Food Science of Animal Resources (한국축산식품학회지)

Korean Society for Food Science of Animal Resources (한국축산식품학회)
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Hypoallergenic and Physicochemical Properties of the A2 β-Casein Fractionof Goat Milk

  • Jung, Tae-Hwan (Department of Health and Bio-Convergence, Sahmyook University) ;
  • Hwang, Hyo-Jeong (Biomaterials Research Institute, Sahmyook University) ;
  • Yun, Sung-Seob (R&D Center, Edam Co. Ltd.) ;
  • Lee, Won-Jae (Department of Animal Bioscience and Institute of Agriculture and Life Science, Gyeongsang National University) ;
  • Kim, Jin-Wook (Department of Animal Bioscience and Institute of Agriculture and Life Science, Gyeongsang National University) ;
  • Ahn, Ji-Yun (Division of Nutrition and Metabolism Research, Korea Food Research Institute) ;
  • Jeon, Woo-Min (Department of Animal Biotechnology and Resource, Sahmyook University) ;
  • Han, Kyoung-Sik (Biomaterials Research Institute, Sahmyook University)
  • Received : 2017.12.04
  • Accepted : 2017.12.08
  • Published : 2017.12.31
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Abstract

Goat milk has a protein composition similar to that of breast milk and contains abundant nutrients, but its use in functional foods is rather limited in comparison to milk from other sources. The aim of this study was to prepare a goat A2 ${\beta}$-casein fraction with improved digestibility and hypoallergenic properties. We investigated the optimal conditions for the separation of A2 ${\beta}$-casein fraction from goat milk by pH adjustment to pH 4.4 and treating the casein suspension with calcium chloride (0.05 M for 1 h at $25^{\circ}C$). Selective reduction of ${\beta}$- lactoglobulin and ${\alpha}_s$-casein was confirmed using sodium dodecyl sulphate-polyacrylamide gel electrophoresis and reverse-phase high-performance liquid chromatography. The hypoallergenic property of A2 ${\beta}$-casein fraction was examined by measuring the release of histamine and tumor necrosis factor alpha from HMC-1 human mast cells exposed to different proteins, including A2 ${\beta}$-casein fraction. There was no significant difference in levels of both indicators between A2 ${\beta}$-casein treatment and the control (no protein treatment). The A2 ${\beta}$-casein fraction is abundant in essential amino acids, especially, branched-chain amino acids (leucine, valine, and isoleucine). The physicochemical properties of A2 ${\beta}$-casein fraction, including protein solubility and viscosity, are similar to those of bovine whole casein which is widely used as a protein source in various foods. Therefore, the goat A2 ${\beta}$-casein fraction may be useful as a food material with good digestibility and hypoallergenic properties for infants, the elderly, and people with metabolic disorders.

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References

  1. Alferez, M. J., Barrionuevo, M., Lopez Aliaga, I., Sanz-Sampelayo, M. R., Lisbona, F., Robles, J. C., and Campos, M. S. (2001) Digestive utilization of goat and cow milk fat in malabsorption syndrome. J. Dairy Res. 68, 451-461.
  2. Bera, M. B. and Mukherjee, R. K. (1989) Solubility, emulsifying and foaming properties of rice bran protein concentrates. J. Food Sci. 54, 142-145. https://doi.org/10.1111/j.1365-2621.1989.tb08587.x
  3. Bernacka, H. (2011) Health-promoting properties of goat milk. Medycyna Weterynaryjna. 67, 507-511.
  4. Bobe, G., Beitz, D. C., Freeman, A. E., and Lindberg, G. L. (1998) Separation and quantification of bovine milk proteins by reversed-phase high-performance liquid chromatography. J. Agric. Food Chem. 16, 458-463.
  5. Bossios, A., Theodoropoulou, M., Mondoulet, L., Rigby, N. M., Papadopoulos, N. G., Bernard, H., Adel-Patient, K., Wal. J. M., Mills, C. E., and Papageorgiou, P. (2011) Effect of simulated gastro-duodenal digestion on the allergenic reactivity of beta-lactoglobulin. Clin. Transl. Allergy DOI: 10.1186/2045-7022-1-6.
  6. Cieslinska, A., Kostyra, E., Kostyra, H., Olenski, K., Fiedorowicz, E., and Kaminski, S. (2012) Milk from cows of different ${\beta}$-casein genotypes as a source of ${\beta}$-casomorphin-7. Int. J. Food Sci. Nutr. 63, 426-430. https://doi.org/10.3109/09637486.2011.634785
  7. Cordle, C. T. (2004) Soy protein allergy: incidence and relative severity. J. Nutr. 134, 1213-1219. https://doi.org/10.1093/jn/134.5.1213S
  8. Cui, C., Song, Y., Liu, J., Ge, H., Li, Q., Huang, H., Hu, L., Zhu, H., Jin, Y., and Zhang Y. (2015) Gene targeting by TALEN-induced homologous recombination in goats directs production of ${\beta}$-lactoglobulin-free, high-human lactoferrin milk. Sci. Rep. DOI: 10.1038/srep10482.
  9. Espejo-Carpio, F. J., Garcia-Moreno, P. J., Perez-Galvez, R., Morales-Medina, R., Guadix, A., and Guadix, E. M. (2016) Effect of digestive enzymes on the bioactive properties of goat milk protein hydrolysates. Int. Dairy J. 54, 21-28. https://doi.org/10.1016/j.idairyj.2015.10.006
  10. Farrell, H., Jimenez-Flores, R., Bleck, G., Brown, E., Butler, J., Creamer, L., Hicks, C., Hollar, C., Ng-Kwai-Hang, K. and Swaisgood, H. (2004) Nomenclature of the proteins of cows' milk-sixth revision. J. Dairy Sci. 87, 1641-1674. https://doi.org/10.3168/jds.S0022-0302(04)73319-6
  11. Gani, A., Broadway, A. A., Masoodi, F. A., Wani, A. A., Maqsood, S., Ashwar, B. A., Shah, A., Rather, S. A., and Gani, A. (2015) Enzymatic hydrolysis of whey and casein protein-effect on functional, rheological, textural and sensory properties of breads. J. Food Sci. Technol. 52, 7697-7709. https://doi.org/10.1007/s13197-015-1840-1
  12. Haenlein, G. F. W. (2004) Goat milk in human nutrition. Small Ruminant Res. 51, 155-163. https://doi.org/10.1016/j.smallrumres.2003.08.010
  13. Ho, S., Woodford, K., Kukuljan, S., and Pal, S. (2014) Comparative effects of A1 versus A2 beta-casein on gastrointestinal measures: a blinded randomised cross-over pilot study. Eur. J. Clin. Nutr. 68, 994-1000. https://doi.org/10.1038/ejcn.2014.127
  14. Jandal, J. M. (1996) Comparative aspects of goat and sheep milk. Small Ruminant Res. 22, 177-185. https://doi.org/10.1016/S0921-4488(96)00880-2
  15. Je, I. G., Shin, T. Y., and Kim, S. H. (2013) Mosla punctulata inhibits mast cell-mediated allergic reactions through the inhibition of histamine release and inflammatory cytokine production. Indian J. Pharm. Sci. 75, 664-671.
  16. Jianqin, S., Leiming, X., Lu, X., Yelland, G. W., Ni, J., and Clarke, A. J. (2016) Effects of milk containing only A2 beta casein versus milk containing both A1 and A2 beta casein proteins on gastrointestinal physiology, symptoms of discomfort, and cognitive behavior of people with self-reported intolerance to traditional cows' milk. Nutr. J. DOI:10.1186/s12937-016-0147-z.
  17. Kawaguchi, T., Yamagishi, S., and Sata, M. (2009) Branched-chain amino acids and pigment epithelium-derived factor: Novel therapeutic agents for hepatitis c virus-associated insulin resistance. Curr. Med. Chem. 16, 4843-4857. https://doi.org/10.2174/092986709789909620
  18. Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685. https://doi.org/10.1038/227680a0
  19. Lee, H. S., Eom, K. Y., Choi, H. S., Kim, D. H., Yoo, S. H., and Kim, W. J. (2006) Functional properties of germinated whole soy flour. Korean J. Food Sci. Technol. 38, 483-487.
  20. Miyazaki, D., Nakamura, T., Toda, M., Cheung-Chau, K. W., Richardson, R. M., and Ono, S. J. (2005) Macrophage inflammatory protein-1alpha as a costimulatory signal for mast cell-mediated immediate hypersensitivity reactions. J. Clin. Invest. 115, 434-442. https://doi.org/10.1172/JCI18452
  21. Murphy, J. F. and Fox, P. F. (1991) Fractionation of sodium caseinate by ultrafiltration. Food Chem. 39, 27-38.
  22. Muto, Y., Sato, S., and Watanabe, A. (2005). Effect of oral branched-chain amino acid granules on event-free survival in patients with liver cirrhosis. Clin. Gastroenterol. Hepatol. 3, 705-713. https://doi.org/10.1016/S1542-3565(05)00017-0
  23. Novak, N., and Bieber, T. (2005) The role of dendritic cell subtypes in the pathophysiology of atopic dermatitis. J. Am. Acad. Dermatol. 53, 171-176. https://doi.org/10.1016/j.jaad.2004.12.026
  24. Park, Y. W. (1994) Hypo-allergenic and therapeutic significance of goat milk. Small Ruminant Res. 14, 151-159. https://doi.org/10.1016/0921-4488(94)90105-8
  25. Park, Y. W., Juárez, M., Ramosc, M., and Haenlein, G. F. W. (2007) Physico-chemical characteristics of goat and sheep milk. Small Ruminant Res. 68, 88-113. https://doi.org/10.1016/j.smallrumres.2006.09.013
  26. Raikos, V., Neacsu, M., Russell, W., and Duthie, G. (2014) Comparative study of the functional properties of lupin, green pea, fava bean, hemp, and buckwheat flours as affected by pH. Food Sci. Nutr. 2, 802-810. https://doi.org/10.1002/fsn3.143
  27. SAS. (2008) SAS/STAT Software for PC. Release 9.2, SAS Institute Inc., Cary, NC, USA.
  28. Tomotake, H., Katagiri, M., Fujita, M., and Yamato, M. (2009) Preparation of fresh cheese from caprine milk as a model for the reduction of allergenicity. J. Nutr. Sci. Vitaminol. 55, 296-300. https://doi.org/10.3177/jnsv.55.296
  29. Tomotake, H., Okuyama, R., Katagiri, M., Fuzita, M., Yamato, M. and Ota, F. (2006) Comparison between Holstein cow's milk and Japanese-Saanen goat's milk in fatty acid composition, lipid digestibility and protein profile. Biosci. Biotechnol. Biochem. 70, 2771-2774. https://doi.org/10.1271/bbb.60267
  30. Wang, X.Y., Li, N., Gu, J., Li, W. Q., and Li, J. S. (2003) The effects of the formula of amino acids enriched BCAA on nutritional support in traumatic patients. World J. Gastroenterol. 9, 599-602. https://doi.org/10.3748/wjg.v9.i3.599
  31. Yangilar, F. (2013) As a potentially functional food: Goat milk and products. J Food Nutr Res. 4, 68-81.
  32. Zhang, N., Li, H., Jia, J., and He, M. (2015) Anti-inflammatory effect of curcumin on mast cell-mediated allergic responses in ovalbumin-induced allergic rhinitis mouse. Cell Immunol. 298, 88-95. https://doi.org/10.1016/j.cellimm.2015.09.010

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