Abstract
The effect of microwave and ultrasonic processing on the secondary structure of egg white protein was evaluated using Fourier-transform infrared spectroscopy and circular dichroism spectroscopy. The influence of these methods on avidin activity was also evaluated. Microwave treatment was performed at 60 °C, 70 °C, and 80 °C for 1, 3, and 5 min. Avidin activity was found to decrease in all the processed samples. However, the reduction in its activity was higher when treated at 80 °C. The secondary structure analysis revealed that the β-sheets increased at temperatures 60 °C and 70 °C as the processing time rose while became almost constant at 80 °C. α-helices were found to decrease with time at each of the temperatures at which microwave was applied. Turns and unordered structures remained constant. Ultrasonic processing was carried out for 1, 4, 8, 12, and 16 min. α-helices declined significantly with remarkable increase of β-sheets when samples were treated for 1 min compared to control. However, the secondary structure content did not change significantly when the duration of ultrasonication was increased, showing minimal processing capabilities of ultrasound.
Similar content being viewed by others
Abbreviations
- HABA:
-
2-(4′-hydoxyazobenzene) benzoic acid
- FTIR:
-
Fourier-transform infrared spectroscopy
- CD:
-
Circular dichroism spectroscopy
- BCA method:
-
Bicinchoninic acid method
References
Abdel-Aal, E.-S. M., Akhtar, H., Zaheer, K., & Ali, R. (2013). Dietary sources of lutein and zeaxanthin carotenoids and their role in eye health. Nutrients, 5(4), 1169–1185.
Balk, E. M., Lichtenstein, A. H., Chung, M., Kupelnick, B., Chew, P., & Lau, J. (2006). Effects of omega-3 fatty acids on serum markers of cardiovascular disease risk: a systematic review. Atherosclerosis, 189(1), 19–30.
Beazley, S. F. (2017). Effects of ultra-sonication process on digestibility of kafirin in sorghum.
Beck, S. M., Knoerzer, K., & Arcot, J. (2017). Effect of low moisture extrusion on a pea protein isolate’s expansion, solubility, molecular weight distribution and secondary structure as determined by Fourier transform infrared spectroscopy (FTIR). Journal of Food Engineering, 214, 166–174.
Bohr, H., & Bohr, J. (2000). Microwave-enhanced folding and denaturation of globular proteins. Physical Review E, 61(4), 4310–4314.
Bovet, P., Faeh, D., Madeleine, G., Viswanathan, B., & Paccaud, F. (2007). Decrease in blood triglycerides associated with the consumption of eggs of hens fed with food supplemented with fish oil. Nutrition, Metabolism and Cardiovascular Diseases, 17(4), 280–287.
Byler, D. M., & Susi, H. (1986). Examination of the secondary structure of proteins by deconvolved FTIR spectra. Biopolymers, 25(3), 469–487.
Delcourt, C., Carriere, I., Delage, M., Barberger-Gateau, P., & Schalch, W. (2006). Plasma lutein and zeaxanthin and other carotenoids as modifiable risk factors for age-related maculopathy and cataract: the POLA study. Investigative Ophthalmology & Visual Science, 47(6), 2329–2335.
Deng, Y., Padilla-Zakour, O., Zhao, Y., & Tao, S. (2015). Influences of high hydrostatic pressure, microwave heating, and boiling on chemical compositions, antinutritional factors, fatty acids, in vitro protein digestibility, and microstructure of buckwheat. Food and Bioprocess Technology, 8(11), 2235–2245.
Durance, T. (1991). Residual avid in activity in cooked egg white assayed with improved sensitivity. Journal of Food Science, 56(3), 707–709.
Durance, T., & Nakai, S. (1988). Simultaneous isolation of avidin and lysozyme from egg albumen. Journal of Food Science, 53(4), 1096–1101.
Durance, T., & Wong, N. (1992). Kinetics of thermal inactivation of avidin. Food Research International, 25(2), 89–92.
Eigenmann, P. A. (2000). Anaphylactic reactions to raw eggs after negative challenges with cooked eggs. Journal of Allergy and Clinical Immunology, 105(3), 587–588.
Enriquez-Matas, A., Sandin, M. I., Martínez, J., Postigo, I., Escudero, C., & Aparicio, V. F. (2007). Egg allergy caused by avidin. Allergy: European Journal of Allergy and Clinical Immunology, 62, 331–332.
Ertas, N. (2013). Dephytinization processes of some legume seeds and cereal grains with ultrasound and microwave applications. Legume Research: An International Journal, 36(5).
Feng, J., Cai, H., Wang, H., Li, C., & Liu, S. (2018). Improved oxidative stability of fish oil emulsion by grafted ovalbumin-catechin conjugates. Food Chemistry, 241, 60–69.
Gale, C. R., Hall, N. F., Phillips, D. I., & Martyn, C. N. (2003). Lutein and zeaxanthin status and risk of age-related macular degeneration. Investigative Ophthalmology & Visual Science, 44(6), 2461–2465.
Gomaa, A., & Boye, J. (2015). Impact of irradiation and thermal processing on the immunochemical detection of milk and egg allergens in foods. Food Research International, 74, 275–283.
Gray, C. L., Goddard, E., Karabus, S., Kriel, M., Lang, A., Manjra, A. I., et al. (2015). Epidemiology of IgE-mediated food allergy. SAMJ: South African Medical Journal, 105(1), 68–69.
Green, N. M. (1975). Avidin. Advances in Protein Chemistry, 29, 85–133.
Grewal, M. K., Chandrapala, J., Donkor, O., Apostolopoulos, V., Stojanovska, L., & Vasiljevic, T. (2017). Fourier transform infrared spectroscopy analysis of physicochemical changes in UHT milk during accelerated storage. International Dairy Journal, 66, 99–107.
Gülseren, İ., Güzey, D., Bruce, B. D., & Weiss, J. (2007). Structural and functional changes in ultrasonicated bovine serum albumin solutions. Ultrasonics Sonochemistry, 14(2), 173–183.
Han, I. H., Swanson, B. G., & Baik, B.-K. (2007). Protein digestibility of selected legumes treated with ultrasound and high hydrostatic pressure during soaking. Cereal Chemistry, 84(5), 518–521.
Han, Y., Wang, J., Li, Y., Hang, Y., Yin, X., & Li, Q. (2015). Circular dichroism and infrared spectroscopic characterization of secondary structure components of protein Z during mashing and boiling processes. Food Chemistry, 188, 201–209.
Handelman, G. J., Nightingale, Z. D., Lichtenstein, A. H., Schaefer, E. J., & Blumberg, J. B. (1999). Lutein and zeaxanthin concentrations in plasma after dietary supplementation with egg yolk. The American Journal of Clinical Nutrition, 70(2), 247–251.
Hefnawy, T. (2011). Effect of processing methods on nutritional composition and anti-nutritional factors in lentils (Lens culinaris). Annals of Agricultural Sciences, 56(2), 57–61.
Hejazi, S. N., & Orsat, V. (2016). Malting process optimization for protein digestibility enhancement in finger millet grain. Journal of Food Science and Technology, 53(4), 1929–1938.
Hester, P. (2016). Egg innovations and strategies for improvements. Academic press.
Jackson, M., & Mantsch, H. H. (1995). The use and misuse of FTIR spectroscopy in the determination of protein structure. Critical Reviews in Biochemistry and Molecular Biology, 30(2), 95–120.
Jiang, L., Wang, J., Li, Y., Wang, Z., Liang, J., Wang, R., Chen, Y., Ma, W., Qi, B., & Zhang, M. (2014). Effects of ultrasound on the structure and physical properties of black bean protein isolates. Food Research International, 62, 595–601.
Kheiralla, A. F., Yousif, H., Hassan, H. G., Khiery, H. A., & Ghanim, M. (2016) Design and development of a low cost semi-automated poultry vaccination machine. In Basic Sciences and Engineering Studies (SGCAC), 2016 Conference of, 2016 (pp. 187–191): IEEE.
Li, H., Yu, J., Ahmedna, M., & Goktepe, I. (2013). Reduction of major peanut allergens Ara h 1 and Ara h 2, in roasted peanuts by ultrasound assisted enzymatic treatment. Food Chemistry, 141(2), 762–768.
McGee, H. (2007). On food and cooking: the science and lore of the kitchen: Simon and Schuster.
Mine, Y., Noutomi, T., & Haga, N. (1990). Thermally induced changes in egg white proteins. Journal of Agricultural and Food Chemistry, 38(12), 2122–2125.
Mondoulet, L., Paty, E., Drumare, M., Ah-Leung, S., Scheinmann, P., Willemot, R., et al. (2005). Influence of thermal processing on the allergenicity of peanut proteins. Journal of Agricultural and Food Chemistry, 53(11), 4547–4553.
Paulsson, M., & Dejmek, P. (1990). Thermal denaturation of whey proteins in mixtures with caseins studied by differential scanning calorimetry. Journal of Dairy Science, 73(3), 590–600.
Qian, J.-Y., Ma, L.-J., Wang, L.-J., & Jiang, W. (2016). Effect of pulsed electric field on structural properties of protein in solid state. LWT-Food Science and Technology, 74, 331–337.
Raso, J., & Barbosa-Cánovas, G. V. (2003). Nonthermal preservation of foods using combined processing techniques.
Rehman, Z.-u., & Shah, W. (2005). Thermal heat processing effects on antinutrients, protein and starch digestibility of food legumes. Food Chemistry, 91(2), 327–331.
Singh, A., & Ramaswamy, H. S. (2014). Thermal and high-pressure inactivation kinetics of avidin. Journal of Food Processing and Preservation, 38(4), 1830–1839.
Singh, A., Lahlali, R., Vanga, S. K., Karunakaran, C., Orsat, V., & Raghavan, V. (2016). Effect of high electric field on secondary structure of wheat gluten. International Journal of Food Properties, 19(6), 1217–1226.
Sreerama, N., & Woody, R. W. (2000). Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Analytical Biochemistry, 287(2), 252–260.
Stadelman, W. J., Newkirk, D., & Newby, L. (2017). Egg science and technology. CRC Press.
Stanic-Vucinic, D., Stojadinovic, M., Atanaskovic-Markovic, M., Ognjenovic, J., Grönlund, H., van Hage, M., Lantto, R., Sancho, A. I., & Velickovic, T. C. (2012). Structural changes and allergenic properties of β-lactoglobulin upon exposure to high-intensity ultrasound. Molecular Nutrition & Food Research, 56(12), 1894–1905.
Stathopulos, P. B., Scholz, G. A., Hwang, Y. M., Rumfeldt, J. A., Lepock, J. R., & Meiering, E. M. (2004). Sonication of proteins causes formation of aggregates that resemble amyloid. Protein Science, 13(11), 3017–3027.
Swamy, M. J., Heimburg, T., & Marsh, D. (1996). Fourier-transform infrared spectroscopic studies on avidin secondary structure and complexation with biotin and biotin-lipid assemblies. Biophysical Journal, 71(2), 840–847.
USDA (2015). USDA National Nutrient Database for standard reference, release 28, Ed. US Department of Agriculture, Agricultural Research Service, Nutrient Data Laboratory.
Vagadia, B. H., Vanga, S. K., Singh, A., Gariepy, Y., & Raghavan, V. (2018). Comparison of conventional and microwave treatment on soymilk for inactivation of trypsin inhibitors and in vitro protein digestibility. Foods, 7(1), 6.
Van Kleef, F. (1986). Thermally induced protein gelation: Gelation and rheological characterization of highly concentrated ovalbumin and soybean protein gels. Biopolymers, 25(1), 31–59.
Vanga, S. K., Singh, A., & Raghavan, V. (2015). Effect of thermal and electric field treatment on the conformation of Ara h 6 peanut protein allergen. Innovative Food Science & Emerging Technologies, 30, 79–88.
Vanga, S. K., Singh, A., Kalkan, F., Gariepy, Y., Orsat, V., & Raghavan, V. (2016). Effect of thermal and high electric fields on secondary structure of peanut protein. International Journal of Food Properties, 19(6), 1259–1271.
Vanga, S. K., Singh, A., & Raghavan, V. (2017). Review of conventional and novel food processing methods on food allergens. Critical Reviews in Food Science and Nutrition, 57(10), 2077–2094.
Vilela, R. M., Lands, L. C., Chan, H. M., Azadi, B., & Kubow, S. (2006). High hydrostatic pressure enhances whey protein digestibility to generate whey peptides that improve glutathione status in CFTR-deficient lung epithelial cells. Molecular Nutrition & Food Research, 50(11), 1013–1029.
Yang, H., Gao, J., Yang, A., & Chen, H. (2015). The ultrasound-treated soybean seeds improve edibility and nutritional quality of soybean sprouts. Food Research International, 77, 704–710.
Acknowledgements
The authors are grateful to NSERC (Natural Science and Engineering Research Council of Canada) for their financial support. The authors also would like to thank Dr. Judith Kornblatt in Department of Chemistry and Biochemistry, Concordia University for her technical help in Circular Dichroism.
Author information
Authors and Affiliations
Corresponding author
Electronic supplementary material
ESM 1
(DOCX 427 kb)
Rights and permissions
About this article
Cite this article
Zhu, Y., Vanga, S.K., Wang, J. et al. Effects of Ultrasonic and Microwave Processing on Avidin Assay and Secondary Structures of Egg White Protein. Food Bioprocess Technol 11, 1974–1984 (2018). https://doi.org/10.1007/s11947-018-2158-6
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s11947-018-2158-6