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Reviews

Potential efficacy of processing technologies for mitigating crustacean allergenicity

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Pages 2807-2830 | Accepted 29 Apr 2018, Published online: 31 May 2018

References

  • Abida, J., B. Rayees, and F. A. Masoodi. 2014. Pulsed light technology: a novel method for food preservation. International Food Research Journal 21 (3):839–48.
  • Abramovitch, J. B., A. L. Lopata, R. E. O'Hehir, and J. M. Rolland. 2017. Effect of thermal processing on T cell reactivity of shellfish allergens-discordance with IgE reactivity. Plos One 12 (3):e0173549. doi:10.1371/journal.pone.0173549.
  • Ahmed, I., H. Lin, L. Zou, A. L. Brody, Z. Li, I. M. Qazi, T. R. Pavase, and L. Lv. 2017. A comprehensive review on the application of active packaging technologies to muscle foods. Food Control 82:163–78. doi:10.1016/j.foodcont.2017.06.009.
  • Ahmed, I., L. Lv, H. Lin, Z. Li, J. Ma, C. Guanzhi, L. Sun, and L. Xu. 2018. Effect of tyrosinase-aided crosslinking on the IgE binding potential and conformational structure of shrimp (Metapenaeus ensis) tropomyosin. Food Chemistry 248:287–95. doi:10.1016/j.foodchem.2017.12.071.
  • Ahmed, I., I. M. Qazi, and S. Jamal. 2016. Developments in osmotic dehydration technique for the preservation of fruits and vegetables. Innovative Food Science and Emerging Technologies 34:29–43. doi:10.1016/j.ifset.2016.01.003.
  • Allen, K. J., P. J. Turner, R. Pawankar, S. Taylor, S. Sicherer, G. Lack, N. Rosario, M. Ebisawa, G. Wong, E. N. C. Mills, K. Beyer, A. Fiocchi, and H. A. Sampson. 2014. Precautionary labelling of foods for allergen content: are we ready for a global framework? World Allergy Organization Journal 7 (1):10–10. doi:10.1186/1939-4551-7-10.
  • ALLERGEN. 2017. Official site for the systematic allergen nomenclature. Retrieved from http://www.allergen.org/. Accessed November 2017.
  • ALLERGOME. 2017. Allergome database, the platform for allergen knowledge, Latina, Italy. Retrieved from http://www.allergome.org/. Accessed November 2017.
  • Apostolovic, D., D. Stanic-Vucinic, H. H. de Jongh, G. A. de Jong, J. Mihailovic, J. Radosavljevic, M. Radibratovic, J. A. Nordlee, J. L. Baumert, M. Milcic, and S. L. Taylor. 2016. Conformational stability of digestion-resistant peptides of peanut conglutins reveals the molecular basis of their allergenicity. Scientific Reports 6:29249. doi:10.1038/srep29249.
  • Ayuso, R., G. Grishina, L. Bardina, T. Carrilo, C. Blanco, M. D. Ibanez, H. A. Sampson, and K. Beyer. 2008. Myosin light chain is a novel shrimp allergen, Lit v 3. Journal of Allergy and Clinical Immunology 122:795–802. doi:10.1016/j.jaci.2008.07.023.
  • Ayuso, R., G. Grishina, M. D. Ibáñez, C. Blanco, T. Carrillo, R. Bencharitiwong, S. Sánchez, A. Nowak-Wegrzyn, and H. A. Sampson. 2009. Sarcoplasmic calcium-binding protein is an EF-hand–type protein identified as a new shrimp allergen. Journal of Allergy and Clinical Immunology 124 (1):114–20. doi:10.1016/j.jaci.2009.04.016.
  • Balasubramaniam, V. M., S. I. Martínez-Monteagudo, and R. Gupta. 2015. Principles and application of high pressure-based technologies in the food industry. Annual Review of Food Science and Technology 6:435–62. doi:10.1146/annurev-food-022814-015539.
  • Bauermeister, K. B., A. Wangorsch, L. P. Garoffo, A. Reuter, A. Conti, S. L. Taylor, J. Lidholm, Å. M. DeWitt, E. Enrique, S. Vieths, and T. Holzhauser. 2011. Generation of a comprehensive panel of crustacean allergens from the North Sea Shrimp Crangon crangon. Mol. Immunol. 48:1983–92. doi:10.1016/j.molimm.2011.06.216.
  • Binder, M., V. Mahler, B. Hayek, W. R. Sperr, M. Schöller, S. Prozell, G. Wiedermann, P. Valent, R. Valenta, and M. Duchêne. 2001. Molecular and immunological characterization of arginine kinase from the Indian meal moth, Plodia interpunctella, a novel cross-reactive invertebrate pan-allergen. Journal of Immunology 167 (9):5470–77. doi:10.4049/jimmunol.167.9.5470.
  • Bobolea, I., P. Barranco, C. Pastor-Vargas, V. Iraola, F. Vivanco, and S. Quirce. 2011. Arginine kinase from the cellar spider (Holocnemus pluchei): a new asthma-causing allergen. International Archives of Allergy and Immunology 155:180–86. doi:10.1159/000319822.
  • Boye, J. I. 2012. Food allergies in developing and emerging economies: need for comprehensive data on prevalence rates. Clinical and Translational Allergy 2 (1):25. doi:10.1186/2045-7022-2-25.
  • Bucchini, L., A. Guzzon, R. Poms, and H. Senyuva. 2016. Analysis and critical comparison of food allergen recalls from the European Union, USA, Canada, Hong Kong, Australia and New Zealand. Food Addit. Contam. Part A. 33 (5):760–71. doi:10.1080/19440049.2016.1169444.
  • Buchert, J., D. Ercili Cura, H. Ma, C. Gasparetti, E. Monogioudi, G. Faccio, M. Mattinen, H. Boer, R. Partanen, E. Selinheimo, and R. Lantto. 2010. Crosslinking food proteins for improved functionality. Annual Review of Food Science and Technology 1:113–38. doi:10.1146/annurev.food.080708.100841.
  • Burks, A., M. Tang, S. Sicherer, A. Muraro, P.A. Eigenmann, M. Ebisawa, A. Fiocchi, W. Chiang, K. Beyer, R. Wood, and J. Hourihane. 2012. ICON: Food allergy. Journal of Allergy and Clinical Immunology 129:906–20. doi:10.1016/j.jaci.2012.02.001.
  • Burney, P., C. Summers, S. Chinn, R. Hooper, R. Van Ree, and J. Lidholm. 2010. Prevalence and distribution of sensitization to foods in the European Community Respiratory Health Survey: a EuroPrevall analysis. Allergy 65 (9):1182–88.
  • Byun, M. W., J. H. Kim, J. W. Lee, J. W. Park, C. S. Hong, and I. J. Kang. 2000. Effects of gamma radiation on the conformational and antigenic properties of a heat-stable allergen in brown shrimp. Journal of Food Protection 63:940–44. doi:10.4315/0362-028X-63.7.940.
  • Byun, M. W., J. W. Lee, H. S. Yook, C. Jo, and H. Y. Kim. 2002. Application of gamma irradiation for inhibition of food allergy. Radiation Physics and Chemistry 63 (3):369–70. doi:10.1016/S0969-806X(01)00528-X.
  • Cao, J., B. Yu, L. Ma, Q. Zheng, X. Zhao, and J. Xu. 2011. Detection of shrimp-derived components in food by real-time fluorescent PCR. J. Food Protect. 74:1776–81. doi:10.4315/0362-028X.JFP-11-020.
  • Chen, H. L., M. J. Cao, Q. F. Cai, W. J. Su, H. Y. Mao, and G. M. Liu. 2013b. Purification and characterisation of sarcoplasmic calcium-binding protein, a novel allergen of red swamp crayfish (Procambarus clarkii). Food Chemistry 139:213–23. doi:10.1016/j.foodchem.2013.01.119.
  • Chen, H. L., H. Y. Mao, M. J. Cao, Q. F. Cai, W. J. Su, Y. X. Zhang, and G. M. Liu. 2013a. Purification, physicochemical and immunological characterization of arginine kinase, an allergen of crayfish (Procambarus clarkii). Food and Chemical Toxicology 62:475–84. doi:10.1016/j.fct.2013.09.014.
  • Chen, Q., X.-D. Pan, and B.-F. Huang. 2017. Authentication of shrimp muscle in complex foodstuff by in-solution digestion and high-resolution mass spectrometry. RSC Advances 7 (52):32903–32908. doi:10.1039/C7RA04967F.
  • Chiang, W. C., M. I. Kidon, W. K. Liew, A. Goh, J. P. L. Tang, and O. M. Chay. 2007. The changing face of food hypersensitivity in an Asian community. Clinical & Experimental Allergy 37:1055–61. doi:10.1111/j.1365-2222.2007.02752.x.
  • Choi, Y., S. Ju, and H. Chang. 2015. Food allergy knowledge, perception of food allergy labeling, and level of dietary practice: A comparison between children with and without food allergy experience. Nutrition Research and Practice 9 (1):92–98. doi:10.4162/nrp.2015.9.1.92.
  • Chu, K. H., S. H. Wong, and P. S. Leung. 2000. Tropomyosin is the major mollusk allergen: reverse transcriptase polymerase chain reaction, expression and IgE reactivity. Marine Biotechnology 2 (5):499–509.
  • Corzo‐Martínez, M., M. Villamiel, and F. J. Moreno. 2017. Impact of high‐intensity ultrasound on protein structure and functionality during food processing. In Ultrasound in Food Processing: Recent Advances, ed. M., Villamiel, J. V., Garcia-Perez, A., Montilla, and J. A., Carcel, 417–36. Chichester: John Wiley & Sons Ltd.
  • Costa, J., T. J. R. Fernandes, C. Villa, M. B. P. P. Oliveira, and I. Mafra. 2017. Advances in food allergen analysis. In Food Safety: Innovative Analytical Tools for Safety Assessment, chapter 9, ed. U. G., Spizzirri and G., Cirillo, 305–60. Beverly: Scrivener Publishing LLC.
  • Costa, J., P. Ansari, I. Mafra, M. B. P. Oliveira, and S. Baumgartner. 2015. Development of a sandwich ELISA-type system for the detection and quantification of hazelnut in model chocolates. Food Chemistry 173:257–265.
  • Daul, C. B., M. Slattery, G. Reese, and S. B. Lehrer. 1994. Identification of the major brown shrimp (Penaeus aztecus) allergen as the muscle protein tropomyosin. International Archives of Allergy and Immunology 105:49–55. doi:10.1159/000236802.
  • Davis, P. J., C. M. Smales, and D. C. James. 2001. How can thermal processing modify the antigenicity of proteins? Allergy 56:56–60. doi:10.1034/j.1398-9995.2001.00918.x.
  • Directive 2007/68/EC of 27. November 2007. amending Annex IIIa to Directive 2000/13/EC regarding certain food ingredients. Off. J. Eur. Union. L310:11–14.
  • Eischeid, A. C. 2016. Development and evaluation of a real-time PCR assay for detection of lobster, a crustacean shellfish allergen. Food Control 59:393–99. doi:10.1016/j.foodcont.2015.06.013.
  • Eischeid, A. C., B.-H. Kim, and S. M. Kasko. 2013. Two quantitative real-time PCR assays for the detection of Penaeid shrimp and blue crab, crustacean shellfish allergens. Journal of Agricultural and Food Chemistry 61:5669–74. doi:10.1021/jf3031524.
  • Eischeid, A. C., and S. R. Stadig. 2018. A group-specific, quantitative real-time PCR assay for detection of crab, a crustacean shellfish allergen, in complex food matrices. Food Chemistry 244:224–31. doi:10.1016/j.foodchem.2017.10.045.
  • Encyclopedia of Life. 2017. Official site for information and pictures of all species known to science. Retrieved from http://www.eol.org/. Accessed November 2017.
  • Faber, M. A., M. Pascal, O. El Kharbouchi, V. Sabato, M. M. Hagendorens, I. I. Decuyper, C.H. Bridts, and D. G. Ebo. 2017. Shellfish allergens: tropomyosin and beyond. Allergy 72 (6):842–48. doi:10.1111/all.13115.
  • FAO/WHO. 2001. Evaluation of allergenicity of genetically modified foods: report of a joint FAO/WHO expert consultation on allergenicity of foods derived from biotechnology. 22–25 January\2001. p. 15. FAO/WHO, Rome, Italy.
  • Fei, D. X., Q. M. Liu, F. Chen, Y. Yang, Z. W. Chen, M. J. Cao, and G. M. Liu. 2016. Assessment of the sensitizing capacity and allergenicity of enzymatic cross‐linked arginine kinase, the crab allergen. Molecular Nutrition &Amp; Food Research 60 (7):1707–18. doi:10.1002/mnfr.201500936.
  • Fernandes, T. J., J. Costa, M. B. P. Oliveira, and I. Mafra. 2015. An overview on fish and shellfish allergens and current methods of detection. Food and Agricultural Immunology 26 (6):848–69. doi:10.1080/09540105.2015.1039497.
  • Fernandes, T. J. R., C. R. Silva, J. Costa, M. B. P. P. Oliveira, and I. Mafra. 2017. High resolution melting analysis of a COI mini-barcode as a new approach for Penaeidae shrimp species discrimination. Food Control 82:8–17. doi:10.1016/j.foodcont.2017.06.016.
  • Fuller, H. R., P. R. Goodwin, and G. E. Morris. 2006. An enzyme-linked immunosorbent assay (ELISA) for the major crustacean allergen, tropomyosin, in food. Food and Agricultural Immunology 17 (1):43–52. doi:10.1080/09540100600572651.
  • Gao, Y., C. M. Gillen, and M. G. Wheatly. 2006. Molecular characterization of the sarcoplasmic calcium-binding protein (SCP) from crayfish Procambarus clarkii. Comparat. Biochem. Physiol. Part B: Biochem. Mol. Biol. 144:478–87. doi:10.1016/j.cbpb.2006.04.007.
  • García-Orozco, K. D., E. Aispuro-Hernandez, G. Yepiz-Plascencia, A. M. Calderon-de-la-Barca, and R. R. Sotelo Mundo. 2007. Molecular characterization of arginine kinase, an allergen from the shrimp Litopenaeus vannamei. International Archives of Allergy and Immunology 144:23–28. doi:10.1159/000102610.
  • Giuffrida, M. G., D. Villalta, G. Mistrello, S. Amato, and R. Asero. 2014. Shrimp allergy beyond tropomyosin in Italy: Clinical relevance of arginine kinase, sarcoplasmic calcium binding protein and hemocyanin. Eur. Ann. Allergy Clin. Immunol. 46:172–77.
  • Gupta, R. K., K. Gupta, A. Sharma, M. Das, I. A. Ansari, and P. D. Dwivedi. 2016. Maillard reaction in food allergy: Pros and cons. Critical Reviews in Food Science and Nutrition 15:1–19.
  • Hales, B. J., I. A. Laing, L. J. Pearce, L. A. Hazell, K. L. Mills, K. Y. Chua, R. B. Thornton, P. Richmond, A. W. Musk, A. L. James, and P. N. Lesouëf. 2007. Distinctive immunoglobulin E anti‐house dust allergen‐binding specificities in a tropical Australian Aboriginal community. Clinical & Experimental Allergy 37 (9):1357–63. doi:10.1111/j.1365-2222.2007.02786.x.
  • Harder, M. N. C., V. Arthur, and L. N. C. Harder. 2017. Gamma radiation effect on allergenic food. In Allergen, chapter 8, ed. S. S., Athari, 139–50. Rijeka: InTech.
  • Heilmann, M., A. Wellner, G. Gadermaier, A. Ilchmann, P. Briza, M. Krause, R. Nagai, S. Burgdorf, S. Scheurer, S. Vieths, and T. Henle. 2014. Ovalbumin modified with pyrraline, a Maillard reaction product, shows enhanced T-cell immunogenicity. Journal of Biological Chemistry 289 (11):7919–28. doi:10.1074/jbc.M113.523621.
  • Heinrich, V., M. Zunabovic, T. Varzakas, J. Bergmair, and W. Kneifel. 2016. Pulsed light treatment of different food types with a special focus on meat: a critical review. Critical Reviews in Food Science and Nutrition 56 (4):591–613. doi:10.1080/10408398.2013.826174.
  • Heinz, V., and R. Buckow. 2010. Food preservation by high pressure. J. Fur Verbraucherschutz Und Lebensmittelsicherheit. 5 (1):73–81. doi:10.1007/s00003-009-0311-x.
  • Henle, T. 2005. Protein-bound advanced glycation endproducts (AGEs) as bioactive amino acid derivatives in foods. Amino Acids. 29 (4):313–22. doi:10.1007/s00726-005-0200-2.
  • Herrero, B., J. M. Vieites, and M. Espiñeira. 2012. Fast real-time PCR for the detection of crustacean allergen in foods. Journal of Agricultural and Food Chemistry 60:1893–97. doi:10.1021/jf2043532.
  • Hodgson, E., and J. I. Spicer. 2001. Subunit compositions of crustacean haemocyanins are species-specific: evidence from non-decapod species. Comp. Biochem. Physiol. Mol. Integr. Physiol. 128:873–88. doi:10.1016/S1095-6433(00)00346-9.
  • Hu, G., Y. Zheng, Z. Liu, Y. Deng, and Y. Zhao. 2016. Structure and IgE-binding properties of α-casein treated by high hydrostatic pressure, UV-C, and far-IR radiations. Food Chemistry 204:46–55. doi:10.1016/j.foodchem.2016.02.113.
  • Hu, Z. H., and D. D. Xie. 2013. A high pressure combined enzyme preparation method of the allergen in a method for lobster method for preparing low-allergen brine shrimp by combination of high pressure and enzyme method. Chinese Patent 201110276942.9.
  • Huang, H. W., C. P. Hsu, B. B. Yang, and C. Y. Wang. 2014. Potential utility of high pressure processing to address the risk of food allergen concerns. Comprehensive Reviews in Food Science and Food Safety 13 (1):78–90. doi:10.1111/1541-4337.12045.
  • Huang, Y. Y., G. M. Liu, Q. F. Cai, W. Y. Weng, S. J. Maleki, W. J. Su, and M. J. Cao. 2010. Stability of major allergen tropomyosin and other food proteins of mud crab (Scylla serrata) by in vitro gastrointestinal digestion. Food and Chemical Toxicology 48 (5):1196–201. doi:10.1016/j.fct.2010.02.010.
  • Iwan, M., Y. M. Vissers, E. Fiedorowicz, H. Kostyra, E. Kostyra, H. F. Savelkoul, and H. J. Wichers. 2011. Impact of Maillard reaction on immunoreactivity and allergenicity of the hazelnut allergen Cor a 11. Journal of Agricultural and Food Chemistry 59 (13):7163–71. doi:10.1021/jf2007375.
  • Jeebhay, M. F., and A. L. Lopata. 2012. Occupational allergies in seafood-processing workers. Advances in Food and Nutrition Research 66:47–73. doi:10.1016/B978-0-12-394597-6.00002-1.
  • Jiménez-Saiz, R., S. Benedé, E. Molina, and I. López-Expósito. 2015. Effect of processing technologies on the allergenicity of food products. Critical Reviews in Food Science and Nutrition 55 (13):1902–17. doi:10.1080/10408398.2012.736435.
  • Jin, Y., Y. Deng, B. Qian, Y. Zhang, Z. Liu, and Y. Zhao. 2015. Allergenic response to squid (Todarodes pacificus) tropomyosin Tod p1 structure modifications induced by high hydrostatic pressure. Food and Chemical Toxicology 76:86–93. doi:10.1016/j.fct.2014.12.002.
  • Júnior, B. R. d. C. L., A. A. L. Tribst, and M. Cristianini. 2017. Effect of high-pressure technologies on enzymes applied in food processing. In Enzyme Inhibitors and Activators, chapter 3, ed. M., Senturk, 49–72. Rijeka: InTech.
  • Junqueira-Gonçalves, M. P., M. J. Galotto, X. Valenzuela, C. M. Dinten, P. Aguirre, and J. Miltz. 2011. Perception and view of consumers on food irradiation and the Radura symbol. Radiation Physics and Chemistry 80 (1):119–22. doi:10.1016/j.radphyschem.2010.08.001.
  • Kalyanasundaram, A., and T. C. Santiago. 2015. Identification and characterization of new allergen troponin C (Pen m 6.0101) from Indian black tiger shrimp Penaeus monodon. European Food Research and Technology 240 (3):509–15. doi:10.1007/s00217-014-2349-y.
  • Kamath, S. D., A. M. A. Rahman, T. Komoda, and A. L. Lopata. 2013. Impact of heat processing on the detection of the major shellfish allergen tropomyosin in crustaceans and molluscs using specific monoclonal antibodies. Food Chemistry 141:4031–39. doi:10.1016/j.foodchem.2013.06.105.
  • Kamath, S. D., A. M. A. Rahman, A. Voskamp, T. Komoda, J. M. Rolland, R. E. O'hehir, and A. L. Lopata. 2014. Effect of heat processing on antibody reactivity to allergen variants and fragments of black tiger prawn: A comprehensive allergenomic approach. Molecular Nutrition & Food Research 58 (5):1144–55. doi:10.1002/mnfr.201300584.
  • Kasera, R., A. B. Singh, S. Lavasa, K. N. Prasad, and N. Arora. 2015. Enzymatic hydrolysis: a method in alleviating legume allergenicity. Food and Chemical Toxicology 76:54–60. doi:10.1016/j.fct.2014.11.023.
  • Kaur, B. P., P. S. Rao, and P. K. Nema. 2016. Effect of hydrostatic pressure and holding time on physicochemical quality and microbial inactivation kinetics of black tiger shrimp (Penaeus monodon). Innovative Food Science and Emerging Technologies 33:47–55. doi:10.1016/j.ifset.2015.12.002.
  • Kebede, G., A. Simachew, H. Disassa, T. Kabeta, and T. Zenebe. 2015. Review on radiation as a means of food preservation and its challenge. Academy Journal of Nutrition 4 (2):77–83.
  • Khanaruksombat, S., C. Srisomsap, D. Chokchaichamnankit, P. Punyarit, and P. Phiriyangkul. 2014. Identification of a novel allergen from muscle and various organs in banana shrimp (Fenneropenaeus merguiensis). Annals of Allergy, Asthma &Amp; Immunology 113:301–306. doi:10.1016/j.anai.2014.06.002.
  • Khora, S. S. 2016. Seafood-associated shellfish allergy: a comprehensive review. Immunological Investigations 45 (6):504–30. doi:10.1080/08820139.2016.1180301.
  • Knorr, D., V. Heinz, and R. Buckow. 2006. High pressure application for food biopolymers. Biochim. Biophys. Acta – Prot. Proteomics. 1764 (3):619–31. doi:10.1016/j.bbapap.2006.01.017.
  • Kobernick, A. K., and A. W. Burks. 2016. Active treatment for food allergy. Allergology International. 65 (4):388–95. doi:10.1016/j.alit.2016.08.002.
  • Konteles, S., V. J. Sinanoglou, A. Batrinou, and K. Sflomos. 2009. Effects of gamma-irradiation on Listeria monocytogenes population, colour, texture and sensory properties of Feta cheese during cold storage. Food Microbiology 26 (2):157–65. doi:10.1016/j.fm.2008.10.006.
  • Korte, R., J. M. Monneuse, E. Gemrot, I. Metton, H. U. Humpf, and J. Brockmeyer. 2016. New high-performance liquid chromatography coupled mass spectrometry method for the detection of lobster and shrimp allergens in food samples via multiple reaction monitoring and multiple reaction monitoring cubed. Journal of Agricultural and Food Chemistry 64 (31):6219–27. doi:10.1021/acs.jafc.6b02620.
  • Kramer, B., J. Wunderlich, and P. Muranyi. 2016. Recent findings in pulsed light disinfection. Journal of Applied Microbiology 122 (4):830–56. doi:10.1111/jam.13389.
  • Kume, T., M. Furuta, S. Todoriki, N. Uenoyama, and Y. Kobayashi. 2009. Status of food irradiation in the world. Radiation Physics and Chemistry 78 (3):222–226.
  • Larsen, R., K. E. Eilertsen, and E. O. Elvevoll. 2011. Health benefits of marine foods and ingredients. Biotechnology Advances 29:508–18. doi:10.1016/j.biotechadv.2011.05.017.
  • Lasekan, A. O., and B. Nayak. 2016. Effects of buffer additives and thermal processing methods on the solubility of shrimp (Penaeus monodon) proteins and the immunoreactivity of its major allergen. Food Chemistry 200:146–53. doi:10.1016/j.foodchem.2016.01.015.
  • Lasekan, A., H. Cao, S. Maleki, and B. B. Nayak. 2017. Shrimp tropomyosin retains antibody reactivity after exposure to acidic condition. Journal of the Science of Food and Agriculture 97 (11):3623–30. doi:10.1002/jsfa.8221.
  • Lee, A. J., I. Gerez, L. P. Shek, and B. W. Lee. 2012. Shellfish allergy – an Asia-Pacific perspective. Asian Pacific Journal of Allergy and Immunology 30:3–10.
  • Lee, P. W., and S. L. Taylor. 2011. Fish, crustaceans, and mollusks. In Food Allergens Analysis Instrumentation and Methods, ed. A. J., Hengel, and L. M. L., Nollet, 117–205. Boca Raton, FL: Taylor and Francis Group, LLC.
  • Lepski, S., and J. Brockmeyer. 2013. Impact of dietary factors and food processing on food allergy. Molecular Nutrition &Amp; Food Research 57:145–52. doi:10.1002/mnfr.201200472.
  • Leung, N. Y. H., C. Y. Y. Wai, S. Shu, J. Wang, T. P. Kenny, K. H. Chu, and P. S. C. Leung. 2014. Current immunological and molecular biological perspectives on seafood allergy: a comprehensive review. Clinical Reviews in Allergy &Amp; Immunology 46 (3):180–97. doi:10.1007/s12016-012-8336-9.
  • Leung, P. S., K. H. Chu, W. K. Chow, A. Ansari, C. I. Bandea, H. S. Kwan, S. M. Nagy, and M. E. Gershwin. 1994. Cloning, expression, and primary structure of Metapenaeus ensis tropomyosin, the major heat stable shrimp allergen. The Journal of allergy and clinical immunology 94:882–90. doi:10.1016/0091-6749(94)90156-2.
  • Li, H., J. Yu, M. Ahmedna, and I. Goktepe. 2013. Reduction of major peanut allergens Ara h 1 and Ara h 2, in roasted peanuts by ultrasound assisted enzymatic treatment. Food Chemistry 141:762–68. doi:10.1016/j.foodchem.2013.03.049.
  • Li, X. Y., Z. Li, H. Lin, and H. Samee. 2011. Effect of power ultrasound on the immunoactivity and texture changes of shrimp (Penaeus vannamei). Czech Journal of Food Science 29:508–14. doi:10.17221/242/2009-CJFS.
  • Li, Z., H. Lin, L. Cao, and K. Jameel. 2006. Effect of high intensity ultrasound on the allergenicity of shrimp. Journal of Zhejiang University Science 7:251–56. doi:10.1631/jzus.2006.B0251.
  • Li, Z., H. Lin, L. Cao, and K. Jamil. 2007. Impact of irradiation and thermal processing on the immunoreactivity of shrimp (Penaeus vannamei) proteins. Journal of the Science of Food and Agriculture 87 (6):951–56. doi:10.1002/jsfa.2746.
  • Lin, H., Z. Li, H. Lin, Y. Song, L. Lv, and Z. Hao. 2015. Effect of pH shifts on IgE binding capacity and conformational structure of tropomyosin from short-neck clam (Ruditapes philippinarum). Food Chemistry 188:248–55. doi:10.1016/j.foodchem.2015.05.007.
  • Liu, G. M., Y. Y. Huang, Q. F. Cai, W. Y. Weng, W. J. Su, and M. J. Cao. 2011. Comparative study of in vitro digestibility of major allergen, tropomyosin and other proteins between Grass prawn (Penaeus monodon) and Pacific white shrimp (Litopenaeus vannamei). Journal of the Science of Food and Agriculture 91:163–70. doi:10.1002/jsfa.4167.
  • Liu, G., H. Cheng, J. B. Nesbit, W. Su, M. Cao, and S. J. Maleki. 2010. Effects of boiling on the IgE-binding properties of tropomyosin of shrimp (Litopenaeus vannamei). Journal of Food Science 75:T1–T5. doi:10.1111/j.1750-3841.2009.01391.x.
  • Liu, G., M. Hu, L. C. Sun, X. Han, Q. Liu, M. Alcocer, D. Fei, M. J. Cao, and G. M. Liu. 2017b. Allergenicity and oral tolerance of enzymatic cross-linked tropomyosin evaluated using cell and mouse models. Journal of Agricultural and Food Chemistry 65 (10):2205–13. doi:10.1021/acs.jafc.6b05816.
  • Liu, R., and W. Xue. 2010. High-pressure treatment with silver carp (Hypophthalmichthys molitrix) protein and its allergic analysis. High Press. Res. 30:438–42. doi:10.1080/08957959.2010.507955.
  • Liu, Y., Z. Li, T. Pavase, Z. Li, Y. Liu, and N. Wang. 2017a. Evaluation of electron beam irradiation to reduce the IgE binding capacity of frozen shrimp tropomyosin. Food and Agricultural Immunology 28 (2):189–201. doi:10.1080/09540105.2016.1251394.
  • Liu, Z., L. Xia, Y. Wu, Q. Xia, J. Chen, and K. H. Roux. 2009. Identification and characterization of an arginine kinase as a major allergen from silkworm (Bombyx mori) larvae. International Archives of Allergy and Immunology 150:8–14. doi:10.1159/000210375.
  • Long, F., X. Yang, R. Wang, X. Hu, and F. Chen. 2015. Effects of combined high pressure and thermal treatments on the allergenic potential of shrimp (Litopenaeus vannamei) tropomyosin in a mouse model of allergy. Innovative Food Science and Emerging Technologies 29:119–24. doi:10.1016/j.ifset.2015.03.002.
  • Lopata, A. L., and M. F. Jeebhay. 2013. Airborne seafood allergens as a cause of occupational allergy and asthma. Current Allergy and Asthma Reports 13 (3):288–97. doi:10.1007/s11882-013-0347-y.
  • Lopata, A. L., J. Kleine-Tebbe, and S. D. Kamath. 2016. Allergens and molecular diagnostics of shellfish allergy. Allergol. J. Int. 25 (7):210–18. doi:10.1007/s40629-016-0124-2.
  • Lopata, A. L., R. E. O'hehir, and S. B. Lehrer. 2010. Shellfish allergy. Clinical & Experimental Allergy 40 (6):850–58. doi:10.1111/j.1365-2222.2010.03513.x.
  • Lu, X., H. Lu, L. Guo, Z. Zhang, X. Zhao, M. Zhong, S. Li, and Y. Zhang. 2015. Cloning and characterization of a novel hemocyanin variant LvHMCV4 from shrimp Litopenaeus vannamei. Fish Shellfish Immunol. 46:398–405. doi:10.1016/j.fsi.2015.06.022.
  • Luo, C., C. Hu, J. Gao, X. Li, Z. Wu, A. Yang, and H. Chen. 2013. A potential practical approach to reduce Ara h 6 allergenicity by gamma irradiation. Food Chemistry 136:1141–47. doi:10.1016/j.foodchem.2012.09.091.
  • Lv, L., H. Lin, Z. Li, I. Ahmed, and G. Chen. 2017b. Determining the effect of malondialdehyde on the IgE‐binding capacity of shrimp tropomyosin upon in vitro digestion. Journal of the Science of Food and Agriculture 97 (13):4588–94. doi:10.1002/jsfa.8328.
  • Lv, L., H. Lin, Z. Li, J. Wang, I. Ahmed, and H. Chen. 2017a. Changes of structure and IgE binding capacity of shrimp (Metapenaeus ensis) tropomyosin followed by acrolein treatment. Food Funct. 8 (3):1028–36. doi:10.1039/C6FO01479H.
  • MacGinnite, A. 2017. Update on potential therapies for IgE-mediated food allergy. Curr. Allergy Asth. Rep. 17 (1):4. doi:10.1007/s11882-017-0671-8.
  • Mäde, D., and D. Rohmberger. 2017. Development of sensitive and specific real-time PCR systems for the detection of crustaceans in food. European Food Research and Technology 243:2105–13. doi:10.1007/s00217-017-2911-5.
  • Madsen, C. B., S. Hattersley, K. J. Allen, K. Beyer, C. H. Chan, S. B. Godefroy, R. Hodgson, E. N. C. Mills, A. Muñoz‐Furlong, S. Schnadt, and R. Ward. 2012. Can we define a tolerable level of risk in food allergy? Report from a EuroPrevall/UK Food Standards Agency workshop. Clinical & Experimental Allergy 42 (1):30–37. doi:10.1111/j.1365-2222.2011.03868.x.
  • Manzocco, L. 2015. Photo-induced modification of food protein structure and functionality. Food Engineering Reviews 7 (3):346–56. doi:10.1007/s12393-015-9110-6.
  • Mawson, R., M. Gamage, M. S. Terefe, and K. Knoerzer. 2011. Ultrasound in enzyme activation and inactivation. In Ultrasound Technologies for Food and Bioprocessing, H., Feng, G. V., Barbosa-Canovas, and J., Weiss, 369–404. USA: Springer.
  • Meinlschmidt, P., V. Brode, R. Sevenich, E. Ueberham, U. Schweiggert-Weisz, J. Lehmann, C. Rauh, D. Knorr, and P. Eisner. 2017. High pressure processing assisted enzymatic hydrolysis–An innovative approach for the reduction of soy immunoreactivity. Innovative Food Science and Emerging Technologies 40:58–67. doi:10.1016/j.ifset.2016.06.022.
  • Meinlschmidt, P., E. Ueberham, J. Lehmann, K. Reineke, O. Schlüter, U. Schweiggert-Weisz, and P. Eisner. 2016. The effects of pulsed ultraviolet light, cold atmospheric pressure plasma, and gamma-irradiation on the immunoreactivity of soy protein isolate. Innovative Food Science and Emerging Technologies 38:374–83. doi:10.1016/j.ifset.2016.06.007.
  • Mejrhit, N., O. Azdad, A. Chda, M. El Kabbaoui, A. Bousfiha, R. Bencheikh, A. Tazi, and L. Aarab. 2017. Evaluation of the sensitivity of Moroccans to shrimp tropomyosin and effect of heating and enzymatic treatments. Food and Agricultural Immunology 28 (6):1–12.
  • Misnan, R., S. Murad, M. Arip, N. Abdullah, and J. Mohamed. 2005. Characterization of immunoglobulin E-binding proteins (IgE) of Scomberomorus commerson Lacepede. J. Sains. Kesihatan Malaysia. 3:79–87.
  • Mita, H., A. Koketsu, S. Ishizaki, and K. Shiomi. 2013. Molecular cloning and functional expression of allergenic sarcoplasmic calcium binding proteins from Penaeus shrimps. Journal of the Science of Food and Agriculture 93:1737–42. doi:10.1002/jsfa.5961.
  • Monaci, L., and A. Visconti. 2009. Mass spectrometry-based proteomics methods for analysis of food allergens. Trac Trends in Analytical Chemistry 28 (5):581–91. doi:10.1016/j.trac.2009.02.013.
  • Monaci, L., and A. Visconti. 2010. Immunochemical and DNA-based methods in food allergen analysis and quality assurance perspectives. Trends in Food Science &Amp; Technology 21 (6):272–83. doi:10.1016/j.tifs.2010.02.003.
  • Mostafavi, H. A., S. M. Mirmajlessi, and H. Fathollahi. 2012. The potential of food irradiation: benefits and limitations. In Trends in Vital Food and Control Engineering, chapter 2, ed. A. A., Eissa, 43–68. Rijeka: InTech.
  • Motoyama, K., Y. Suma, S. Ishizaki, Y. Nagashima, and K. Shiomi. 2007. Molecular cloning of tropomyosins identified as allergens in six species of crustaceans. Journal of Agricultural and Food Chemistry 55 (3):985–91. doi:10.1021/jf062798x.
  • Muraro, A., T. Werfel, K. Hoffmann-Sommergruber, G. Roberts, K. Beyer, C. Bindslev-Jensen, V. Cardona, A. Dubois, G. Dutoit, P. Eigenmann, and M. Fernandez Rivas. 2014. EAACI Food Allergy and Anaphylaxis Guidelines: diagnosis and management of food allergy. Allergy 69 (8):1008–25. doi:10.1111/all.12429.
  • Nagai, H., T. Minatani, and K. Goto. 2015. Development of a method for crustacean allergens using liquid chromatography/tandem mass spectrometry. Journal of Aoac International 98 (5):1355–65. doi:10.5740/jaoacint.14-248.
  • Nakamura, A., K. Watanabe, T. Ojima, D. Ahn, and H. Saeki. 2005. Effect of maillard reaction on allergenicity of scallop tropomyosin. Journal of Agricultural and Food Chemistry 53:7559–7564.
  • Nakamura, A., F. Sasaki, K. Watanabe, T. Ojima, D. Ahn, and H. Saeki. 2006. Changes in allergenicity and digestibility of squid tropomyosin during the maillard reaction with ribose. Journal of Agricultural and Food Chemistry 54:9529–9534.
  • Nayak, B., Z. Li, I. Ahmed, and H. Lin. 2017. Ultrasound: advances for food processing and preservation. In Removal of Allergens in some Food Products using Ultrasound, ed. D., Bermudez-Aguirre, 267–92. Elsevier, USA: Academic Press.
  • Nowacka, M., A. Fijalkowska, A. Wiktor, M. Dadan, U. Tylewicz, M. Dalla Rosa, and D. Witrowa-Rajchert. 2018. Influence of power ultrasound on the main quality properties and cell viability of osmotic dehydrated cranberries. Ultrason 83:33–41. doi:10.1016/j.ultras.2017.07.014.
  • Nowacka, M., U. Tylewicz, L. Laghi, M. Dalla Rosa, and D. Witrowa-Rajchert. 2014. Effect of ultrasound treatment on the water state in kiwifruit during osmotic dehydration. Food Chemistry 144:18–25. doi:10.1016/j.foodchem.2013.05.129.
  • Ortea, I., B. Cañas, and J. M. Gallardo. 2011. Selected tandem mass spectrometry ion monitoring for the fast identification of seafood species. Journal of Chromatography A 1218 (28):4445–51. doi:10.1016/j.chroma.2011.05.032.
  • Pal, M., A. Shimelis, W. Mamo, A. M. Barot, S. V. Pinto, and J. P. Prajapati. 2017. Hurdle technology: a novel approach for food preservation. Bev. Food World. 44 (1):20–26.
  • Pascal, M., G. Grishina, A. C. Yang, S. Sánchez-García, J. Lin, D. Towle, M. D. Ibañez, J. Sastre, H. A. Sampson, and R. Ayuso. 2015. Molecular diagnosis of shrimp allergy: efficiency of several allergens to predict clinical reactivity. J. Allergy Clin. Immunol. Prac. 3 (4):521–29. doi:10.1016/j.jaip.2015.02.001.
  • Pascoal, A., J. Barros-Velázquez, I. Ortea, A. Cepeda, J. M. Gallardo, and P. Calo-Mata. 2011. Molecular identification of the black tiger shrimp (Penaeus monodon), the white leg shrimp (Litopenaeus vannamei) and the Indian white shrimp (Fenneropenaeus indicus) by PCR targeted to the 16S rRNA mtDNA. Food Chemistry 125:1457–61. doi:10.1016/j.foodchem.2010.10.053.
  • Pedrosa, M., T. Boyano-Martínez, C. García-Ara, and S. Quirce. 2015. Shellfish allergy: a comprehensive review. Clinical Reviews in Allergy &Amp; Immunology 49 (2):203–16. doi:10.1007/s12016-014-8429-8.
  • Pellicer, J. A., and V. M. Gómez-López. 2017. Pulsed light inactivation of horseradish peroxidase and associated structural changes. Food Chemistry 237:632–37. doi:10.1016/j.foodchem.2017.05.151.
  • Perez-Macalalag, E., M. Sumpaico, and B. Agbayani. 2007. Shrimp allergy: effect of vinegar soaking on allergenic capacity. World Allergy Organ. J. S317. doi:10.1097/01.WOX.0000301535.72234.d6.
  • Piboonpocanun, S., O. Jirapongsananuruk, T. Tipayanon, S. Boonchoo, and R. E. Goodman. 2011. Identification of hemocyanin as a novel noncross-reactive allergen from the giant freshwater shrimp Macrobrachium rosenbergii. Mol. Nutr. Food Res. 55:1492–98. doi:10.1002/mnfr.201000602.
  • Pottier, L., G. Villamonte, and M. de Lamballerie. 2017. Applications of high pressure for healthier foods. Curr. Opin. Food Sci. 16:21–27. doi:10.1016/j.cofs.2017.06.009.
  • Prado, M., I. Ortea, S. Vial, J. Rivas, P. Calo-Mata, and J. Barros-Velazquez. 2016. Advanced DNA- and protein-based methods for the detection and investigation of food allergens. Critical Reviews in Food Science and Nutrition 56:2511–42. doi:10.1080/10408398.2013.873767.
  • Radosavljevic, J., E. Nordlund, L. Mihajlovic, M. Krstic, T. Bohn, J. Buchert, T.C. Velickovic, and J. Smit. 2014. Sensitizing potential of enzymatically cross‐linked peanut proteins in a mouse model of peanut allergy. Molecular Nutrition &Amp; Food Research 58 (3):635–46. doi:10.1002/mnfr.201300403.
  • Rahaman, T., T. Vasiljevic, and L. Ramchandran. 2016. Effect of processing on conformational changes of food proteins related to allergenicity. Trends in Food Science &Amp; Technology 49:24–34. doi:10.1016/j.tifs.2016.01.001.
  • Rahaman, T., T. Vasiljevic, and L. Ramchandran. 2015. Conformational changes of β lactoglobulin induced by shear, heat, and pH – Effects on antigenicity. Journal of Dairy Science 98 (7):4255–65. doi:10.3168/jds.2014-9010.
  • Rahman, A. M. A., R. J. Helleur, M. F. Jeebhay, and A. L. Lopata. 2012. Characterization of seafood proteins causing allergic diseases. In Allergic Diseases – Highlights in the Clinic, Mechanisms and Treatment, chapter 5, ed. C., Pereira, 107–40. Rijeka: InTech.
  • Rahman, A. M. A., S. D. Kamath, S. Gagné, A. L. Lopata, and R. Helleur. 2013. Comprehensive proteomics approach in characterizing and quantifying allergenic proteins from northern shrimp: toward better occupational asthma prevention. Journal of Proteome Research 12 (2):647–56. doi:10.1021/pr300755p.
  • Rahman, A. M. A., S. D. Kamath, A. L. Lopata, J. J. Robinson, and R. J. Helleur. 2011. Biomolecular characterization of allergenic proteins in snow crab (Chionoecetes opilio) and de novo sequencing of the second allergen arginine kinase using tandem mass spectrometry. J. Proteomics. 74 (2):231–41. doi:10.1016/j.jprot.2010.10.010.
  • Rahman, A. M. A., S. Kamath, A. L. Lopata, and R. J. Helleur. 2010. Analysis of the allergenic proteins in black tiger prawn (Penaeus monodon) and characterization of the major allergen tropomyosin using mass spectrometry. Rapid Communications in Mass Spectrometry: Rcm 24 (16):2462–70. doi:10.1002/rcm.4664.
  • Reese, G., R. Ayuso, and S. B. Lehrer. 1999. Tropomyosin: an invertebrate pan allergen. International Archives of Allergy and Immunology 119 (4):247–58. doi:10.1159/000024201.
  • Reese, G., B. J. Jeoung, C. B. Daul, and S. B. Lehrer. 1997. Characterization of recombinant shrimp allergen Pen a 1 (tropomyosin). International Archives of Allergy and Immunology 113:240–42. doi:10.1159/000237558.
  • Regulation (EU) No 1169/2011 of 25. October 2011. On the provision of food information to consumers, amending Regulations (EC) No 1924/2006 and (EC) No 1925/2006 of the European Parliament and of the Council, and repealing Commission Directive 87/250/EEC, Council Directive 90/496/EEC, Commission Directive 1999/10/EC, Directive 2000/13/EC of the European Parliament and of the Council, Commission Directives 2002/67/EC and 2008/5/EC and Commission Regulation (EC) No 608/2004. Off. J. Eur. Union L304:18–63.
  • Rodríguez, Ó., V. Eim, C. Rosselló, A. Femenia, J. A. Cárcel, and S. Simal. 2018. Application of power ultrasound on the convective drying of fruits and vegetables: effects on quality. Journal of the Science of Food and Agriculture 98 (5):1660–73. doi:10.1002/jsfa.8673.
  • Ross, M. P., M. Ferguson, D. Street, K. Klontz, T. Schroeder, and S. Luccioli. 2008. Analysis of food-allergic and anaphylactic events in the National Electronic Injury Surveillance System. Journal of Allergy and Clinical Immunology 121 (1):166–71. doi:10.1016/j.jaci.2007.10.012.
  • Seiki, K., H. Oda, H. Yoshioka, S. Sakai, A. Urisu, H. Akiyama, and Y. Ohno. 2007. A reliable and sensitive immunoassay for the determination of crustacean protein in processed foods. Journal of Agricultural and Food Chemistry 55 (23):9345–50. doi:10.1021/jf0715471.
  • Shanti, K. N., B. M. Martin, S. Nagpal, D. D. Metcalfe, and P. V. Subba Rao. 1993. Identification of tropomyosin as the major shrimp allergen and characterization of its IgE binding epitopes. Journal of Immunology 151:5354–63.
  • Sharp, M. F., and A. L. Lopata. 2014. Fish allergy: in review. Clinical Reviews in Allergy &Amp; Immunology 46:258–71. doi:10.1007/s12016-013-8363-1.
  • Shek, L. P. C., E. A. Cabrera-Morales, S. E. Soh, I. Gerez, P. Zhing, F. C. Yi, S. Ma, and B. W. Lee. 2010. A population-based questionnaire survey on the prevalence of peanut, tree nut, and shellfish allergy in 2 Asian populations. Journal of Allergy and Clinical Immunology 126:324–31. doi:10.1016/j.jaci.2010.06.003.
  • Shen, H. W., M. J. Cao, Q. F. Cai, M. M. Ruan, H. Y. Mao, W. J. Su, and G. M. Liu. 2012. Purification, cloning, and immunological characterization of arginine kinase, a novel allergen of Octopus fangsiao. J. Agric. Food Chemistry 60 (9):2190–99. doi:10.1021/jf203779w.
  • Shimakura, K., Y. Tonomura, Y. Hamada, Y. Nagashima, and K. Shiomi. 2005. Allergenicity of crustacean extractives and its reduction by protease digestion. Food Chemistry 91 (2):247–53. doi:10.1016/j.foodchem.2003.11.010.
  • Shiomi, K., Y. Sato, S. Hamamoto, H. Mita, and K. Shimakura. 2008. Sarcoplasmic calcium binding protein: identification as a new allergen of the black tiger shrimp Penaeus monodon. International Archives of Allergy and Immunology 146:91–98. doi:10.1159/000113512.
  • Shriver, S. K., and W. W. Yang. 2011. Thermal and non thermal methods for food allergen control. Food Engineering Reviews 3:26–43. doi:10.1007/s12393-011-9033-9.
  • Shriver, S., W. Yang, S. Y. Chung, and S. Percival. 2011. Pulsed ultraviolet light reduces immunoglobulin E binding to Atlantic white shrimp (Litopenaeus setiferus) extract. Int. J. Environ. Res. Public Health. 8 (7):2569–83. doi:10.3390/ijerph8072569.
  • Sicherer, S. H., and H. A. Sampson. 2010. Food allergy. Journal of Allergy and Clinical Immunology 125:116–25. doi:10.1016/j.jaci.2009.08.028.
  • Sicherer, S. H., and H. A. Sampson. 2018. Food allergy: A review and update on epidemiology, pathogenesis, diagnosis, prevention, and management. Journal of Allergy and Clinical Immunology 141 (1):41–58. doi:10.1016/j.jaci.2017.11.003.
  • Sicherer, S. H., A. Muñoz-Furlong, and H. A. Sampson. 2004. Prevalence of seafood allergy in the United States determined by a random telephone survey. Journal of Allergy and Clinical Immunology 114 (1):159–65. doi:10.1016/j.jaci.2004.04.018.
  • Singh, S., and R. Shalini. 2016. Effect of hurdle technology in food preservation: a review. Critical Reviews in Food Science and Nutrition 56 (4):641–49. doi:10.1080/10408398.2012.761594.
  • Sockalingam, K., R. Misnan, and Z. H. M. Yadzir. 2017. The effects of thermal treatments on protein profiles of Macrobrachium rosenbergii (giant river prawn). In AIP Conference Proceedings, Vol. 1847 (1):090001. AIP Publishing.
  • Sookrung, N., W. Chaicumpa, A. Tungtrongchitr, P. Vichyanond, C. Bunnag, P. Ramasoota, P. Tongtawe, Y. Sakolvaree, and P. Tapchaisri. 2006. Periplaneta Americana arginine kinase as a major cockroach allergen among Thai patients with major cockroach allergies. Environmental Health Perspectives 114 (6):875–80. doi:10.1289/ehp.8650.
  • Srinroch, C., C. Srisomsap, D. Chokchaichamnankit, P. Punyarit, and P. Phiriyangkul. 2015. Identification of novel allergen in edible insect, Gryllus bimaculatus and its cross-reactivity with Macrobrachium spp, allergens. Food Chemistry 184:160–66. doi:10.1016/j.foodchem.2015.03.094.
  • Stanić-Vučinić, D., and T. Ć. Veličković. 2012. Enzymatic and chemical modifications of food allergens. In Allergic Diseases – Highlights in the Clinic, Mechanisms and Treatment, chapter 4, ed. C., Pereira, 83–106. Rijeka: InTech.
  • Suzuki, M., Y. Kobayashi, Y. Hiraki, H. Nakata, and K. Shiomi. 2011. Paramyosin of the disc abalone Haliotis discus discus: identification as a new allergen and cross-reactivity with tropomyosin. Food Chemistry 124:921–26. doi:10.1016/j.foodchem.2010.07.020.
  • Taylor, S. L., J. L. Baumert, A. G. Kruizinga, B. C. Remington, R. W. R. Crevel, S. Brooke Taylor, K. J. Allen, and G. Houben. 2014. Establishment of reference doses for residues of allergenic foods: report of the VITAL expert panel. Food and Chemical Toxicology 63:9–17. doi:10.1016/j.fct.2013.10.032.
  • Teodorowicz, M., J. van Neerven, and H. Savelkoul. 2017. Food processing: the influence of the Maillard reaction on immunogenicity and allergenicity of food proteins. Nutr. 9 (8):835.
  • Toda, M., M. Heilmann, A. Ilchmann, and S. Vieths. 2014. The Maillard reaction and food allergies: is there a link? Clinical Chemistry and Laboratory Medicine 52:61–67. doi:10.1515/cclm-2012-0830.
  • Tsabouri, S., M. Triga, M. Makris, D. Kalogeromitros, M. K. Church, and K. N. Priftis. 2012. Fish and shellfish allergy in children: review of a persistent food allergy. Pediatric Allergy and Immunology 23:608–15. doi:10.1111/j.1399-3038.2012.01275.x.
  • United States Nuclear Regulatory Commission. 2016. Backgrounder on commercial irradiator. Available at: https://www.nrc.gov/reading-rm/doc-collections/fact-sheets/commercial-irradiators.html/ Accessed on 10 August 2017.
  • Usui, M., A. Harada, T. Ishimaru, E. Sakumichi, F. Saratani, C. Sato-Minami, H. Azakami, T. Miyasaki, and K. I. Hanaoka. 2013. Contribution of structural reversibility to the heat stability of the tropomyosin shrimp allergen. Bioscience, Biotechnology, and Biochemistry 77 (5):948–53. doi:10.1271/bbb.120887.
  • Vanga, S. K., and V. Raghavan. 2016. Processing effects on tree nut allergens: a review. Critical Reviews in Food Science and Nutrition 57 (17):3794–806. doi:10.1080/10408398.2016.1175415.
  • Vanga, S. K., A. Singh, and V. Raghavan. 2017. Review of conventional and novel food processing methods on food allergens. Critical Reviews in Food Science and Nutrition 57 (10):2077–94. doi:10.1080/10408398.2015.1045965.
  • Verhoeckx, K. C. M., Y. M. Vissers, J. L. Baumert, R. Faludi, M. Feys, S. Flanagan, C. Herouet-Guicheney, T. Holzhauser, R. Shimojo, N. van der Bolt, H. Wichers, and I. Kimber. 2015. Food processing and allergenicity. Food and Chemical Toxicology 80:223–40. doi:10.1016/j.fct.2015.03.005.
  • Vierk, K. A., K. M. Koehler, S. B. Fein, and D. A. Street. 2007. Prevalence of self-reported food allergy in American adults and use of food labels. Journal of Allergy and Clinical Immunology 119 (6):1504–10. doi:10.1016/j.jaci.2007.03.011.
  • Wai, C. Y., N. Y. Leung, M. H. Ho, L. J. Gershwin, S. A. Shu, P. S. Leung, and K. H. Chu. 2014. Immunization with hypoallergens of shrimp allergen tropomyosin inhibits shrimp tropomyosin specific IgE reactivity. Plos One 9 (11):e111649. doi:10.1371/journal.pone.0111649.
  • Wang, B., Y. Zhang, C. Venkitasamy, B. Wu, Z. Pan, and H. Ma. 2017. Effect of pulsed light on activity and structural changes of horseradish peroxidase. Food Chemistry 234:20–25. doi:10.1016/j.foodchem.2017.04.149.
  • Wang, J., and H. A. Sampson. 2007. Food anaphylaxis. Clinical and Experimental Allergy 37 (5):651–60. doi:10.1111/j.1365-2222.2007.02682.x.
  • Werner, M. T., C. K. Fæste, and E. Egaas. 2007. Quantitative sandwich ELISA for the determination of tropomyosin from crustaceans in foods. Journal of Agricultural and Food Chemistry 55 (20):8025–32. doi:10.1021/jf070806j.
  • Wilwet, L., G. Jeyasekaran, R. J. Shakila, B. Sivaraman, and P. Padmavathy. 2018. A single enzyme PCR-RFLP protocol targeting 16S rRNA/tRNAval region to authenticate four commercially important shrimp species in India. Food Chemistry 239:369–76. doi:10.1016/j.foodchem.2017.06.132.
  • Woo, C. K., and S. M. Bahna. 2011. Not all shellfish “allergy” is allergy! Clinical and Translational Allergy 1:1–7. doi:10.1186/2045-7022-1-3.
  • Wood, R. A. 2016. Food allergen immunotherapy: Current status and prospects for the future. Journal of Allergy and Clinical Immunology 137 (4):973–82. doi:10.1016/j.jaci.2016.01.001.
  • Wu, T. C., T. C. Tsai, C. F. Huang, F. Y. Chang, C. C. Lin, I. F. Huang, C. H. Chu, B. H. Lau, L. Wu, H. J. Peng, and R. B. Tang. 2012. Prevalence of food allergy in Taiwan: a questionnaire‐based survey. Internal Medicine Journal 42 (12):1310–15. doi:10.1111/j.1445-5994.2012.02820.x.
  • Yang, W. W., S. K. Shriver, S. Y. Chung, S. Percival, M. J. Correll, and T. M. Rababah. 2012. In vitro gastric and intestinal digestions of pulsed light-treated shrimp extracts. Applied Biochemistry and Biotechnology 166 (6):1409–22. doi:10.1007/s12010-011-9534-2.
  • Yang, X., J. Sun, J. Tao, Y. Ma, J. Wei, and F. Long. 2017. The allergenic potential of walnuts treated with high pressure and heat in a mouse model of allergy. Innovative Food Science and Emerging Technologies 39:165–70. doi:10.1016/j.ifset.2016.12.001.
  • Yao, C. L., C. G. Wua, J. H. Xiang, and B. Dong. 2005. Molecular cloning and response to laminarin stimulation of arginine kinase in haemolymph in Chinese shrimp. Fenneropenaeus chinensis. Fish Shellfish Immunol. 19:317–29. doi:10.1016/j.fsi.2005.01.006.
  • Yohannes, S., R. Buckow, R. O'Hehir, and A. Lopata. 2008. Effects of heat treatment and high pressure processing on the allergenicity of tropomyosin from prawns. Internal Medicine Journal 38:A168.
  • Yu, C. J., Y. F. Lin, B. L. Chiang, and L. P. Chow. 2003. Proteomics and immunological analysis of a novel shrimp allergen, Pen m 2. Journal of Immunology 170:445–53. doi:10.4049/jimmunol.170.1.445.
  • Yu, H. L., M. J. Cao, Q. F. Cai, W. Y. Weng, W. J. Su, and G. M. Liu. 2011. Effects of different processing methods on digestibility of Scylla paramamosain allergen (tropomyosin). Food and Chemical Toxicology 49 (4):791–98. doi:10.1016/j.fct.2010.11.046.
  • Yu, J. 2016. Methods for reducing allergenicity of peanuts and peanut derived products – their efficacy, feasibility and safety. Austin Food Sci. 1 (3):1012.
  • Yuan, F., L. Lv, Z. Li, N. Mi, H. Chen, and H. Lin. 2017. Effect of transglutaminase-catalyzed glycosylation on the allergenicity and conformational structure of shrimp (Metapenaeus ensis) tropomyosin. Food Chemistry 219:215–22. doi:10.1016/j.foodchem.2016.09.139.
  • Zagon, J., J. Schmidt, A. S. Schmidt, H. Broll, A. Lampen, T. Seidler, and A. Braeuning. 2017. A novel screening approach based on six real-time PCR systems for the detection of crustacean species in food. Food Control 79:27–34. doi:10.1016/j.foodcont.2017.03.019.
  • Zhang, H., Y. Lu, H. Ushio, and K. Shiomi. 2014. Development of sandwich ELISA for detection and quantification of invertebrate major allergen tropomyosin by a monoclonal antibody. Food Chemistry 150:151–57. doi:10.1016/j.foodchem.2013.10.154.
  • Zhang, Y., Y. Deng, and Y. Zhao. 2017. Structure-based modelling of hemocyanin allergenicity in squid and its response to high hydrostatic pressure. Scientific Reports 7:40021. doi:10.1038/srep40021.

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