Oxidative Modification of the Proteins of Breast and Cow Milk


One of the important modern characteristics of the nutritional and biological value of milk and dairy products is the antioxidant properties. The high stability and sensitivity of the determination of carbonyl derivatives of proteins, as well as the informative value of the action of antioxidants, allow using them as the markers of oxidative damage. The purpose of this paper was to compare the level of carbonyl derivatives of proteins in breast and cow milk. The determination of the oxidative modification of proteins was based on the reaction of carbonyl derivatives of amino acid residues with 2, 4-dinitrophenylhydrazine. The content of the products was determined during spontaneous and metal-catalyzed oxidative modification of the proteins. During the determination of the spontaneously formed carbonyl derivatives of the proteins, their significantly higher content in cow milk compared to breast milk was established. This increase ranged from 46% to 83% at different wavelengths. Thus, the determination of carbonyl derivatives of amino acid residues of the proteins made it possible to reveal significant differences in the antioxidant properties of breast and cow milk, manifested in a lower level of carbonyl derivatives in breast milk. The lower level of carbonyl derivatives in the composition of breast milk proteins is likely associated with the increased activity of the antioxidant system of breast milk or the increased rate of removal of damaged proteins upon activation of milk proteases.

Keywords: carbonyl derivatives, oxidative modification, proteins, human milk, breast milk, metal-catalyzed

[1] Tutelyan, V. A., et al. (2009). The Nature of Nutrition of Infants and Young Children in the Russian Federation: The Practice of Introducing Complementary Foods. Pediatrics, vol. 88, issue 6, pp. 77-83.

[2] Blanc, B. (1981). Biochemical Aspects of Human Milk-Comparison with Bovine Milk. Wold Review of Nutrion and Dietics issue 36, pp. 1-89.

[3] Machneva, I. V., et al. (2020). A Modern Look at the Breast Milk Proteome. Journal of Grodno State Medical University, vol. 18, issue 1, pp. 5-10.

[4] Sapozhnikov, V. G. and Tarasova, O. V. (2019). Modern Approaches to Child Nutrition in Health and Disease. Tula: Polygraphinvest.

[5] Socha, P., et al. (2011). Milk Protein Intake, the Metabolic-Endocrine Response, and Growth in Infancy: Data from a Randomized Clinical Trial. The American journal of clinical nutrition. vol. 94, issue 6, pp. 1776S-1784S.

[6] Haschke, F., Haiden, N. and Thakkar, S. K. (2016). Nutritive and Bioactive Proteins in Breastmilk. Annals of Nutrition and Metabolism, vol. 69, issue 2, pp. 17-26.

[7] Zhu, J. and Dingess, K. A. (2019). The Functional Power of the Human Milk Proteome. Nutrients, vol. 11, issue 8, p. 1834.

[8] Kay, P. (2013). Modification of Peptide and Protein Cysteine Thiol Groups by Conjugation with a Degradation Product of Ascorbate. Chemical Research in Toxicology, vol. 26, issue 9, pp. 1333-1339.

[9] Yan, L. J. (2009). Analysis of Oxidative Modification of Proteins. Current protocols in protein science, vol.56, issue1.

[10] Radi, R. (2013). Protein Tyrosine Nitration: Biochemical Mechanisms and Structural Basis of Functional Effects. Accounts of Chemical Research, vol. 46, pp. 550–559.

[11] Cai, Z. and Yan, J. (2013). Protein Oxidative Modifications: Beneficial Roles in Disease and Health. Journal of Biochemical and Pharmacological Research, vol. 1, issue 1, pp. 15-26.

[12] Baraibar, M. A., Ladouce, R. and Friguet, B. (2013). Proteomic Quantification and Identification of Carbonylated Proteins upon Oxidative Stress and During Cellular Aging. Journal of Proteomics, vol. 92, pp. 67-70.

[13] Halliwell, B. (2007). Biochemistry of Oxidative Stress.Biochemical society transactions, vol. 35, pp. 1147-1150.

[14] Dalle-Donnea, I. (2003). Protein Carbonyl Groups as Biomarkers of Oxidative Stress. Clinica Chimica Acta, vol. 329, pp. 23–38.

[15] Purdel, N. C., Margina, D. and Llie, M. (2014). Current Methods Used in Protein Carbonil Assay. Annual Research & Review in Biology, vol. 4, issue 12, pp. 2015-2026.

[16] Kim, J. Y., et al. (2013). Association of Age-Related Changes in Circulating Intermediary Lipid Metabolites, Inflammatory and Oxidative Stress Markers, and Arterial Stiffness in Middle-Aged Men. Age (Dordrecht, Netherlands), vol. 35, issue 14, pp. 1507–1519.

[17] Vysokogorskiy, V., et al. (2019) Carbonyl Derivatives of Proteins–as Markers of Free Radical Processes in Dairy Products. The Fifth Technological Order: Prospects for the Development and Modernization of the Russian Agro-Industrial Sector (TFTS), Omsk. Russia, oktober 2019. – Amsterdam, Netherlands: Atlantis Press. vol. 393, pp. 13-16.

[18] Zakharova, I. N., Machneva, E. B. and Oblogin, I. S. (2017). Breast Milk is Living Tissue! How to Keep Breastfeeding? Meditsinsky Sovet, vol.19, pp. 24-29.

[19] Gavrilova, N. B., Chernopolskaya, N. L. and Konovalov, S. A. (2019) Substantiated Screening of Functional Ingredients for Extended Shelf Life of Fermented Milk Products. The Fifth Technological Order: Prospects for the Development and Modernization of the Russian Agro-Industrial Sector (TFTS). Omsk. Russia, October 2019. Amsterdam, Netherlands: Atlantis Press. vol. 393, pp. 9-12.

[20] Goldberg, A. L. (2003). Protein Degradation and Protection Against Misfolded or Damaged Proteins. Nature., vol. 426, pp. 895-899.

[21] Haglund, K. and Dikis, I. (2005). Ubiquitylation and Cell Signaling. The EMBO Journal, vol. 24, pp. 3353-3359.