Effect of Ultrasound Treatment on the Physicochemical, Nutraceutical, and Functional Properties of Lupine Flour

Document Type : Original Research

Authors
1 Department of Nutrition and Food Technology, Jordan University of Science and Technology, P.O. Box 3030, Irbid 22110.
2 Department of Physics, Jordan University of Science and Technology, P.O. Box 3030, Irbid 22110.
3 Department of Medicinal Chemistry and Pharmacognosy, Faculty of Pharmacy, Yarmouk University, Shafiq Irshidat st Irbid 21163, Jordan.
Abstract
This study aimed to convert sweet and bitter lupine protein isolates to nano-emulsions and to develop products with the nano-emulsion and examine the stability; develop emulsification with ultrasonication; develop and characterize food protein-stabilized nanoemulsions; and to modify lupine protein properties with pH shifting and ultrasonication. The antioxidant activity of sweet and bitter isolates was decreased in the nano-particle sized samples when compared to non-nano particle-sized samples, as well as the inhibitory activity of both angiotensin-converting enzyme and alpha-amylase, while it increased in sweet and bitter lupine isolates. For both types of lupine, water holding capacity was increased, and foaming stability of nano treatment was increased in protein isolate samples. In lupine, albumins and three globulins fractions, namely, β-conglutin, α-conglutin, and γ-conglutin, were characterized as the main storage proteins. No clear differences were observed between nano and non-nano samples regarding albumins and three globulins fractions. The results of microstructure characterization showed that sonication leads to distortion/breakage of protein particles shape, which results in smaller proteins that can be used as a top-down approach for the formation of nano-sized protein particles. In this regard, sonication can be considered as a heterogeneous approach that may lead to de-aggregation, breaking of protein particles, and distortion of their shape.

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1. Abbastabr B. , Azizi M. H., and Nabavi S. R. 2020. Curcumin microparticles produced by electrospraying technique with whey protein isolate and β-cyclodextrin complex. Journal of Agricultural Science and Technology, 22(3): 709-722.
2. Ahmed, S.H., Ahmed, I.A.M., Eltayeb, M.M., Ahmed, S.O. and Babiker, E.E.2011. Functional properties of selected legumes flour as influenced by pH. Journal of Agricultural Technology, 7(5): 1291-1302.
3. Alu’datt, M., Rababah, T., Alhamad, M., Ereifej, K., Gammoh, S., Kubow, S. and Tawalbeh, D. 2017. Preparation of mayonnaise from extracted plant protein isolates of chickpea, broad bean and lupin flour: chemical, physiochemical, nutritional and therapeutic properties. Journal of Food Science and Technology, 54(6): 1395-1405.
4. Alu’datt, M., Rababah, T., Ereifej, K., Alli, I., Alrababah, M., Almajwal, A., Masadeh, N. and Alhamad, M. 2012. Effects of barley flour and barley protein isolate on chemical, functional, nutritional and biological properties of Pita bread. Food Hydrocolloids, 26(1): 135-143.
5. Barton, S., Bullock, C., and Weir, D. 1996. The effects of ultrasound on the activities of some glycosidase enzymes of industrial importance. Enzyme and Microbial Technology, 18:190-194.
6. Beverung, C., Radke, C. and Blanch, H. 1999. Protein adsorption at the oil/water interface: characterization of adsorption kinetics by dynamic interfacial tension measurements. Biophysical Chemistry, 81(1): 59-80.
7. Cushman DW, Cheung HS 1971 Spectrometric assay and properties of the angiotensin-Converting-I-enzyme of rabbit lung. Biochemcal Pharmacology, 20:1637–1648.
8. Daskaya-Dikmen, C., Yucetepe,A., Karbancioglu-Guler, F., Daskaya, H., and Ozcelik, B. (2017). Angiotensin-I-Converting Enzyme (ACE)-Inhibitory Peptides from Plants. Nutrients, 9(4): 316-321.
9. Dervas, G., Doxastakis, G., Hadjisavva-Zinoviadi, S., and Triantafillakos, N. 1999. Lupin flour addition to wheat flour doughs and effect on rheological properties. Food Chemistry, 66(1): 67-73.
10. Duranti, M., Consonni, A., Magni, C., Sessa, F., and Scarafoni, A. 2008. The major proteins of lupin seed: Characterisation and molecular properties for use as functional and nutraceutical ingredients. Trends in Food Science and Technology, 19(12): 624-633.
11. Duranti, M., Restani, P., Poniatowska, M., and Cerletti, P. 1981. The seed globulins of Lupinus albus. Phytochemistry, 20(9): 2071-2075.
12. Fahmideh, L. Mazaraie, A., and Tavakoli, M. 2019. Total phenol/flavonoid content, antibacterial and DPPH free radical scavenging activities of medicinal plants. Journal of Agricultural Science and Technology, 21(6): 1459-1471.
13. Hondelmann, W. 1984. The lupin -ancient and modern crop plant. Theoretical and Applied Genetics, 68-68(1-2): 1-9.
14. Jiang, S., Ding, J., Andrade, J., Rababah, T., Almajwal, A., Abulmeaty, M. and Feng, H. 2017. Modifying the physicochemical properties of pea protein by pH-shifting and ultrasound combined treatments. Ultrasonics Sonochemistry, 38: 835-842.
15. Karaca, A., Low, N. and Nickerson, M. 2011. Emulsifying properties of chickpea, faba bean, lentil and pea proteins produced by isoelectric precipitation and salt extraction. Food Research International, 44(9): 2742-2750.
16. Lam, R. and Nickerson, M. 2013. Food proteins: A review on their emulsifying properties using a structure–function approach. Food Chemistry, 141(2): 975-984.
17. Ling, Q. D., Liaw, D. J., Zhu, C., Chan, D. S. H., Kang, E. T., and Neoh, K. G. 2008. Polymer electronic memories: Materials, devices and mechanisms. Progress in polymer science, 33(10): 917-978.
18. Liu, S., Chen, D. and Xu, J. 2018. The Effect of Partially Substituted Lupin, Soybean, and Navy Bean Flours on Wheat Bread Quality. Food and Nutrition Sciences, 09(07): 840-854.
19. Lqari, H., Vioque, J., Pedroche, J. and Millán, F. 2002. Lupinus angustifolius protein isolates: chemical composition, functional properties and protein characterization. Food Chemistry, 76(3): 349-356.
20. Makri, E., Papalamprou, E. and Doxastakis, G., 2005. Study of functional properties of seed storage proteins from indigenous European legume crops (lupin, pea, broad bean) in admixture with polysaccharides. Food Hydrocolloids, 19(3): 583-594.
21. Malik, M., Sharma, H. and Saini, C. 2017. High intensity ultrasound treatment of protein isolate extracted from dephenolized sunflower meal: Effect on physicochemical and functional properties. Ultrasonics Sonochemistry, 39: 511-519.
22. Martínez-Villaluenga, C., Frías, J., and Vidal-Valverde, C. 2006. Functional lupin seeds (Lupinus albus L. and Lupinus luteus L.) after extraction of α-galactosides. Food Chemistry, 98(2): 291-299.
23. McCue P, Kwon YI, Shetty K. 2005. Anti-amylase, anti-glucosidase and anti-angiotensin I-converting enzyme potential of selected foods. Food Biotechnolgy 29: 278–294.
24. Mülayim, M., Tamkoç, A., and Babaoglu, M. 2002. Sweet white lupins versus local bitter genotype: agronomic characteristics as affected by different planting densities in the Göller region of Turkey. European Journal of Agronomy, 17(3): 181-189.
25. O'connell, M. J., Bachilo, S. M., Huffman, C. B., Moore, V. C., Strano, M. S., Haroz, E. H., and Ma, J. 2003. Band gap fluorescence from individual single-walled carbon nanotubes. Science, 297(5581): 593-596.
26. Peng, D., Jin, W., Tang, C., Lu, Y., Wang, W., Li, J. and Li, B. 2018. Foaming and surface properties of gliadin nanoparticles: Influence of pH and heating temperature. Food Hydrocolloids, 77:107-116.
27. Pilvi, T., Jauhiainen, T., Cheng, Z., Mervaala, E., Vapaatalo, H. and Korpela, R. 2006. Lupin protein attenuates the development of hypertension and normalises the vascular function of NaCl-loaded Goto-Kakizaki rats. Journal of physiology and pharmacology, 57(2):167-176.
28. Piornos, J., Burgos-Díaz, C., Ogura, T., Morales, E., Rubilar, M., Maureira-Butler, I. and Salvo-Garrido, H. 2015. Functional and physicochemical properties of a protein isolate from Alu Prot -CGNA: A novel protein-rich lupin variety (Lupinus luteus). Food Research International, 76:719-724
29. Ruíz-Henestrosa, V. P., Sánchez, C. C., Escobar, M. D. M. Y., Jiménez, J. J. P., Rodríguez, F. M., and Patino, J. M. R. 2007. Interfacial and foaming characteristics of soy globulins as a function of pH and ionic strength. Colloids and Surfaces A: Physicochemical and Engineering Aspects, 309(1-3): 202-215.
30. Shevkani, K., Singh, N., Kaur, A. and Rana, J. 2014. Physicochemical, Pasting, and Functional Properties of Amaranth Seed Flours: Effects of Lipids Removal. Journal of Food Science, 79(7): 1271-1277.
31. Smith, K. R., and Olson, K. E. 2010. U.S. Patent No. 7,666,826. Washington, DC: U.S. Patent and Trademark Office.
32. Soria, A. and Villamiel, M. 2010. Effect of ultrasound on the technological properties and bioactivity of food: a review. Trends in Food Science & Technology, 21(7):323-331.
33. Subagio, A. 2006. Characterization of hyacinth bean (Lablab purpureus (L.) sweet) seeds from Indonesia and their protein isolate. Food Chemistry, 95(1), pp.65-70.
34. Tsoukala, A., Papalamprou, E., Makri, E., Doxastakis, G. and Braudo, E. 2006. Adsorption at the air–water interface and emulsification properties of grain legume protein derivatives from pea and broad bean. Colloids and Surfaces B: Biointerfaces, 53(2): 203-208.
35. Wan, Z., Yang, X., and Sagis, L. M. 2016. Nonlinear surface dilatational rheology and foaming behavior of protein and protein fibrillar aggregates in the presence of natural surfactant. Langmuir, 32(15): 3679-3690.
36. Wang, J. M., Xia, N., Yang, X. Q., Yin, S. W., Qi, J. R., He, X. T., and Wang, L. J. 2012. Adsorption and dilatational rheology of heat-treated soy protein at the oil–water interface: Relationship to structural properties. Journal of agricultural and food chemistry, 60(12): 3302-3310.
37. Weiss, D. N., Brokmann, X., Calvet, L. E., Kastner, M. A., and Bawendi, M. G. 2006. Multi-island single-electron devices from self-assembled colloidal nanocrystal chains. Applied physics letters, 88(14), 143507.
38. Xu, S., Olenyuk, B. Z., Okamoto, C. T., and Hamm-Alvarez, S. F. 2013. Targeting receptor-mediated endocytotic pathways with nanoparticles: rationale and advances. Advanced drug delivery reviews, 65(1):121-138.
39. Zhou, C., Ma, H., Ding, Q., Lin, L., Yu, X., Luo, L., Dai, C. and Yagoub, A. 2013. Ultrasonic pretreatment of corn gluten meal proteins and neutrase: Effect on protein conformation and preparation of ACE (angiotensin converting enzyme) inhibitory peptides. Food and Bioproducts Processing, 91: 665-671.