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Hypoallergenic and Physicochemical Properties of the A2 β-Casein Fractionof Goat Milk

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 β-casein fraction with improved digestibility and hypoallerge...

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Autores principales: Jung, Tae-Hwan, Hwang, Hyo-Jeong, Yun, Sung-Seob, Lee, Won-Jae, Kim, Jin-Wook, Ahn, Ji-Yun, Jeon, Woo-Min, Han, Kyoung-Sik
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Korean Society for Food Science of Animal Resources 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5932946/
https://www.ncbi.nlm.nih.gov/pubmed/29725217
http://dx.doi.org/10.5851/kosfa.2017.37.6.940
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author Jung, Tae-Hwan
Hwang, Hyo-Jeong
Yun, Sung-Seob
Lee, Won-Jae
Kim, Jin-Wook
Ahn, Ji-Yun
Jeon, Woo-Min
Han, Kyoung-Sik
author_facet Jung, Tae-Hwan
Hwang, Hyo-Jeong
Yun, Sung-Seob
Lee, Won-Jae
Kim, Jin-Wook
Ahn, Ji-Yun
Jeon, Woo-Min
Han, Kyoung-Sik
author_sort Jung, Tae-Hwan
collection PubMed
description 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 β-casein fraction with improved digestibility and hypoallergenic properties. We investigated the optimal conditions for the separation of A2 β-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°C). Selective reduction of β-lactoglobulin and α(s)-casein was confirmed using sodium dodecyl sulphate-polyacrylamide gel electrophoresis and reverse-phase high-performance liquid chromatography. The hypoallergenic property of A2 β-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 β-casein fraction. There was no significant difference in levels of both indicators between A2 β-casein treatment and the control (no protein treatment). The A2 β-casein fraction is abundant in essential amino acids, especially, branched-chain amino acids (leucine, valine, and isoleucine). The physicochemical properties of A2 β-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 β-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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spelling pubmed-59329462018-05-03 Hypoallergenic and Physicochemical Properties of the A2 β-Casein Fractionof Goat Milk Jung, Tae-Hwan Hwang, Hyo-Jeong Yun, Sung-Seob Lee, Won-Jae Kim, Jin-Wook Ahn, Ji-Yun Jeon, Woo-Min Han, Kyoung-Sik Korean J Food Sci Anim Resour Article 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 β-casein fraction with improved digestibility and hypoallergenic properties. We investigated the optimal conditions for the separation of A2 β-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°C). Selective reduction of β-lactoglobulin and α(s)-casein was confirmed using sodium dodecyl sulphate-polyacrylamide gel electrophoresis and reverse-phase high-performance liquid chromatography. The hypoallergenic property of A2 β-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 β-casein fraction. There was no significant difference in levels of both indicators between A2 β-casein treatment and the control (no protein treatment). The A2 β-casein fraction is abundant in essential amino acids, especially, branched-chain amino acids (leucine, valine, and isoleucine). The physicochemical properties of A2 β-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 β-casein fraction may be useful as a food material with good digestibility and hypoallergenic properties for infants, the elderly, and people with metabolic disorders. Korean Society for Food Science of Animal Resources 2017 2017-12-31 /pmc/articles/PMC5932946/ /pubmed/29725217 http://dx.doi.org/10.5851/kosfa.2017.37.6.940 Text en Copyright © 2017, Korean Society for Food Science of Animal Resources http://creativecommons.org/licences/by-nc/3.0 This is an open access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licences/by-nc/3.0) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Article
Jung, Tae-Hwan
Hwang, Hyo-Jeong
Yun, Sung-Seob
Lee, Won-Jae
Kim, Jin-Wook
Ahn, Ji-Yun
Jeon, Woo-Min
Han, Kyoung-Sik
Hypoallergenic and Physicochemical Properties of the A2 β-Casein Fractionof Goat Milk
title Hypoallergenic and Physicochemical Properties of the A2 β-Casein Fractionof Goat Milk
title_full Hypoallergenic and Physicochemical Properties of the A2 β-Casein Fractionof Goat Milk
title_fullStr Hypoallergenic and Physicochemical Properties of the A2 β-Casein Fractionof Goat Milk
title_full_unstemmed Hypoallergenic and Physicochemical Properties of the A2 β-Casein Fractionof Goat Milk
title_short Hypoallergenic and Physicochemical Properties of the A2 β-Casein Fractionof Goat Milk
title_sort hypoallergenic and physicochemical properties of the a2 β-casein fractionof goat milk
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5932946/
https://www.ncbi.nlm.nih.gov/pubmed/29725217
http://dx.doi.org/10.5851/kosfa.2017.37.6.940
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