Journal of Food and Nutrition Research
ISSN (Print): 2333-1119 ISSN (Online): 2333-1240 Website: Editor-in-chief: Prabhat Kumar Mandal
Open Access
Journal Browser
Journal of Food and Nutrition Research. 2020, 8(5), 216-224
DOI: 10.12691/jfnr-8-5-1
Open AccessArticle

Effect of Microwave Irradiation Nonuniformity on the Digestion and Allergenicity of the Glycated Ovalbumin

Bi-zhen Zhong1, Zong-cai Tu1, 2, and Hui Wang1

1State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang, Jiangxi 330047, China{Chesnik, 2011 #29}

2National R&D Center for conventional Freshwater Fish Processing, and Engineering Research Center of Freshwater Fish High-value Utilization of Jiangxi Province, Jiangxi Normal University, Nanchang 330022, China

Pub. Date: June 07, 2020

Cite this paper:
Bi-zhen Zhong, Zong-cai Tu and Hui Wang. Effect of Microwave Irradiation Nonuniformity on the Digestion and Allergenicity of the Glycated Ovalbumin. Journal of Food and Nutrition Research. 2020; 8(5):216-224. doi: 10.12691/jfnr-8-5-1


The glycated OVA by microwave irradiation was digested by different methods (gastric digestion, intestinal digestion, and two-step digestion). Digestibility properties change of glycated OVA after digestion were evaluated in this work. The results showed that the samples were mainly digested in the stomach and they were hardly hydrolyzed by trypsin. Glycated OVA digested in stomach or in intestines produced more free amino groups than that by two-step digestion. Calcium ion chelating ability of glycated OVA was much higher than OVA when digested in stomach and intestines; glycated OVA had stronger ferrous ion chelating abilities by intestinal digestion. Glycated OVA after being digested hold the better antioxidant activity than the digested OVA, especially the Sample 3. IgG and IgE binding of all samples after intestinal digestion and two-step digestion were lower than that by gastric digestion. The IgG binding of glycated OVAs were lower than OVA, the result of the IgE binding was the opposite.

ovalbumin glycation digestion microwave

Creative CommonsThis work is licensed under a Creative Commons Attribution 4.0 International License. To view a copy of this license, visit


[1]  Qin, L. "Structural analysis of proteins in thermally induced ovalbumin and egg white gels." Doctoral dissertation, 1961.
[2]  Wang, Z., Zhang, C., Zhang, T., Ju, X. and He, R. "Effects of acylation and glycation treatments on physicochemical and gelation properties of rapeseed protein isolate." RSC Advances, 8(70):40395-40406, 2018.
[3]  Liu, J., Tu, Z. C., Shao, Y. H., Wang, H., Liu, G. X., Sha, X. M., Zhang, L. and Yang, P. "Improved antioxidant activity and glycation of α-lactalbumin after ultrasonic pretreatment revealed by high-resolution mass spectrometry." Journal of Agricultural & Food Chemistry, 65(47):10317-10324, 2017.
[4]  Chen, Y., Tu, Z., Wang, H., Zhang, L., Sha, X., Pang, J., Yang, P., Liu, G. and Yang, W. "Glycation of beta-lactoglobulin under dynamic high pressure microfluidization treatment: Effects on IgE-binding capacity and conformation." Food Research and International, 89(Pt 1):882-888, 2016.
[5]  Guan, Y. G., Hua, L., Zhong, H., Wang, J., Yu, S. J., Zeng, X. A., Liu, Y. Y., Xu, C. H. and Sun, W. W. "Effects of pulsed electric field treatment on a bovine serum albumin-dextran model system, a means of promoting the Maillard reaction." Food Chemistry, 123(2):275-280, 2010.
[6]  Xiang, B. Y., Ngadi, M. O., Ochoa-Martinez, L. A. and Simpson, M. V. "Pulsed Electric Field-Induced Structural Modification of Whey Protein Isolate." Food & Bioprocess Technology, 4(8): 1341-1348, 2011.
[7]  Chi, Y., Yinnan, L. I. and Zhao, Y. "Effect of Dynamic High-pressure Microfluidization on Egg White Protein Allergenicity and Digestibility." Transactions of the Chinese Society for Agricultural Machinery, 2017.
[8]  Zhang, Z. Y., Jian, W., Hong-Ru, G. E., Xu, Z., Jiang, L. Z., Wang, X. B. and Song, Y. L. "Freeze-thaw Stability of Soy Protein Isolate Modified by Ultrasonic Assisted Glycosylation." Modern Food Science & Technology, 2016.
[9]  Jiménez-Casta?o, L., Villamiel, M., Martín-álvarez, P. J., Olano, A. and López-Fandi?o, R. "Effect of the dry-heating conditions on the glycosylation of β-lactoglobulin with dextran through the Maillard reaction." Food Hydrocolloids, 19(5):831-837, 2005.
[10]  Cheison, S. C., Josten, E. and Kulozik, U. "Impact of milieu conditions on the α-lactalbumin glycosylation in the dry state." Journal of Food Engineering, 116(1):176-183, 2013.
[11]  Xia, X., Hong, Y., Zheng, H. and Jiang, L. "Effect of Wet Glycosylation Modification on Sobubility and Emulsifying Activity of Soybean Protein Isolate." Journal of Chinese Institute of Food Science & Technology, 2016.
[12]  Wang, S., Xia, X. F., Li, H., Ding, Y. and Yang, M. "Effect of Glycosylation under Wet-Heating Condition on Functional Properties of Soybean Protein Isolate." Food Science, 2014.
[13]  Yang, W., Tu, Z., Wang, H., Zhang, L. and Song, Q. "Glycation of ovalbumin after high-intensity ultrasound pretreatment: Effects on conformation, IgG/IgE binding ability and antioxidant activity." Journal of the Science of Food & Agriculture, 2018.
[14]  Bornaghi, L. F. and Poulsen, S. A. "Microwave-Accelerated Fischer Glycosylation." Cheminform, 362005.
[15]  An, Y., Cui, B., Wang, Y., Jin, W., Geng, X., Yan, X. and Li, B. "Functional properties of ovalbumin glycosylated with carboxymethyl cellulose of different substitution degree." Food Hydrocolloids, 40: 1-8, 2014.
[16]  Kato, Y., Matsuda, T., Watanabe, K. and Nakamura, R. "Alteration of ovalbumin immunogenic activity by glycosylation through maillard reaction." Agricultural and Biological Chemistry, 49(2): 423-427, 1985.
[17]  Duan, D. l., Tu, Z. c., Wang, H., Sha, X. m. and Huang, T. "Physicochemical and functional properties of glycated ovalbumin in solid-state by microwave." Food and Fermentation Industries, 42(11):48, 2016.
[18]  Corbo, M. R., Bevilacqua, A., Gallo, M., Speranza, B. and Sinigaglia, M. "Immobilization and microencapsulation of Lactobacillus plantarum : Performances and in vivo applications." Innovative Food Science & Emerging Technologies, 18(2):196-201, 2013.
[19]  Zaki, D. Y. I., Hamzawy, E. M. A., Halim, S. A. E. and Amer, M. A. "Effect of simulated gastric juice on surface characteristics of direct esthetic restorations." Australian Journal of Basic & Applied Sciences, 6(3):686-694, 2012.
[20]  Chew, S. C., Tan, C. P., Long, K. and Nyam, K. L. "In-vitro evaluation of kenaf seed oil in chitosan coated-high methoxyl pectin-alginate microcapsules." Industrial Crops & Products, 76: 230-236, 2015.
[21]  Schã¤Gger, H. "Tricine-SDS-PAGE." Nature Protocols, 1(1): 16-22, 2006.
[22]  Pang, Z., Deeth, H., Sopade, P., Sharma, R. and Bansal, N. "Rheology, texture and microstructure of gelatin gels with and without milk proteins." Food Hydrocolloids, 35(3):484-493, 2014.
[23]  Church, F. C., Swaisgood, H. E., Porter, D. H. and Catignani, G. L. "Spectrophotometric Assay Using o -Phthaldialdehyde for Determination of Proteolysis in Milk and Isolated Milk Proteins 1." Journal of Dairy Science, 66(6):1219-1227, 1983.
[24]  Jiménez, M. D. A., Gil, M. I. S., Corvillo, M. A. P. and Díez, L. M. P. "Determination of calcium and magnesium in milk by complexometric titration using protein precipitation and complexation with Palladiazo or other indicators." Analyst, 113(4): 633-5, 1988.
[25]  Liu, Z. "Aluminium Chloride Extraction-EDTA Volumetric Method for Determination of Calcium Fluoride in Fluorite." Guangdong Chemical Industry, 2014.
[26]  Ntailianas, H. A. and Whitney, R. M. "Calcein as an indicator for the determination of total calcium and magnesium and calcium alone in the same aliquot of milk." Journal of Dairy Science, 47(1): 19-27, 1964.
[27]  Xu, X. M., Cao, R. Y., He, L. and Yang, N. "Antioxidant activity of hydrolysates derived from porcine plasma." Journal of the Science of Food & Agriculture, 89(11): 1897-1903, 2009.
[28]  Tang, C.-H., Sun, X. and Foegeding, E. A. "Modulation of Physicochemical and Conformational Properties of Kidney Bean Vicilin (Phaseolin) by Glycation with Glucose: Implications for Structure–Function Relationships of Legume Vicilins." Journal of Agricultural & Food Chemistry, 59(18): 10114-10123, 2011.
[29]  Gu, F., Kim, J. M., Hayat, K., Xia, S., Feng, B. and Zhang, X. "Characteristics and antioxidant activity of ultrafiltrated Maillard reaction products from a casein–glucose model system." Food Chemistry, 117(1):48-54, 2009.
[30]  Chawla, S. P., Chander, R. and Sharma, A. "Antioxidant properties of Maillard reaction products obtained by gamma-irradiation of whey proteins." Food Chemistry, 116(1): 122-128, 2009.
[31]  Corzo-Martínez, M., Soria, A. C., Belloque, J., Villamiel, M. and Moreno, F. J. "Effect of glycation on the gastrointestinal digestibility and immunoreactivity of bovine β-lactoglobulin." International Dairy Journal, 20(11):742-752, 2010.
[32]  Taheri-Kafrani, A., Gaudin, J.-C., Rabesona, H., Nioi, C., Agarwal, D., Drouet, M., Chobert, J.-M., Bordbar, A.-K. and Haertle, T. "Effects of Heating and Glycation of β-Lactoglobulin on Its Recognition by IgE of Sera from Cow Milk Allergy Patients." Journal of Agricultural & Food Chemistry, 57(11):4974-4982, 2009.
[33]  Tu, Z. C., Zhong, B. Z. and Wang, H. "Identification of glycated sites in ovalbumin under freeze-drying processing by liquid chromatography high-resolution mass spectrometry." Food Chem, 226:1-7, 2017.
[34]  Cheng, J., Chen, D. L., Meng, N. I., Chen, D. W., Yang, G. Y. and Wang, A. J. "Absorption experiment of calcium collagen peptide chelate." Food Science & Technology, 2012.
[35]  Cook, J. D. and Monsen, E. R. "Food iron absorption in human subjects. III. Comparison of the effect of animal proteins on nonheme iron absorption." American Journal of Clinical Nutrition, 29(8): 859-67, 1976.