Effect of different pH and ion strength on IgG/IgE binding capacity of sarcoplasmic protein of black carp (Mylopharyngodon piceus)

  • ZHU Yidan ,
  • XIE Guojin ,
  • GAO Ling ,
  • YANG Fang ,
  • GAO Pei ,
  • YU Dawei ,
  • JIANG Qixing ,
  • XU Yanshun ,
  • XIA Wenshui
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  • 1(State Key Laboratory of Food Science and Technology, School of Food Science and Technology, Collaborative Innovation Center of Food Safety and Quality Control in Jiangsu Province, Jiangnan University, Wuxi 214122, China)
    2(Children's Hospital of Nanjing Medical University, Nanjing 210000, China)

Received date: 2020-02-09

  Online published: 2020-08-17

Abstract

Freshwater fish is the main source of protein for Chinese. The increased fish consumption correlates with increased hypersensitive reactions, which could reduce consumer’s living quality. The aim of this article was to evaluate the IgG/IgE binding capacity and structure of sarcoplasmic protein of black carp (Mylopharyngodon piceus) exposed to different pH and ion strength. The IgG/IgE binding capacity was determined by indirect ELISA, SDS-PAGE and western blotting. And protein structure was determined by secondary structure, surface hydrophobicity and intrinsic fluorescence intensity. The results showed that the IgG/IgE binding capacity of sarcoplasmic protein decreased slightly with pH shifting from 4.0 to 7.0, and along with the increased α-helix and decreased random coil in the secondary structure. The surface hydrophobicity decreased significantly and the tryptophan hydrophobic base was exposed to the polar environment. However, the increase of ion strength from 0 to 1.0 had no significant impact on sensitization. The change of immunological properties of sarcoplasmic protein was related to its conformational epitopes, which was mainly caused by the change of secondary structure.

Cite this article

ZHU Yidan , XIE Guojin , GAO Ling , YANG Fang , GAO Pei , YU Dawei , JIANG Qixing , XU Yanshun , XIA Wenshui . Effect of different pH and ion strength on IgG/IgE binding capacity of sarcoplasmic protein of black carp (Mylopharyngodon piceus)[J]. Food and Fermentation Industries, 2020 , 46(14) : 34 -39 . DOI: 10.13995/j.cnki.11-1802/ts.023558

References

[1] FERNANDES T J R, COSTA J, CARRAPATOSO I,et al. Advances on the molecular characterization, clinical relevance, and detection methods of Gadiform parvalbumin allergens[J]. Crit Rev Food Sci Nutr,2017,57(15): 3 281-3 296.
[2] SHARP M F, KAMATH S D, KOEBERL M, et al. Differential IgE binding to isoallergens from Asian seabass (Lates calcarifer) in children and adults[J]. Mol Immunol,2014, 62(1): 77-85.
[3] 陈香梅,张亮,齐立明,等.北京地区3236例过敏性疾病患者血清过敏原的季节差异分析[J].河北医科大学学报,2019,40(10):1 180-1 184.
[4] ZHAO Yongjuan,CAI Qiufeng,JIN Tengchuan,et al. Effect of Maillard reaction on the structural and immunological properties of recombinant silver carp parvalbumin[J]. LWT - Food Science and Technology,2017,75: 25-33.
[5] LIU Rong,KRISHNAN H B,Xue Wenton, et al. Characterization of allergens isolated from the freshwater fish blunt snout bream (Megalobrama amblycephala)[J]. J Agric Food Chem,2011, 59(1): 458-463.
[6] 石径,罗永康,江米足.多种鱼类肌浆蛋白与过敏患者血清特异性IgE结合情况检测与分析[J]. 中国渔业质量与标准, 2017(1):22-28.
[7] KOBAYASHI A,TANAKA H,HAMADA Y, et al.Comparison of allergenicity and allergens between fish white and dark muscles[J]. Allergy,2006, 61(3): 357-363.
[8] SHARP M F, LOPATA A L.Fish allergy: In review[J]. Clinical Reviews in Allergy & Immunology,2013,46(3): 258-271.
[9] BUGAJSKA-SCHRETTER A,GROTE M, VANGELISTA L, et al.Purification, biochemical, and immunological characterisation of a major food allergen: Different immunoglobulin E recognition of the apo- and calcium-bound forms of carp parvalbumin[J]. Gut,2000 46(5): 661-669.
[10] LIU R, HOLCKA L,YANG E, et al.Tropomyosin from tilapia (Oreochromis mossambicus) as an allergen[J].Clinical & Experimental Allergy,2013,43: 365-377.
[11] VOGEL S V, HENTGES F. Identification of enolases and aldolases as important fish allergens in cod,salmon and tuna: Component resolved diagnosis using parvalbumin and the new allergens[J]. Clinical & Experimental Allergy,2013,43: 811-822.
[12] 刘楚怡,刘蓉,薛文通,等.四种淡水鱼致敏蛋白免疫原性研究[J].食品工业科技,2011,32(11):164-165;167.
[13] 张晶宇,翟子扬,顾盼,等.反相液相色谱-串联质谱法筛选牙鲆鱼蛋白质中潜在的过敏原[J].食品安全质量检测学报,2019,10(7):1 797-1 803.
[14] LIU Xiaoyu,LUO Yongkang, LI Zheng. Effects of pH, temperature, enzyme-to-substrate ratio and reaction time on the antigenicity of casein hydrolysates prepared by papain[J]. Food and Agricultural Immunology,2010, 23(1): 69-82.
[15] LIN Haixin,LI Zhenxing,LIN Hong,et al.Effect of pH shifts on IgE-binding capacity and conformational structure of tropomyosin from short-neck clam (Ruditapes philippinarum)[J]. Food Chemistry,2015,188: 248-255.
[16] MA J,PAVASE T R,LI Z,et al.Optimisation of an extraction technique of fish allergens suitable for detection and diagnosis[J]. Czech Journal of Food Sciences,2017,35(1): 24-31.
[17] LYU Liangtao,LIN Hong,LI Zhenxing,et al. Determining the effect of malondialdehyde on the IgE-binding capacity of shrimp tropomyosin upon in vitro digestion[J]. J Sci Food Agric,2017, 97(13): 4 588-4 594.
[18] WANG Weixin,XIA Wenshui,GAO Pei,et al. Proteolysis during fermentation of Suanyu as a traditional fermented fish product of China[J]. International Journal of Food Properties,2017, 20(sup1): S166-S176.
[19] ZHANG Yongxia,CHEN Hengli,MALEKI S J,et al., Purification, characterization, and analysis of the allergenic properties of myosin light chain in procambarus clarkii[J]. J Agric Food Chem, 2015, 63(27): 6 271-6 282.
[20] 杨方.鱼肉内源酶对发酵鱼糜凝胶和抗氧化特性的影响的研究[D].无锡:江南大学,2016.
[21] SKJERVOLD P O, TAYLOR R G, WOLD J P, et al. Development of intrinsic fluorescent multispectral imagery specific for fat, connective tissue, and myofibers in meat[J]. Journal of Food Science, 2003, 68(4): 1 161-1 168.
[22] MORO A, GATTI C, DELORENOI N. Hydrophobicity of whey protein concentrates measured by fluorescence quenching and its relation with surface functional properties[J]. Journal of Agricultural and Food Chemistry, 2001, 49(10): 4 784-4 789.
[23] DUFOUR E, DEVAUX M, FORTIER P, et al. Delineation of the structure of soft cheeses at the molecular level by fluorescence spectroscopy-relationship with texture[J]. International Dairy Journal, 2001, 11(4): 465-473.
[24] LEFEVRE F, FAUCONNEAU B, THOMPSON J W, et al. Thermal denaturation and aggregation properties of Atlantic salmon myofibrils and myosin from white and red muscles[J]. Journal of Agricultural and Food Chemistry, 2007, 55(12): 4 761-4 770.
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