PREREQUISITES FOR THE FORMATION OF D - ENANTIOMERS OF AMINO ACIDS OF ANIMAL PROTEINS IN THE MANUFACTURING PROCESS OF MEAT PRODUCTS
The paper presents studies on the presence or formation of d - enantiomers of amino acids in animal tissues or organs, in meat products during its production processes. It is shown that the process of epimerization of L - amino acid residues with the formation of D-enantiomers affect the reduction of the properties of food products, including the formation of oncoassociated subsequent effects on the human body.
Modern control of the quantitative and qualitative composition of d-enantiomers of amino acids in food products, monitoring for stratification of the increased risk of toxic compounds in food are becoming an urgent medical and social problem. The studies planned in this paper are aimed at developing approaches to the creation of food products that reduce the oncogenic alimentary load on human health by solving the problem of technological modification of production, eliminating or minimizing post - translational modifications in proteins that contribute to the formation of d-enantiomers of amino acids. These studies will create a scientific and technological database associated with the risk assessment of carcinogenesis in protein matrices of animal origin. Based on the presented analysis, the task of developing and testing a method to control the accumulation of D-isomers in the course of various technological processes of meat production is extremely popular.
About the AuthorsNatal’ya L. Vostrikova
candidate of technical sciences, head of laboratory «Scientific and methodical work, biological and analytical research»
109316, Moscow, Talalikhina str., 26 . Tel.: +7-495-676-79-81
Oksana A. Kuznetsova
doctor of technical sciences, director
109316, Moscow, Talalikhina str., 26. Tel.: +7-495-676-72-11
Valentina B. Krylova
doctor of technical sciences, professor, chief researcher of the Department of technological developments
109316, Moscow, Talalikhina str., 26 . Tel.: +7-495-676-74-01.
Andrey V. Kulikovskii
candidate of technical sciences, a head chromatography laboratory, leading scientific worker of the Laboratory «Scientific and methodical work, biological and analytical research»
109316, Moscow, Talalikhina str., 26. Tel.: +-495-676-60-11
1. About Strategy of scientific and technological development of the Russian Federation [Electronic resource: http://docs.cntd.ru/ document/420384257. Access date 11.09.2018] (in Russian)
2. Mogilnyi, M.P., Tutelyan, V.A. (2014). Nutritional characteristics of the working population. Voprosy Pitaniia, 83(S3), 29. (in Russian)
3. Stepanenko, O.V., Verkhusha, V.V., Kuznetsova, I.M., Uversky, V.N., Turoverov, K.K. (2008). Fluorescent proteins as biomarkers and biosensors: throwing color lights on molecular and cellular processes. Current Protein and Peptide Science, 9(4), 338–369. DOI:10.2174/138920308785132668.
4. Picariello, G., De Martino, A., Mamone, G., Pasquale Ferranti, P., Francesco Addeo, F., Faccia, M., SpagnaMusso, S., Di Luccia, A. (2006). Proteomic study of muscle sarcoplasmic proteins using AUT-PAGE/SDS/PAGE as two-dimensional gel electrophoresis. Journal of Chromatography B, 833(1), 101-108. DOI :10.1016/j. jchromb.2006.01.024
5. Zapata, I., Zerby, H. N., Wick, M. (2009). Functional proteomic analysis predicts beef tenderness and the tenderness differential. Journal of agricultural and food chemistry, 57(11), 4956-4963. DOI: 10.1021/jf900041j
6. Vostrikova, N.L., Kuznetsova, O.A., Kulikovskii, A.V., Minaev, M.Y. (2017). Formation of the scientific basis of metadata associated with estimates of «onco-» risks linked to meat products. Theory and practice of meat processing, 2(4), 96-113. DOI: 10.21323/2414-438X-2017-2-4-96-113
7. Jensen, O.N. (2006). Interpreting the protein language using proteomics. Nature Reviews Molecular Cell Biology, 7, 391-403. DOI:10.1038/nrm1939.
8. Spirin, A.S. (1996). Molecular biology. The structure and function of proteins. М: Vysshaya shkola. -335 p. (in Russian)
9. The use of amino acids in medicine. [Electronic resource: http://surgeryzone.net/medicina/ispolzovanie-aminokislot-vmedicine.html. Access date 12.09.2018] (in Russian)
10. Epimerization of L-amino acid residues. [Electronic resource: http://humbio.ru/humbio/genexp/0015f42d.htm Access date 12.09.2018]. (in Russian)
11. Yakubke, H.D., Eshkait, H. (1985). Amino acids, peptides, proteins. М: Mir. – 456 p. (in Russian)
12. Huang, M.B., Li, H.K., Li, G.L., Yan, C.T., Wang, L.P. (1996). Planar chromatographic direct separation of some aromatic amino acids and aromatic amino alcohols into enantiomers using cyclodextrin mobile phase additives. Journal of Chromatography A, 742(1-2), 289-294. DOI: 10.1016/0021-9673(96)00259-2
13. Konno. R., Brückner, H., D’Aniello, A., Fisher, G.H., Fujii, N., Homma, H. (2009). D-Amino Acids: Practical Methods and Protocols Volume 3: D-Amino Acids in Peptides and Proteins, -130 p. ISBN: 978-1-60741-378-3
14. Glavin, D.P., Dworkin, J.P. (2009). Enrichment of the amino acid L-isovaline by aqueous alteration on CI and CM meteorite parent bodies. Proceedings of National Academy of Sciences, 106(14), 5487-5492. DOI: 10.1073/pnas.0811618106
15. Konya, Y., Taniguchi, M., Fukusaki, E. (2017). Novel highthroughput and widely-targeted liquid chromatography-time of flight mass spectrometry method for D-amino acids in foods. Journal of Bioscience and Bioengineering, 123(1.1), 126-123. DOI: 10.1016/j.jbiosc.2016.07.009
16. Auclair J. L., Patton R.L. (1950). On the occurrence of d-Alanine in the haemolymph of the milkweed bug, oncopeltus fasciatus. Revue Canadienne de Biologie Experimentale, 9(1), 3-8.
17. Beatty, I.M., Magrath, D.I., Ennor, A.H. (1959). Biochemistry of lombricine: Occurrence of D-serine in lombricine. Nature, 183(4661), 591.
18. Corrigan J.J., N.G. Srinivasan. (1966). The occurrence of certain D-amino acids in insects. Biochemistry, 5,1185–1190.
19. Kreil, G. (1994). Peptides containing a D-amino acid from frogs and molluscs. Journal of Biological Chemistry, 269(15), 10967– 10970.
20. Preston, R.L. (1987). Occurrence of d-amino acids in higher organisms: A survey of the distribution of d-amino acids in marine invertebrates. Comparative Biochemistry and Physiology. Part B, 87(1), 55–62.
21. Helfman, P.M., Bada, J.L., Shou, M.Y. (1977). Considerations on the role of aspartic acid racemization in the aging process. Gerontology, 23(6),419–425.
22. Masters, P.M., Bada, J.L., Zigler, J. S. (1977). Aspartic acid racemisation in the human lens during ageing and in cataract formation. Nature, 268(5615), 71-73.
23. Fujii, N. (2005). D-amino acid in elderly tissues. Biological and Pharmaceutical Bulletin ,8(9), 1585-1589. DOI: 10.1248/ bpb.28.1585
24. Shapira, R., Chou, C.H. (1987). Differential racemization of aspartate and serine in human myelin basic protein. Biochemical and Biophysical Research Communications, 146(3), 1342-1349.
25. Roher, A.E., Lowenson, J.D., Clarke, S., Wolkow, C., Wang, R., Cotter, R.J., Reardon, I. M., Zurcher-Neely, H.A., Heinrikson, R.L., Ball, M. J., Greenberg, B.D. (1993). Structural alterations in the peptide backbone of β-amyloid core protein may account for its deposition and stability in Alzheimer's disease. Journal of Biological Chemistry, 268(5), 3072-3083.
26. Kaneko, I., Yamada, N., Sakuraba, Y., Kamenosono, M., Tutumi, S. (1995). Suppression of Mitochondrial Succinate Dehydrogenase, a Primary Target of β-Amyloid, and Its Derivative Racemized at Ser Residue. Journal of Neurochemistry, 65(6), 2585- 2593.
27. Towse, C.-L., Hopping, G., Vulovic, I., Daggett, V., Fersht, A. (2014). Nature versus design: The conformational propensities of D-amino acids and the importance of side chain chirality. Protein Engineering, Design and Selection, 27(11), 447-455. DOI: 10.1093/ protein/gzu037
28. Chervyakov A.V. (2010). Interruption of amino acids molecular asymmetry (D/L- enantiomers) during normal aging and neurodegenerative diseases. Journal of Asymmetry, 4(2), 77-112. (in Russian)
29. Chervyakov, A.V., Zaharova, M.N., Pestov, M.N. (2014). D-amino acids in the pathogenesis of neurodegenerative diseases and in normal ageing. Annals of clinical and experimental neurology, 8(2), 51-58. (in Russian)
30. Bakston, Sh., Roberts, S. (2009). Guide to Organic Stereochemistry. М: Mir. – 311 p. (in Russian)
31. Chernobrovkin, M.G., Anan'eva, I.A., Shapovalova, E.N., Shpigun, O.A. (2004). Determination of amino acid enantiomers in pharmaceuticals by reversed-phase high-performance liquid chromatography. Journal of Analytical Chemistry, 59(1), 55-63. DOI: 10.1023/B:JANC.0000011669.08932.d8
32. Golubev, I.V., Komarova n.v. Ryzhenkova K.V., Chubar, T.A., Savin S.S., Tishkov V.I. (2014). A study of the relationship structure-function-stability in the yeast oxidase d-amino acids: hydrophobization of alpha-helices. Acta Naturae, 6(22), 76-88.
33. Mor, A., Amiche, M., Nicolas, P. (1992). Enter a new posttranslational modification: D-amino acids in gene-encoded peptides. Trends in Biochemical Sciences, 17(12), 481–485.
34. Soyez, D., Toullec, J.-Y., Montagné, N., Ollivaux, C. (2011). Experimental strategies for the analysis of d-amino acid containing peptides in crustaceans: A review. Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences, 879(29), 3102-3107. DOI: 10.1016/j.jchromb.2011.03.032
For citation: Vostrikova N.L., Kuznetsova O.A., Krylova V.B., Kulikovskii A.V. PREREQUISITES FOR THE FORMATION OF D - ENANTIOMERS OF AMINO ACIDS OF ANIMAL PROTEINS IN THE MANUFACTURING PROCESS OF MEAT PRODUCTS. Theory and practice of meat processing. 2019;4(1):30-36. https://doi.org/10.21323/2414-438X-2019-4-1-30-36
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