Germination as a Bioprocessing Strategy for Enhancing Functional Properties and Protein Structural Profiles of Moringa Oleifera Seed Protein Isolates: A Comparative Review with Soy Protein Isolates
Authors
Department of Chemistry, Centre for Food Technology and Research, Benue State University, Makurdi, Nigeria (Nigeria)
Department of Chemistry, Centre for Food Technology and Research, Benue State University, Makurdi, Nigeria (Nigeria)
Article Information
DOI: 10.51244/IJRSI.2026.1305000163
Subject Category: Agriculture
Volume/Issue: 13/5 | Page No: 1829-1840
Publication Timeline
Submitted: 2026-05-08
Accepted: 2026-05-13
Published: 2026-06-05
Abstract
Moringa oleifera seed protein isolates (MPI) have gained increasing attention as sustainable plant protein alternatives; however, their functional properties remain highly variable and underutilized compared to soy protein isolate (SPI). This review critically evaluates germination as a bioprocessing strategy for enhancing MPI structural and functional properties, including SDS PAGE, solubility, foaming, water holding capacity (WHC), and oil holding capacity (OHC), while providing a comparative perspective with SPI.
Evidence indicates that germination improves MPI functionality primarily through enzymatic proteolysis of storage globulins, resulting in reduced molecular weight, increased surface polarity, and improved protein-water and protein-lipid interactions. Optimal germination (~48 h) enhances solubility by 10-15%, foaming capacity by 15-30%, WHC by up to 50%, and OHC by approximately 20-30%. However, SPI consistently outperforms MPI in foaming and gelation due to its structured glycinin and β-conglycinin fractions.
The review further highlights strong geographic origin effects on MPI functionality, driven by variations in protein composition, particularly the ratio of globulins to cationic albumins. Indian MPI shows acid-soluble albumin dominance, Thai MPI exhibits soy-like solubility behavior, and Cameroonian MPI displays mixed functional profiles. Despite these advances, key gaps remain in molecular characterization, standardization of extraction methods, and integration of omics-based approaches. Germination represents a low-cost, sustainable strategy to enhance MPI functionality, but full industrial competitiveness with SPI will require integrated bioprocessing and a better understanding of genotype-environment-protein interactions.
Keywords
Moringa oleifera; germination; Protein Isolate; Solubility; SDS-PAGE; foaming; water holding capacity; oil holding capacity; soy protein
Downloads
References
1. Aiking, H., & de Boer, J. (2020). The next protein transition. Animal Frontiers, 10(3), 21–28. [Google Scholar] [Crossref]
2. Alghooneh, A., Gharibzahedi, S. M. T., & Jafari, S. M. (2023). Functional properties of Moringa oleifera protein isolates as influenced by different isolation techniques, pH, and ionic strength. Food and Bioprocess Technology, 16, 2567–2581. https://doi.org/10.1007/s11947-023-03279-8 [Google Scholar] [Crossref]
3. Anyiam, C. K., Suwannakorn, W., & Charoensiddhi, S. (2025). Influence of extraction methods on the functional and structural properties of moringa seed protein isolates. Foods, 14(17), 3046. [Google Scholar] [Crossref]
4. Atuna, R. A., Mensah, M.-A. S., Koomson, G., Akabanda, F., Dorvlo, S. Y., & Amagloh, F. K. (2023). Physico-functional and nutritional characteristics of germinated pigeon pea (Cajanus cajan) flour as a functional food ingredient. Scientific Reports, 13(1), 16627. https://doi.org/10.1038/s41598-023-43607-8 [Google Scholar] [Crossref]
5. Aviles-Gaxiola, S., Chuck-Hernandez, C., Rocha-Pizana, M. R., Garcia-Lara, S., Lopez-Castillo, L. M., & Serna-Saldivar, S. O. (2018). Inactivation methods of trypsin inhibitor in legumes: A review. Journal of Food Science, 83(1), 17-29. [Google Scholar] [Crossref]
6. Barac, M. B., Pesic, M. B., Stanojevic, S. P., Kostic, A. Z., & Cabrilo, S. B. (2017). Functional properties of pea protein isolates—the influence of extraction pH. LWT - Food Science and Technology, 81, 65-72. [Google Scholar] [Crossref]
7. Bera, I., O’Sullivan, M., Flynn, D., & Shields, D. C. (2023). Relationship between protein digestibility and the proteolysis of legume proteins during seed germination. Molecules, 28(7), 3204. https://doi.org/10.3390/molecules28073204 [Google Scholar] [Crossref]
8. Bewley, J. D., Bradford, K. J., Hilhorst, H. W. M., & Nonogaki, H. (2013). Seeds: Physiology of development, germination and dormancy (3rd ed.). Springer. [Google Scholar] [Crossref]
9. Boye, J., Zare, F., & Pletch, A. (2010). Pulse proteins: Processing, characterization, functional properties and applications. Food Research International, 43(2), 414-431. [Google Scholar] [Crossref]
10. Cheng, H., et al. (2021). Soy protein isolate: an overview on foaming properties and air–liquid interface. International Journal of Food Science & Technology, 57(1), 188–197. [Google Scholar] [Crossref]
11. Damodaran, S. (2008). Amino acids, peptides, and proteins. In S. Damodaran, K. L. Parkin, & O. R. Fennema (Eds.), Fennema’s food chemistry (4th ed., pp. 217-330). CRC Press. [Google Scholar] [Crossref]
12. Dickinson, E. (1992). An introduction to food colloids. Oxford University Press. [Google Scholar] [Crossref]
13. Dong, K., Zhen, S., Cheng, Z., Cao, H., Ge, P., & Yan, Y. (2015). Proteomic analysis reveals key proteins and phosphoproteins upon seed germination of wheat (Triticum aestivum L.). Frontiers in plant science, 6, 1017. [Google Scholar] [Crossref]
14. Foegeding, E. A., & Davis, J. P. (2011). Food protein functionality: A comprehensive approach. Food Hydrocolloids, 25(8), 1853-1864. [Google Scholar] [Crossref]
15. Ghumman, A., Kaur, A., & Singh, N. (2016). Impact of germination on flour, protein and starch characteristics of lentil and horsegram. LWT - Food Science and Technology, 65, 137-144. [Google Scholar] [Crossref]
16. Illingworth, K. A., Lee, Y. Y., & Siow, L. F. (2022). The effect of isolation techniques on the physicochemical properties of Moringa oleifera protein isolates. Food Chemistry Advances, 1, 100029. [Google Scholar] [Crossref]
17. Jain, P., Nema, P. K., & Rout, P. K. (2019). Processing of Moringa oleifera seeds to obtain protein isolate. Journal of Food Science and Technology, 56(10), 4655-4662. [Google Scholar] [Crossref]
18. Jakubczyk, A., Karaś, M., Złotek, U., & Szymanowska, U. (2020). Nutritional composition and bioactive compounds in seeds sprouts and microgreens–An overview. Molecules, 25(23), 5611. [Google Scholar] [Crossref]
19. Kaur, M., & Singh, N. (2007). Characterization of protein isolates from chickpea cultivars. Food Chemistry, 102(1), 366-374. [Google Scholar] [Crossref]
20. Khattab, R. Y., & Arntfield, S. D. (2009). Nutritional quality of legume seeds as affected by physical treatments. LWT - Food Science and Technology, 42(6), 1113-1118. [Google Scholar] [Crossref]
21. Kinsella, J. E. (1979). Functional properties of soy proteins. Journal of the American Oil Chemists’ Society, 56(3), 242-258. [Google Scholar] [Crossref]
22. Lam, A. C. Y., Karaca, A. C., Tyler, R. T., & Nickerson, M. T. (2018). Pea protein isolates: Structure, extraction, and functionality. Food Reviews International, 34(2), 126-147. [Google Scholar] [Crossref]
23. Liu, S., Zhou, R., Tian, S., & Gai, J. (2007). A study on subunit groups of soybean protein extracts under SDS-PAGE. Journal of the American Oil Chemists' Society, 84(9), 793-801. [Google Scholar] [Crossref]
24. Martin-Cabrejas, M. A., et al. (2017). Effect of germination on legumes. Food Chemistry, 107(3), 1045-1052. [Google Scholar] [Crossref]
25. Mensink, R. P., Zock, P. L., Kester, A. D., & Katan, M. B. (2016). Effects of dietary fatty acids and carbohydrates on the ratio of serum total to HDL cholesterol and on serum lipids and apolipoproteins. American Journal of Clinical Nutrition, 77(5), 1146–1155. [Google Scholar] [Crossref]
26. Moure, A., Sineiro, J., Dominguez, H., & Parajo, J. C. (2006). Functionality of oilseed protein products. Food Research International, 39(9), 945-963. [Google Scholar] [Crossref]
27. Moyo, B., Masika, P. J., Hugo, A., & Muchenje, V. (2011). Nutritional characterization of Moringa (Moringa oleifera Lam.) leaves. African Journal of Biotechnology, 10(60), 12925–12933. [Google Scholar] [Crossref]
28. Mubarak, A. E. (2005). Nutritional composition and antinutritional factors of mung bean. Food Chemistry, 89(4), 489-495. [Google Scholar] [Crossref]
29. Mune Mune, M. A., Minka, S. R., & Mbome, I. L. (2016). Functional properties of Moringa oleifera seed protein concentrates. Cogent Food & Agriculture, 2(1), 1220352. [Google Scholar] [Crossref]
30. Nishinari, K., Fang, Y., Guo, S., & Phillips, G. O. (2014). Soy proteins and food emulsions. Food Hydrocolloids, 39, 301–318. [Google Scholar] [Crossref]
31. Nkhata, S. G., Ayua, E., Kamau, E. H., & Shingiro, J. B. (2018). Germination improves nutritional quality of cereals and legumes. Food Science & Nutrition, 6(8), 2446-2458. [Google Scholar] [Crossref]
32. Nosworthy, M. G., et al. (2018). Effect of processing on protein quality of peas. Food Chemistry, 241, 236-240. [Google Scholar] [Crossref]
33. Olson, M. E., & Fahey, J. W. (2011). Moringa oleifera nutritional potential. Emirates Journal of Food and Agriculture, 23(4), 320-333. [Google Scholar] [Crossref]
34. Peng, W., Kong, X., Chen, Y., Zhang, C., Yang, Y., & Hua, Y. (2016). Heat treatment effects on pea protein foaming. Food Hydrocolloids, 52, 301-310. [Google Scholar] [Crossref]
35. Pojic, M., Misan, A., & Tiwari, B. (2018). Eco-innovative protein extraction technologies. Trends in Food Science & Technology, 75, 93-104. [Google Scholar] [Crossref]
36. Renkema, J. M. S., & van Vliet, T. (2002). Soy protein gelation. Journal of Agricultural and Food Chemistry, 50(6), 1569-1573. [Google Scholar] [Crossref]
37. Sangronis, E., & Machado, C. J. (2007). Germination effects on legumes. LWT - Food Science and Technology, 40(1), 116-120. [Google Scholar] [Crossref]
38. Shevkani, K., Singh, N., Kaur, A., & Rana, J. C. (2015). Functional properties of legume proteins. Food Hydrocolloids, 43, 679-689. [Google Scholar] [Crossref]
39. Teixeira, E. M. B., et al. (2014). Protein fractions of Moringa oleifera. Food Chemistry, 147, 51-54. [Google Scholar] [Crossref]
40. Toews, R., & Wang, N. (2013). Functional properties of pulse proteins. Food Research International, 52(2), 445-451. [Google Scholar] [Crossref]
41. Wang, Z., Zhang, L., Zhang, X., Zeng, M., He, Z., & Chen, J. (2021). Interfacial rheology and foaming properties of soy protein and hydrolysates under acid condition. Food Biophysics, 16(4), 484–491. [Google Scholar] [Crossref]
42. Wilde, P. J. (2000). Protein interfaces in foams and emulsions. Current Opinion in Colloid & Interface Science, 5(3-4), 176-181. [Google Scholar] [Crossref]
Metrics
Views & Downloads
Similar Articles
- Breeding for a Greener Future: Selective Breeding and Crossbreeding Approaches to Minimize Methane Emissions in Ruminant Livestock
- Determinants of Adoption of Post-Harvest Losses Prevention Techniques among Banana/Plantain Marketers in Lagos State, Nigeria
- Enhancing Rice Yield Prediction Using UAV-Based Multispectral Imaging and Machine Learning Algorithms
- Seed-Borne Fungi of Groundnuts (Arachis Hypogaea) and Their Management with Ginger (Zingiber Officinale) Extract In Makurdi, Nigeria
- The Influence of Landforms and Slope on Agricultural Cropping Patterns in Chhatrapati Sambhajinagar District