Effect of Different Classes of Proteases on Techno-functional Properties of Pea Protein Isolates

Cover Page

Cite item

Full Text

Open Access Open Access
Restricted Access Access granted
Restricted Access Subscription or Fee Access

Abstract

The effect of four enzyme preparations: bacillolysin, agroprot, protozyme and protozyme C (Russia) on solubility, emulsifying activity, emulsion stability, foaming and foam stability of isolates preparated from two varieties of peas was studied. It is shown that treatment with enzymes can increase the solubility of isolates at pH 5 by more than 7 times, the index of emulsifying activity at pH 5 by 1.5 to 2 times, and at pH 6 by almost 1.5 times; the stability index of the emulsion increased by about 20% at pH 5, and by 1.7 times (in one of the varieties) at pH 6; foaming increased by 2.4 to 3 times at pH 5, and at pH 6 by 1.8 to 3.7 times; foam stability increased by 25 to 33% at pH 5 and by more than 1.5 times (in one of the varieties) at pH 6. The results obtained made it possible to select an enzyme preparation (bacterial alkaline serine protease) to improve the parameters of pea protein isolates intended for the manufacture of analogues of fermented milk products.

Full Text

Restricted Access

About the authors

I. V. Kravchenko

Research Center of Biotechnology of the RAS

Author for correspondence.
Email: ink71@yandex.ru

Bach Institute of Biochemistry

Russian Federation, Moscow, 119071

V. A. Furalyov

Research Center of Biotechnology of the RAS

Email: ink71@yandex.ru

Bach Institute of Biochemistry

Russian Federation, Moscow, 119071

E. V. Kostyleva

All-Russian Scientific Research Institute of Food Biotechnology — a Branch of the Federal Research Center for Nutrition, Biotechnology and Food Safety

Email: ink71@yandex.ru
Russian Federation, Moscow, 111033

A. S. Sereda

All-Russian Scientific Research Institute of Food Biotechnology — a Branch of the Federal Research Center for Nutrition, Biotechnology and Food Safety

Email: ink71@yandex.ru
Russian Federation, Moscow, 111033

E. I. Kurbatova

All-Russian Scientific Research Institute of Food Biotechnology — a Branch of the Federal Research Center for Nutrition, Biotechnology and Food Safety

Email: ink71@yandex.ru
Russian Federation, Moscow, 111033

N. V. Tsurikova

All-Russian Scientific Research Institute of Food Biotechnology — a Branch of the Federal Research Center for Nutrition, Biotechnology and Food Safety

Email: ink71@yandex.ru
Russian Federation, Moscow, 111033

E. S. Pshennikova

Research Center of Biotechnology of the RAS

Email: ink71@yandex.ru

Bach Institute of Biochemistry

Russian Federation, Moscow, 119071

T. V. Boyarintseva

Research Center of Biotechnology of the RAS

Email: ink71@yandex.ru

Bach Institute of Biochemistry

Russian Federation, Moscow, 119071

V. O. Popov

Research Center of Biotechnology of the RAS

Email: ink71@yandex.ru

Bach Institute of Biochemistry

Russian Federation, Moscow, 119071

A. N. Fedorov

Research Center of Biotechnology of the RAS

Email: ink71@yandex.ru

Bach Institute of Biochemistry

Russian Federation, Moscow, 119071

References

  1. Tesarowicz I., Zawiślak A., Maciejaszek I., Surówka K. // International J. Food Sciences. 2022. V. 2022. P. 6187441. https://doi.org/10.1155/2022/6187441
  2. Schlegel K., Sontheimer K., Eisner P., Schweiggert-Weisz U. // Food Science & Nutrition. 2019. V. 8. P. 3041–3051. https://doi.org/10.1002/fsn3.1286
  3. Meinlschmidt P., Schweiggert-Weisz U., Brode V., Eisner P. // LWT — Food Science & Technology. 2016. V. 68. P. 707–716. https://doi.org/10.1016/j.lwt.2016.01.023
  4. Yust M. M., Pedroche J., Millán-Linares M. C., Alcaide-Hidalgo J.M., Millán F. // Food Chemistry. 2010. V. 122. № 4. P. 1212–1217. https://doi.org/10.1016/j.foodchem.2013.11.053
  5. Yust M. M., Millán-Linares M. D. C., Alcaide-Hidalgo J. M., Millán F., Pedroche J. // Food Science & Technology International. 2013. V. 19. P. 217–223. https://doi.org/10.1177/1082013212442197
  6. Paraman I., Hettiarachchy N. S., Schaefer C., Beck M. I. // Cereal Chemistry. 2007. V. 84. P. 343–349. https://doi.org/10.1094/CCHEM-84-4-0343
  7. Neves V. A., Lourenço E. J., da Silva M. A. // Arch. Latinoam. Nutr. 1996. V. 46. № 3. P. 238–242.
  8. Higgins T. J., Chandler P. M., Randall P. J., Spencer D., Beach L. R., Blagrove R. J., Kortt A. A., Inglis A. S. // J. Biol. Chem. 1986. V. 261. P. 11124–11130. https://doi.org/10.1016/S0021-9258(18)67357-0
  9. Stone A. K., Karalash A., Tyler R. T., Warkentin T. D., Nickerson N. T. // Food Research International. 2015. V. 76. P. 31–38. doi: 10.1016/j.foodres.2014.11.017
  10. Asen N. D., Aluko R. E. // Front Nutr. 2022. V. 9. P. 852225. https://doi.org/10.3389/fnut.2022.852225
  11. Ivanova P., Kalaydzhiev H., Dessev T. T., Silva C. L. M., Rustad T., Chalova V. I. J. // Food Sci. Technol. 2018. V. 55. № 9. P. 3792–3798. https://doi.org/10.1007/s13197-018-3311-y
  12. Nielsen P. M., Petersen D., Dambmann C. // J. Food Sci. 2001. V. 66. № 5. P. 642–646. https://doi.org/10.1111/j.1365-2621.2001.tb04614.x
  13. Adler-Nissen J. Enzymic Hydrolysis of Food Proteins. // New York: Elsevier Applied Science Publishers, 1986. 427 р.
  14. Matoba T. // Agric Biol Ghem. 1972. V. 36. P. 1423–1443. https://doi.org/10.1080/00021369.1972.10860410
  15. Barac M., Cabrilo S., Pesiesic M., Stanojevic S., Zilic S., Macej O., Ristic N. // Int. J. Mol. Sci. 2010. V. 1. P. 4973–4990. https://doi.org/10.3390/ijms11124973
  16. Robinson G. H.; Domoney C. // Plant Physiol. Biochem. 2021. V. 158. P. 353–362. https://doi.org/10.1016/j.plaphy.2020.11.020
  17. Klost M., Drusch S. // Food Hydrocoll. 2019. V. 86. P. 134–140. https://doi.org/10.14279/depositonce-9553

Supplementary files

Supplementary Files
Action
1. JATS XML
Download
2. Fig. 1. Laemmli electrophoresis of protein isolates obtained from pea varieties Rodnik (a, c, d, g) and Fokor (b, d, f, h) and treated with 8.9 units/ml BNP (a, b), 1.5 units/ml GKP (c, d), 1.5 units/ml GSP (d, f) and 1.5 units/ml BSCP (g, h): 1 — untreated isolate, 2 — 15 min, 3 — 30 min, 4 — 1 h, 5 — 2 h of treatment; M — molecular weight markers.

Download (258KB)
Indexing metadata
3. Fig. 2. Effect of treatment with BNP, GKP, GSHP and BSCHP on the solubility of pea protein isolates of the Rodnik (a, c) and Fokor (b, d) varieties at pH 5.0 (a, b) and 6 (c, d) and different treatment times: 1 - no treatment, 2 - 15 min; 3 - 30 min; 4 - 1 h; 5 - 2 h.

Download (735KB)
Indexing metadata
4. Fig. 3. Effect of treatment with BNP, GKP, GSHP and BSCHP on the emulsifying activity index of pea protein isolates of the Rodnik (a, c) and Fokor (b, d) varieties at pH 5.0 (a, b) and 6.0 (c, d) with different treatment times: 1 - no treatment, 2 - 15 min; 3 - 30 min; 4 - 1 h; 5 - 2 h.

Download (678KB)
Indexing metadata
5. Fig. 4. Effect of BNP, GKP, GSHP and BSCP treatment on the emulsion stability index of pea protein isolates of the Rodnik (a, c) and Fokor (b, d) varieties at pH 5 (a, b) and 6 (c, d) with different treatment times: 1 — no treatment, 2 — 15 min; 3 — 30 min; 4 — 1 h; 5 — 2 h.

Download (670KB)
Indexing metadata
6. Fig. 5. Effect of BNP, GKP, GSHP and BSCP treatment on foaming of pea protein isolates of the Rodnik (a, c) and Fokor (b, d) varieties at pH 5 (a, b) and 6 (c, d) with different treatment times: 1 — no treatment; 2 — 15 min; 3 — 30 min; 4 — 1 h; 5 — 2 h.

Download (678KB)
Indexing metadata
7. Fig. 6. Effect of treatment with BNP, GKP, GSHP and BSHP on the foam stability of pea protein isolates of the Rodnik (a, c) and Fokor (b, d) varieties at pH 5.0 (a, b) and 6 (c, d) for different treatment times: 1 - no treatment, 2 - 15 min; 3 - 30 min; 4 - 1 h; 5 - 2 h.

Download (830KB)
Indexing metadata

Copyright (c) 2024 Russian Academy of Sciences