Antioxidant activity of whey proteins hydrolysate

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Whey proteins has the highest biological value among all proteins, but the main disadvantage of their use in food technologies is the presence of antigenic epitopes in the molecules that can cause allergic reactions in the human body. The most efficient way to reduce the allergenicity of whey proteins is their enzymatic hydrolysis, which leads to the destruction of antigenic sites and the release of biologically active peptides, including those with antioxidant effects. The purpose of the research is the determination of the whey proteins hydrolysis efficiency in an ultrafiltration concentrate (UF-concentrate) of cheese whey to reduce its allergenicity, as well as to establish the antioxidant activity of the obtained hydrolysate. The experimental studies were carried out at the Core Facilities Centre "Structural and Functional Research of Proteins and RNA" at the FSBSI "Institute of Protein of the Russian Academy of Sciences", as well as "Control and Management of Energy-efficient Projects" at FSBEI HE VSUET. Evaluation of the effectiveness of exposure to whey proteins in the UF-concentrate of cheese whey was carried out by the molecular weight distribution, length and charge of hydrolysis products. ?-lactoglobulin's derivatives containing from 5 to 17 amino acid residues with a molecular weight of 561 to 1943 Da were found in the finishing hydrolysate. At the same time, hydrolysis made it possible to increase the mass fraction of short-chain peptides, including those with antioxidant properties. As a result of the whey proteins proteolysis in the UF-concentrate of cheese whey, its antioxidant activity increased by 2 times. The degree of hydrolysis of the main allergenic protein, ?-lactoglobulin, was 90-91%. The obtained hydrolysate of whey proteins can be recommended for use in the technology of various assortment groups of dairy products for dietary food with reduced allergenicity and antioxidant effect.

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Allergenicity, whey proteins, milk, proteolysis, antioxidant properties, peptides

Короткий адрес: https://sciup.org/140257267

IDR: 140257267   |   DOI: 10.20914/2310-1202-2020-4-213-218

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