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http://dx.doi.org/10.5851/kosfa.2017.37.6.940

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)
Publication Information
Food Science of Animal Resources / v.37, no.6, 2017 , pp. 940-947 More about this Journal
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.
Keywords
goat A2 ${\beta}$-casein; ${\alpha}_s$-casein; ${\beta}$-lactoglobulin; hypoallergenic property; physicochemical property;
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