Optimisation of plant protein hydrolysis in presence of yeast proteases

Cover Page

Cite item

Full Text

Abstract

A methodology is described for optimizing the process of enzymatic hydrolysis of plant proteins by yeast proteases Saccharomyces carlsbergensis using model soy protein as a substrate. Enzymatic treatment was carried out under the influence of autolyzed brewer’s yeast waste containing up to 40 % active yeast cells. It is shown that as a result of process optimization using the simplex method of experiment planning, optimal conditions for conducting the process of enzymatic hydrolysis of plant proteins in the presence of brewer’s yeast biomass were found, which were: protein concentration in the suspension 30 %, amount of added yeast suspension 40 %, sodium citrate content 5,6 %, ethanol 4,2 %, added water 20,2 %. The time of hydrolytic treatment at the optimum temperature of 58 °C was 4,3 hours. The product yield, assessed by the nitrogen content of free amino groups, increased from 10...12 % without optimization to 34 % as a result of the optimization of process parameters. It has been shown that the maximum rate of the process of hydrolytic decomposition of plant proteins under optimal conditions is more than 0,48∙10–3 mgNH2/ml∙min, and the activation energy Ea is 80,7 kJ/mol. The possibility of additionally increasing the yield of the target hydrolyzate by re-introducing the enzyme preparation pancreatin into the system was established, as a result of which it was possible to increase the yield of the product to 52...55 % and obtain a product balanced in amino acid composition. It was found that the amino acid composition of the resulting enzymatic hydrolyzate included all essential amino acids, g/100 g protein: Ile 4,7; Leu 7,0; Lys 6,9; Met 1,6; Cys 3,7; Phe 5,8; Tyr 4,1; Tre 4,2; Trp 1,5; Val 6,8; as well as non-essential amino acids: Ala 5,9; Arg 5,5; Asp 8,8; His 3,3; Gly 3,8; Glu 10,2; Pro 5,1; Ser 9,0. It has been shown that the enzymatic hydrolyzate has potentially high biological value, which can facilitate its effective use as part of highly nutritious systems.

About the authors

Andrey N. Ivankin

BMSTU (Mytishchi branch)

Author for correspondence.
Email: aivankin@mgul.ac.ru

Dr. Sci. (Chem.), Member of the International Higher Education Academy of Sciences (IHEAS), Professor of the Department of Chemistry

Russian Federation, 1 st. Institutskaya, 141005, Mytischi, Moscow reg.

References

  1. Mileti О., Baldino N., Lupi F.R., Gabriele D. Interfacial behavior of vegetable protein isolates at sunflower oil/water interface. Colloids and Surfaces B: Biointerfaces, 2023, v. 221, p. 113035. doi.org/10.1016/j.colsurfb.2022.113035
  2. Adeva-Andany M.A., Fernandez-Fernandez C., Carneiro-Freire N., Vila-Altesor M., Ameneiros-Rodríguez E. The differential effect of animal versus vegetable dietary protein on the clinical manifestations of diabetic kidney disease in humans. Clinical Nutrition ESPEN, 2022, v. 48, pp. 21–35. doi.org/10.1016/j.clnesp.2022.01.030
  3. Castro-Rubio A. ,García M.C.,Marina M.L. Rapid separation of soybean and cereal (wheat, corn, and rice) proteins in complex mixtures: Application to the selective determination of the soybean protein content in commercial cereal-based products. Analytica Chimica Acta, 2006, v. 558, no. 2, pp.28–34. doi.org/10.1016/j.aca.2005.10.076
  4. Ijarotimi O.S., Fakayejo D.A., Oluwajuyitan T.D. Nutritional characteristics, glycaemic index and blood glucose lowering property of gluten-free composite flour from wheat, soybean, oat-bran and rice-bran. Applied Food Research, 2021, v. 1, no. 2, p. 100022. doi.org/10.1016/j.afres.2021.100022
  5. Dizlek H., Girard A.L., Awika J.M. High protein and gliadin content improves tortilla quality of a weak gluten wheat. LWT, 2022, v. 160, no. 4, p. 113320. doi.org/10.1016/j.lwt.2022.113320
  6. Sadh P.K., Chawla P., Kumar S., Das A., Kumar R., Bains A., Sridhar K., Duhan J.S., Sharma M. Recovery of agricultural waste biomass: A path for circular bioeconomy. Science of The Total Environment, 2023, v. 870, no. 4, p. 161904. doi. org/10.1016/j.scitotenv.2023.161904
  7. Kuznetsova T.G., Ivankin A.N., Kulikovskiy A.V. Nanosensornyy analiz myasnogo syr’ya i rastitel’nyh ob’ektov. [Nanosensor analysis of meat raw materials and plant objects]. Saarbrücken: LAMBERT Academic Publishing, 2012, 232 p.
  8. Awogbemi О., Von Kallon D.V. Pretreatment techniques for agricultural waste. Case Studies in Chemical and Environmental Engineering, 2022, v. 6, no. 12, p. 100229. doi.org/10.1016/j.cscee.2022.100229
  9. Korkmaz K., Tokur B. Optimization of hydrolysis conditions for the production of protein hydrolysates from fish wastes using response surface methodology. Food Bioscience, 2022, v. 45, no. 2, p. 101312. doi.org/10.1016/j.fbio.2021.101312
  10. Ariaeenejad S., Kavousi K., Sheykh A., Mamaghani A., Ghasemitabesh R., Salekdeh G.H. Simultaneous hydrolysis of various protein-rich industrial wastes by a naturally evolved protease from tannery wastewater microbiota. Science of The Total Environment, 2022, v. 815, no. 4, p. 152796. doi.org/10.1016/j.scitotenv.2021.152796
  11. Srivastava R. K., Nedungadi S.V., Akhtar N., Sarangi P.K., Subudhi S., Shadangi K.P., Govarthanan M. Effective hydrolysis for waste plant biomass impacts sustainable fuel and reduced air pollution generation: A comprehensive review. Science of The Total Environment, 2023, v. 859(2), no. 2, p. 160260. doi.org/10.1016/j.scitotenv.2022.160260
  12. Kadyrov F.F., Yabbarov A.M., Paramonova T.A., Gnusarev S.S. Proekt kompleksnoy bezotkhodnoy zagotovki i pererabotki drevesiny [Project for integrated waste-free harvesting and processing of wood]. Intensifikatsiya ispol'zovaniya i vosproizvodstva lesov [Intensification of forest use and reproduction]. Ulyanovsk, 2024, pp. 91–96.
  13. Kumar D., Tarafdar F., Kumar Y., Dass S.L., Pareek S., Badgujar P.C. Production of functional spent hen protein hydrolysate powder and its fortification in food supplements: A waste to health strategy. Food Bioscience, 2022, v. 50(B), no. 12, p. 102193. doi.org/10.1016/j.fbio.2022.102193
  14. Muhammad Mustafa Abeer M.M., Trajkovic S., Brayden D.J. Measuring the oral bioavailability of protein hydrolysates derived from food sources: A critical review of current bioassays. Biomedicine & Pharmacotherapy, 2021, v. 144, no. 12, p. 112275. doi.org/10.1016/j.biopha.2021.112275
  15. Neklyudov A.D., Ivankin A.N., Berdutina A.V. Production and purification of protein hydrolysates (review). Applied Biochemistry and Microbiology, 2000, v. 36, no. 4, pp. 317–324.
  16. Marson G.V., Machado M.T., de Castro R.J., Hubinger M.D. Sequential hydrolysis of spent brewer’s yeast improved its physico-chemical characteristics and antioxidant properties: A strategy to transform waste into added-value biomolecules. Process Biochemistry, 2019, v. 84, no. 9, pp. 91–102. doi.org/10.1016/j.procbio.2019.06.018
  17. Lisitsyn A.B., Ivankin A.N., Neklyudov A.D. Metody prakticheskoy biotehnologii [Methods of practical biotechnology]. Moscow: VNIIMP, 2002, 408 p.
  18. Ivankin A.N., Oliferenko G.L., Kulikovsky A.V. Analiticheskaya himiya [Analytical chemistry]. Moscow: Knorus, 2021, 300 p.
  19. Neklyudov A.D., Berdutina A.V., Ivankin A.N., Karpo B.S., Osoka A.V. Determination of the kinetic constants of hydrolysis of keratin-containing raw materials. Applied Biochemistry and Microbiology, 1999, v. 35, no. 1, pp. 45–49.
  20. Ivankin A.N., Krasnoshtanova A.A. Gidroliz nanobiomakromolekulyarnyh sistem [Hydrolysis of nanobio-macromolecular systems]. Moscow: Moscow State Forest University, 2010, 396 p.
  21. Liu P., Zhao Y., Guo H., Chang J.S., Lee D.J. Enzymolysis kinetics of corn straw by impeded Michaelis model and Box- Behnken design // Environmental Research, 2024, v. 242, no. 2, 117658. doi.org/10.1016/j.envres.2023.117658
  22. Douglas J., Carter C.W., Wills P.R. A Michaelis-Menten model for non-homogeneous enzyme mixtures //iScience, 2024, v. 27, no. 2, p. 108977. doi.org/10.1016/j.isci.2024.108977
  23. Yang M., Ye A., Yang Z., Everett D.W., Gilbert E.P., Singh H. Kinetics of pepsin-induced hydrolysis and the coagulation of milk proteins // Journal of Dairy Science, 2022, v. 105, no. 2, pp. 990–1003. doi.org/10.3168/jds.2021-21177
  24. Raska P., Ulrych Z. Comparison of Modified Downhill Simplex and Differential Evolution with other Selected Optimization Methods used for Discrete Event Simulation Models // Procedia Engineering, 2015, v. 100, no. 2, pp. 807–815. doi.org/10.1016/j.proeng.2015.01.435
  25. Lakin G.F. Biometriya [Biometrics]. Moscow: Higher School, 1990, 351 p.
  26. Bychkova E., Rozhdestvenskaya L., Podgorbunskikh E., Kudachyova P. The problems and prospects of developing food products from high-protein raw materials // Food Bioscience, 2023, v. 56, no. 12, p. 103286. doi.org/10.1016/j.fbio.2023.103286
  27. Feng L., Wu Y., Han Y., Yao X., Li Q., Liu M., Cao Y. Structural characteristics, functional properties and nutritional value of walnut protein by limited enzymatic hydrolysis // LWT, 2024. v. 197, no. 4, p. 115923. doi.org/10.1016/j.lwt.2024.115923
  28. Sautin S.N. Planirovanie eksperimenta v himii i himicheskoy tehnologii [Planning an experiment in chemistry and chemical technology]. Leningrad: Chemistry, 1975, 48 p.
  29. Chat GPT neural network. Available at: https://gpt-chatbot.ru/ (accessed 15.05.2023).
  30. Dai H., An H. Effect of protease hydrolysis pretreatment on extruder response and the structural characteristics of high-moisture plant-protein extrudates // Journal of Food Engineering, 2024, no. 3, p. 112062. doi.org/10.1016/j.jfoodeng.2024.112062
  31. Wang Y., Li Z., Li H., Selomulya K. Effect of hydrolysis on the emulsification and antioxidant properties of plant-sourced proteins // Current Opinion in Food Science, 2022, v. 48, no. 12, p. 100949. doi.org/10.1016/j.cofs.2022.100949
  32. Neklyudov A.D., Fedorova N.V., Ilyukhina V.P., Lisitsa E.P. Enzymatic profile of autolyzing yeast of the genus Saccharomyces // Applied Biochemistry and Microbiology, 1993, v. 29, no. 5, pp. 734–743.
  33. Blayo C., Vidcoq O., Lazennec F., Dumay E. Effects of high pressure processing (hydrostatic high pressure and ultra-high pressure homogenisation) on whey protein native state and susceptibility to tryptic hydrolysis at atmospheric pressure // Food Research International, 2016, v. 79, no. 1, pp. 40–53. doi.org/10.1016/j.foodres.2015.11.024
  34. Luo L., Yan B., Xu S., Zhou J., Liang J., Zhao J., Tyagi R.D., Wong W.C. Regulation of acidogenic fermentation through exogenous additives for promoting carbon conversion of food waste in two-phase anaerobic system // Bioresource Technology, 2023, v. 368, no. 1, p. 128368. doi.org/10.1016/j.biortech.2022.128368
  35. Zhao Q., Fan Y., Zhao L., Zhu Y., Jiang Y., Gu J., Xue Y., Hao Z., Shen Q. Identification and molecular binding mechanism of novel pancreatic lipase and cholesterol esterase inhibitory peptides from heat-treated adzuki bean protein hydrolysates // Food Chemistry, 2024, v. 439, no. 5, p. 138129. doi.org/10.1016/j.foodchem.2023.138129

Supplementary files

Supplementary Files
Action
1. JATS XML
Download

Copyright (c) 2024 Ivankin A.N.

Creative Commons License
This work is licensed under a Creative Commons Attribution 4.0 International License.
СМИ зарегистрировано Федеральной службой по надзору в сфере связи, информационных технологий и массовых коммуникаций (Роскомнадзор).
Регистрационный номер и дата принятия решения о регистрации СМИ: серия ПИ № ФС 77 - 68118 от  21.12.2016.