Browse > Article
http://dx.doi.org/10.5851/kosfa.2016.36.4.516

Hydrolysis by Alcalase Improves Hypoallergenic Properties of Goat Milk Protein  

Jung, Tae-Hwan (Department of Animal Biotechnology and Resource, 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)
Ha, Ho-Kyung (Department of Animal Bioscience and Institute of Agriculture and Life Science, Gyeongsang National University)
Yoo, Michelle (Centre for Food Science, School of Sciences, Auckland University of Technology)
Hwang, Hyo-Jeong (Department of Animal Biotechnology and Resource, Sahmyook University)
Jeon, Woo-Min (Department of Animal Biotechnology and Resource, Sahmyook University)
Han, Kyoung-Sik (Department of Animal Biotechnology and Resource, Sahmyook University)
Publication Information
Food Science of Animal Resources / v.36, no.4, 2016 , pp. 516-522 More about this Journal
Abstract
Goat milk is highly nutritious and is consumed in many countries, but the development of functional foods from goat milk has been slow compared to that for other types of milk. The aim of this study was to develop a goat milk protein hydrolysate (GMPH) with enhanced digestibility and better hypoallergenic properties in comparison with other protein sources such as ovalbumin and soy protein. Goat milk protein was digested with four commercial food-grade proteases (separately) under various conditions to achieve the best hydrolysis of αs -casein and β-lactoglobulin. It was shown that treatment with alcalase (0.4%, 60℃ for 30 min) effectively degraded these two proteins, as determined by SDS-PAGE, measurement of nonprotein nitrogen content, and reverse-phase high-performance liquid chromatography. Hydrolysis with alcalase resulted in a significant decrease in β-lactoglobulin concentration (almost to nil) and a ~40% reduction in the level of αs-casein. Quantification of histamine and TNF-α released from HMC-1 cells (human mast cell line) showed that the GMPH did not induce an allergic response when compared to the control. Hence, the GMPH may be useful for development of novel foods for infants, the elderly, and convalescent patients, to replace cow milk.
Keywords
goat milk protein hydrolysate; α s-casein; β -lactoglobulin; alcalase;
Citations & Related Records
Times Cited By KSCI : 3  (Citation Analysis)
연도 인용수 순위
1 Ahmed, A. S., El-Bassiony, T., Elmalt, L. M., and Ibrahim, H. R. (2015) Identification of potent antioxidant bioactive peptides from goat milk proteins. Food Res. Int. 74, 88-80.
2 Alférez, M. J., Barrionuevo, M., López 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.
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 Cordle, C. T. (2004) Soy protein allergy: Incidence and relative severity. J. Nutr. 134, 1213-1219.
6 De Gobba, C., Espejo-Carpio, F. J., and Skibsted, L. H. (2014) Antioxidant peptides from goat milk protein fractions hydrolysed by two commercial proteases. Int. Dairy J. 39, 28-40.   DOI
7 Espejo-Carpio, F. J., De Gobba, C., Guadix, A., Guadix, E. M., and Otte, J. (2013) Angiotensin I-converting enzyme inhibitory activity of enzymatic hydrolysates of goat milk protein fractions. Int. Dairy J. 32, 175-183.   DOI
8 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.   DOI
9 Kalesnikoff, J. and Galli, S. J. (2008) New developments in mast cell biology. Nat. Immunol. 9, 1215-1223.   DOI
10 Haenlein, G. F. W. (2004) Goat milk in human nutrition. Small Ruminant Res. 51, 155-163.   DOI
11 Hinz, K., O'Connor, P. M., Huppertz, T., Ross, R. P., and Kelly, A. L. (2012) Comparison of the principal proteins in bovine, caprine, buffalo, equine and camel milk. J. Dairy Res. 79, 185-191.   DOI
12 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.
13 Kaminarides, S. E. and Anifantakis, E. M. (1993) Comparative study of the separation of casein from bovine, ovine and caprine milks using HPLC. J. Dairy Res. 60, 495-504.   DOI
14 Kim, H. H., Park, Y. S., and Yoon, S. S. (2014) Major components of caprine milk and its significance for human nutrition. Korean J. Food Sci. Technol. 46, 121-126.   DOI
15 Kim, H. H., Yun, S. S., Oh, C. H., and Yoon, S. S. (2015) Galactooligosaccharide and sialyllactose content in commercial lactose powders from goat and cow milk. Korean J. Food Sci. Ani. Resour. 35, 572-576.   DOI
16 Kim, H. R., Jung, J. Y., Cho, I. Y., Yu, D. H., Shin, S. S., Son, C. H., Ok, K. S., Hur, T. Y., Jung, Y. H., Choi, C. Y., and Suh, G. H. (2013) Seasonal variation of goat milk composition and somatic cell count in Jeonnam province. Korean J. Vet. Serv. 36, 263-272.   DOI
17 Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.   DOI
18 Lim, Y. S., Kwak, H. S., and Lee, S. K. (2006) Characteristics of goat milk and current utilizing trends in Korea. J. Korean Dairy Technol. Sci. 24, 1-9.
19 Osman, A., Goda, H. A., Abdel-Hamid, M., Badran, S. M., and Otte, J. (2016) Antibacterial peptides generated by alcalase hydrolysis of goat whey. Food Sci. Technol. 65, 480-486.
20 Lowry, O. H., Rosenbrough, N. J., Farr, A. L., and Randall, R. J. (1951) Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193, 265-275.
21 Matsui, N., Ito, D., Takabatake, Y., Nashioka, E., Tada, S., Kanagawa, M., Fukuishi, N., and Akagi, M. (2015) Compound 48/80, a mast cell stimulator, enhances synthesis of IgE and IgG induced by intranasal application of ovalbumin in mice. Biol Pharm Bull. 38, 1954-1959.   DOI
22 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.   DOI
23 Park, S. Y. (2006) Production and consumption of goat milk products in korea. J. Kor. Dairy Tech. Sci. 24, 39-45.
24 Park, Y. W. (1994) Hypo-allergenic and therapeutic significance of goat milk. Small Ruminant Res. 14, 151-159.   DOI
25 Rutherfurd, S. M., Darragh, A. J., Hendriks, W. H., Prosser, C. G., and Lowry, D. (2006) Mineral retention in three-weekold piglets fed goat and cow milk infant formulas. J. Dairy Sci. 89, 4520-4526.   DOI
26 Sanz Ceballos, L., Sanz Sampelayo, M. R., Gil Extremera, F., and Rodríguez Osorio, M. (2009) Evaluation of the allergenicity of goat milk, cow milk, and their lactosera in a guinea pig model. J. Dairy Sci. 92, 837-846.   DOI
27 Urbiene, S., Ciuckinas, A., and Margelyke, J. (1997) Physical and chemical properties and the biological value of goat's, cow's and human milk. Milchwissenschaft 52, 427-430.
28 Xu, M., Wei, L., Dai, Z., Zhang, Y., Li, Y., and Wang, J. (2015) Effects of goat milk-based formula on development in weaned rats. Food Nutr. Res. 59, 28610.   DOI
29 Yangilar, F. (2013) As a potentially functional food: Goat milk and products. J. Food Nutr. Res. 4, 68-81.
30 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.   DOI