High-intensity ultrasound enhances the immunoglobulin (Ig)G and IgE binding of ovalbumin

Journal of the Science of Food and Agriculture

Volumn 97, Issue 9, 2017, Pages 2714-2720

  Yang, Wen Hua ^a   Tu, Zong Cai ^a,b   Wang, Hui ^a   Li, Xue ^a   Tian, Ming ^a  

^a NANCHANG UNIVERSITY   (China)

^b JIANGXI NORMAL UNIVERSITY   (China)

Author keywords

egg allergy; IgE binding; IgG binding; ovalbumin; structural change; ultrasound

Indexed keywords

IMMUNOGLOBULIN E; IMMUNOGLOBULIN G; OVALBUMIN;

CHEMICAL PHENOMENA; CHEMISTRY; EGG ALLERGY; FOOD HANDLING; HUMAN; IMMUNOLOGY; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN CONFORMATION; PROTEIN FOLDING; ULTRASOUND;

EGG HYPERSENSITIVITY; ELECTROPHORESIS, POLYACRYLAMIDE GEL; FOOD HANDLING; HUMANS; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; IMMUNOGLOBULIN E; IMMUNOGLOBULIN G; OVALBUMIN; PROTEIN CONFORMATION; PROTEIN FOLDING; ULTRASONICS;

EID: 85006381846     PISSN: 00225142     EISSN: 10970010     Source Type: Journal    
DOI: 10.1002/jsfa.8095     Document Type: Article

References (36)

1. Macchia D, Melioli G, Pravettoni V, Nucera E, Piantanida M, Caminati M et al., Guidelines for the use and interpretation of diagnostic methods in adult food allergy. Clin Mol Allergy 13:1–12 (2015).
2. Jiménez-Saiz R, Benedé S, Molina E and López-Expósito I, Effect of processing technologies on the allergenicity of food products. Crit Rev Food Sci Nutr 55:1902–1917 (2015).
3. Verhoeckx KCM, Vissers YM, Baumert JL, Faludi R, Feys M, Flanagan S et al., Food processing and allergenicity. Food Chem Toxicol 80:223–240 (2015).
4. Osborne NJ, Koplin JJ, Martin PE, Gurrin LC, Lowe AJ, Matheson MC et al., Prevalence of challenge-proven IgE-mediated food allergy using population-based sampling and predetermined challenge criteria in infants. J Allergy Clin Immunol 127:668–U188 (2011).
5. Lee J-W, Seo J-H, Kim J-H, Lee S-Y and Byun M-W, Comparison of the changes of the antigenicities of a hen's egg albumin by a gamma and an electron beam irradiation. Radiat Phys Chem 76:879–885 (2007).
6. Lopez-Exposito I, Chicon R, Belloque J, Recio I, Alonso E and Lopez-Fandino R, Changes in the ovalbumin proteolysis profile by high pressure and its effect on IgG and IgE binding. J Agric Food Chem 56:11809–11816 (2008).
7. Ma XJ, Chen HB, Gao JY, Hu CQ and Li X, Conformation affects the potential allergenicity of ovalbumin after heating and glycation. Food Addit Contam Part A Chem Anal Control Expo Risk Assess 30:1684–1692 (2013).
8. Caner C and Yuceer M, Maintaining functional properties of shell eggs by ultrasound treatment. J Sci Food Agric 95:2880–2891 (2015).
9. O'Sullivan J, Murray B, Flynn C and Norton I, The effect of ultrasound treatment on the structural, physical and emulsifying properties of animal and vegetable proteins. Food Hydrocolloids 53:141–154 (2016).
10. Tao Y and Sun D-W, Enhancement of food processes by ultrasound: a review. Crit Rev Food Sci Nutr 55:570–594 (2015).
11. Ozuna C, Paniagua-Martínez I, Castaño-Tostado E, Ozimek L and Amaya-Llano SL, Innovative applications of high-intensity ultrasound in the development of functional food ingredients: production of protein hydrolysates and bioactive peptides. Food Res Int 77:685–696 (2015).
12. Ellman GL, Tissue sulfhydryl groups. Arch Biochem Biophys 82:70–77 (1959).
13. Li H, Zhu K, Zhou H, Peng W and Guo X, Comparative study of four physical approaches about allergenicity of soybean protein isolate for infant formula. Food Agric Immunol 27:604–623 (2016).
14. Stanic-Vucinic D, Stojadinovic M, Atanaskovic-Markovic M, Ognjenovic J, Grönlund H, van Hage M et al., Structural changes and allergenic properties of β-lactoglobulin upon exposure to high-intensity ultrasound. Mol Nutr Food Res 56:1894–1905 (2012).
15. Tammineedi CVRK, Choudhary R, Perez-Alvarado GC and Watson DG, Determining the effect of UV-C, high intensity ultrasound and nonthermal atmospheric plasma treatments on reducing the allergenicity of α-casein and whey proteins. LWT – Food Sci Technol 54:35–41 (2013).
16. Anet J, Back JF, Baker RS, Barnett D, Burley RW and Howden MEH, Allergens in the white and yolk of hens egg. Int Arch Allergy Immunol 77:364–371 (1985).
17. Nisbet AD, Saundry RH, Moir AJG, Fothergill LA and Fothergill JE, The complete amino-acid-sequence of hen ovalbumin. Eur J Biochem 115:335–345 (1981).
18. Roy I, Rao MVS and Gupta MN, An integrated process for purification of lysozyme, ovalbumin, and ovomucoid from hen egg white. Appl Biochem Biotechnol 111:55–63 (2003).
19. Ma XJ, Gao JY and Chen HB, Combined effect of glycation and sodium carbonate-bicarbonate buffer concentration on IgG binding, IgE binding and conformation of ovalbumin. J Sci Food Agric 93:3209–3215 (2013).
20. Tong P, Gao JY, Chen HB, Li X, Zhang Y, Jian S et al., Effect of heat treatment on the potential allergenicity and conformational structure of egg allergen ovotransferrin. Food Chem 131:603–610 (2012).
21. Matulis D and Lovrien R, 1-anilino-8-naphthalene sulfonate anion-protein binding depends primarily on ion pair formation. Biophys J 74:422–429 (1998).
22. Li Z-X, Lin H, Cao L-M and Jameel K, Effect of high intensity ultrasound on the allergenicity of shrimp. J Zhejiang Univ Sci B 7:251–256 (2006).
23. Rahaman T, Vasiljevic T and Ramchandran L, Effect of processing on conformational changes of food proteins related to allergenicity. Trends Food Sci Technol 49:24–34 (2016).
24. Li H, Zhu K, Zhou H and Peng W, Effects of high hydrostatic pressure treatment on allergenicity and structural properties of soybean protein isolate for infant formula. Food Chem 132:808–814 (2012).
25. Huntington JA and Stein PE, Structure and properties of ovalbumin. J Chromatogr B 756:189–198 (2001).
26. Hu H, Wu JH, Li-Chan ECY, Zhu L, Zhang F, Xu XY et al., Effects of ultrasound on structural and physical properties of soy protein isolate (SPI) dispersions. Food Hydrocolloids 30:647–655 (2013).
27. Fernandez-Diaz MD, Barsotti L, Dumay E and Cheftel JC, Effects of pulsed electric fields on ovalbumin solutions and dialyzed egg white. J Agric Food Chem 48:2332–2339 (2000).
28. Gulseren I, Guzey D, Bruce BD and Weiss J, Structural and functional changes in ultrasonicated bovine serum albumin solutions. Ultrason Sonochem 14:173–183 (2007).
29. Jiang L, Wang J, Li Y, Wang Z, Liang J, Wang R et al., Effects of ultrasound on the structure and physical properties of black bean protein isolates. Food Res Int 62:595–601 (2014).
30. Divsalar A, Saboury AA, Ahmad F and Moosavi-Movahedi AA, Effects of temperature and chromium (III) ion on the structure of bovine beta-lactoglobulin-A. J Braz Chem Soc 20:1782–1789 (2009).
31. Yang M, Dutta C and Tiwari A, Disulfide-bond scrambling promotes amorphous aggregates in lysozyme and bovine serum albumin. J Phys Chem B 119:3969–3981 (2015).
32. Xiong W, Wang Y, Zhang C, Wan J, Shah BR, Pei Y et al., High intensity ultrasound modified ovalbumin: structure, interface and gelation properties. Ultrason Sonochem 31:302–309 (2016).
33. Chandrapala J, Zisu B, Palmer M, Kentish S and Ashokkumar M, Effects of ultrasound on the thermal and structural characteristics of proteins in reconstituted whey protein concentrate. Ultrason Sonochem 18:951–957 (2011).
34. Stathopulos PB, Scholz GA, Hwang YM, Rumfeldt JA, Lepock JR and Meiering EM, Sonication of proteins causes formation of aggregates that resemble amyloid. Protein Sci 13:3017–3027 (2004).
35. Arzeni C, Martinez K, Zema P, Arias A, Perez OE and Pilosof AMR, Comparative study of high intensity ultrasound effects on food proteins functionality. J Food Eng 108:463–472 (2012).
36. Mine Y and Zhang JW, Comparative studies on antigenicity and allergenicity of native and denatured egg white proteins. J Agric Food Chem 50:2679–2683 (2002).