meatTheory and practice of meat processingТеория и практика переработки мяса2414-438X2414-441XФГБНУ «Федеральный научный центр пищевых систем им. В.М. Горбатова» РАН10.21323/2414-438X-2019-4-3-19-23meat-120Research ArticleСтатьиTHE STUDY OF THERMAL DENATURATION OF BEEF, PORK, CHICKEN AND TURKEY MUSCLE PROTEINS USING DIFFERENTIAL SCANNING CALORIMETRYTHE STUDY OF THERMAL DENATURATION OF BEEF, PORK, CHICKEN AND TURKEY MUSCLE PROTEINS USING DIFFERENTIAL SCANNING CALORIMETRYAgafonkinaIrina V.AgafonkinaIrina V.

Postgraduate student, junior scientist of Laboratory of thermophysical properties and thermotechnical measurements

127422, Moscow, str. Kostyakova, 12. Tel: +7–916–650–91–84.

Postgraduate student, junior scientist of Laboratory of thermophysical properties and thermotechnical measurements

127422, Moscow, str. Kostyakova, 12. Tel: +7–916–650–91–84.

agafonkina.vnihi@yandex.ruKorolevIgor A.KorolevIgor A.

Postgraduate student, junior scientist of Laboratory of thermophysical properties and thermotechnical measurements

127422, Moscow, str. Kostyakova, 12. Tel: 976–09–63.

Postgraduate student, junior scientist of Laboratory of thermophysical properties and thermotechnical measurements

127422, Moscow, str. Kostyakova, 12. Tel: 976–09–63.

korolev.vnihi@mail.ruSarantsevTaras A.SarantsevTaras A.

Master, engineer-researcher of Laboratory of thermophysical properties and thermotechnical measurements

127422, Moscow, str. Kostyakova, 12. Tel: +7–915–282–18–24.

Master, engineer-researcher of Laboratory of thermophysical properties and thermotechnical measurements

127422, Moscow, str. Kostyakova, 12. Tel: +7–915–282–18–24.

codyjeps@gmail.comAll-Russian Scientific Research Institute of Refrigeration Industry — Branch of V. M. Gorbatov Federal Research Center for Food Systems of RASРоссияAll-Russian Scientific Research Institute of Refrigeration Industry — Branch of V. M. Gorbatov Federal Research Center for Food Systems of RASRussian Federation201915102019431923Copyright © Agafonkina I.V., Korolev I.A., Sarantsev T.A., 20192019Agafonkina I.V., Korolev I.A., Sarantsev T.A.Agafonkina I.V., Korolev I.A., Sarantsev T.A.Данная работа распространяется под лицензией Creative Commons Attribution 4.0.This work is licensed under a Creative Commons Attribution 4.0 License.https://www.meatjournal.ru/jour/article/view/120

In the temperature range from 45 °C to 90 °C the process of thermal denaturation of a whole complex of muscle proteins in meat takes place. An effective mode to register the thermal denaturation process is the method of differential scanning calorimetry (DSC). As a result of studies the differences during the process of thermal denaturation of muscle proteins of pork, beef, chicken and turkey were defined by the appearance of endothermic peaks in DSC thermograms. The main variances are associated with the process of denaturation of myosin and sacroplasmic proteins and indicate indirectly their quantitative ratio in meat. The values of effective specific heat capacity in the temperature range from 20 °C to 90 °C are obtained as well as those of heat spent on the denaturation process.

At reheating, the values of specific heat capacity increased by 0.1 J/(g*K) on the average, and peaks of thermal denaturation were not detected, that certifies the irreversibility of the denaturation process and the decrease in the bound moisture proportion in meat after thermal processing. Knowledge of the nature of protein thermal denaturation of each kind of meat product is one of the necessary tools for developing the technology of meat product thermal processing.

In the temperature range from 45 °C to 90 °C the process of thermal denaturation of a whole complex of muscle proteins in meat takes place. An effective mode to register the thermal denaturation process is the method of differential scanning calorimetry (DSC). As a result of studies the differences during the process of thermal denaturation of muscle proteins of pork, beef, chicken and turkey were defined by the appearance of endothermic peaks in DSC thermograms. The main variances are associated with the process of denaturation of myosin and sacroplasmic proteins and indicate indirectly their quantitative ratio in meat. The values of effective specific heat capacity in the temperature range from 20 °C to 90 °C are obtained as well as those of heat spent on the denaturation process.

At reheating, the values of specific heat capacity increased by 0.1 J/(g*K) on the average, and peaks of thermal denaturation were not detected, that certifies the irreversibility of the denaturation process and the decrease in the bound moisture proportion in meat after thermal processing. Knowledge of the nature of protein thermal denaturation of each kind of meat product is one of the necessary tools for developing the technology of meat product thermal processing.

DSCprotein denaturationeffective specific heatporkbeefchickenturkeyDSCprotein denaturationeffective specific heatporkbeefchickenturkeyReferencesAntipova, L.V., Tolpyginam I. N., Kalachev, A.A. (2011).). Technology and equipment for sausage and half-finished products production. St. Petersburg: GIORD. — 600 p. ISBN 978–598879–134–8. (In Russian)Antipova, L.V., Tolpyginam I. N., Kalachev, A.A. (2011).). Technology and equipment for sausage and half-finished products production. St. Petersburg: GIORD. — 600 p. ISBN 978–598879–134–8. (In Russian)Bowers, J.A., Craig, J.A., Kropf, D.H., Tucker, T.J. (1987). Flavor, color and other characteristics of beef longissimus muscle heated to seven internal temperatures between 55 °C and 85 °C. Journal of Food Science, 52(3), 533–536. DOI: 10.1111/j.1365–2621.1987.tb06668.xBowers, J.A., Craig, J.A., Kropf, D.H., Tucker, T.J. (1987). Flavor, color and other characteristics of beef longissimus muscle heated to seven internal temperatures between 55 °C and 85 °C. Journal of Food Science, 52(3), 533–536. DOI: 10.1111/j.1365–2621.1987.tb06668.xLevitskiy, D.I. (2004). The use of differential scanning calorimetry for structural and functional studies of muscle proteins. Biological chemistry reviews, 44, 133–170. (In Russian)Levitskiy, D.I. (2004). The use of differential scanning calorimetry for structural and functional studies of muscle proteins. Biological chemistry reviews, 44, 133–170. (In Russian)Lubarev, A.E., Kurganov.B.I. (2000). Study of protein irreversible thermal denaturation by differential scanning calorimetry. Biological chemistry reviews, 40, 43–84. (In Russian)Lubarev, A.E., Kurganov.B.I. (2000). Study of protein irreversible thermal denaturation by differential scanning calorimetry. Biological chemistry reviews, 40, 43–84. (In Russian)Tamilmani, P., Pandey, M.C. (2016). Thermal analysis of meat and meat products: A review. Journal of Thermal Analysis and Calorimetry, 123, 1899–1917. DOI: 10.1007/s10973–015–4696–8Tamilmani, P., Pandey, M.C. (2016). Thermal analysis of meat and meat products: A review. Journal of Thermal Analysis and Calorimetry, 123, 1899–1917. DOI: 10.1007/s10973–015–4696–8Farkas, J., Mohácsi-Farkas, C. (1996). Application of differential scanning calorimetry in food research and food quality assurance. Journal of thermal analysis, 47(6), 1787–1803. DOI: 10.1007/BF01980925.Farkas, J., Mohácsi-Farkas, C. (1996). Application of differential scanning calorimetry in food research and food quality assurance. Journal of thermal analysis, 47(6), 1787–1803. DOI: 10.1007/BF01980925.Findlay, C.J., Parkin, K.L., Stanley, D.W. (1986). Differential scanning calorimetry can determine kinetics of thermal denaturation of beef muscle proteins. Journal of Food Biochemistry, 10(1), 1–15. DOI: 10.1111/j.1745–4514.1986.tb00085.x.Findlay, C.J., Parkin, K.L., Stanley, D.W. (1986). Differential scanning calorimetry can determine kinetics of thermal denaturation of beef muscle proteins. Journal of Food Biochemistry, 10(1), 1–15. DOI: 10.1111/j.1745–4514.1986.tb00085.x.Shnyrov, V.L., Sanchez-Ruiz, J.M., Boiko, B.N., Zhadan, G.G., Permyakov, E.A. (1997). Application of scanning microcalorimetry in biophysics and biochemistry. Thermochimica acta, 302(1–2), 165–180. DOI: 10.1016/S0040–6031(97)00238–4.Shnyrov, V.L., Sanchez-Ruiz, J.M., Boiko, B.N., Zhadan, G.G., Permyakov, E.A. (1997). Application of scanning microcalorimetry in biophysics and biochemistry. Thermochimica acta, 302(1–2), 165–180. DOI: 10.1016/S0040–6031(97)00238–4.Wright, D., Winding, P. (1984). Differential scanning calorimetric study of muscle and its proteins: myosin and its subfragments. Journal of the Science of Food and Agriculture, 35(3), 357–372. DOI: 10.1002/jsfa.2740350317.Wright, D., Winding, P. (1984). Differential scanning calorimetric study of muscle and its proteins: myosin and its subfragments. Journal of the Science of Food and Agriculture, 35(3), 357–372. DOI: 10.1002/jsfa.2740350317.Ledward, D.A., Lawrie, R.A. (1975). A note on the dependence of meat texture on the temperature of measurement. Journal of the Science of Food and Agriculture, 26(5), 691–695. DOI: 10.1002/jsfa.2740260515.Ledward, D.A., Lawrie, R.A. (1975). A note on the dependence of meat texture on the temperature of measurement. Journal of the Science of Food and Agriculture, 26(5), 691–695. DOI: 10.1002/jsfa.2740260515.Martens, H., Vold, E. (1976). DSC studies of muscle tissue protein denaturation. In congress documentation; Proceedings of the 22nd European meeting of meat research workers, J 9.3.Martens, H., Vold, E. (1976). DSC studies of muscle tissue protein denaturation. In congress documentation; Proceedings of the 22nd European meeting of meat research workers, J 9.3.Stabursvik, E., Martens, H. (1980). Thermal denaturation of proteins in post rigor muscle tissue as studied by differential scanning calorimetry. Journal of the Science of Food and Agriculture, 31(10), 1034–1042. DOI: 10.1002/jsfa.2740311010.Stabursvik, E., Martens, H. (1980). Thermal denaturation of proteins in post rigor muscle tissue as studied by differential scanning calorimetry. Journal of the Science of Food and Agriculture, 31(10), 1034–1042. DOI: 10.1002/jsfa.2740311010.Radchenko, M.V. (2016). Study of the influence of a long low-temperature thermal processing on quality characteristics of boiled pork products at different autolysis processes. Author’s abstract of the dissertation for the scientific degree of Candidate of Technical Sciences. Orel: — 24p. (In Russian)Radchenko, M.V. (2016). Study of the influence of a long low-temperature thermal processing on quality characteristics of boiled pork products at different autolysis processes. Author’s abstract of the dissertation for the scientific degree of Candidate of Technical Sciences. Orel: — 24p. (In Russian)Tunieva, E.K., Dederer, I. (2016). Study of sodium, potassium, and calcium salts influence on protein stability by differential scanning calorimetry. Theory and practice of meat processing, 1(1),19–24. DOI: 10.21323/2414–438X-2016–1–1–19–24. (In Russian)Tunieva, E.K., Dederer, I. (2016). Study of sodium, potassium, and calcium salts influence on protein stability by differential scanning calorimetry. Theory and practice of meat processing, 1(1),19–24. DOI: 10.21323/2414–438X-2016–1–1–19–24. (In Russian)Armenteros, M., Aristoy, M.C., Barat, J.M., Toldrá, F. (2012). Biochemical and sensory changes in dry-cured ham salted with partial replacements of NaCl by other chloride salts. Meat science, 90(2), 361–367. DOI: 10.1016/j.meatsci.2011.07.023.Armenteros, M., Aristoy, M.C., Barat, J.M., Toldrá, F. (2012). Biochemical and sensory changes in dry-cured ham salted with partial replacements of NaCl by other chloride salts. Meat science, 90(2), 361–367. DOI: 10.1016/j.meatsci.2011.07.023.Graiver, N., Pinotti, A., Califano, A., Zaritzky, N. (2006). Diffusion of sodium chloride in pork tissue. Journal of Food Engineering, 77(4), 910–918. DOI: 10.1016/j.jfoodeng.2005.08.018.Graiver, N., Pinotti, A., Califano, A., Zaritzky, N. (2006). Diffusion of sodium chloride in pork tissue. Journal of Food Engineering, 77(4), 910–918. DOI: 10.1016/j.jfoodeng.2005.08.018.Kijowski, J.M., Mast, M.G. (1988). Effect of sodium chloride and phosphates on the thermal properties of chicken meat proteins. Journal of Food Science, 53(2), 367–370. DOI: 10.1111/j.1365–2621.1988.tb07707.x.Kijowski, J.M., Mast, M.G. (1988). Effect of sodium chloride and phosphates on the thermal properties of chicken meat proteins. Journal of Food Science, 53(2), 367–370. DOI: 10.1111/j.1365–2621.1988.tb07707.x.Ginzburg, A.S. (1990). Thermal characteristics of foods. Reference book. Moscow: Agropromizdat. — 288 p. (In Russian)Ginzburg, A.S. (1990). Thermal characteristics of foods. Reference book. Moscow: Agropromizdat. — 288 p. (In Russian)ASHRAE Handbook. (2014). Chapter 19. Refrigeration. — 31 p. ISBN 978–1–936504–72–5.ASHRAE Handbook. (2014). Chapter 19. Refrigeration. — 31 p. ISBN 978–1–936504–72–5.Höhne, G., Hemminger, W. F., & Flammersheim, H. J. (2013). Differential scanning calorimetry. Springer Science & Business Media. — 298 p.Höhne, G., Hemminger, W. F., & Flammersheim, H. J. (2013). Differential scanning calorimetry. Springer Science & Business Media. — 298 p.

The authors declare that there are no conflicts of interest present.