PROTEIN ISOLATES FROM DEFATTED PEA FLOUR: PRODUCTION AND QUALITY ASSESSMENT
Abstract and keywords
Abstract:
Advances in pea protein isolate technology are driving interest across research and industrial food sectors. Without defatting stage, pea protein isolate tends to demonstrate lower quality and protein content (80–85%), compared to animal or vegetable analogues (≥ 90%). This article introduces an improved pea protein isolate technology with increased protein mass fraction. Protein isolate samples were obtained from pea flour by alkaline extraction with isoelectric deposition. N-hexane, acetone, and ethanol served as defatters. The chemical composition, whiteness, solubility, amino acid composition, and IR spectra of proteins were studied using standard physicochemical methods. The solvent used at the defatting stage proved to affect the properties of protein isolate and protein flour. The defatted flour was whiter, and the color of the finished product was better. The protein content in the defatted protein isolate was 84.7% when using n-hexane, 88.0% for acetone, and 89.6% for ethanol. The protein was rich in essential amino acids; the water solubility improved. The IR spectra revealed no structural changes. Acetone proved to be the most suitable solvent, yielding a protein-rich product with improved characteristics. Defatting significantly increased protein yield and improved the color profile of protein isolate. These insights are applicable for optimizing the processing of both plant and animal-derived proteins.

Keywords:
Vegetable raw material, peas, pea flour, protein product, protein isolate, defatting, technology improvement, amino acid composition, product quality
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References

1. Glukharev AYu, Bordiyan VV, Kuzina TD, Kuchina YuA, Derkach SR. Production and use of mussel shell protein in dry fish sauce. Food Systems. 2025;8(1):134–143. (In Russ.) https://doi.org/10.21323/2618-9771-2025-8-1-134-143

2. Wan M-C, Qin W, Lei C, Li Q, Meng M, et al. Biomaterials from the sea: Future building blocks for biomedical applications. Bioactive Materials. 2021;6(12):4255–4285. https://doi.org/10.1016/j.bioactmat.2021.04.028

3. Wu G. Dietary protein intake and human health. Food & Function. 2016;7(3):1251–1265. https://doi.org/10.1039/C5FO01530H

4. Derkach SR, Grokhovsky VA, Kuranova LK, Volchenko VI. Nutrient analysis of underutilized fish species for the production of protein food. Foods and Raw Materials. 2017;5(2):15–23. http://doi.org/10.21603/2308-4057-2017-2-15-23

5. Derkach SR, Kuchina YA, Kolotova DS, Petrova LA, Volchenko VI, et al. Properties of protein isolates from marine hydrobionts obtained by isoelectric solubilisation/precipitation: Influence of temperature and processing time. International Journal of Molecular Sciences. 2022;23:14221. https://doi.org/10.3390/ijms232214221

6. Saeed F, Zohra KT, Naveed K, Zia A, Khaliq M, et al. Algal Proteins for sustainable nutrition and functional food innovation. Applied Food Research. 2025;100752. https://doi.org/10.1016/j.afres.2025.100752

7. Xu X, Sharma P, Shu S, Lin T, Ciais P, et al. Global greenhouse gas emissions from animal-based foods are twice those of plant-based foods. Nature Food. 2021;2(9):724–732. https://doi.org/10.1038/s43016-021-00358-x

8. Henchion M, Hayes M, Mullen AM, Fenelon M, Tiwari B. Future protein supply and demand: Strategies and factors influencing a sustainable equilibrium. Foods. 2017;6(7):53. https://doi.org/10.3390/foods6070053

9. Aidoo R, Abe-Inge V, Kwofie EM, Baum JI, Kubow S. Sustainable healthy diet modeling for a plant-based dietary transitioning in the United States. npj Science of Food. 2023;7:61. https://doi.org/10.1038/s41538-023-00239-6

10. Smith K, Watson AW, Lonnie M, Peeters WM, Oonincx D, et al. Meeting the global protein supply requirements of a growing and ageing population. European Journal of Nutrition. 2024;63:1425–1433. https://doi.org/10.1007/s00394-024-03358-2

11. Gharaviri M, Aleksanochkin DI, Ahangaran M, Fomenko IA, Kovalev LI, Kovaleva MA, et al. Chickpea protein hydrolysates: Production, bioactivity, functional profile, and technological properties. Foods and Raw Materials. 2026;14(1):198–213. https://doi.org/10.21603/2308-4057-2026-1-666

12. Boukid F, Rosell CM, Castellari M. Pea protein ingredients: A mainstream ingredient to (re)formulate innovative foods and beverages. Trends in Food Science & Technology. 2021;110:729–742. https://doi.org/10.1016/j.tifs.2021.02.040

13. Meganaharshini M, Sudhakar V, Bharathi ND, Deepak S. Review on recent trends in the application of protein concentrates and isolates – a food industry perspective. Food and Humanity. 2023;1:308–325. https://doi.org/10.1016/j.foohum.2023.05.022

14. Zhang T, Dou W, Zhang X, Zhao Y, Zhang Y, et al. The development history and recent updates on soy proteinbased meat alternatives. Trends in Food Science & Technology. 2021;109:702–710. https://doi.org/10.1016/j.tifs.2021.01.060

15. Khrulyov AA, Beschetnikova NA, Fedotov IA. Development tendencies and economic aspects of the pea protein production. Food Industry. 2016;4:24–29. (In Russ.) https://elibrary.ru/TWSNMN

16. Aschemann-Witzel J, Gantriis RF, Fraga P, Perez-Cueto FJA. Plant-based food and protein trend from a business perspective: Markets, consumers, and the challenges and opportunities in the future. Critical Reviews in Food Science and Nutrition. 2020;61(18):3119–3128. https://doi.org/10.1080/10408398.2020.1793730

17. Ismail BP, Senaratne-Lenagala L, Stube A, Brackenridge A. Protein demand: Review of plant and animal proteins used in alternative protein product development and production. Animal Frontiers. 2020;10(4):53–63. https://doi.org/10.1093/af/vfaa040

18. Shanthakumar P, Klepacka J, Bains A, Chawla P, Dhull SB, et al. The current situation of pea protein and its application in the food industry. Molecules. 2022;27:5354. https://doi.org/10.3390/molecules27165354

19. Taylor SL, Baumert JL. Worldwide food allergy labeling and detection of allergens in processed foods. Chemical Immunology and Allergy. 2015;101:227–234. https://doi.org/10.1159/000373910

20. Guillin FM, Gaudichon C, Guérin-Deremaux L, Lefranc-Millot C, Azzout-Marniche D, et al. Multi-criteria assessment of pea protein quality in rats: A comparison between casein, gluten and pea protein alone or supplemented with methionine. British Journal of Nutrition. 2021;125(4):389–397. https://doi.org/10.1017/S0007114520002883

21. Guillin FM, Gaudichon C, Guérin-Deremaux L, Lefranc-Millot C, Airinei G, et al. Real ileal amino acid digestibility of pea protein compared to casein in healthy humans: A randomized trial. The American Journal of Clinical Nutrition. 2022;115(2):353–363. https://doi.org/10.1093/ajcn/nqab354

22. Porzucek H, Larsson-Raźnikiewicz M, Klepacka M. In vitro protein digestibility of flours and protein isolates from seeds of some leguminous plants. Swedish Journal of Agricultural Research. 1991;21(2):49–53.

23. Melchior S, Moretton M, Alongi M, Calligaris S, Nicoli MC, Anese M. Comparison of protein in vitro digestibility under adult and elderly conditions: The case study of wheat, pea, rice, and whey proteins. Food Research International. 2023;163:112147. https://doi.org/10.1016/j.foodres.2022.112147

24. Santos-Hernández M, Alfieri F, Gallo V, Miralles B, Masi P, et al. Compared digestibility of plant protein isolates by using the INFOGEST digestion protocol. Food Research International. 2020;137:109708. https://doi.org/10.1016/j.foodres.2020.109708

25. Taylor SL, Marsh JT, Koppelman SJ, Kabourek JL, Johnson PE, et al. A perspective on pea allergy and pea allergens. Trends in Food Science & Technology. 2021;116:186–198. https://doi.org/10.1016/j.tifs.2021.07.017

26. Abi-Melhem R, Hassoun Y. Is pea our hidden allergen? An American pediatric case series. Journal of Allergy and Clinical Immunology: Global. 2023;2(2):100090. https://doi.org/10.1016/j.jacig.2023.100090

27. Ivashchenko LV, Ambartsumov TG, Zakharova UE. Analysis of the possibility of producing pea isolate: Proceedings of the XII Congress of Young Scientists. Saint Petersburg, 2023;26–28. (In Russ.) https://elibrary.ru/HORZXH

28. Kolpakova VV, Kulikov DS, Ulanova RV, Chumikina LV. Food and feed protein preparations from peas and chickpeas: Production, properties, application. Food Processing: Techniques and Technology. 2021;51(2):333–348. (In Russ.) https://doi.org/10.21603/2074-9414-2021-2-333-348

29. Begeulov MSh. Fundamentals of soybean seed processing. Moscow: DeLi print; 2006. 181 p. (In Russ.) https://elibrary.ru/QNGPGD

30. Dolgopolov VG. Vegetable protein. Moscow: Agropromizdat; 1991. 684 p. (In Russ.)

31. Gao Z, Shen P, Lan Y, Cui L, Ohm JB, et al. Effect of alkaline extraction pH on structure properties, solubility, and beany flavor of yellow pea protein isolate. Food Research International. 2020;131:109045. https://doi.org/10.1016/j.foodres.2020.109045

32. Vogelsang-O’Dwyer M, Zannini E, Arendt EK. Production of pulse protein ingredients and their application in plantbased milk alternatives. Trends in Food Science & Technology. 2021;110:364–374. https://doi.org/10.1016/j.tifs.2021.01.090

33. Alemu TM, Janssen AE, Padt A, Boom RM. Micro-and ultrafiltration of pea proteins from a water-only extraction process. Separation and Purification Technology. 2025;133663. https://doi.org/10.1016/j.seppur.2025.133663

34. Sharma S, Kaur M, Goyal R, Gill BS. Physical characteristics and nutritional composition of some new soybean (Glycine max (L.) Merrill) genotypes. Journal of Food Science and Technology. 2014;51(3):551–557. https://doi.org/10.1007/s13197-011-0517-7

35. Esteves EA, Martino HSD, Oliveira FCE, Bressan J, Costa NMB. Chemical composition of a soybean cultivar lacking lipoxygenases (LOX2 and LOX3). Food Chemistry. 2010;122(1):238–242. https://doi.org/10.1016/j.foodchem.2010.02.069

36. Gravel A, Marciniak A, Couture M, Doyen A. Effects of hexane on protein profile, solubility and foaming properties of defatted proteins extracted from Tenebrio molitor larvae. Molecules. 2021;26(2):351. https://doi.org/10.3390/molecules26020351

37. Trindler C, Kopf-Bolanz KA, Denkel C. Aroma of peas, its constituents and reduction strategies – effects from breeding to processing. Food Chemistry. 2022;376:131892. https://doi.org/10.1016/j.foodchem.2021.131892

38. Wang D, Xiao H, Lyu X, Chen H, Wei F. Lipid oxidation in food science and nutritional health: A comprehensive review. Oil Crop Science. 2023;8(1):35–44. https://doi.org/10.1016/j.ocsci.2023.02.002

39. Gravel A, Dubois-Laurin F, Doyen A. Effects of hexane on protein profile and techno-functional properties of pea protein isolates. Food Chemistry. 2023;406:135069. https://doi.org/10.1016/j.foodchem.2022.135069

40. L’hocine L, Boye JI, Arcand Y. Composition and functional properties of soy protein isolates prepared using alternative defatting and extraction procedures. Journal of Food Science. 2006;71(3):137–145. https://doi.org/10.1111/j.1365-2621.2006.tb15609.x

41. Dirr S, Karslioglu OO, Ates EG, Oztop MH. Defatting strategies for chia protein production: Effects on physicochemical properties. Future Foods. 2025;100729. https://doi.org/10.1016/j.fufo.2025.100729

42. Russin TA, Boye JI, Arcand Y, Rajamohamed SH. Alternative techniques for defatting soy: A practical review. Food and Bioprocess Technology. 2011;4(2):200–223. https://doi.org/10.1007/s11947-010-0367-8

43. Apyantseva YV, Borisova II, Baranenko DA. A review of chickpea isolation technology. Polzunovskiy Vestnik. 2024;(2):27–36. (In Russ.) https://doi.org/10.25712/astu.2072-8921.2024.02.004

44. Berghout JAM, Boom RM, Van Der Goot AJ. The potential of aqueous fractionation of lupin seeds for high-protein foods. Food Chemistry. 2014;159:64–70. https://doi.org/10.1016/j.foodchem.2014.02.166

45. Wanniarachchi PC, Mocerino M, Hackett MJ, Nesbit M, Shea G, et al. Comparative analysis of thermal, structural and rheological properties of protein isolates and kernel flour from Australian sweet lupin varieties using soy as a reference. Food Hydrocolloids. 2026;172(Part 2):112000. https://doi.org/10.1016/j.foodhyd.2025.112000

46. Liang G, Chen W, Guo K, Zhaojun W, Qiuming C, et al. The impact of pH-shifting and heat treatment on soy protein isolates: Structural changes and foaming properties. Food Bioscience. 2025;74:107844. https://doi.org/10.1016/j.fbio.2025.107844

47. Capellini MC, Giacomini V, Cuevas MS, Rodrigues CE. Rice bran oil extraction using alcoholic solvents: Physicochemical characterization of oil and protein fraction functionality. Industrial Crops and Products. 2017;104:133–143. https://doi.org/10.1016/j.indcrop.2017.04.017

48. Nikiforova TA, Severinenko SM, Kulikov DA, Ponomarev SG. Potentialities of cereal industries by-products. Vestnik Orenburg State University. 2010;5(111):141–144. (In Russ.) https://elibrary.ru/MSOJSD

49. Wei S-T, Ou L-C, Luo MR, Hutchings JB. Optimisation of food expectations using product colour and appearance. Food Quality and Preference. 2012;23(1):49–62. https://doi.org/10.1016/j.foodqual.2011.07.004

50. Edelenbos M, Christensen LP, Grevsen K. HPLC determination of chlorophyll and carotenoid pigments in processed green pea cultivars (Pisum sativum L.). Journal of Agricultural and Food Chemistry. 2001;49(10):4768–4774. https://doi.org/10.1021/jf010569z

51. Cheng M, McPhee KE, Baik BK. Bleaching of green peas and changes in enzyme activities of seeds under simulated climatic conditions. Journal of Food Science. 2004;69(7):511–518. https://doi.org/10.1111/j.1365-2621.2004.tb13644.x

52. Steet JA, Tong CH. Degradation kinetics of green color and chlorophylls in peas by colorimetry and HPLC. Journal of Food Science. 1996;61(5):924–928. https://doi.org/10.1111/j.1365-2621.1996.tb10903.x

53. Ashokkumar K, Diapari M, Jha AB, Tar’an B, Arganosa G, et al. Genetic diversity of nutritionally important carotenoids in 94 pea and 121 chickpea accessions. Journal of Food Composition and Analysis. 2015;43:49–60. https://doi.org/10.1016/j.jfca.2015.04.014

54. Ashokkumar K, Tar’an B, Diapari M, Arganosa G, Warkentin TD. Effect of cultivar and environment on carotenoid profile of pea and chickpea. Crop Science. 2014;54(5):2225–2235. https://doi.org/10.2135/cropsci2013.12.0827

55. Ndiritu AK, Kinyuru JN, Kenji GM, Gichuhi PN. Extraction technique influences the physico-chemical characteristics and functional properties of edible crickets (Acheta domesticus) protein concentrate. Journal of Food Measurement and Characterization. 2017;11(4):2013–2021. https://doi.org/10.1007/s11694-017-9584-4

56. Senarathna SC, Malalgoda M. Impact of defatting method on oat protein isolate structure-function characteristics. Journal of Cereal Science. 2024;117:103876. https://doi.org/10.1016/j.jcs.2024.103876

57. Feng Y, Ma X, Kong B, Chen Q, Liu Q. Ethanol induced changes in structural, morphological, and functional properties of whey proteins isolates: Influence of ethanol concentration. Food Hydrocolloids. 2021;111:106379. https://doi.org/10.1016/j.foodhyd.2020.106379

58. Tan JX, Tan CC, Dharmawan J, Leong SSJ. Effects of ethanol washing on off-flavours removal and protein functionalities of pea protein concentrate. Food and Bioproducts Processing. 2023;141:73–80. https://doi.org/10.1016/j.fbp.2023.07.004

59. Ma H, Li J, Guan Y, Song Z, Chen H, et al. A systematic study of the influence of structural differences in soy protein isolates on gel properties: A comparison based on different cultivars. Food Bioscience. 2025;69:106987. https://doi.org/10.1016/j.fbio.2025.106987

60. Hanley L, Dobson S, Stobbs J, Marangoni AG. Physicochemical and functional characterization of plant protein isolates and their influence on plant-based mozzarella cheese performance. Food Hydrocolloids. 2025;164:111222. https://doi.org/10.1016/j.foodhyd.2025.111222

61. Derkach SR, Voron’ko NG, Sokolan NI, Kolotova DS, Kuchina YA. Interactions between gelatin and sodium alginate: UV and FTIR studies. Journal of Dispersion Science and Technology. 2019;41(5):690–698. https://doi.org/10.1080/01932691.2019.1611437


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