Differential Scanning Calorimetry of Edible Plant-based Protein Using Glycerol as a Medium

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Abstract

Plant-based protein isolates are common food ingredients. Differential scanning calorimetry is used to forecast functional properties of these isolates as well as to evaluate the propensity of these isolates for bioplastic formation through heat-induced formation of intermolecular disulfide, hydrophobic, and other types of bonds. In this work, differential scanning calorimetry was employed in the study of a suspension containing soy protein isolate and glycerol. It was shown that heat release occurred upon heating the isolate in the presence of glycerol. Preheating-induced denaturation of soy proteins in aqueous solution (95°С, 30 min) made the observed heat more exothermic, whereas exothermic reaction was not observed during enzymatic hydrolysis of the protein. Since adding β-mercaptoethanol to soy protein isolate had no effect on the observed exothermic process, this chemical compound could not contribute to formation of new disulfide bonds. Thus, bioplastic formation using soy protein isolate occurs independently of the formation of new disulfide bonds, and differential scanning calorimetry can be used to assess protein solubility.

About the authors

A. M Lukin

Institute for Biological Instrumentation, Russian Academy of Sciences

Email: email@example.com
Institutskaya ul. 5, Pushchino, Moscow Region, 142290, Russia

M. M Dotlov

Institute for Biological Instrumentation, Russian Academy of Sciences

Email: email@example.com
Institutskaya ul. 5, Pushchino, Moscow Region, 142290, Russia

N. V Pozdnyakov

Institute for Biological Instrumentation, Russian Academy of Sciences; Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences

Email: email@example.com
Institutskaya ul. 5, Pushchino, Moscow Region, 142290, Russia

S. V Shilov

Institute for Biological Instrumentation, Russian Academy of Sciences

Email: email@example.com
Institutskaya ul. 5, Pushchino, Moscow Region, 142290 Russia

R. Kh Sadreeva

Almetyevsk State Oil Institute

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ul. Lenina 2, Almetyevsk, Republic of Tatarstan, 423462 Russia

D. S Beloklokov

Almetyevsk State Oil Institute

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ul. Lenina 2, Almetyevsk, Republic of Tatarstan, 423462, Russia

A. A Zalyatdinov

Almetyevsk State Oil Institute

Email: email@example.com
ul. Lenina 2, Almetyevsk, Republic of Tatarstan, 423462, Russia

V. V Kononenko

Institute for Biological Instrumentation, Russian Academy of Sciences

Email: email@example.com
Institutskaya ul. 5, Pushchino, Moscow Region, 142290, Russia

E. A Sogorin

Institute for Biological Instrumentation, Russian Academy of Sciences

Email: evgenysogorin@gmail.com
Institutskaya ul. 5, Pushchino, Moscow Region, 142290, Russia

References

  1. Hu X.-Z., Cheng Y.-Q., Fan J.-F., Lu Z.-H., Yamaki K., and Li L.-T. Effects of drying method on physicochemical and functional properties of soy protein isolates. J. Food Processing and Preservation, 34 (3), 520–540 (2010).
  2. Astawan M. and Prayudani A. P. The overview of food technology to process soy protein isolate and its application toward food industry. World Nutrition J., 4 (S1), 12–17 (2020).
  3. Liang G., Chen W., Qie X., Zeng M., Qin F., He Z., and Chen J. Modification of soy protein isolates using combined pre-heat treatment and controlled enzymatic hydrolysis for improving foaming properties. Food Hydrocolloids, 105, 105764 (2020).
  4. Meinlschmidt P., Schweiggert-Weisz U., and Eisner P. Soy protein hydrolysates fermentation: Effect of debittering and degradation of major soy allergens. LWTFood Sci. Technol., 71, 202–212 (2016).
  5. Jung S., Murphy P. A., and Johnson L. A. Physicochemical and functional properties of soy protein substrates modified by low levels of protease hydrolysis. J. Food Sci., 70 (2), C180–C187 (2005).
  6. Kempka A., Honaiser T., Fagundes E., and Prestes R. Functional properties of soy protein isolate of crude and enzymatically hydrolysed at different times. Int. Food Res. J., 21 (6), 2229–2236 (2014).
  7. Keeratiurai M., Wang Z., and Corredig M. Adsorption of soy protein isolate in oil-in-water emulsions: difference between native and spray dried isolate. J. Am. Oil Chem. Soc., 88, 1593–1602 (2011).
  8. Keeratiurai M. and Corredig M. Heat-induced changes occurring in oil/water emulsions stabilized by soy glycinin and β-conglycinin. J. Agricultural Food Chem., 58 (16), 9171–9180 (2010).
  9. Keeratiurai M. and Corredig M. Heat-induced changes in oil-in-water emulsions stabilized with soy protein isolate. Food Hydrocolloids, 23 (8), 2141–2148 (2009). doi: 10.1016/j.foodhyd.2009.05.010
  10. Sousa I. M., Mitchell J. R., Ledward D. A., Hill S. E., and Beirao da Costa M. L. Differential scanning calorimetry of lupin and soy proteins. Zeitschrift fur Lebensmittel-Untersuchung und Forschung, 201, 566–569 (1995).
  11. Arntfield S. and Murray E. The influence of processing parameters on food protein functionality I. Differential scanning calorimetry as an indicator of protein denaturation. Can. Institute Food Sci. Technol. J., 14 (4), 289–294 (1981).
  12. Ryan M., McEvoy E., Duignan S., Crowley C., Fenelon M., O’Callaghan D., and FitzGerald R. Thermal stability of soy protein isolate and hydrolysate ingredients. Food Chemistry, 108 (2), 503–510 (2008).
  13. Burova T. V., Grinberg N. V., Grinberg V. Y., Rariy R. V., and Klibanov A. M. Calorimetric evidence for a native-like conformation of hen egg-white lysozyme dissolved in glycerol. Biochim. Biophys. Acta – Protein Structure and Molecular Enzymology, 1478 (2), 309–317 (2000).
  14. Fatkhutdinova A., Mukhametzyanov T., and Schick C. Refolding of lysozyme in glycerol as studied by fast scanning calorimetry. Int. J. Mol. Sci., 23 (5), 2773 (2022).
  15. Cinelli S., De Francesco A., Onori G., and Paciaroni A., Thermal stability and internal dynamics of lysozyme as affected by hydration. Phys.Chem. Chem. Phys., 6 (13), 3591–3595 (2004).
  16. Wang S., Sue H.-J., and Jane J. Effects of polyhydric alcohols on the mechanical properties of soy protein plastics. J. Macromol. Sci. Part A: Pure and Applied Chemistry, 33 (5), 557–569 (1996).
  17. Mo X., Sun X. S. и Wang Y. Effects of molding temperature and pressure on properties of soy protein polymers. J. Appl. Polymer Sci., 73 (13), 2595–2602 (1999).
  18. Swain S., Biswal S., Nanda P., and Nayak P. L. Biodegradable soy-based plastics: opportunities and challenges. J. Polymers Environ., 12, 35–42 (2004).
  19. Gennadios A. and Weller C. Edible films and coatings from soymilk and soy protein. Cereal foods world, 36 (12), 1004–1009 (1991).
  20. Calva-Estrada S. J., Jimenez-Fernandez M., and Lugo-Cervantes E. Protein-based films: Advances in the development of biomaterials applicable to food packaging. Food Eng. Rev., 11, 78–92 (2019).
  21. Pozdnyakov N., Shilov S., Lukin A., Bolshakov M., and Sogorin E., Investigation of enzymatic hydrolysis kinetics of soy protein isolate: laboratory and semi-industrial scale. Bioresources and Bioprocessing 9 (1), 1–13 (2022).
  22. Рахманкулов Д. Л., Кимсанов Б. Х. и Чанышев Р. Р. Физические и химические свойства глицерина, Под общ. ред. акад. АН РБ Д. Л. Рахманкулова (Химия, М., 2003).
  23. Ruan Q., Chen Y., Kong X. and Hua Y. Analysis using fluorescence labeling and mass spectrometry of disulfidemediated interactions of soy protein when heated. J. Agricult. Food Chem., 63 (13), 3524–3533 (2015).
  24. Ruan Q., Chen Y., Kong X., and Hua Y. Heat-induced aggregation and sulphydryl/disulphide reaction products of soy protein with different sulphydryl contents. Food Chem., 156, 14–22 (2014).

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