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THE PHYSICAL PROPERTIES OF THE CASEIN IN SOLUTION: EFFECT OF ULTRA-HIGH PRESSURE

https://doi.org/10.21323/2618-9771-2018-1-3-4-12

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Abstract

The aim of this work was to study the effect of pressure (50; 90; 160; 250; 350 MPa) on a physical property of casein micelle: hydrodynamic radius, tyrosine and tryptophan fluorescence and IR spectra characteristics. According to photon-correlation spectroscopy, the average hydrodynamic radius of the casein micelle was 128 nm, increasing at 50 MPa to 467 nm with the formation of conglomerates. Further increase of pressure led to the formation of two fractions of particles, differing in hydrodynamic radius. At a pressure of 350 MPa, an average radius of 75 % of particles was 121 nm. Comparison of hydrodynamic radius and tyrosine fluorescence revealed a decrease in the intensity of the glow with an increase in the proportion of large particles and an increase in the radiation in the solution with a decrease of the micelles size. The increase of casein fluorescence by tryptophan and its decrease by tyrosine indicate a change in the conformation of protein molecules during pressure treatment. FTIR spectroscopy revealed a change in the intensity of the optical density in the range of amide I, amide II and valence bonds of tyrosine, confirming the absence of new bonds. The obtained physical data indicate a change in the structure of casein micelles with an increase in the proportion (25 %) of large particles after the action of high pressure (350mpa), which should be taken into account in milk processing. The fluorescence of casein during pressure treatment is a poorly investigated physical indicator and can be important for the processing of raw milk.

About the Authors

Roman O. Budkevich
North-Caucasus Federal University, Stavropol
Russian Federation

Candidate of Biological Sciences (PhD), associate professor, Head of the Laboratory, Laboratory for Nanobiotechnology and Biophysics Center of bioengineering
355009, Stavropol, Pushkin Street, 1.
Tel.: +7–962–445–20–91



Anastasia I. Eremina
North-Caucasus Federal University, Stavropol
Russian Federation

post-graduate student, Engineer, Laboratory for Nanobiotechnology and Biophysics Center of bioengineering
355009, Stavropol, Pushkin Street, 1.
Tel.: +7–918–759–07–60



Ivan A. Evdokimov
North-Caucasus Federal University, Stavropol
Russian Federation

Doctor of Technical Sciences, Head of the basic Department of milk and dairy products technology
355009, Stavropol, Pushkin Street, 1.
Tel.: +7–962–403–08–47



Nikita M. Fedortsov
North-Caucasus Federal University, Stavropol
Russian Federation

master, Engineer, Laboratory for Nanobiotechnology and Biophysics Center of bioengineering
355009, Stavropol, Pushkin Street, 1.
Tel.: +7–928–329–20–53



Alexey A. Martak
North-Caucasus Federal University, Stavropol
Russian Federation

Engineer, Laboratory for Nanobiotechnology and Biophysics Center of bioengineering
355009, Stavropol, Pushkin Street, 1.
Tel.: +7–961–446–52–56



Elena V. Budkevich
North-Caucasus Federal University, Stavropol
Russian Federation

Candidate of Medical Sciences (PhD), Engineer, Center of bioengineering
355009, Stavropol, Pushkin Street, 1.
Tel.: +7–962–444–89–94



References

1. Bolumar, T., Middendorf, D., Toepfl, S., Heinz, V. (2016). Structural Changes in Foods Caused by High-Pressure Processing. In: High pressure processing of food: principles, technology and applications. New York: Springer, 509–537 p. ISBN978–1–4939–3234–4.

2. Huppertz, T., Kelly, A.L., Fox, P.F. (2002). Effects of high pressure on constituents and properties of milk. International Dairy Journal, 12(7), 561–572.

3. Fox, P.F, Brodkorb, A. (2008). The casein micelle: historical aspects, current concepts and significance. International Dairy Journal, 18(7), 677– 684.

4. Bannikova, A.V., Evdokimov, I.A. (2015). Innovative approach to the creation of enriched dairy products with high protein content. M: DeLi print. — 135 p. ISBN978–5–905170–170–72–0. (in Russian).

5. Evdokimov, I.A., Golovach, T.N., Kurchenko, V.P., Alieva, L.R., Budkevich, R.O. (2013). Modern problems of science in food and processing industries of the agroindustrial complex. Part I. Specific properties of milk proteins and their modification during technological processing (textbook). Stavropol: North-Caucasus Federal University. — 21 p. (in Russian)

6. Horne, D.S. (2006). Casein micelle structure: Models and muddles. Current Opinion in Colloid & Interface Science,11(2–3), 148–153.

7. Huppertz, T., Smiddy, M.A., Upadhyay, V.K., Kelly, A.L. (2006). High-pressure-induced changes in bovine milk: A review. International Journal of Dairy Technology, 59(2), 58–66.

8. Huppertz, T., Fox, P.F., Kelly, A.L. (2004). High-pressure treatment of bovine milk: effects on casein micelles and whey proteins. Journal of Dairy Research,71(1), 97–106.

9. Khramtsov, A.G., Evdokimov, I.A., Lodygin, A.D., Budkevich, R.O. (2014). Technology development for the food industry: a conceptual model. Foods and Raw Materials, 2(1), 22–26.

10. Patel, H.A., Huppertz, T. (2014). Effects of high-pressure processing on structure and interactions of milk proteins. In: Milk Proteins: From Expression to Food. 2nd ed. Amsterdam, The Netherlands: Elsevier Inc. 243–267 p. ISBN9780124051751.

11. Broyard, C., Gaucheron, F. (2015). Modifications of structures and functions of caseins: a scientific and technological challenge. Dairy science & technology, 95(6), 831–862.

12. Needs, E.C., Stenning, R.A., Gill, A L., Ferragut, V., Rich, G.T. (2000). Highpressure treatment of milk: Effects on casein micelle structure and on enzymic coagulation. Journal of Dairy Research, 67(1), 31–42.

13. Shaikh, S.M.T., Seetharamappa, J., Kandagal, P.B., Manjunatha, D.H., Ashoka, S. (2007). Spectroscopic investigations on the mechanism of interaction of bioactive dye with bovine serum albumin. Dyes and Pigments, 74(3), 665–671.

14. Vekshin N.L. (2008). Fluorescence Spectroscopy of Biomacromolecules. M: Photon-century. — 168 p. ISBN9785040144716. (in Russian)

15. Larson, B.L., Smith, V.R. (1974). Lactation: a Comprehensive Treatise, Volume 3: Nutrition and Biochemistry of Milk/Maintenance. Academic press. — 440 p. ISBN: 0–12–436703–8.

16. Wang, Y.X., Li, L., Sheng, L.J., Song, G.W., Xu, Z.S. (2011). Spectroscopic study on the inherent binding information of cationic perfluorinated surfactant with bovine serum albumin. Journal of Fluorine Chemistry, 132(7), 489–494.

17. Qi, P.X., Ren, D., Xiao, Y., Tomasula, P.M. (2015) Effect of homogenization and pasteurization on the structure and stability of whey protein in milk. Journal of Dairy Science, 98(5), 2884–2897.

18. Kong, J., Yu, S. (2007). Fourier transform infrared spectroscopic analysis of protein secondary structures. Acta Biochimica et Biophysica Sinica, 39(8), 549–559.

19. Cadesky, L., Walkling-Ribeiro, M., Kriner, K.T., Karwe, M.V., Moraru, C.I. (2017). Structural changes induced by high-pressure processing in micellar casein and milk protein concentrates. Journal of Dairy Science, 100(9), 7055–7070.

20. Ruan, K., Lange, R., Meersman, F., Heremans, K., Balny, C. (1999). Fluorescence and FTIR study of the pressure-induced denaturation of bovine pancreas trypsin. European Journal of Biochemistry, 265(1), 79–85.

21. Gebhardt, R., Takeda, N., Kulozik, U., Doster, W. (2011). Structure and Stabilizing Interactions of Casein Micelles Probed by High-Pressure Light Scattering and FTIR. Journal of Physical Chemistry B, 115(10), 2349–2359.

22. O’Loughlin, I.B., Kelly, P.M., Murray, B.A., Fitzgerald, R.J., Brodkorb A. (2015). Concentrated whey protein ingredients: A Fourier transformed infrared spectroscopy investigation of thermally induced denaturation. International Journal of Dairy Technology, 68(3), 349–356.


For citation:


Budkevich R.O., Eremina A.I., Evdokimov I.A., Fedortsov N.M., Martak A.A., Budkevich E.V. THE PHYSICAL PROPERTIES OF THE CASEIN IN SOLUTION: EFFECT OF ULTRA-HIGH PRESSURE. Food systems. 2018;1(3):4-12. (In Russ.) https://doi.org/10.21323/2618-9771-2018-1-3-4-12

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ISSN 2618-9771 (Print)
ISSN 2618-7272 (Online)