Milk | Open Access Journals

Journal of Experimental Food Chemistry

ISSN: 2472-0542

Open Access


The milk of all species is essentially similar, but there are significant species-specific differences. Humans have used the milk of other species in their diets for about 8000 years, and a major industry has developed around the processing of milk of a few species, especially cattle, buffalo, sheep, and goats, for human foods. Milk processing, which exploits certain physicochemical properties of milk, is practiced worldwide, especially in Europe and North America. Milk is a very flexible raw material, from which a wide range of different products, including about 1000 varieties of cheese, are produced. An international meeting dedicated to the topic of milk and sort 1 diabetes concluded in 1999 that there was nothing unique about milk which variety of different food types may be diabetogenic. Cow milk contains quite 20 protein allergens which will cause allergies. The main proteins are casein and whey proteins. Casein fractions (αs1-casein, αs2-casein, and β-casein) and β-lg are the most allergens in cow milk. Allergic reactions to bovine albumin (BSA), immunoglobulin G (IgG) heavy chain and α-lactalbumin (α-la) have also been noted. Genetic polymorphisms of milk proteins play a crucial role in MPA development.  This is very interesting and should have great potentials in selecting goat breeds for various casein genotypes, especially for αs2-casein, which is found in less amount in milk comparing to αs1-casein. Allergic responses to lactoferrin and a few milk enzymes are detected in some patients with MPA but none to mammalian lysozyme. Cow's milk features a high nutritive value and bioactive properties, except for some sensitized patients it is often a severe allergenic factor. Polysensitization to many proteins is most frequently common and every one milk proteins appear to be potential allergens. Nevertheless, their high nutritive value, accessibility, low price, and susceptibility to modifications cause milk proteins to be the foremost popular sources of proteins for formula production. A variety of methods has been wonted to attempt decreasing the allergenicity of cow's milk food products: thermal processing like, cooking, pasteurization, sterilization, and ultrahigh heating; physical processing, such as homogenization, micro articulation, ultra-filtration, microwaves, ultrasonic, and irradiation; and chemical processes, like proteolysis and fermentation. Purified milk proteins are more vulnerable to enzymatic degradation than proteins in “ecrude” milk samples. To date, however, there's no example of a food allergen that has been rendered completely barren of allergenic activity using these methods. This is thanks to the very fact that every food contains variety of allergenic proteins, each with multiple allergenic epitopes. Unless these methods can eliminate all of those proteins or modify all allergenic epitopes, the remaining proteins or epitopes could still elicit a reaction in sensitive individuals.


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