Effects of saccharide on the structure and antigenicity of β-conglycinin in soybean protein isolate by glycation

European Food Research and Technology

Volumn 240, Issue 2, 2015, Pages 285-293

  Bu, Guanhao ^a   Zhu, Tingwei ^a   Chen, Fusheng ^a   Zhang, Nan ^a   Liu, Kunlun ^a   Zhang, Lifen ^a   Yang, Hongshun ^b  

^a HENAN UNIVERSITY OF TECHNOLOGY   (China)

^b NATIONAL UNIVERSITY OF SINGAPORE   (Singapore)

Author keywords

Antigenicity; ELISA; Glycation; Soybean protein; conglycinin

Indexed keywords

ALLERGENS; BIOCATALYSTS; GLUCOSE; GLYCOSYLATION;

ANTIGENICITY; CONGLYCININ; ELISA; GLYCATION; SOYBEAN PROTEINS;

PROTEINS;

GLYCINE MAX;

EID: 84921033814     PISSN: 14382377     EISSN: 14382385     Source Type: Journal    
DOI: 10.1007/s00217-014-2326-5     Document Type: Article

References (36)

1. Fritsche R (2003) Role of technology in dairy allergy. Aust J Dairy Technol 58:89–91
2. Tryphonas H, Arvanitakis G, Vavasour E, Bondy G (2003) Animal models to detect allergenicity to foods and genetically modified products: workshop summary. Environ Health Perspect 111:221
3. Shannon-Wilson BS, Blaschek K, Mejia EG (2005) Allergenic proteins in soybean: processing and reduction of P34 allergenicity. Nutr Rev 63:47–58
4. Gomaa A, Boye JI (2013) Impact of thermal processing time and cookie size on the detection of casein, egg, gluten and soy allergens in food. Food Res Int 52:483–489
5. Cucu T, Platteau C, Taverniers I, Devreese B, De Loose M, De Meulenaer B (2013) Effect of partial hydrolysis on the hazelnut and soybean protein detectability by ELISA. Food Control 30:497–503
6. Song YS, Frias J, Martinez-Villaluenga C, Vidal-Valdeverde C, De Mejia EG (2008) Immunoreactivity reduction of soybean meal by fermentation, effect on amino acid composition and antigenicity of commercial soy products. Food Chem 108:571–581
7. Usui M, Tamura H, Nakamura K, Ogawa T, Muroshita M, Azakami H, Kato A (2004) Enhanced bactericidal action and masking of allergen structure of soy protein by attachment of chitosan through Maillard-type protein–polysaccharide conjugation. Food/Nahrung 48:69–72
8. Holzhauser T, Wackermann O, Ballmer-Weber BK, Bindslev-Jensen C, Scibilia J, Perono-Garoffo L, Utsumi S, Poulsen LK, Vieths S (2008) Soybean (Glycine max) allergy in Europe: gly m 5 (β-conglycinin) and Gly m 6 (glycinin) are potential diagnostic markers for severe allergic reactions to soy. J Allergy Clin Immunol 123:453–458
9. Maruyama N, Katsube T, Wada Y, Oh MH, Barba De La Rosa AP, Okuda E, Utsumi S (1998) The roles of the N-linked glycans and extension regions of soybean β-conglycinin in folding, assembly and structural features. Eur J Biochem 258:854–862
10. Prak K, Nakatani K, Katsube-Tanaka T, Adachi M, Maruyama N, Utsumi S (2005) Structure–function relationships of soybean proglycinins at subunit levels. J Agric Food Chem 53:3650–3657
11. Bu G, Luo Y, Chen F, Liu K, Zhu T (2013) Milk processing as a tool to reduce cow’s milk allergenicity: a mini-review. Dairy Sci Technol 93:211–223
12. Liu Y, Zhao G, Zhao M, Ren J, Yang B (2012) Improvement of functional properties of peanut protein isolate by conjugation with dextran through Maillard reaction. Food Chem 131:901–906
13. Hattori M, Miyakawa S, Ohama Y, Kawamura H, Yoshida T, To-o K, Takahashi K (2004) Reduced immunogenicity of β-lactoglobulin by conjugation with acidic oligosaccharides. J Agric Food Chem 52:4546–4553
14. Hiller B, Lorenzen PC (2010) Functional properties of milk proteins as affected by Maillard reaction induced oligomerisation. Food Res Int 43:1155–1166
15. Xue F, Li C, Zhu X, Wang L, Pan S (2013) Comparative studies on the physicochemical properties of soy protein isolate–maltodextrin and soy protein isolate-gum acacia conjugate prepared through Maillard reaction. Food Res Int 51:490–495
16. Van de Lagemaat J, Manuel Silván J, Javier Moreno F, Olano A, Dolores del Castillo M (2007) In vitro glycation and antigenicity of soy proteins. Food Res Int 40:153–160
17. Bielikowicz K, Kostyra H, Kostyra E, Teodorowicz M, Rigby N, Wojtacha P (2012) The influence of non-enzymatic glycosylation on physicochemical and biological properties of pea globulin 7S. Food Res Int 48:831–838
18. Zhang X, Qi J, Li K, Yin SW, Wang JM, Zhu JH, Yang XQ (2012) Characterization of soy β-conglycinin–dextran conjugate prepared by Maillard reaction in crowded liquid system. Food Res Int 49:648–654
19. Kasran M, Cui SW, Goff HD (2013) Covalent attachment of fenugreek gum to soy whey protein isolate through natural Maillard reaction for improved emulsion stability. Food Hydrocoll 30:552–558
20. Diftis N, Kiosseoglou V (2006) Physicochemical properties of dry-heated soy protein isolate–dextran mixtures. Food Chem 96:228–233
21. Nissen JN (1979) Determination of the degress of hydrolysis of food protein hydrolysates by trinitribenzenesulfonic acid. J Agric Food Chem 27:1256–1263
22. Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacterophage T4. Nature 227:680–685
23. Tong P, Gao J, Chen H, Li X, Zhang Y, Jian S, Liu F (2012) Effect of heat treatment on the potential allergenicity and conformational structure of egg allergen ovotransferrin. Food Chem 131:603–610
24. Zhao X, Chen F, Xue W, Lee L (2008) FTIR spectra studies on the secondary structures of 7S and 11S globulins from soybean proteins using AOT reverse micellar exteaction. Food Hydrocoll 22:568–575
25. Bu G, Luo Y, Lu J, Zhang Y (2010) Reduced antigenicity of β-lactoglobulin by conjugation with glucose through controlled Maillard reaction conditions. Food Agric Immunol 21:143–156
26. Zhang M, Zheng J, Ge K, Zhang H, Fang B, Jiang L, Ren F (2014) Glycation of α-lactalbumin with different size saccharides: effect on protein structure and antigenicity. Int Dairy J 34:220–228
27. Jiang SJ, Zhao XH (2010) Transglutaminase-induced cross-linking and glucosamineconjugation in soybean protein isolates and its impacts on some functional properties of the products. Eur Food Res Technol 231:679–689
28. Taheri-Kafrani A, Gaudin JC, Rabesona H, Nioi C, Agarwal D, Drouet M, Haertle T (2009) Effects of heating and glycation of β-lactoglobulin on its recognition by IgE of sera from cow milk allergy patients. J Agric Food Chem 57:4974–4982
29. Bu G, Luo Y, Zheng Z, Zheng H (2009) Effect of heat treatment on the antigenicity of bovine a-lactalbumin and β-lactoglobulin in whey protein isolate. Food Agric Immunol 20:195–206
30. Shriver SK, Yang WW (2011) Thermal and nonthermal methods for food allergen control. Food Eng Rev 3:26–43
31. Pallarès I, Vendrell J, Avilès FX, Ventura S (2004) Amyloid fibril formation by a partially structured intermediate state of α-chymotrypsin. J Mol Biol 342:321–331
32. Chen X, Ru Y, Chen F, Wang X, Zhao X, Ao Q (2013) FTIR spectroscopic characterization of soy proteins obtained through AOT reverse micelles. Food Hydrocoll 31:435–437
33. Hou HJ, Chang KC (2004) Structural characteristics of purified β-conglycinin from soybean stored under four conditions. J Agric Food Chem 52:7931–7937
34. Kleber N, Maier S, Hinrichs J (2007) Antigenic response of bovine β-lactoglobulin influenced by ultra-high pressure treatment and temperature. Innov Food Sci Emerg Technol 8:39–45
35. Zhao YN, Xin Y, Jiang ZM (2010) Whey protein glycosylation reaction properties and oxidation resistance. China Dairy Industry 8:18–21
36. Li Y, Lu F, Luo CR (2009) Functional properties of the Maillard reaction products of rice protein with sugar. Food Chem 117:69–74