahaman, T., Vasiljevic, T. and Ramchandran, L. (2016). Effect of processing on conformational changes of food proteins related to allergenicity. Trends Food Sci. Technol. 49:24–34.doi: 10.1016/j.tifs.2016.01.001
   Web of Science ®Google Scholar
• Rahimi, R., Nikfar, S., Larijani, B. and Abdollahi, M. (2005). A review on the role of antioxidants in the management of diabetes and its complications. Biomed. Pharmacother. 59(7):365–373. doi: 10.1016/j.biopha.2005.07.002
   PubMed Web of Science ®Google Scholar
• Rajapakse, N., Mendis, E., Jung, W. K., Je, J. Y. and Kim, S. K. (2005). Purification of a radical scavenging peptide from fermented mussel sauce and its antioxidant properties. Food Res. Int. 38(2):175–182. doi: 10.1016/j.foodres.2004.10.002
   Web of Science ®Google Scholar
• Ranathunga, S., Rajapakse, N. and Kim, S. K. (2006). Purification and characterization of antioxidative peptide derived from muscle of conger eel (Conger myriaster). Eur. Food Res. Technol. 222(3–4):310–315. doi: 10.1007/s00217-005-0079-x
   Web of Science ®Google Scholar
• Recio, I. and Visser, S. (1999a). Identification of two distinct antibacterial domains within the sequence of bovine αs2-casein. Biochim. Biophys. Acta Gen. Subj. 1428(2–3):314–326. doi: 10.1016/S0304-4165(99)00079-3
   PubMed Web of Science ®Google Scholar
• Recio, I. and Visser, S. (1999b). Two ion-exchange chromatographic methods for the isolation of antibacterial peptides from lactoferrin. In situ enzymatic hydrolysis on an ion-exchange membrane. J. Chromatogr. A. 831(2):191–201. doi: 10.1016/S0021-9673(98)00950-9
   PubMed Web of Science ®Google Scholar
• Reddi, S., Kapila, R., Dang, A. K. and Kapila, S. (2012). Evaluation of allergenic response of milk bioactive peptides using mouse mast cell. Milchwissenschaft. 67(2):189–191.
   Google Scholar
• Ren, J., Zhao, M., Shi, J., Wang, J., Jiang, Y., Cui, C., Kakuda, Y. and Xue, S. J. (2008). Purification and identification of antioxidant peptides from grass carp muscle hydrolysates by consecutive chromatography and electrospray ionization-mass spectrometry. Food Chem. 108(2):727–736. doi: 10.1016/j.foodchem.2007.11.010
   PubMed Web of Science ®Google Scholar
• Rival, S. G., Boeriu, C. G. and Wichers, H. J. (2001). Caseins and casein hydrolysates. 2. Antioxidative properties and relevance to lipoxygenase inhibition. J. Agric. Food. Chem. 49(1):295–302. doi: 10.1021/jf0003911
   PubMed Web of Science ®Google Scholar
• Rizzello, C. G., Losito, I., Gobbetti, M., Carbonara, T., De Bari, M. D. and Zambonin, P. G. (2005). Antibacterial activities of peptides from the water-soluble extracts of Italian cheese varieties. J. Dairy Sci. 88(7):2348–2360.
   PubMed Web of Science ®Google Scholar
• Saadi, S., Saari, N., Anwar, F., Hamid, A. A. and Ghazali, H. M. (2015). Recent advances in food biopeptides: Production, biological functionalities and therapeutic applications. Biotechnol. Adv. 33(1):80–116. doi: 10.1016/j.biotechadv.2014.12.003
   PubMed Web of Science ®Google Scholar
• Sah, B. N. P., Vasiljevic, T., McKechnie, S. and Donkor, O. N. (2014). Effect of probiotics on antioxidant and antimutagenic activities of crude peptide extract from yogurt. Food Chem. 156:264–270. doi: 10.1016/j.foodchem.2014.01.105
   PubMed Web of Science ®Google Scholar
• Sah, B. N. P., Vasiljevic, T., McKechnie, S. and Donkor, O. N. (2015a). Effect of refrigerated storage on probiotic viability and the production and stability of antimutagenic and antioxidant peptides in yogurt supplemented with pineapple peel. J. Dairy Sci. 98(9):5905–5916. doi: 10.3168/jds.2015-9450
   PubMed Web of Science ®Google Scholar
• Sah, B. N. P., Vasiljevic, T., McKechnie, S. and Donkor, O. N. (2015b). Identification of anticancer peptides from bovine milk proteins and their potential roles in management of cancer: A critical review. Compr. Rev. Food Sci. Food Saf. 14(2):123–138. doi: 10.1111/1541-4337.12126
   PubMed Web of Science ®Google Scholar
• Sah, B. N. P., Vasiljevic, T., McKechnie, S. and Donkor, O. N. (2016a). Antibacterial and antiproliferative peptides in synbiotic yogurt–Release and stability during refrigerated storage. J. Dairy Sci. 99(6):4233–4242. doi: 10.3168/jds.2015-10499
   PubMed Web of Science ®Google Scholar
• Sah, B. N. P., Vasiljevic, T., McKechnie, S. and Donkor, O. N. (2016b). Effect of pineapple waste powder on probiotic growth, antioxidant and antimutagenic activities of yogurt. J Food Sci Technol. 53(3):1698–1708. doi: 10.1007/s13197-015-2100-0
   PubMed Web of Science ®Google Scholar
• Sah, B. N. P., Vasiljevic, T., McKechnie, S. and Donkor, O. N. (2016c). Physicochemical, textural and rheological properties of probiotic yogurt fortified with fibre-rich pineapple peel powder during refrigerated storage. LWT–Food Sci. Technol. 65:978–986.doi: 10.1016/j.lwt.2015.09.027
   Web of Science ®Google Scholar
• Sah, B. N. P., Vasiljevic, T., McKechnie, S. and Donkor, O. N. (2016d). Antioxidant peptides isolated from synbiotic yoghurt exhibit antiproliferative activities against HT-29 colon cancer cells. Int. Dairy J. 63:99–106. doi: 10.1016/j.idairyj.2016.08.003
   Web of Science ®Google Scholar
• Saha, B. C. and Hayashi, K. (2001). Debittering of protein hydrolyzates. Biotechnol. Adv. 19(5):355–370. doi: 10.1016/S0734-9750(01)00070-2
   PubMed Web of Science ®Google Scholar
• Sakanaka, S., Tachibana, Y., Ishihara, N. and Juneja, L. R. (2005). Antioxidant properties of casein calcium peptides and their effects on lipid oxidation in beef homogenates. J. Agric. Food. Chem. 53(2):464–468.
   PubMed Web of Science ®Google Scholar
• Sarmadi, B. H. and Ismail, A. (2010). Antioxidative peptides from food proteins: A review. Peptides. 31(10):1949–1956. doi: 10.1016/j.peptides.2010.06.020
   PubMed Web of Science ®Google Scholar
• Sedaghati, M., Ezzatpanah, H., Boojar, M. M. A., Ebrahimi, M. T. and Aminafshar, M. (2014). Plasmin digest of κ-casein as a source of antibacterial peptides. J. Dairy Res. 81(2):245–251. doi: 10.1017/S0022029914000120
   PubMed Web of Science ®Google Scholar
• Segura-Campos, M., Chel-Guerrero, L., Betancur-Ancona, D. and Hernandez-Escalante, V. M. (2011). Bioavailability of bioactive peptides. Food Rev. Int. 27(3):213–226. doi: 10.1080/87559129.2011.563395
   Web of Science ®Google Scholar
• Sharma, N. (2014). Free radicals, antioxidants and disease. Biol. Med. 6(3):doi: 10.4172/0974-8369.1000214
   Google Scholar
• Sienkiewicz-Szlapka, E., Jarmolowska, B., Krawczuk, S., Kostyra, E., Kostyra, H. and Bielikowicz, K. (2009). Transport of bovine milk-derived opioid peptides across a Caco-2 monolayer. Int. Dairy J. 19(4):252–257. doi: 10.1016/j.idairyj.2008.10.007
   Web of Science ®Google Scholar
• Srigiridhar, K., Nair, K. M., Subramanian, R. and Singotamu, L. (2001). Oral repletion of iron induces free radical mediated alterations in the gastrointestinal tract of rat. Mol. Cell. Biochem. 219(1–2):91–98. doi: 10.1023/A:1011023111048
   PubMed Web of Science ®Google Scholar
• Su, R., Qi, W., He, Z., Yuan, S. and Zhang, Y. (2007). Pancreatic hydrolysis of bovine casein: Identification and release kinetics of phosphopeptides. Food Chem. 104(1):276–286. doi: 10.1016/j.foodchem.2006.11.039
   Web of Science ®Google Scholar
• Suetsuna, K., Ukeda, H. and Ochi, H. (2000). Isolation and characterization of free radical scavenging activities peptides derived from casein. J. Nutr. Biochem. 11(3):128–131. doi: 10.1016/S0955-2863(99)00083-2
   PubMed Web of Science ®Google Scholar
• Sun, J., He, H. and Bi, J. X. (2004). Novel antioxidant peptides from fermented mushroom Ganoderma lucidum. J. Agric. Food. Chem. 52(21):6646–6652. doi: 10.1021/jf0495136
   PubMed Web of Science ®Google Scholar
• Tang, W., Yuan, H., Zhang, H., Wang, L., Qian, H. and Qi, X. (2015). An antimicrobial peptide screened from casein hydrolyzate by Saccharomyces cerevisiae cell membrane affinity method. Food Control. 50:413–422.doi: 10.1016/j.foodcont.2014.09.030
   Web of Science ®Google Scholar
• Tekiner-Gulbas, B., Westwell, A. D. and Suzen, S. (2013). Oxidative stress in carcinogenesis: New synthetic compounds with dual effects upon free radicals and cancer. Curr. Med. Chem. 20(36):4451–4459. doi: 10.2174/09298673113203690142
   PubMed Web of Science ®Google Scholar
• van Aardt, M., Duncan, S. E., Long, T. E., O'Keefe, S. F., Marcy, J. E. and Sims, S. R. (2004). Effect of antioxidants on oxidative stability of edible fats and oils: Thermogravimetric analysis. J. Agric. Food. Chem. 52(3):587–591. doi: 10.1021/jf030304f
   PubMed Web of Science ®Google Scholar
• Viljanen, K., Kivikari, R. and Heinonen, M. (2004). Protein-lipid interactions during liposome oxidation with added anthocyanin and other phenolic compounds. J. Agric. Food. Chem. 52(5):1104–1111. doi: 10.1021/jf034785e
   PubMed Web of Science ®Google Scholar
• Vizioli, J. and Salzet, M. (2002). Antimicrobial peptides from animals: focus on invertebrates. Trends Pharmacol. Sci. 23(11):494–495. doi: 10.1016/S0165-6147(02)02105-3
   PubMed Web of Science ®Google Scholar
• Xie, N., Wang, C., Ao, J. and Li, B. (2013). Non-gastrointestinal-hydrolysis enhances bioavailability and antioxidant efficacy of casein as compared with its in vitro gastrointestinal digest. Food Res. Int. 51(1):114–122. doi: 10.1016/j.foodres.2012.12.001
   Web of Science ®Google Scholar
• Yamauchi, K., Tomita, M., Giehl, T. J., and Ellison III, R. T. (1993). Antibacterial activity of lactoferrin and a pepsin-derived lactoferrin peptide fragment. Infect. Immun. 61(2):719–728.
   PubMed Web of Science ®Google Scholar
• Yeaman, M. R. and Yount, N. Y. (2003). Mechanisms of antimicrobial peptide action and resistance. Pharmacol. Rev. 55(1):27–55. doi: 10.1124/pr.55.1.2
   PubMed Web of Science ®Google Scholar
• Zucht, H. D., Raida, M., Adermann, K., Mägert, H. J. and Forssmann, W. G. (1995). Casocidin-I: a casein-αs2 derived peptide exhibits antibacterial activity. FEBS Lett. 372(2–3):185–188. doi: 10.1016/0014-5793(95)00974-E
   PubMed Web of Science ®Google Scholar