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High hydrostatic pressure (HHP) effects on antigenicity and structural properties of soybean β-conglycinin

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Abstract

In this study, the effect of high hydrostatic pressure (HHP) on antigenicity, free sulfhydryl group (SH) content, hydrophobicity (Ho), fluorescence intensity and circular dichroism data of soybean β-conglycinin was studied. The antigenicity of soybean β-conglycinin was decreased significantly at pressures 200–400 MPa. The antigenicity inhibition rate of β-conglycinin declined from 92.72 to 55.15%, after being treated at 400 MPa for 15 min. Results indicated that free sulphydryl (SH) groups and surface Ho of β-conglycinin were significantly increased at pressures 200–400 MPa and 5–15 min, whereas these properties decreased at the treatments above 400 MPa and 15 min. The maximum fluorescence intensity was noticed at 400 MPa and 15 min. The circular dichroism data analysis revealed that the amount of β-turns and unordered structure significantly increased, while the content of α-helix1 and β-strand1 noticeably decreased. These results provide evidence that HHP-induced the structural modification of β-conglycinin and could alter the antigenicity of β-conglycinin.

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References

  • Ambrosi V, Polenta G, Gonzalez C, Ferrari G, Maresca P (2016) High hydrostatic pressure assisted enzymatic hydrolysis of whey proteins. Innov Food Sci Emerg 38:294–301

    Article  CAS  Google Scholar 

  • Beveridge T, Toma SJ, Nakai S (1974) Determination of sh- and ss-groups in some food proteins using ellman’s reagent. J Food Sci 39(1):49–51

    Article  CAS  Google Scholar 

  • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72(1–2):248–254

    Article  CAS  Google Scholar 

  • Cabanillas B, Maleki SJ, Rodríguez J, Cheng H, Teuber SS, Wallowitz ML, Crespo JF (2014) Allergenic properties and differential response of walnut subjected to processing treatments. Food Chem 157(1):141–147

    Article  CAS  Google Scholar 

  • Cabanillas B, Cuadrado C, Rodriguez J, Hart J, Burbano C, Crespo JF, Novak N (2015) Potential changes in the allergenicity of three forms of peanut after thermal processing. Food Chem 183:18–25

    Article  CAS  Google Scholar 

  • Elahi R, Mu TH (2017) High hydrostatic pressure (HHP)-induced structural modification of patatin and its antioxidant activities. Molecules 22(3):438

    Article  Google Scholar 

  • Galazka VB, Dickinson E, Ledward DA (2000) Influence of high pressure processing on protein solutions and emulsions. Curr Opin Colloid In 5(3–4):182–187

    Article  CAS  Google Scholar 

  • Hancock JD, Cao H, Kim IH, Li DF, Aumaitre A, Lee BD (2000) Effects of processing technologies and genetic modifications on nutritional value of full-fat soybeans in pigs. Asian Austral J Anim 13(4):356–375

    Google Scholar 

  • He L, Han M, Qiao S, He P, Li D, Li N, Ma X (2015) Soybean antigen proteins and their intestinal sensitization activities. Curr Protein Pept Sc 16(7):613–621

    Article  CAS  Google Scholar 

  • Hu C, Chen H, Gao J, Luo C, Ma X, Tong P (2011) High-pressure microfluidisation-induced changes in the antigenicity and conformation of allergen ara h 2 purified from chinese peanut. J Sci Food Agric 91(7):1304–1309

    Article  CAS  Google Scholar 

  • Hu G, Zheng Y, Liu Z, Deng Y, Zhao Y (2016) Structure and ige-binding properties of α-casein treated by high hydrostatic pressure, UV-c, and far-IR radiations. Food Chem 204:46–55

    Article  CAS  Google Scholar 

  • Kajiyama N, Isobe S, Uemura K, Noguchi A (1995) Changes of soy protein under ultra-high hydraulic pressure. Int J Food Sci Tech 30(2):147–158

    Article  CAS  Google Scholar 

  • Koshiyama I, Fukushima D (1973) Comparison of conformations of 7s and 11s soybean globulins by optical rotatory dispersion and circular dichroism studies. Cereal Chem 50(1):114–121

    CAS  Google Scholar 

  • Krishnan HB, Kim WS, Jang S, Kerley MS (2009) All three subunits of soybean beta conglycinin are potential food allergens. J Agric Food Chem 57:938–943

    Article  CAS  Google Scholar 

  • Li YQ, Chen ZX, Mo HZ (2007) Effects of pulsed electric fields on physicochemical properties of soybean protein isolates. LWT Food Sci Technol 40(7):1167–1175

    Article  CAS  Google Scholar 

  • Li H, Zhu K, Zhou H, Peng W (2012) Effects of high hydrostatic pressure treatment on allergenicity and structural properties of soybean protein isolate for infant formula. Food Chem 132(2):808–814

    Article  CAS  Google Scholar 

  • Li H, Zhu K, Zhou H, Peng W, Guo X (2016) Comparative study of four physical approaches about allergenicity of soybean protein isolate for infant formula. Food Agric Immunol 27(5):1–20

    Article  Google Scholar 

  • Ma X, He P, Sun P, Han P (2010) Lipoic acid: an immunomodulator that attenuates glycinin-induced anaphylactic reactions in a rat model. J Agric Food Chem 58(8):5086–5092

    Article  CAS  Google Scholar 

  • Meng X, Bai Y, Gao J, Xin L, Chen H (2017) Effects of high hydrostatic pressure on the structure and potential allergenicity of the major allergen bovine β-lactoglobulin. Food Chem 219:290–296

    Article  CAS  Google Scholar 

  • Messens W, Camp JV, Huyghebaert A (1997) The use of high pressure to modify the functionality of food proteins. Trends Food Sci Technol 8(4):107–112

    Article  CAS  Google Scholar 

  • Molina E, Papadopoulou A, Ledward DA (2001) Emulsifying properties of high pressure treated soy protein isolate and 7s and 11s globulins. Food Hydrocolloid 15(3):263–269

    Article  CAS  Google Scholar 

  • Nagano T, Hirotsuka M, Mori H, Kohyama K, Nishinari K (1992) Dynamic viscoelastic study on the gelation of 7s globulin from soybeans. J Agric Food Chem 40(6):941–944

    Article  CAS  Google Scholar 

  • Ogawa T, Bando N, Tsuji H, Nishikawa K, Kitamura K (1995) Alpha-subunit of beta-conglycinin, an allergenic protein recognized by IgE antibodies of soybean-sensitive patients with atopic dermatitis. Biosci Biotechnol Biochem 59(5):831–833

    Article  CAS  Google Scholar 

  • Omi Y, Kato T, Ishida K, Kato H, Matsuda T (1996) Pressure-induced release of basic 7s globulin from cotyledon dermal tissue of soybean seeds. J Agric Food Chem 44(12):3763–3767

    Article  CAS  Google Scholar 

  • Peñas E, Gomez R, Frias J, Baeza ML, Vidal-Valverde C (2011) High hydrostatic pressure effects on immunoreactivity and nutritional quality of soybean products. Food Chem 125(2):423–429

    Article  Google Scholar 

  • Prieto N, Burbano C, Iniesto E, Rodríguez J, Cabanillas B, Crespo JF, Cuadrado C (2014) A novel proteomic analysis of the modifications induced by high hydrostatic pressure on hazelnut water-soluble proteins. Foods 3(2):279–289

    Article  CAS  Google Scholar 

  • Puppo C, Chapleau N, Speroni F, De Lamballerie-Anton M, Michel F, Añón C, Anton M (2004) Physicochemical modifications of high-pressure-treated soybean protein isolates. J Agric Food Chem 52(6):1564–1571

    Article  CAS  Google Scholar 

  • Puppo MC, Beaumal V, Speroni F, Lamballerie MD, Añón MC, Anton M (2011) β-conglycinin and glycinin soybean protein emulsions treated by combined temperature-high-pressure treatment. Food Hydrocolloid 25(3):389–397

    Article  CAS  Google Scholar 

  • Sen M, Kopper R, Pons L, Abraham EC, Burks AW, Bannon GA (2002) Protein structure plays a critical role in peanut allergen stability and may determine immunodominant IgE-binding epitopes. J Immunol 169(2):882–887

    Article  CAS  Google Scholar 

  • Wang XS, Tang CH, Li BS, Yang XQ, Li L, Ma CY (2008) Effects of high-pressure treatment on some physicochemical and functional properties of soy protein isolates. Food Hydrocolloid 22(4):560–567

    Article  CAS  Google Scholar 

  • Wang JM, Yang XQ, Yin SW, Zhang Y, Tang CH, Li BS, Yuan DB, Guo J (2011) Structural rearrangement of ethanol-denatured soy proteins by high hydrostatic pressure treatment. J Agric Food Chem 59(13):7324

    Article  CAS  Google Scholar 

  • Whitmore L, Wallace BA (2004) Dichroweb, an online server for protein secondary structure analyses from circular dichroism spectroscopic data. Nucleic Acids Res 32(Web Server issue):W668–W673

    Article  CAS  Google Scholar 

  • Wilson S, Blaschek K, Mejia E (2004) Allergenic proteins in soybean: processing and reduction of p34 allergenicity. Nutr Rev 63(2):47–58

    Article  Google Scholar 

  • Zhang H, Li L, Tatsumi E, Kotwal S (2003) Influence of high pressure on Conformational changes of soybean glycinin. Innov Food Sci Emerg 4(3):269–275

    Article  CAS  Google Scholar 

  • Zhang M, Zheng J, Ge K, Zhang H, Fang B, Jiang L, Guo H, Ding Q, Ren F (2014) Glycation of α-lactalbumin with different size saccharides: effect on protein structure and antigenicity. Int Dairy J 34(2):220–228

    Article  CAS  Google Scholar 

  • Zhou H, Wang C, Ye J, Chen H, Tao R, Cao F (2016) Effects of high hydrostatic pressure treatment on structural, allergenicity, and functional properties of proteins from ginkgo seeds. Innov Food Sci Emerg 34:187–195

    Article  CAS  Google Scholar 

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Acknowledgements

This work was supported by National Natural Science Foundation of China (NSFC, 31671778) and Key Scientific Research Projects of Henan Colleges and Universities under Grant No. (16A550001).

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Authors and Affiliations

  1. School of Food Science and Technology, Henan University of Technology, Zhengzhou, 450001, Henan, China

    Jun Xi & Mengxue He

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  1. Jun Xi
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  2. Mengxue He
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Correspondence to Jun Xi.

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Fig. 1

SDS-PAGE and Western Blot of purified β-conglycinin (A: SDS-PAGE of purified β-conglycinin; B: Western Blot of purified β-conglycinin) (M: Marker; 1: purified β-conglycinin) (TIFF 1272 kb)

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Xi, J., He, M. High hydrostatic pressure (HHP) effects on antigenicity and structural properties of soybean β-conglycinin. J Food Sci Technol 55, 630–637 (2018). https://doi.org/10.1007/s13197-017-2972-2

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  • DOI: https://doi.org/10.1007/s13197-017-2972-2

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