Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2013 May;93(3):211-223.
doi: 10.1007/s13594-013-0113-x. Epub 2013 Mar 13.

Milk processing as a tool to reduce cow's milk allergenicity: a mini-review

Guanhao Bu  1 , Yongkang Luo, Fusheng Chen, Kunlun Liu, Tingwei Zhu
Affiliations

Milk processing as a tool to reduce cow's milk allergenicity: a mini-review

Guanhao Bu et al. Dairy Sci Technol. 2013 May.

Abstract

Milk processing technologies for the control of cow's milk protein allergens are reviewed in this paper. Cow's milk is a high nutritious food; however, it is also one of the most common food allergens. The major allergens from cow's milk have been found to be β-lactoglobulin, α-lactalbumin and caseins. Strategies for destroying or modifying these allergens to eliminate milk allergy are being sought by scientists all over the world. In this paper, the main processing technologies used to prevent and eliminate cow's milk allergy are presented and discussed, including heat treatment, glycation reaction, high pressure, enzymatic hydrolysis and lactic acid fermentation. Additionally, how regulating and optimizing the processing conditions can help reduce cow's milk protein allergenicity is being investigated. These strategies should provide valuable support for the development of hypoallergenic milk products in the future.

Keywords: Allergen; Control technologies; Cow’s milk protein; Milk processing.

PubMed Disclaimer

References

    1. Ahmadova A, El-Ghaish S, Choiset Y, Rabesona H, Drouet M, Chobert J-M, Kuliev AA, Haertlé T (2012) Modification of IgE binding to β- and αS1-caseins by proteolytic activity of Lactobacillus helveticus A75. J Food Biochem. doi:10.11/j.1745-4514.2012.00664.x
    1. Babiker E, Hiroyuki A, Matsudomi N, Iwata H, Ogawa T, Bando N, Kato A. Effect of polysaccharide conjugation or transglutaminase treatment on the allergenicity and functional properties of soy protein. J Agric Food Chem. 1998;46:866–871. doi: 10.1021/jf9705072. - DOI
    1. Baldo BA. Milk allergies. Aust J Dairy Technol. 1984;39:120–128.
    1. Beran M, Klubal R, Molik P, Strohalm J, Urban M, Klaudyova AA, Prajzlerova K. Influence of high-hydrostatic pressure on tryptic and chymotryptic hydrolysis of milk proteins. High Press Res. 2009;29:23–27. doi: 10.1080/08957950802492142. - DOI
    1. Bertrand-Harb C, Baday A, Dalgalarrondo M, Chobert J-M, Haertlé T. Thermal modifications of structure and codenaturation of α-lactalbumin and β-lactoglobulin induce changes of solubility and susceptibility to proteases. Nahrung. 2002;46:283–289. doi: 10.1002/1521-3803(20020701)46:4<283::AID-FOOD283>3.0.CO;2-A. - DOI - PubMed