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Biological and Physiological Activities of Whey Proteins and Their Derivatives

Year 2010, Volume: 8 Issue: 1, 23 - 31, 01.02.2010

Abstract

Milk proteins have received increasing attention as potential ingredients of functional foods reducing or preventing the risk of diet-related diseases, such as cardiovascular disease, diabetes type two and obesity. Due to these properties, studies have recently been focused on milk proteins and their bioactive peptides. Such peptides are inactive within the sequence of the milk protein and can be released by digestive enzymes during gastrointestinal transit or by starter cultures used for fermentation or ripening of dairy products. Bioactive peptides have been defined as specific protein fragments that have a positive impact on body functions and may ultimately influence human health. Whey contains a multitude of biologically active proteins and peptides. Physiologically active serum proteins are serum albumine, immunoglobulins, proteose-peptone, lactoferrin, lactoperoxidase and growth factors. In addition to these, enzymatic degradation of serum proteins releases a number of bioactive peptides such as α-lactophorin, β-lactophorin, βlactotensin, lactokinin, albutensin, serophorin and lactoferricin

References

  • Regester, G.O., McIntosh, G.H., Lee, V.W.K., Smithers, G.W. 1996. Whey proteins as nutritional and functional food ingredients. Food Australia 48: 123-127.
  • Walzem R.L., Dillard C.J., German J.B. 2002. Whey components: functionalities for mammalian nutrition: what we know and what we may be overlooking. Critical Review on Food Science and Nutrition 42: 353-375.
  • Marshall, K. 2004. Therapeutic applications of whey protein. Alternative Medicine Review 9:136-156.
  • Smithers, G.W. 2008. Whey and whey proteins— From ‘gutter-to-gold’. International Dairy Journal 18: 695-704.
  • Smilowitz, J.T., Dillard, C.J., German, J.B. 2005. Milk beyond essential nutrients: The metabolic food. Australian Journal of Dairy Technology 60: 77-83.
  • Moller, N. P., Scholz-Ahrens, K. E., Roos, N., Schrezenmeir, J. 2008. Bioactive peptides and proteins from foods: Indication for health effects. European Journal of Nutrition 47: 171-182.
  • McIntosh, G.H., Royle, P.J., Le Leu, R.K., Regester, G. O., Johnson, M. A., Grinsted, R. L., et al. 1998. Whey proteins as functional food ingredients? International Dairy Journal 8: 425-434.
  • [8] McMahon, D.J., Oommen, B.S. 2008. Supramolecular structure of the casein micelle. Journal of Dairy Science 91:1709–1721.
  • de Wit, J.N. 1998. Nutritional and functional characteristics of whey proteins in food products. Journal of Dairy Science 81: 597-608.
  • Aimutis, R.W. 2004. Bioactive properties of milk proteins with particular focus on anticariogenesis. The Journal of Nutrition 20: 989-995.
  • FAO, 2006. Food Outlook no. 2, December 2006. http://www.faoorg/docrep/009/.
  • [Özen, A.E., Kılıç, M. 2007. Peynir altı suyundan elde edilen serum proteinlerinin fonksiyonel özellikleri. Gıda Teknolojileri Elektronik Dergisi 3: 45-49.
  • Ha, E., Zemel, M.B. 2003. Functional properties of whey, whey components, and essential amino acids: Mechanisms underlying health benefits for active people. Journal of Nutritional Biochemistry 14: 251-258.
  • Zemel, M.B. 2004. Role of calcium and dairy products in energy partitioning and weight management. American Journal of Clinical Nutrition 79(Suppl.): 907S-912S.
  • Kimball, S.R. 2002. Regulation of global and specific mRNA translation by amino acids. Journal of Nutrition132: 883-886.
  • Shoveller, A. K., Stoll, B., Ball, R. O., Burrin, D. G. 2005. Nutritional and functional importance of intestinal sulphur amino acid metabolism. Journal of Nutrition 135: 1609-1612.
  • Meisel, H., Schlimme, E. 1996. Bioactive peptides derived from milk proteins: Ingredients of functional foods? Forschungsberichte 48: 343-357.
  • Milchwirtschaftliche
  • Korhonen, H., Pihlanto-Leppala, A., Rantamaki, P., Tupasela, T. 1998. Impact of processing on bioactive proteins and peptides. Trends in Food Science and Technology 9: 307-319.
  • Shah, P.N. 2000. Effects of milk-derived bioactives: an overview. British Journal of Nutrition 84(Suppl.): 1, S3-S10.
  • Pihlanto-Leppala, A., Koskinen, P., Piilola, K., Tupasela, T., Korhonen, H. 2000. Angiotensin I- converting enzyme inhibitory properties of whey protein digests: Concentration and characterization of active peptides. Journal of Dairy Research 67: 53-64.
  • Lee, Y.M., Skurk, T., Hennig, M., Hauner, H. 2007. Effect of a milk drink supplemented with whey peptides on blood pressure in patients with mild hypertension. European Journal of Nutrition 46: 21- 27.
  • Karagözlü, C., Bayarer, M. 2004. Peyniraltı Suyu Proteinlerinin Fonksiyonel Özellikleri Ve Sağlık Üzerine Etkileri. Ege Üniv. Ziraat Fakültesi Dergisi 41: 197-207.
  • Bounous, G., Batist, G., Gold, P. 1991. Whey proteins in cancer prevention. Cancer Letters 57: 91-94.
  • Dillar, C.J., Walzem, R.L., German, J.B. 2002. Whey components: Millenia of Evolution create functionalities for mammalian nutrition. Critical Review on Food Science and Nutrition 42: 353-375.
  • Haque, E., Chand, R. 2008. Antihypertensive and antimicrobial bioactive peptides from milk proteins. European Food Research and Technology 227: 7- 15.
  • Nutte, R.L., Kettering, J.D., Aprecio, R.M., Weeks, D.A., Gridley, D.S. 1990. Effect of dietary fat and proetin on DMH induced tumor development and immune responses. Nutrition and Cancer 13: 141- 152.
  • Mcintosh, G. H., G. D. Regester, R. K. Lelue, P. J. Royle, and G. W. Smithers. 1995. Dairy proteins protect against dimethylhydrazine-induced intestinal cancers in rats. Journal of Nutrition 125:809-816.
  • Pins, J. J., Keenan, J. M. 2006. Effects of whey peptides on cardiovascular disease risk factors. Journal of Clinical Hypertension 8: 775-782.
  • Papiz, M.Z., Sawyer, L., Eliopoulas, E.E., North, A.C., Findlay, J.B., Sivaprosadaro, R., Jones, T.A., Newcomer, M.E., Kraulis, P.J. 1986. The structure of β-lactoglobulin and its similarity to plasma retinol- binding protein. Nature (Lond.) 324: 383-385.
  • Gold, P., Inventors G.B., 1993. Method of treatment of HIV-seropositive individuals with dietary whey proteins. WHO Pat. No. 93/20831.
  • Fleet, J.C. 1995. New role for lactoferrin: DNA- binding and transcription activation. Nutrition Reviews 53: 226-227.
  • Cross, M.L., Gill, H.S. 2000. Immunomodulatory properties of milk. British Journal of Nutrition 84:S81-S89.
  • Brock, J.H. 1980. Lactoferrin in human milk: its role in iron absorption and protection against enteric infection in the newborn infant. Archives of Disease in Childhood 55: 417-421.
  • Tsuji, S., Hirata, Y., Mukai, F., Ohtagaki, S. 1990. Comparison of lactoferrin content in colostrum between different cattle breeds. Journal of Dairy Science 73: 125-128.
  • Viljoen, M. 1995. Lactoferrin: a general review. Haematologica 80: 252-267.
  • Steijns, J.M., van Hooijdonk, A.C. 2000. Occurrence, structure, biochemical properties and technological characteristics of lactoferrin. British Journal of Nutrition 84:S11-S17.
  • Tomita, M., Bellamy, W., Takase, M., Yamauchi, K., Wakabayashi, H., Kawase, K. 1991. Potent antibacterial peptides generated by pepsin digestion of bovine lactoferrin. Journal of Dairy Science 74: 4137-4142.
  • Bezault, J., Bhimani, R., Wiprovnick, J., Furmanski, P. 1994. Human lactoferrin inhibits growth of solid tumors metastases in mice. Cancer Research 54: 2310- 2312. of experimental
  • Shimazaki, K. 2000. Lactoferrin: a marvelous protein in milk? Animal Science of Journal 71: 329- 347.
  • Cornish, J. 2004. Lactoferrin promotes bone growth. BioMetals 17: 331–335.
  • Cornish, J., Palmano, K., Callon, K.E., Watson, M., Lin, J.M., Valenti, P., Naot, D., Grey, A.B., Reid, I.R. 2006. Lactoferrin and bone; structure–activity relationships. Biochemistry of Cell Biology 84: 297- 302.
  • Kussendrager, K.D., van Hooijdonk, A.C. 2000. Lactoperoxidase: occurrence, mechanism of action and applications. British Journal of Nutrition 84: S19-S25. properties
  • Tenovuo, J. 2002. Clinical applications of antimicrobial lysozyme and lactoferrin in xerostomia: Efficacy and safety. Oral Diseases 8: 23-29. lactoperoxidase
  • Boots, J.W., Floris, R. 2006. Lactoperoxidase: From catalytic mechanism to practical applications. International Dairy Journal 16: 1272-1276.
  • Manso, M. A., Lopez-Fandino, R. 2004. κ-casein macropeptides Physicochemical, technological features for possible uses. Food Reviews International 20: 329–355. whey: and nutritional
  • Kawasaki, Y., Isoda, H., Tanimoto, M., Dosako, S., Idota, T., Ahiko, K. 1992. Inhibition by lactoferrin and κ-casein glycomacropeptide of binding of cholera Biotechnology and Biochemistry 56: 195–198.
  • Kawasaki, Y., Isoda, K., Shinmoto, H., Tanimoto, M., Dosako, S., Idota, T., Nakajima, I. 1993. Inhibition by κ-casein glycomacropeptide and lactoferrin of influenza virus hemagglutination. Bioscience, Biotechnology and Biochemistry 57: 1214-1215.
  • Poch, M., Bezkorovainy, A. 1991. Bovine milk κ- casein trypsin digest is a growth enhancer for the genus Bifidobacterium. Journal of Agriculture and Food Chemistr, 39: 73-77.
  • Minervini, F., Algaron, F., Rizella, C.G., Fox, P.F., Monnet, V., Gogetti, M. 2003. Angiotensin I- converting-enzyme-inhibitory and antibacterial peptides from Lactobacillus helveticus PR4 proteinase-hydrolyzed caseins of milk from six species. Applied and Environmental Microbiology 69: 5297-5305.
  • 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.
  • Meisel, H. 2005. Biochemical properties of peptides encrypted in bovine milk proteins. Current Medicinal Chemistry 12: 1905-1919.
  • Mellander, O. 1950. The physiological importance of the casein phosphopeptide calcium salts II. Peroral calcium dosage of infants. Acta of the Society of Medicine of Uppsala 55: 247-255.
  • FitzGerald, R.J., Meisel, H., 2000. Milk protein- derived converting enzyme. British Journal of Nutrition 84: S33-S37. of angiotensin-I
  • Pihlanto, A. 2006. Antioxidative peptides derived from milk proteins. International Dairy Journa, 16: 1306-1314.
  • Hartmann, R., Meisel, H. 2007. Food-derived peptides with biological activity: From research to food applications. Current Opinion in Biotechnology 18: 1-7.
  • Korhonen H., 2009. Milk-derived bioactive peptides: From science to applications. Journal of Functional Foods (in press), doi:10.1016/j.jff.2009.01.007.
  • Mullally, M. M., Meisel, H., FitzGerald, R. J. 1997. Identification of a novel angiotensin-I converting enzyme inhibitory peptide corresponding to a tryptic fragment of bovine β lactoglobulin. FEBS Letter, 402: 99-101.
  • Clare, D.A., Swoisgoodt. 2000. Bioactive Milk Peptides: A Prospectus. Journal of Dairy Science 83: 1187-1195.
  • Roufik, S., Gauthier, S. F., Turgeon, S. L. 2006. In vitro digestibility of bioactive peptides derived from bovine β-lactoglobulin. International Dairy Journal 16: 294-302.
  • Kınık, Ö., Gürsoy, O. 2002. Süt proteinleri kaynaklı biyoaktif peptitler. Mühendislik Bilimleri Dergisi 8: 195-208.
  • Silva, S.V., Malcata, F.X. 2005. Caseins as source of bioactive peptides. International Dairy Journa, 15: 1-15.
  • Meisel, H., 1998. Overview on Milk Protein-Derived Peptides. International of Dairy Journal 8: 363-373.
  • Meisel, H., Bockelmann, W. 1999. Bioactive peptides encrypted in milk proteins: Proteolytic activation and thropho-functional properties. Antonie van Leeuwenhoek 76: 207-215.
  • Paakkari, I., Jarvinen, A., Antila, P., Mattila, M.J., Pihlanto-Leppalla, A. 1994. Opoid effects of the milk whey-protein derived peptides α- and β- lactorphin in β-casomorphins and related peptides. Recent development (Brantl, V., Teschemacher, H., eds.), VCH, Weicheim, pp 33-37. [65] Kitts, D.D., Caseinophosphopeptides bioavailability. Trends in Food Science and Technolog 3: 31-35. Y.V., 1992. calcium and
  • Ariyoshi, Y., 1993. Angiotensin-converting-enzyme inhibitors derived from food proteins. Trends in Food Science and Technolog 4: 139-144.
  • Gobbetti, M., Minervini, F., Rizzello, C.G. 2004. Angiotensin I converting-enzyme-inhibitory and antimicrobial bioactive peptides. International Journal of Dairy Technolog 57: 172-188.
  • Gauthier, S. F., Pouliot, Y., Saint-Sauveur, D. 2006. Immunomodulatory peptides obtained by the enzymatic hydrolysis of whey proteins. International Dairy Journal 16: 1315-1323.
  • Faith, R.E., Liang, H.J., Murgo, A.J., Plotnikoff, N.P., enkephalins: enhancement of human natural killer (NK) cell activity in vitro. Clinical Immunology and Immunopathology 31: 412-418. with
  • Zimecki, M., Kruzel, M.L. 2007. Milk-derived proteins and peptides of potential therapeutic and nutritive value. Journal of Experimental Therapy and Oncolog 6: 89-106.
  • Pouliot, Y., Gauthier, S.F., Groleau, P.E. 2006. Membrane-based fractionation and purification strategies for bioactive peptides. In Y. Mine, F. Shahidi (Eds.). Nutraceutical proteins and peptides in health and disease nutraceutical science and technology (Vol. 4). Boca Raton, FL: Taylor and Francis, pp. 639-658.
  • Korhonen, H., Pihlanto, A. 2007. Technological options for the production of health-promoting proteins and peptides derived from milk and colostrum. Current Pharmaceutical Design 13: 829- 843.

Süt Serum Proteinleri ve Türevlerinin Biyolojik ve Fizyolojik Aktiviteleri

Year 2010, Volume: 8 Issue: 1, 23 - 31, 01.02.2010

Abstract

Süt proteinlerine, kalp-damar rahatsızlıkları, tip II diyabet ve obezite gibi beslenmeye bağlı olarak ortaya çıkan hastalıkların görülme riskinin azaltılmasında veya önlenmesinde potansiyel fonksiyonel gıda bileşenleri olarak oldukça fazla ilgi duyulmaktadır. Buna bağlı olarak son yıllarda süt proteinleri ve bunlardan kaynaklanan biyoaktif peptidler üzerinde çalışmalar yoğunlaşmıştır. Biyoaktif peptidler, süt protein molekülerinin içerisinde inaktif olarak bulunan, ancak sütün tüketilmesiyle beraber sindirim sisteminde parçalanması veya süt ürünlerinin fermantasyonu ya da olgunlaşması için kullanılan starter kültürlerin aktiviteleri sonucunda açığa çıkmaktadırlar. Biyoaktif peptidler, vücut fonksiyonları ve sağlık üzerine doğrudan pozitif etkileri bulunan proteinler olarak tanımlanmaktadır. Serum proteinleri, biyoaktif özellikteki birçok protein ve peptidleri içermektedir. Serum albümini, immunoglobulinler, proteoz-peptonlar, laktoferrin, laktoperoksidaz ve büyüme faktörleri fizyolojik aktiviteye sahip olan proteinlerdir. Bunların yanı sıra, serum proteinlerinin enzimatik parçalanması sonucunda da α-laktoforin, β-laktoforin, β-laktotensin, laktokinin, albutensin, seroforin, laktoferrisin gibi birçok biyoaktif peptid açığa çıkmaktadır

References

  • Regester, G.O., McIntosh, G.H., Lee, V.W.K., Smithers, G.W. 1996. Whey proteins as nutritional and functional food ingredients. Food Australia 48: 123-127.
  • Walzem R.L., Dillard C.J., German J.B. 2002. Whey components: functionalities for mammalian nutrition: what we know and what we may be overlooking. Critical Review on Food Science and Nutrition 42: 353-375.
  • Marshall, K. 2004. Therapeutic applications of whey protein. Alternative Medicine Review 9:136-156.
  • Smithers, G.W. 2008. Whey and whey proteins— From ‘gutter-to-gold’. International Dairy Journal 18: 695-704.
  • Smilowitz, J.T., Dillard, C.J., German, J.B. 2005. Milk beyond essential nutrients: The metabolic food. Australian Journal of Dairy Technology 60: 77-83.
  • Moller, N. P., Scholz-Ahrens, K. E., Roos, N., Schrezenmeir, J. 2008. Bioactive peptides and proteins from foods: Indication for health effects. European Journal of Nutrition 47: 171-182.
  • McIntosh, G.H., Royle, P.J., Le Leu, R.K., Regester, G. O., Johnson, M. A., Grinsted, R. L., et al. 1998. Whey proteins as functional food ingredients? International Dairy Journal 8: 425-434.
  • [8] McMahon, D.J., Oommen, B.S. 2008. Supramolecular structure of the casein micelle. Journal of Dairy Science 91:1709–1721.
  • de Wit, J.N. 1998. Nutritional and functional characteristics of whey proteins in food products. Journal of Dairy Science 81: 597-608.
  • Aimutis, R.W. 2004. Bioactive properties of milk proteins with particular focus on anticariogenesis. The Journal of Nutrition 20: 989-995.
  • FAO, 2006. Food Outlook no. 2, December 2006. http://www.faoorg/docrep/009/.
  • [Özen, A.E., Kılıç, M. 2007. Peynir altı suyundan elde edilen serum proteinlerinin fonksiyonel özellikleri. Gıda Teknolojileri Elektronik Dergisi 3: 45-49.
  • Ha, E., Zemel, M.B. 2003. Functional properties of whey, whey components, and essential amino acids: Mechanisms underlying health benefits for active people. Journal of Nutritional Biochemistry 14: 251-258.
  • Zemel, M.B. 2004. Role of calcium and dairy products in energy partitioning and weight management. American Journal of Clinical Nutrition 79(Suppl.): 907S-912S.
  • Kimball, S.R. 2002. Regulation of global and specific mRNA translation by amino acids. Journal of Nutrition132: 883-886.
  • Shoveller, A. K., Stoll, B., Ball, R. O., Burrin, D. G. 2005. Nutritional and functional importance of intestinal sulphur amino acid metabolism. Journal of Nutrition 135: 1609-1612.
  • Meisel, H., Schlimme, E. 1996. Bioactive peptides derived from milk proteins: Ingredients of functional foods? Forschungsberichte 48: 343-357.
  • Milchwirtschaftliche
  • Korhonen, H., Pihlanto-Leppala, A., Rantamaki, P., Tupasela, T. 1998. Impact of processing on bioactive proteins and peptides. Trends in Food Science and Technology 9: 307-319.
  • Shah, P.N. 2000. Effects of milk-derived bioactives: an overview. British Journal of Nutrition 84(Suppl.): 1, S3-S10.
  • Pihlanto-Leppala, A., Koskinen, P., Piilola, K., Tupasela, T., Korhonen, H. 2000. Angiotensin I- converting enzyme inhibitory properties of whey protein digests: Concentration and characterization of active peptides. Journal of Dairy Research 67: 53-64.
  • Lee, Y.M., Skurk, T., Hennig, M., Hauner, H. 2007. Effect of a milk drink supplemented with whey peptides on blood pressure in patients with mild hypertension. European Journal of Nutrition 46: 21- 27.
  • Karagözlü, C., Bayarer, M. 2004. Peyniraltı Suyu Proteinlerinin Fonksiyonel Özellikleri Ve Sağlık Üzerine Etkileri. Ege Üniv. Ziraat Fakültesi Dergisi 41: 197-207.
  • Bounous, G., Batist, G., Gold, P. 1991. Whey proteins in cancer prevention. Cancer Letters 57: 91-94.
  • Dillar, C.J., Walzem, R.L., German, J.B. 2002. Whey components: Millenia of Evolution create functionalities for mammalian nutrition. Critical Review on Food Science and Nutrition 42: 353-375.
  • Haque, E., Chand, R. 2008. Antihypertensive and antimicrobial bioactive peptides from milk proteins. European Food Research and Technology 227: 7- 15.
  • Nutte, R.L., Kettering, J.D., Aprecio, R.M., Weeks, D.A., Gridley, D.S. 1990. Effect of dietary fat and proetin on DMH induced tumor development and immune responses. Nutrition and Cancer 13: 141- 152.
  • Mcintosh, G. H., G. D. Regester, R. K. Lelue, P. J. Royle, and G. W. Smithers. 1995. Dairy proteins protect against dimethylhydrazine-induced intestinal cancers in rats. Journal of Nutrition 125:809-816.
  • Pins, J. J., Keenan, J. M. 2006. Effects of whey peptides on cardiovascular disease risk factors. Journal of Clinical Hypertension 8: 775-782.
  • Papiz, M.Z., Sawyer, L., Eliopoulas, E.E., North, A.C., Findlay, J.B., Sivaprosadaro, R., Jones, T.A., Newcomer, M.E., Kraulis, P.J. 1986. The structure of β-lactoglobulin and its similarity to plasma retinol- binding protein. Nature (Lond.) 324: 383-385.
  • Gold, P., Inventors G.B., 1993. Method of treatment of HIV-seropositive individuals with dietary whey proteins. WHO Pat. No. 93/20831.
  • Fleet, J.C. 1995. New role for lactoferrin: DNA- binding and transcription activation. Nutrition Reviews 53: 226-227.
  • Cross, M.L., Gill, H.S. 2000. Immunomodulatory properties of milk. British Journal of Nutrition 84:S81-S89.
  • Brock, J.H. 1980. Lactoferrin in human milk: its role in iron absorption and protection against enteric infection in the newborn infant. Archives of Disease in Childhood 55: 417-421.
  • Tsuji, S., Hirata, Y., Mukai, F., Ohtagaki, S. 1990. Comparison of lactoferrin content in colostrum between different cattle breeds. Journal of Dairy Science 73: 125-128.
  • Viljoen, M. 1995. Lactoferrin: a general review. Haematologica 80: 252-267.
  • Steijns, J.M., van Hooijdonk, A.C. 2000. Occurrence, structure, biochemical properties and technological characteristics of lactoferrin. British Journal of Nutrition 84:S11-S17.
  • Tomita, M., Bellamy, W., Takase, M., Yamauchi, K., Wakabayashi, H., Kawase, K. 1991. Potent antibacterial peptides generated by pepsin digestion of bovine lactoferrin. Journal of Dairy Science 74: 4137-4142.
  • Bezault, J., Bhimani, R., Wiprovnick, J., Furmanski, P. 1994. Human lactoferrin inhibits growth of solid tumors metastases in mice. Cancer Research 54: 2310- 2312. of experimental
  • Shimazaki, K. 2000. Lactoferrin: a marvelous protein in milk? Animal Science of Journal 71: 329- 347.
  • Cornish, J. 2004. Lactoferrin promotes bone growth. BioMetals 17: 331–335.
  • Cornish, J., Palmano, K., Callon, K.E., Watson, M., Lin, J.M., Valenti, P., Naot, D., Grey, A.B., Reid, I.R. 2006. Lactoferrin and bone; structure–activity relationships. Biochemistry of Cell Biology 84: 297- 302.
  • Kussendrager, K.D., van Hooijdonk, A.C. 2000. Lactoperoxidase: occurrence, mechanism of action and applications. British Journal of Nutrition 84: S19-S25. properties
  • Tenovuo, J. 2002. Clinical applications of antimicrobial lysozyme and lactoferrin in xerostomia: Efficacy and safety. Oral Diseases 8: 23-29. lactoperoxidase
  • Boots, J.W., Floris, R. 2006. Lactoperoxidase: From catalytic mechanism to practical applications. International Dairy Journal 16: 1272-1276.
  • Manso, M. A., Lopez-Fandino, R. 2004. κ-casein macropeptides Physicochemical, technological features for possible uses. Food Reviews International 20: 329–355. whey: and nutritional
  • Kawasaki, Y., Isoda, H., Tanimoto, M., Dosako, S., Idota, T., Ahiko, K. 1992. Inhibition by lactoferrin and κ-casein glycomacropeptide of binding of cholera Biotechnology and Biochemistry 56: 195–198.
  • Kawasaki, Y., Isoda, K., Shinmoto, H., Tanimoto, M., Dosako, S., Idota, T., Nakajima, I. 1993. Inhibition by κ-casein glycomacropeptide and lactoferrin of influenza virus hemagglutination. Bioscience, Biotechnology and Biochemistry 57: 1214-1215.
  • Poch, M., Bezkorovainy, A. 1991. Bovine milk κ- casein trypsin digest is a growth enhancer for the genus Bifidobacterium. Journal of Agriculture and Food Chemistr, 39: 73-77.
  • Minervini, F., Algaron, F., Rizella, C.G., Fox, P.F., Monnet, V., Gogetti, M. 2003. Angiotensin I- converting-enzyme-inhibitory and antibacterial peptides from Lactobacillus helveticus PR4 proteinase-hydrolyzed caseins of milk from six species. Applied and Environmental Microbiology 69: 5297-5305.
  • 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.
  • Meisel, H. 2005. Biochemical properties of peptides encrypted in bovine milk proteins. Current Medicinal Chemistry 12: 1905-1919.
  • Mellander, O. 1950. The physiological importance of the casein phosphopeptide calcium salts II. Peroral calcium dosage of infants. Acta of the Society of Medicine of Uppsala 55: 247-255.
  • FitzGerald, R.J., Meisel, H., 2000. Milk protein- derived converting enzyme. British Journal of Nutrition 84: S33-S37. of angiotensin-I
  • Pihlanto, A. 2006. Antioxidative peptides derived from milk proteins. International Dairy Journa, 16: 1306-1314.
  • Hartmann, R., Meisel, H. 2007. Food-derived peptides with biological activity: From research to food applications. Current Opinion in Biotechnology 18: 1-7.
  • Korhonen H., 2009. Milk-derived bioactive peptides: From science to applications. Journal of Functional Foods (in press), doi:10.1016/j.jff.2009.01.007.
  • Mullally, M. M., Meisel, H., FitzGerald, R. J. 1997. Identification of a novel angiotensin-I converting enzyme inhibitory peptide corresponding to a tryptic fragment of bovine β lactoglobulin. FEBS Letter, 402: 99-101.
  • Clare, D.A., Swoisgoodt. 2000. Bioactive Milk Peptides: A Prospectus. Journal of Dairy Science 83: 1187-1195.
  • Roufik, S., Gauthier, S. F., Turgeon, S. L. 2006. In vitro digestibility of bioactive peptides derived from bovine β-lactoglobulin. International Dairy Journal 16: 294-302.
  • Kınık, Ö., Gürsoy, O. 2002. Süt proteinleri kaynaklı biyoaktif peptitler. Mühendislik Bilimleri Dergisi 8: 195-208.
  • Silva, S.V., Malcata, F.X. 2005. Caseins as source of bioactive peptides. International Dairy Journa, 15: 1-15.
  • Meisel, H., 1998. Overview on Milk Protein-Derived Peptides. International of Dairy Journal 8: 363-373.
  • Meisel, H., Bockelmann, W. 1999. Bioactive peptides encrypted in milk proteins: Proteolytic activation and thropho-functional properties. Antonie van Leeuwenhoek 76: 207-215.
  • Paakkari, I., Jarvinen, A., Antila, P., Mattila, M.J., Pihlanto-Leppalla, A. 1994. Opoid effects of the milk whey-protein derived peptides α- and β- lactorphin in β-casomorphins and related peptides. Recent development (Brantl, V., Teschemacher, H., eds.), VCH, Weicheim, pp 33-37. [65] Kitts, D.D., Caseinophosphopeptides bioavailability. Trends in Food Science and Technolog 3: 31-35. Y.V., 1992. calcium and
  • Ariyoshi, Y., 1993. Angiotensin-converting-enzyme inhibitors derived from food proteins. Trends in Food Science and Technolog 4: 139-144.
  • Gobbetti, M., Minervini, F., Rizzello, C.G. 2004. Angiotensin I converting-enzyme-inhibitory and antimicrobial bioactive peptides. International Journal of Dairy Technolog 57: 172-188.
  • Gauthier, S. F., Pouliot, Y., Saint-Sauveur, D. 2006. Immunomodulatory peptides obtained by the enzymatic hydrolysis of whey proteins. International Dairy Journal 16: 1315-1323.
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There are 72 citations in total.

Details

Primary Language Turkish
Journal Section Research Article
Authors

Filiz Gür This is me

Melih Güzel This is me

Nilgün Öncül This is me

Zeliha Yıldırım This is me

Metin Yıldırım This is me

Publication Date February 1, 2010
Published in Issue Year 2010 Volume: 8 Issue: 1

Cite

APA Gür, F., Güzel, M., Öncül, N., Yıldırım, Z., et al. (2010). Süt Serum Proteinleri ve Türevlerinin Biyolojik ve Fizyolojik Aktiviteleri. Akademik Gıda, 8(1), 23-31.
AMA Gür F, Güzel M, Öncül N, Yıldırım Z, Yıldırım M. Süt Serum Proteinleri ve Türevlerinin Biyolojik ve Fizyolojik Aktiviteleri. Akademik Gıda. February 2010;8(1):23-31.
Chicago Gür, Filiz, Melih Güzel, Nilgün Öncül, Zeliha Yıldırım, and Metin Yıldırım. “Süt Serum Proteinleri Ve Türevlerinin Biyolojik Ve Fizyolojik Aktiviteleri”. Akademik Gıda 8, no. 1 (February 2010): 23-31.
EndNote Gür F, Güzel M, Öncül N, Yıldırım Z, Yıldırım M (February 1, 2010) Süt Serum Proteinleri ve Türevlerinin Biyolojik ve Fizyolojik Aktiviteleri. Akademik Gıda 8 1 23–31.
IEEE F. Gür, M. Güzel, N. Öncül, Z. Yıldırım, and M. Yıldırım, “Süt Serum Proteinleri ve Türevlerinin Biyolojik ve Fizyolojik Aktiviteleri”, Akademik Gıda, vol. 8, no. 1, pp. 23–31, 2010.
ISNAD Gür, Filiz et al. “Süt Serum Proteinleri Ve Türevlerinin Biyolojik Ve Fizyolojik Aktiviteleri”. Akademik Gıda 8/1 (February 2010), 23-31.
JAMA Gür F, Güzel M, Öncül N, Yıldırım Z, Yıldırım M. Süt Serum Proteinleri ve Türevlerinin Biyolojik ve Fizyolojik Aktiviteleri. Akademik Gıda. 2010;8:23–31.
MLA Gür, Filiz et al. “Süt Serum Proteinleri Ve Türevlerinin Biyolojik Ve Fizyolojik Aktiviteleri”. Akademik Gıda, vol. 8, no. 1, 2010, pp. 23-31.
Vancouver Gür F, Güzel M, Öncül N, Yıldırım Z, Yıldırım M. Süt Serum Proteinleri ve Türevlerinin Biyolojik ve Fizyolojik Aktiviteleri. Akademik Gıda. 2010;8(1):23-31.

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