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Review Article

A comprehensive review on glycation and its potential application to reduce food allergenicity

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References

  • Aalberse, R. C., and R. Crameri. 2011. IgE-binding epitopes: A reappraisal. Allergy 66 (10):1261–74. doi:10.1111/j.1398-9995.2011.02656.x.
  • Alessandri, C., D. Zennaro, E. Scala, R. Ferrara, M. L. Bernardi, M. Santoro, P. Palazzo, and A. Mari. 2012. Ovomucoid (Gal d 1) specific IgE detected by microarray system predict tolerability to boiled hen’s egg and an increased risk to progress to multiple environmental allergen sensitisation. Clinical and Experimental Allergy: Journal of the British Society for Allergy and Clinical Immunology 42 (3):441–50. doi:10.1111/j.1365-2222.2011.03915.x.
  • Ando, H., R. Movérare, Y. Kondo, I. Tsuge, A. Tanaka, M. P. Borres, and A. Urisu. 2008. Utility of ovomucoid-specific IgE concentrations in predicting symptomatic egg allergy. The Journal of Allergy and Clinical Immunology 122 (3):583–8. doi:10.1016/j.jaci.2008.06.016.
  • Ayuso, R., G. Grishina, L. Bardina, T. Carrillo, C. Blanco, M. D. Ibáñez, H. A. Sampson, and K. Beyer. 2008. Myosin light chain is a novel shrimp allergen, Lit v 3. The Journal of Allergy and Clinical Immunology 122 (4):795–802. doi:10.1016/j.jaci.2008.07.023.
  • Babiker, E. E., A. Hiroyuki, N. Matsudomi, H. Iwata, T. Ogawa, N. Bando, and A. Kato. 1998. Effect of polysaccharide conjugation or transglutaminase treatment on the allergenicity and functional properties of soy protein. Journal of Agricultural and Food Chemistry 46 (3):866–71. doi:10.1021/jf9705072.
  • Barre, A., G. Jacquet, C. Sordet, R. Culerrier, and P. Rougé. 2007. Homology modelling and conformational analysis of IgE-binding epitopes of Ara h 3 and other legumin allergens with a cupin fold from tree nuts. Molecular Immunology 44 (12):3243–55. doi:10.1016/j.molimm.2007.01.023.
  • Bauermeister, K., A. Wangorsch, L. P. Garoffo, A. Reuter, A. Conti, S. L. Taylor, J. Lidholm, A. M. Dewitt, E. Enrique, S. Vieths, et al. 2011. Generation of a comprehensive panel of crustacean allergens from the North Sea Shrimp Crangon crangon. Molecular Immunology 48 (15-16):1983–92. doi:10.1016/j.molimm.2011.06.216.
  • Becker, W. M., and U. Jappe. 2014. Peanut allergens. Chemical Immunology and Allergy 100:256–67. doi:10.1159/000359916.
  • Berin, M. C., and H. A. Sampson. 2013. Mucosal immunology of food allergy. Current Biology: CB 23 (9):R389–R400. doi:10.1016/j.cub.2013.02.043.
  • Beyer, K., G. Grishina, L. Bardina, A. Grishin, and H. A. Sampson. 2002. Identification of an 11S globulin as a major hazelnut food allergen in hazelnut-induced systemic reactions. The Journal of Allergy and Clinical Immunology 110 (3):517–23. doi:10.1067/mai.2002.127434.
  • Blanc, F., Y. M. Vissers, K. Adel-Patient, N. M. Rigby, A. R. Mackie, A. P. Gunning, N. K. Wellner, P. S. Skov, L. Przybylski-Nicaise, B. Ballmer-Weber, et al. 2011. Boiling peanut Ara h 1 results in the formation of aggregates with reduced allergenicity. Molecular Nutrition & Food Research 55 (12):1887–94. doi:10.1002/mnfr.201100251.
  • Bloom, K. A., F. R. Huang, R. Bencharitiwong, L. Bardina, A. Ross, H. A. Sampson, and A. Nowak-Węgrzyn. 2014. Effect of heat treatment on milk and egg proteins allergenicity. Pediatric Allergy and Immunology: Official Publication of the European Society of Pediatric Allergy and Immunology 25 (8):740–6. doi:10.1111/pai.12283.
  • Bogdanov, I. V., E. I. Finkina, D. N. Melnikova, R. H. Ziganshin, and T. V. Ovchinnikova. 2021. Investigation of sensitization potential of the soybean allergen Gly m 4 by using Caco-2/immune cells co-culture model. Nutrients 13 (6):2058. doi:10.3390/nu13062058.
  • Boonpiyathad, T., Z. C. Sözener, M. Akdis, and C. A. Akdis. 2020. The role of Treg cell subsets in allergic disease. Asian Pacific Journal of Allergy and Immunology 38 (3):139–49. doi:10.12932/AP-030220-0754.
  • Borad, S. G., A. Kumar, and A. K. Singh. 2017. Effect of processing on nutritive values of milk protein. Critical Reviews in Food Science and Nutrition 57 (17):3690–702. doi:10.1080/10408398.2016.1160361.
  • Bosman, G. P., S. Oliveira, P. J. Simons, J. Sastre Torano, G. W. Somsen, L. M. J. Knippels, R. Haselberg, R. J. Pieters, J. Garssen, and K. Knipping. 2021. Limited lactosylation of beta-lactoglobulin from cow’s milk exerts strong influence on antigenicity and degranulation of mast cells. Nutrients 13 (6):2041. doi:10.3390/nu13062041.
  • Briceno Noriega, D., H. E. Zenker, C. A. Croes, A. Ewaz, J. Ruinemans-Koerts, H. Savelkoul, R. van Neerven, and M. Teodorowicz. 2022. Receptor mediated effects of advanced glycation end products (AGEs) on innate and adaptative immunity: relevance for food allergy. Nutrients 14 (2):371. doi:10.3390/nu14020371.
  • Bu, G., N. Zhang, and F. Chen. 2015. The influence of glycosylation on the antigenicity, allergenicity, and structural properties of 11S-lactose conjugates. Food Research International (Ottawa, Ont.) 76 (Pt 3):511–7. doi:10.1016/j.foodres.2015.08.004.
  • Bu, G., T. Zhu, and F. Chen. 2017. The structural properties and antigenicity of soybean glycinin by glycation with xylose. Journal of the Science of Food and Agriculture 97 (7):2256–62. doi:10.1002/jsfa.8036.
  • Burks, A. W. 2008. Peanut allergy. Lancet (London, England) 371 (9623):1538–46. doi:10.1016/S0140-6736(08)60659-5.
  • Cabanillas, B., and N. Novak. 2019. Effects of daily food processing on allergenicity. Critical Reviews in Food Science and Nutrition 59 (1):31–42. doi:10.1080/10408398.2017.1356264.
  • Cabanillas, B., U. Jappe, and N. Novak. 2018. Allergy to peanut, soybean, and other legumes: recent advances in allergen characterization, stability to processing and IgE cross-reactivity. Molecular Nutrition & Food Research 62 (1): 1700446. doi:10.1002/mnfr.201700446.
  • Caubet, J. C., Y. Kondo, A. Urisu, and A. Nowak-Węgrzyn. 2011. Molecular diagnosis of egg allergy. Current Opinion in Allergy and Clinical Immunology 11 (3):210–5. doi:10.1097/ACI.0b013e3283464d1b.
  • Chen, H.-L., H.-Y. Mao, M.-J. Cao, Q.-F. Cai, W.-J. Su, Y.-X. Zhang, and G.-M. Liu. 2013. Purification, physicochemical and immunological characterization of arginine kinase, an allergen of crayfish (Procambarus clarkii). Food and Chemical Toxicology: An International Journal Published for the British Industrial Biological Research Association 62:475–84. doi:10.1016/j.fct.2013.09.014.
  • Chhabra, G. S., C. Liu, M. Su, M. Venkatachalam, K. H. Roux, and S. K. Sathe. 2017. Effects of the Maillard reaction on the immunoreactivity of amandin in food matrices. Journal of Food Science 82 (10):2495–503. doi:10.1111/1750-3841.13839.
  • Chu, D. K., A. Llop-Guevara, T. D. Walker, K. Flader, S. Goncharova, J. E. Boudreau, C. L. Moore, T. Seunghyun In, S. Waserman, A. J. Coyle, et al. 2013. IL-33, but not thymic stromal lymphopoietin or IL-25, is central to mite and peanut allergic sensitization. The Journal of Allergy and Clinical Immunology 131 (1):187–200. doi:10.1016/j.jaci.2012.08.002.
  • Cianferoni, A. 2016. Wheat allergy: Diagnosis and management. Journal of Asthma and Allergy 9:13–25. doi:10.2147/JAA.S81550.
  • Cianferoni, A. 2020. Non-IgE mediated food allergy. Current Pediatric Reviews 16 (2):95–105. doi:10.2174/1573396315666191031103714.
  • Claude, M., R. Lupi, G. Bouchaud, M. Bodinier, C. Brossard, and S. Denery-Papini. 2016. The thermal aggregation of ovalbumin as large particles decreases its allergenicity for egg allergic patients and in a murine model. Food Chemistry 203:136–44. doi:10.1016/j.foodchem.2016.02.054.
  • Comstock, S. S., S. J. Maleki, and S. S. Teuber. 2016. Boiling and frying peanuts decreases soluble peanut (Arachis hypogaea) allergens Ara h 1 and Ara h 2 but does not generate hypoallergenic peanuts. PLoS One 11 (6):e0157849. doi:10.1371/journal.pone.0157849.
  • Conneely, O. M. 2001. Antiinflammatory activities of lactoferrin. Journal of the American College of Nutrition 20 (5 Suppl):389S–97S. doi:10.1080/07315724.2001.10719173.
  • Costa, J., S. L. Bavaro, S. Benedé, A. Diaz-Perales, C. Bueno-Diaz, E. Gelencser, J. Klueber, C. Larré, D. Lozano-Ojalvo, R. Lupi, et al. 2022. Are physicochemical properties shaping the allergenic potency of plant allergens? Clinical Reviews in Allergy & Immunology 62 (1):37–63. doi:10.1007/s12016-020-08810-9.
  • Cucu, T., B. De Meulenaer, C. Bridts, B. Devreese, and D. Ebo. 2012. Impact of thermal processing and the Maillard reaction on the basophil activation of hazelnut allergic patients. Food and Chemical Toxicology: An International Journal Published for the British Industrial Biological Research Association 50 (5):1722–8. doi:10.1016/j.fct.2012.02.069.
  • Dang, T. D., R. L. Peters, J. J. Koplin, S. C. Dharmage, L. C. Gurrin, A. L. Ponsonby, D. J. Martino, M. Neeland, M. Tang, and K. J. Allen. 2019. Egg allergen specific IgE diversity predicts resolution of egg allergy in the population cohort HealthNuts. Allergy 74 (2):318–26. doi:10.1111/all.13572.
  • Davidson, E. A. 2023. Carbohydrate. Encyclopedia Britannica. https://www.britannica.com/science/carbohydrate
  • Davis, C. M., R. S. Gupta, O. N. Aktas, V. Diaz, S. D. Kamath, and A. L. Lopata. 2020. Clinical management of seafood allergy. The Journal of Allergy and Clinical Immunology. In Practice 8 (1):37–44. doi:10.1016/j.jaip.2019.10.019.
  • de Jongh, H. H., C. L. Robles, E. Timmerman, J. A. Nordlee, P. W. Lee, J. L. Baumert, R. G. Hamilton, S. L. Taylor, and S. J. Koppelman. 2013. Digestibility and IgE-binding of glycosylated codfish parvalbumin. BioMed Research International 2013:756789. doi:10.1155/2013/756789.
  • Dills, W. L.Jr 1993. Protein fructosylation: Fructose and the Maillard reaction. The American Journal of Clinical Nutrition 58 (5 Suppl):779S–87S. doi:10.1093/ajcn/58.5.779S.
  • Dolence, J. J., T. Kobayashi, K. Iijima, J. Krempski, L. Y. Drake, A. L. Dent, and H. Kita. 2018. Airway exposure initiates peanut allergy by involving the IL-1 pathway and T follicular helper cells in mice. The Journal of Allergy and Clinical Immunology 142 (4):1144–e8–1158.e8. doi:10.1016/j.jaci.2017.11.020.
  • Dreskin, S. C., S. J. Koppelman, S. Andorf, K. C. Nadeau, A. Kalra, W. Braun, S. S. Negi, X. Chen, and C. H. Schein. 2021. The importance of the 2S albumins for allergenicity and cross-reactivity of peanuts, tree nuts, and sesame seeds. The Journal of Allergy and Clinical Immunology 147 (4):1154–63. doi:10.1016/j.jaci.2020.11.004.
  • Duan, C. C., A. L. Li, L. J. Yang, R. Zhao, W. G. Fan, and G. C. Huo. 2014. Comparison of immunomodulating properties of Beta-lactoglobulin and its hydrolysates. Iranian Journal of Allergy, Asthma, and Immunology 13 (1):26–32.
  • Dunwell, J. M., A. Purvis, and S. Khuri. 2004. Cupins: The most functionally diverse protein superfamily? Phytochemistry 65 (1):7–17. doi:10.1016/j.phytochem.2003.08.016.
  • Eisenbarth, S. C. 2019. Dendritic cell subsets in T cell programming: Location dictates function. Nature Reviews. Immunology 19 (2):89–103. doi:10.1038/s41577-018-0088-1.
  • Ekezie, F. C., J. H. Cheng, and D. W. Sun. 2019. Effects of atmospheric pressure plasma jet on the conformation and physicochemical properties of myofibrillar proteins from king prawn (Litopenaeus vannamei). Food Chemistry 276:147–56. doi:10.1016/j.foodchem.2018.09.113.
  • Evrard, B., J. Cosme, M. Raveau, M. Junda, E. Michaud, and B. Bonnet. 2022. Utility of the basophil activation test using Gly m 4, Gly m 5 and Gly m 6 molecular allergens for characterizing anaphylactic reactions to soy. Frontiers in Allergy 3:908435. doi:10.3389/falgy.2022.908435.
  • 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):842–8. doi:10.1111/all.13115.
  • Frischmeyer-Guerrerio, P. A., M. Rasooly, W. Gu, S. Levin, R. D. Jhamnani, J. D. Milner, K. Stone, A. L. Guerrerio, J. Jones, M. P. Borres, et al. 2019. IgE testing can predict food allergy status in patients with moderate to severe atopic dermatitis. Annals of Allergy, Asthma & Immunology: Official Publication of the American College of Allergy, Asthma, & Immunology 122 (4):393–400.e2. doi:10.1016/j.anai.2019.01.001.
  • Fu, L., C. Wang, J. Wang, S. Ni, and Y. Wang. 2019. Maillard reaction with ribose, galacto-oligosaccharide or chitosan-oligosaccharide reduced the allergenicity of shrimp tropomyosin by inducing conformational changes. Food Chemistry 274:789–95. doi:10.1016/j.foodchem.2018.09.068.
  • Gajda, E., and G. Bugla-Płoskońska. 2014. Lizozym–występowanie w przyrodzie, właściwości biologiczne imożliwości zastosowań [Lysozyme–occurrence in nature, biological properties and possible applications]. Postepy Higieny i Medycyny Doswiadczalnej (Online) ) 68:1501–15. doi:10.5604/17322693.1133100.
  • Gao, Y., C. M. Gillen, and M. G. Wheatly. 2006. Molecular characterization of the sarcoplasmic calcium-binding protein (SCP) from crayfish Procambarus clarkii. Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology 144 (4):478–87. doi:10.1016/j.cbpb.2006.04.007.
  • Garg, V., and C. Kühn. 2022. Subcellular dynamics and protein-protein interactions of plant sucrose transporters. Journal of Plant Physiology 273:153696. doi:10.1016/j.jplph.2022.15369.
  • Gasparini, A., S. Buhler, A. Faccini, S. Sforza, and T. Tedeschi. 2020. Thermally-induced lactosylation of whey proteins: identification and synthesis of lactosylated β-lactoglobulin epitope. Molecules (Basel, Switzerland) 25 (6):1294. doi:10.3390/molecules25061294.
  • Gerrard, J. A., M. Lasse, J. Cottam, J. P. Healy, S. E. Fayle, I. Rasiah, P. K. Brown, S. M. BinYasir, K. H. Sutton, and N. G. Larsen. 2012. Aspects of physical and chemical alterations to proteins during food processing - some implications for nutrition. The British Journal of Nutrition 108 Suppl 2:S288–S297. doi:10.1017/S000711451200236X.
  • Ghosh, S., N. K. Pandey, A. Singha Roy, D. R. Tripathy, A. K. Dinda, and S. Dasgupta. 2013. Prolonged glycation of hen egg white lysozyme generates non amyloidal structures. PloS One 8 (9):e74336. doi:10.1371/journal.pone.0074336.
  • Giansanti, F., L. Leboffe, G. Pitari, R. Ippoliti, and G. Antonini. 2012. Physiological roles of ovotransferrin. Biochimica et Biophysica Acta 1820 (3):218–25. doi:10.1016/j.bbagen.2011.08.004.
  • 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. European Annals of Allergy and Clinical Immunology 46 (5):172–7.
  • Gordon, M. K., and R. A. Hahn. 2010. Collagens. Cell and Tissue Research 339 (1):247–57. doi:10.1007/s00441-009-0844-4.
  • Gou, J., R. Liang, H. Huang, and X. Ma. 2022. Maillard reaction induced changes in allergenicity of food. Foods (Basel, Switzerland) 11 (4):530. doi:10.3390/foods11040530.
  • Gruber, P., W. M. Becker, and T. Hofmann. 2005. Influence of the maillard reaction on the allergenicity of rAra h 2, a recombinant major allergen from peanut (Arachis hypogaea), its major epitopes, and peanut agglutinin. Journal of Agricultural and Food Chemistry 53 (6):2289–96. doi:10.1021/jf048398w.
  • Guillon, B., H. Bernard, M. F. Drumare, S. Hazebrouck, and K. Adel-Patient. 2016. Heat processing of peanut seed enhances the sensitization potential of the major peanut allergen Ara h 6. Molecular Nutrition & Food Research 60 (12):2722–35. doi:10.1002/mnfr.201500923.
  • Gupta, R. K., K. Gupta, A. Sharma, M. Das, I. A. Ansari, and P. D. Dwivedi. 2018. Maillard reaction in food allergy: Pros and cons. Critical Reviews in Food Science and Nutrition 58 (2):208–26. doi:10.1080/10408398.2016.1152949.
  • Hammad, H., and B. N. Lambrecht. 2008. Dendritic cells and epithelial cells: Linking innate and adaptive immunity in asthma. Nature Reviews. Immunology 8 (3):193–204. doi:10.1038/nri2275.
  • Han, T. J., F. Huan, M. Liu, M. S. Li, Y. Yang, G. X. Chen, D. Lai, M. J. Cao, and G. M. Liu. 2021. IgE epitope analysis of sarcoplasmic-calcium-binding protein, a heat-resistant allergen in Crassostrea angulata. Food & Function 12 (18):8570–82. doi:10.1039/d1fo01058a.
  • Han, T. J., M. Liu, F. Huan, M. S. Li, F. Xia, Y. Y. Chen, G. X. Chen, M. J. Cao, and G. M. Liu. 2020. Identification and cross-reactivity analysis of sarcoplasmic-calcium-binding protein: A novel allergen in Crassostrea angulata. Journal of Agricultural and Food Chemistry 68 (18):5221–31. doi:10.1021/acs.jafc.0c01543.
  • Han, X. Y., H. Yang, S. T. Rao, G. Y. Liu, M. J. Hu, B. C. Zeng, M. J. Cao, and G. M. Liu. 2018. The Maillard reaction reduced the sensitization of tropomyosin and arginine kinase from Scylla paramamosain, simultaneously. Journal of Agricultural and Food Chemistry 66 (11):2934–43. doi:10.1021/acs.jafc.7b05195.
  • Hayashi, M., R. Pawankar, S. Yamanishi, and Y. Itoh. 2020. Food-dependent exercise-induced anaphylaxis to soybean: Gly m 5 and Gly m 6 as causative allergen components. The World Allergy Organization Journal 13 (7):100439. doi:10.1016/j.waojou.2020.100439.
  • Hemmings, O., G. Du Toit, S. Radulovic, G. Lack, and A. F. Santos. 2020. Ara h 2 is the dominant peanut allergen despite similarities with Ara h 6. The Journal of Allergy and Clinical Immunology 146 (3):621–30.e5. doi:10.1016/j.jaci.2020.03.026.
  • Hilger, C., M. van Hage, and A. Kuehn. 2017. Diagnosis of allergy to mammals and fish: Cross-reactive vs. specific markers. Current Allergy and Asthma Reports 17 (9):64. doi:10.1007/s11882-017-0732-z.
  • Hitchcock-DeGregori, S. E., and B. Barua. 2017. Tropomyosin structure, function, and interactions: A Dynamic regulator. Sub-Cellular Biochemistry 82:253–84. doi:10.1007/978-3-319-49674-0_9.
  • Hochwallner, H., U. Schulmeister, I. Swoboda, S. Spitzauer, and R. Valenta. 2014. Cow’s milk allergy: From allergens to new forms of diagnosis, therapy and prevention. Methods (San Diego, Calif.) 66 (1):22–33. doi:10.1016/j.ymeth.2013.08.005.
  • Hodgson, E., and J. I. Spicer. 2001. Subunit compositions of crustacean haemocyanins are species-specific: Evidence from non-decapod species. Comparative Biochemistry and Physiology. Part A, Molecular & Integrative Physiology 128 (4):873–88. doi:10.1016/s1095-6433(00)00346-9.
  • Hu, M. J., G. Y. Liu, Y. Yang, T. M. Pan, Y. X. Liu, L. C. Sun, M. J. Cao, and G. M. Liu. 2017. Cloning, expression, and the effects of processing on sarcoplasmic-calcium-binding protein: An important allergen in mud crab. Journal of Agricultural and Food Chemistry 65 (30):6247–57. doi:10.1021/acs.jafc.7b02381.
  • Isgrò, M. A., P. Bottoni, and R. Scatena. 2015. Neuron-specific enolase as a biomarker: Biochemical and clinical aspects. Advances in Experimental Medicine and Biology 867:125–43. doi:10.1007/978-94-017-7215-0_9.
  • 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.
  • Jensen, S. A., A. Fiocchi, T. Baars, G. Jordakieva, A. Nowak-Wegrzyn, I. Pali-Schöll, S. Passanisi, C. L. Pranger, F. Roth-Walter, K. Takkinen, et al. 2022. Diagnosis and rationale for action against cow’s milk allergy (DRACMA) guidelines update - III - Cow’s milk allergens and mechanisms triggering immune activation. The World Allergy Organization Journal 15 (9):100668. doi:10.1016/j.waojou.2022.100668.
  • Jiang, S., Z. Zhou, Y. Sun, and S. Wang. 2010. Sheng wu yi xue gong cheng xue za zhi. Journal of Biomedical Engineering = Shengwu Yixue Gongchengxue Zazhi 27 (6):1401–5.
  • Jiménez-Saiz, R., J. Belloque, E. Molina, and R. López-Fandiño. 2011. Human immunoglobulin E (IgE) binding to heated and glycated ovalbumin and ovomucoid before and after in vitro digestion. Journal of Agricultural and Food Chemistry 59 (18):10044–51. doi:10.1021/jf2014638.
  • Jin, Y., H. G. Acharya, D. Acharya, R. Jorgensen, H. Gao, J. Secord, P. K. W. Ng, and V. Gangur. 2019. Advances in molecular mech anisms of wheat allergenicity in animal models: A comprehensive review. Molecules (Basel, Switzerland) 24 (6):1142. doi:10.3390/molecules24061142.
  • Jones, S. M., and A. W. Burks. 2017. Food allergy. The New England Journal of Medicine 377 (12):1168–76. doi:10.1056/NEJMcp1611971.
  • Juhász, A., T. Belova, C. G. Florides, C. Maulis, I. Fischer, G. Gell, Z. Birinyi, J. Ong, G. Keeble-Gagnère, A., et al. 2018. Genome mapping of seed-borne allergens and immunoresponsive proteins in wheat. Science Advances 4 (8):eaar8602. doi:10.1126/sciadv.aar8602.
  • Kalic, T., F. Morel-Codreanu, C. Radauer, T. Ruethers, A. C. Taki, I. Swoboda, C. Hilger, K. Hoffmann-Sommergruber, M. Ollert, C. Hafner, et al. 2019. Patients allergic to fish tolerate ray based on the low allergenicity of its parvalbumin. The Journal of Allergy and Clinical Immunology. In Practice 7 (2):500–8.e11. doi:10.1016/j.jaip.2018.11.011.
  • 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.
  • Kazatsky, A. M., and R. A. Wood. 2016. Classification of food allergens and cross-reactivity. Current Allergy and Asthma Reports 16 (3):22. doi:10.1007/s11882-016-0601-1.
  • Kennard, L., I. Thomas, K. Rutkowski, V. Azzu, P. Yong, B. Kasternow, H. Hunter, N. Cabdi, A. Nakonechna, and A. Wagner. 2018. A multicenter evaluation of diagnosis and management of omega-5 gliadin allergy (also known as wheat-dependent exercise-induced anaphylaxis) in 132 adults. The Journal of Allergy and Clinical Immunology. In Practice 6 (6):1892–7. doi:10.1016/j.jaip.2018.02.013.
  • Khan, M. U., I. Ahmed, H. Lin, Z. Li, J. Costa, I. Mafra, Y. Chen, and Y. N. Wu. 2019. Potential efficacy of processing technologies for mitigating crustacean allergenicity. Critical Reviews in Food Science and Nutrition 59 (17):2807–30. doi:10.1080/10408398.2018.1471658.
  • 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 & Immunology: Official Publication of the American College of Allergy, Asthma, & Immunology 113 (3):301–6. doi:10.1016/j.anai.2014.06.002.
  • Klemans, R. J., E. F. Knol, A. Michelsen-Huisman, S. G. Pasmans, W. de Kruijf-Broekman, C. A. Bruijnzeel-Koomen, E. van Hoffen, and A. C. Knulst. 2013. Components in soy allergy diagnostics: Gly m 2S albumin has the best diagnostic value in adults. Allergy 68 (11):1396–402. doi:10.1111/all.12259.
  • Komata, T., L. Söderström, M. P. Borres, H. Tachimoto, and M. Ebisawa. 2007. The predictive relationship of food-specific serum IgE concentrations to challenge outcomes for egg and milk varies by patient age. The Journal of Allergy and Clinical Immunology 119 (5):1272–4. doi:10.1016/j.jaci.2007.01.038.
  • Koppelman, S. J., S. L. Hefle, S. L. Taylor, and G. A. de Jong. 2010. Digestion of peanut allergens Ara h 1, Ara h 2, Ara h 3, and Ara h 6: A comparative in vitro study and partial characterization of digestion-resistant peptides. Molecular Nutrition & Food Research 54 (12):1711–21. doi:10.1002/mnfr.201000011.
  • Kuehn, A., F. Codreanu-Morel, C. Lehners-Weber, V. Doyen, S. A. Gomez-André, F. Bienvenu, J. Fischer, N. Ballardini, M. van Hage, J. M. Perotin, et al. 2016. Cross-reactivity to fish and chicken meat - a new clinical syndrome. Allergy 71 (12):1772–81. doi:10.1111/all.12968.
  • Kuehn, A., C. Hilger, C. Lehners-Weber, F. Codreanu-Morel, M. Morisset, C. Metz-Favre, G. Pauli, F. de Blay, D. Revets, C. P. Muller, et al. 2013. Identification of enolases and aldolases as important fish allergens in cod, salmon and tuna: Component resolved diagnosis using parvalbumin and the new allergens. Clinical and Experimental Allergy: Journal of the British Society for Allergy and Clinical Immunology 43 (7):811–22. doi:10.1111/cea.12117.
  • Kuehn, A., I. Swoboda, K. Arumugam, C. Hilger, and F. Hentges. 2014. Fish allergens at a glance: Variable allergenicity of parvalbumins, the major fish allergens. Frontiers in Immunology 5:179. doi:10.3389/fimmu.2014.00179.
  • Li, J. L., J. Liu, Y. H. Ye, P. Yang, and Z. C. Tu. 2019. Reduced IgE/IgG binding capacities of bovine α-Lactalbumin by glycation after dynamic high-pressure microfluidization pretreatment evaluated by high resolution mass spectrometry. Food Chemistry 299:125166. doi:10.3389/fimmu.2014.00179.
  • Li, X., S. Yuan, M. Huang, J. Gao, Z. Wu, P. Tong, A. Yang, and H. Chen. 2016. Identification of IgE and IgG epitopes on native Bos d4 allergen specific to allergic children. Food & Function 7 (7):2996–3005. doi:10.1039/c6fo00416d.
  • Liao, Z. W., Y. H. Ye, H. Wang, Y. Chen, X. M. Sha, L. Zhang, T. Huang, Y. M. Hu, and Z. C. Tu. 2018. The mechanism of decreased IgG/IgE-binding of ovalbumin by preheating treatment combined with glycation identified by liquid chromatography and high-resolution mass spectrometry. Journal of Agricultural and Food Chemistry 66 (41):10693–702. doi:10.1021/acs.jafc.8b04165.
  • Liu, J., W. M. Chen, Y. H. Shao, J. L. Zhang, and Z. C. Tu. 2020. The mechanism of the reduction in allergenic reactivity of bovine α-lactalbumin induced by glycation, phosphorylation and acetylation. Food Chemistry 310:125853. doi:10.1016/j.foodchem.2019.125853.
  • Liu, J., C. Fang, X. Xu, Q. Su, P. Zhao, and Y. Ding. 2019. Physico-chemical and functional properties of silver carp myosin glycated with konjac oligo-glucomannan: Effects of deacetylation. Food Chemistry 291:223–30. doi:10.1016/j.foodchem.2019.03.153.
  • Liu, J., Z. C. Tu, G. X. Liu, C. D. Niu, H. L. Yao, H. Wang, X. M. Sha, Y. H. Shao, and I. A. Kaltashov. 2018. Ultrasonic pretreatment combined with dry-state glycation reduced the immunoglobulin E/immunoglobulin G-binding ability of α-lactalbumin revealed by high-resolution mass spectrometry. Journal of Agricultural and Food Chemistry 66 (22):5691–8. doi:10.1021/acs.jafc.8b00489.
  • Liu, K., S. Chen, H. Chen, P. Tong, and J. Gao. 2018. Cross-linked ovalbumin catalyzed by polyphenol oxidase: Preparation, structure and potential allergenicity. International Journal of Biological Macromolecules 107 (Pt B):2057–64. doi:10.1016/j.ijbiomac.2017.10.072.
  • Liu, Y. F., I. Oey, P. Bremer, P. Silcock, and A. Carne. 2018. Proteolytic pattern, protein breakdown and peptide production of ovomucin-depleted egg white processed with heat or pulsed electric fields at different pH. Food Research International (Ottawa, Ont.) 108:465–74. doi:10.1016/j.foodres.2018.03.075.
  • Liu, Y. Y., M. J. Cao, M. L. Zhang, J. W. Hu, Y. X. Zhang, L. J. Zhang, and G. M. Liu. 2014. Purification, characterization and immunoreactivity of β’-component, a major allergen from the roe of large yellow croaker (Pseudosciaena crocea). Food and Chemical Toxicology: An International Journal Published for the British Industrial Biological Research Association 72:111–21. doi:10.1016/j.fct.2014.07.015.
  • Loke, I., D. Kolarich, N. H. Packer, and M. Thaysen-Andersen. 2016. Emerging roles of protein mannosylation in inflammation and infection. Molecular Aspects of Medicine 51:31–55. doi:10.1016/j.mam.2016.04.004.
  • Lopata, A. L., J. Kleine-Tebbe, and S. D. Kamath. 2016. Allergens and molecular diagnostics of shellfish allergy: Part 22 of the series molecular allergology. Allergo Journal International 25 (7):210–8. doi:10.1007/s40629-016-0124-2.
  • Lopata, A. L., R. E. O’Hehir, and S. B. Lehrer. 2010. Shellfish allergy. Clinical and Experimental Allergy: Journal of the British Society for Allergy and Clinical Immunology 40 (6):850–8. doi:10.1111/j.1365-2222.2010.03513.x.
  • Lorenz, A. R., S. Scheurer, and S. Vieths. 2015. Food allergens: Molecular and immunological aspects, allergen databases and cross-reactivity. Chemical Immunology and Allergy 101:18–29. doi:10.1159/000371647.
  • Luo, C., Y. Guo, Z. Li, I. Ahmed, S. N. Pramod, X. Gao, L. Lv, and H. Lin. 2020. Lipid emulsion enhances fish allergen parvalbumin’s resistance to in vitro digestion and IgG/IgE binding capacity. Food Chemistry 302:125333. doi:10.1016/j.foodchem.2019.125333.
  • Ma, J., J. Zhou, L. Chen, H. Zhang, Y. Wang, and L. Fu. 2021. Effects of deglycosylation and the Maillard reaction on conformation and allergenicity of the egg ovomucoid. Journal of Food Science 86 (7):3014–22. doi:10.1111/1750-3841.15791.
  • Ma, X. J., H. B. Chen, J. Y. Gao, C. Q. Hu, and X. Li. 2013. Conformation affects the potential allergenicity of ovalbumin after heating and glycation. Food Additives & Contaminants. Part A, Chemistry, Analysis, Control, Exposure & Risk Assessment 30 (10):1684–92. doi:10.1080/19440049.2013.822105.
  • Madureira, A. R., C. I. Pereira, A. M. P. Gomes, M. E. Pintado, and F. Xavier Malcata. 2007. Bovine whey proteins – Overview on their main biological properties. Food Research International 40 (10):1197–211. doi:10.1016/j.foodres.2007.07.005.
  • Maleki, S. J., S. Y. Chung, E. T. Champagne, and J. P. Raufman. 2000. The effects of roasting on the allergenic properties of peanut proteins. The Journal of Allergy and Clinical Immunology 106 (4):763–8. doi:10.1067/mai.2000.109620.
  • Martín-Orozco, E., M. Norte-Muñoz, and J. Martínez-García. 2017. Regulatory T cells in allergy and asthma. Frontiers in Pediatrics 5:117. doi:10.3389/fped.2017.00117.
  • Marxen, J. C., C. Pick, T. H. Oakley, and T. Burmester. 2014. Occurrence of hemocyanin in ostracod crustaceans. Journal of Molecular Evolution 79 (1-2):3–11. doi:10.1007/s00239-014-9636-x.
  • Matricardi, P. M., J. Kleine-Tebbe, H. J. Hoffmann, R. Valenta, C. Hilger, S. Hofmaier, R. C. Aalberse, I. Agache, R. Asero, B. Ballmer-Weber, et al. 2016. EAACI Molecular allergology user’s guide. Pediatric Allergy and Immunology: Official Publication of the European Society of Pediatric Allergy and Immunology 27 Suppl 23 (Suppl 23):1–250. doi:10.1111/pai.12563.
  • Matsuo, H., T. Yokooji, and T. Taogoshi. 2015. Common food allergens and their IgE-binding epitopes. Allergology International: Official Journal of the Japanese Society of Allergology 64 (4):332–43. doi:10.1016/j.alit.2015.06.009.
  • Mbonye, U. R., C. Yuan, C. E. Harris, R. S. Sidhu, I. Song, T. Arakawa, and W. L. Smith. 2008. Two distinct pathways for cyclooxygenase-2 protein degradation. The Journal of Biological Chemistry 283 (13):8611–23. doi:10.1074/jbc.M710137200.
  • McWilliam, V., R. Peters, M. Tang, S. Dharmage, A. L. Ponsonby, L. Gurrin, K. Perrett, J. Koplin, and K. J. Allen. 2019. Patterns of tree nut sensitization and allergy in the first 6 years of life in a population-based cohort. The Journal of Allergy and Clinical Immunology 143 (2):644–50.e5. doi:10.1016/j.jaci.2018.07.038.
  • Messina, M., M. M. Rogero, M. Fisberg, and D. Waitzberg. 2017. Health impact of childhood and adolescent soy consumption. Nutrition Reviews 75 (7):500–15. doi:10.1093/nutrit/nux016.
  • 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 (7):1737–42. doi:10.1002/jsfa.5961.
  • Mitra, N., S. Sinha, T. N. Ramya, and A. Surolia. 2006. N-linked oligosaccharides as outfitters for glycoprotein folding, form and function. Trends in Biochemical Sciences 31 (3):156–63. doi:10.1016/j.tibs.2006.01.003.
  • Mittag, D., J. Akkerdaas, B. K. Ballmer-Weber, L. Vogel, M. Wensing, W. M. Becker, S. J. Koppelman, A. C. Knulst, A. Helbling, S. L. Hefle, et al. 2004. Ara h 8, a Bet v 1-homologous allergen from peanut, is a major allergen in patients with combined birch pollen and peanut allergy. The Journal of Allergy and Clinical Immunology 114 (6):1410–1417. doi:10.1016/j.jaci.2004.09.014.
  • Moonesinghe, H., H. Mackenzie, C. Venter, S. Kilburn, P. Turner, K. Weir, and T. Dean. 2016. Prevalence of fish and shellfish allergy: A systematic review. Annals of Allergy, Asthma & Immunology: Official Publication of the American College of Allergy, Asthma, & Immunology 117 (3):264–72.e4. doi:10.1016/j.anai.2016.07.015.
  • Mori, Y., T. Ugajin, K. Okada, Y. Handa, N. Umemoto, H. Iijima, K. Igawa, and H. Yokozeki. 2021. Epicutaneously sensitized food-induced anaphylaxis is ameliorated with "oral tolerance" to antigen. Experimental Dermatology 30 (3):367–76. doi:10.1111/exd.14216.
  • Mousan, G., and D. Kamat. 2016. Cow’s milk protein allergy. Clinical Pediatrics 55 (11):1054–63. doi:10.1177/0009922816664512.
  • Mueller, G. A., S. J. Maleki, K. Johnson, B. K. Hurlburt, H. Cheng, S. Ruan, J. B. Nesbit, A. Pomés, L. L. Edwards, A. Schorzman, et al. 2013. Identification of Maillard reaction products on peanut allergens that influence binding to the receptor for advanced glycation end products. Allergy 68 (12):1546–54. doi:10.1111/all.12261.
  • Munblit, D., M. R. Perkin, D. J. Palmer, K. J. Allen, and R. J. Boyle. 2020. Assessment of evidence about common infant symptoms and cow’s milk allergy. JAMA Pediatrics 174 (6):599–608. doi:10.1001/jamapediatrics.2020.0153.
  • Musallam, N., I. Dalal, M. Almog, L. Epov, A. Romem, E. Bamberger, A. Mandelberg, and A. Kessel. 2021. Food allergic reactions during the Covid-19 pandemic lockdown in Israeli children. Pediatric Allergy and Immunology: Official Publication of the European Society of Pediatric Allergy and Immunology 32 (7):1580–4. doi:10.1111/pai.13540.
  • Mylne, J. S., I. Hara-Nishimura, and K. J. Rosengren. 2014. Seed storage albumins: Biosynthesis, trafficking and structures. Functional Plant Biology: FPB 41 (7):671–7. doi:10.1071/FP14035.
  • Nakamura, A., K. Watanabe, T. Ojima, D. H. Ahn, and H. Saeki. 2005. Effect of maillard reaction on allergenicity of scallop tropomyosin. Journal of Agricultural and Food Chemistry 53 (19):7559–64. doi:10.1021/jf0502045.
  • Nilsson, N., S. Sjölander, A. Baar, M. Berthold, S. Pahr, S. Vrtala, R. Valenta, E. Morita, G. Hedlin, M. P. Borres, et al. 2015. Wheat allergy in children evaluated with challenge and IgE antibodies to wheat components. Pediatric Allergy and Immunology: Official Publication of the European Society of Pediatric Allergy and Immunology 26 (2):119–25. doi:10.1111/pai.12334.
  • Okolie, C. L., A. N. A. Aryee, and C. C. Udenigwe. 2018. Detection and deactivation of allergens in food. In Proteins in food processing, 367–87. Food Science, Technology and Nutrition. doi:10.1016/B978-0-08-100722-8.00015-2.
  • Olivier, C. E., M. B. Villas-Boas, F. M. Netto, and R. D. L. Zollner. 2012. Allergenicity of Bos d 5 in children with cow’s milk allergy is reduced by transglutaminase polymerization. Pediatric Allergy, Immunology, and Pulmonology 25 (1):30–3. doi:10.1089/ped.2011.0101.
  • Ozdemir, C., M. Akdis, and C. A. Akdis. 2010. T-cell response to allergens. Chemical Immunology and Allergy 95:22–44. doi:10.1159/000315936.
  • Palladino, C., and H. Breiteneder. 2018. Peanut allergens. Molecular Immunology 100:58–70. doi:10.1016/j.molimm.2018.04.005.
  • Palosuo, K., A. K. Kukkonen, A. S. Pelkonen, and M. J. Mäkelä. 2018. Gal d 1-specific IgE predicts allergy to heated egg in Finnish children. Pediatric Allergy and Immunology: Official Publication of the European Society of Pediatric Allergy and Immunology 29 (6):637–43. doi:10.1016/j.molimm.2018.04.005.
  • Palosuo, K., E. Varjonen, O. M. Kekki, T. Klemola, N. Kalkkinen, H. Alenius, and T. Reunala. 2001. Wheat omega-5 gliadin is a major allergen in children with immediate allergy to ingested wheat. The Journal of Allergy and Clinical Immunology 108 (4):634–8. doi:10.1067/mai.2001.118602.
  • Papia, F., C. Bellia, and C. G. Uasuf. 2021. Tropomyosin: A panallergen that causes a worldwide allergic problem. Allergy and Asthma Proceedings 42 (5):e145–e151. doi:10.2500/aap.2021.42.210057.
  • Park, H. Y., T. J. Yoon, H. H. Kim, Y. S. Han, and H. D. Choi. 2017. Changes in the antigenicity and allergenicity of ovalbumin in chicken egg white by N-acetylglucosaminidase. Food Chemistry 217:342–5. doi:10.1016/j.foodchem.2016.08.112.
  • Pedrosa, M., T. Boyano-Martínez, C. García-Ara, and S. Quirce. 2015. Shellfish allergy: A comprehensive review. Clinical Reviews in Allergy & Immunology 49 (2):203–16. doi:10.1007/s12016-014-8429-8.
  • Pérez-Tavarez, R., H. M. Moreno, J. Borderias, D. Loli-Ausejo, M. Pedrosa, J. L. Hurtado, R. Rodriguez-Pérez, and M. Gasset. 2021. Fish muscle processing into seafood products reduces β-parvalbumin allergenicity. Food Chemistry 364:130308. doi:10.1016/j.foodchem.2021.130308.
  • Pham, M. N., and J. Wang. 2017. Mammalian milk allergy: Case presentation and review of prevalence, diagnosis, and treatment. Annals of Allergy, Asthma & Immunology: Official Publication of the American College of Allergy, Asthma, & Immunology 118 (4):406–10. doi:10.1016/j.anai.2017.02.018.
  • Piersma, S. R., M. Gaspari, S. L. Hefle, and S. J. Koppelman. 2005. Proteolytic processing of the peanut allergen Ara h 3. Molecular Nutrition & Food Research 49 (8):744–55. doi:10.1002/mnfr.200500020.
  • Pouessel, G., and G. Lezmi. 2023. Oral immunotherapy for food allergy: Translation from studies to clinical practice? The World Allergy Organization Journal 16 (2):100747. doi:10.1016/j.waojou.2023.100747.
  • Prester, L. 2016. Seafood allergy, toxicity, and intolerance: A review. Journal of the American College of Nutrition 35 (3):271–83. doi:10.1080/07315724.2015.1014120.
  • Qi, X., and R. F. Tester. 2019. Fructose, galactose and glucose - In health and disease. Clinical Nutrition ESPEN 33:18–28. doi:10.1016/j.clnesp.2019.07.004.
  • Quan, W., Y. Li, Y. Jiao, C. Xue, G. Liu, Z. Wang, Z. He, F. Qin, M. Zeng, and J. Chen. 2020. Simultaneous generation of acrylamide, β-carboline heterocyclic amines and advanced glycation ends products in an aqueous Maillard reaction model system. Food Chemistry 332:127387. doi:10.1016/j.foodchem.2020.127387.
  • Quirce, S., F. Marañón, A. Umpiérrez, M. de las Heras, E. Fernández-Caldas, and J. Sastre. 2001. Chicken serum albumin (Gal d 5*) is a partially heat-labile inhalant and food allergen implicated in the bird-egg syndrome. Allergy 56 (8):754–62. doi:10.1034/j.1398-9995.2001.056008754.x.
  • Jacobsen, B., K. Hoffmann-Sommergruber, T. T. Have, N. Foss, P. Briza, C. Oberhuber, C. Radauer, S. Alessandri, A. C. Knulst, M. Fernandez-Rivas, et al. 2008. The panel of egg allergens, Gal d 1-Gal d 5: Their improved purification and characterization. Molecular Nutrition & Food Research 52 Suppl 2 (Suppl 2):S176–S185. doi:10.1002/mnfr.200700414.
  • 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. Kamath, A. L. Lopata, and R. J. Helleur. 2010. Analysis of theallergenic 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.
  • Rao, Q., X. Jiang, Y. Li, M. Samiwala, and T. P. Labuza. 2018. Can glycation reduce food allergenicity? Journal of Agricultural and Food Chemistry 66 (17):4295–9. doi:10.1021/acs.jafc.8b00660.
  • Ren, B., L. Wang, A. Mulati, Y. Liu, Z. Liu, and X. Liu. 2021. Methionine restriction improves gut barrier function by reshaping diurnal rhythms of inflammation-related microbes in aged mice. Frontiers in Nutrition 8:746592. doi:10.3389/fnut.2021.746592.
  • Renz, H., K. J. Allen, S. H. Sicherer, H. A. Sampson, G. Lack, K. Beyer, and H. c Oettgen. 2018. Food allergy. Nature Reviews. Disease Primers 4 (1):17098. doi:10.1038/nrdp.2017.98.
  • Rial Prado, M. J., B. Batolomé, C. Pastor, J. Cuesta, and A. Parra. 2017. Troponin as a cause of hypersensitivity to barnacle. Journal of Investigational Allergology & Clinical Immunology 27 (3):194–5. doi:10.18176/jiaci.0159.
  • Rinninella, E., M. Cintoni, P. Raoul, L. R. Lopetuso, F. Scaldaferri, G. Pulcini, G. A. D. Miggiano, A. Gasbarrini, and M. C. Mele. 2019. Food components and dietary habits: Keys for a healthy gut microbiota composition. Nutrients 11 (10):2393. doi:10.3390/nu11102393.
  • Robotham, J. M., F. Wang, V. Seamon, S. S. Teuber, S. K. Sathe, H. A. Sampson, K. Beyer, M. Seavy, and K. H. Roux. 2005. Ana o 3, an important cashew nut (Anacardium occidentale L.) allergen of the 2S albumin family. The Journal of Allergy and Clinical Immunology 115 (6):1284–90. doi:10.1016/j.jaci.2005.02.028.
  • Roth, Z., S. Weil, E. D. Aflalo, R. Manor, A. Sagi, and I. Khalaila. 2013. Identification of receptor-interacting regions of vitellogenin within evolutionarily conserved β-sheet structures by using a peptide array. Chembiochem: A European Journal of Chemical Biology 14 (9):1116–22. doi:10.1002/cbic.201300152.
  • Ruethers, T., A. C. Taki, E. B. Johnston, R. Nugraha, T. Le, T. Kalic, T. R. McLean, S. D. Kamath, and A. L. Lopata. 2018. Seafood allergy: A comprehensive review of fish and shellfish allergens. Molecular Immunology 100:28–57. doi:10.1016/j.molimm.2018.04.008.
  • Rupa, P., and Y. Mine. 2019. Comparison of glycated ovalbumin-monosaccharides in the attenuation of ovalbumin-induced allergic response in a BALB/C mouse model. Journal of Agricultural and Food Chemistry 67 (29):8138–48. doi:10.1021/acs.jafc.9b02132.
  • Sathe, S. K., C. Liu, and V. D. Zaffran. 2016. Food allergy. Annual Review of Food Science and Technology 7:191–220. doi:10.1146/annurev-food-041715-033308.
  • Schorer, M., V. K. Kuchroo, and N. Joller. 2019. Role of co-stimulatory molecules in T helper cell differentiation. Advances in Experimental Medicine and Biology 1189:153–77. doi:10.1007/978-981-32-9717-3_6.
  • Shamji, M. H., R. Valenta, T. Jardetzky, V. Verhasselt, S. R. Durham, P. A. Würtzen, and R. J. J. van Neerven. 2021. The role of allergen-specific IgE, IgG and IgA in allergic disease. Allergy 76 (12):3627–41. doi:10.1111/all.14908.
  • Shao, Y. H., Y. Zhang, M. F. Zhu, J. Liu, and Z. C. Tu. 2020. Glycation of β-lactoglobulin combined by sonication pretreatment reduce its allergenic potential. International Journal of Biological Macromolecules 164:1527–35. doi:10.1016/j.ijbiomac.2020.07.223.
  • 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. Journal of Agricultural and Food Chemistry 60 (9):2190–9. doi:10.1021/jf203779w.
  • Shi, Y., M. Wang, Y. Ding, J. Chen, B. Niu, and Q. Chen. 2020. Effects of Maillard reaction on structural modification and potential allergenicity of peanut 7S globulin (Ara h 1). Journal of the Science of Food and Agriculture 100 (15):5617–26. doi:10.1002/jsfa.10614.
  • Shimamura, T., and H. Uke. 2012. Maillard reaction in milk - effect of heat treatment. InTech (Chapter 5). 147–158. doi:10.5772/50079.
  • Sicherer, S. H., and H. A. Sampson. 2018. Food allergy: A review andupdate on epidemiology, pathogenesis, diagnosis, prevention, and management. The Journal of Allergy and Clinical Immunology 141 (1):41–58. doi:10.1016/j.jaci.2017.11.003.
  • Silva, J., R. Ferraz, P. Dupree, A. M. Showalter, and S. Coimbra. 2020. Three decades of advances in arabinogalactan-protein biosynthesis. Frontiers in Plant Science 11:610377. doi:10.3389/fpls.2020.610377.
  • Simic, Z., M. Weiwad, A. Schierhorn, C. Steegborn, and M. Schutkowski. 2015. The ɛ-amino group of protein lysine residues is highly susceptible to nonenzymatic acylation by several physiological Acyl-CoA thioesters. Chembiochem: A European Journal of Chemical Biology 16 (16):2337–47. doi:10.1002/cbic.201500364.
  • Skypala, I. J., R. Asero, D. Barber, L. Cecchi, A. Diaz Perales, K. Hoffmann-Sommergruber, E. A. Pastorello, I. Swoboda, J. Bartra, D. G. Ebo, Clinical Immunology (EAACI) Task Force: Non‐specific Lipid Transfer Protein Allergy Across Europe., et al. 2021. Non-specific lipid-transfer proteins: Allergen structure and function, cross-reactivity, sensitization, and epidemiology. Clinical and Translational Allergy 11 (3):e12010. doi:10.1002/clt2.12010.
  • Smeekens, J. M., K. Bagley, and M. Kulis. 2018. Tree nut allergies: Allergen homology. cross-reactivity, and implications for therapy. Clinical and Experimental Allergy: Journal of the British Society for Allergy and Clinical Immunology 48 (7):762–72. doi:10.1111/cea.13163.
  • Solá, R. J., and K. Griebenow. 2009. Effects of glycosylation on the stability of protein pharmaceuticals. Journal of Pharmaceutical Sciences 98 (4):1223–45. doi:10.1002/jps.21504.
  • Specks, U., D. N. Fass, J. D. Finkielman, A. M. Hummel, M. A. Viss, R. D. Litwiller, and C. J. McDonald. 2007. Functional significance of Asn-linked glycosylation of proteinase 3 for enzymatic activity, processing, targeting, and recognition by anti-neutrophil cytoplasmic antibodies. Journal of Biochemistry 141 (1):101–12. doi:10.1093/jb/mvm008.
  • Strasser, R. 2016. Plant protein glycosylation. Glycobiology 26 (9):926–39. doi:10.1093/glycob/cww023.
  • 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 (3):921–6. doi:10.1016/j.foodchem.2010.07.020.
  • Taguchi, K., and Y. Takagi. 2001. Rinsho byori. The Japanese Journal of Clinical Pathology Suppl 116:117–24.
  • Tanabe, S., R. Shibata, and T. Nishimura. 2004. Hypoallergenic and T cell reactive analogue peptides of bovine serum albumin, the major beef allergen. Molecular Immunology 41 (9):885–90. doi:10.1016/j.molimm.2004.04.028.
  • Tănciuc, N., A. A. Creţu, I. Banu, and I. Aprodu. 2018. Advances on the impact of thermal processing on structure and antigenicity of chicken ovomucoid. Journal of the Science of Food and Agriculture 98 (8):3119–28. doi:10.1002/jsfa.8813.
  • Teo, S. L., I. F. A. Gerez, E. Y. Ang, and L. P. Shek. 2009. Food-dependent exercise induced anaphylaxis -A review of 5 cases. Annals of the Academy of Medicine, Singapore 38 (10):905–9. doi:10.47102/annals-acadmedsg.V38N10p905.
  • Teodorowicz, M., J. van Neerven, and H. Savelkoul. 2017. Food processing: The influence of the maillard reaction on immunogenicity and allergenicity of food proteins. Nutrients 9 (8):835. doi:10.3390/nu9080835.
  • Tian, Y., H. Rao, K. Zhang, S. Tao, and W. T. Xue. 2018. Effects of different thermal processing methods on the structure and allergenicity of peanut allergen Ara h 1. Food Science & Nutrition 6 (6):1706–14. doi:10.1002/fsn3.742.
  • Toda, M., M. Hellwig, T. Henle, and S. Vieths. 2019. Influence of the Maillard reaction on the allergenicity of food proteins and the development of allergic inflammation. Current Allergy and Asthma Reports 19 (1):4. doi:10.1007/s11882-019-0834-x.
  • Tordesillas, L., M. C. Berin, and H. A. Sampson. 2017. Immunology of food allergy. Immunity 47 (1):32–50. doi:10.1016/j.immuni.2017.07.004.
  • Troy, F. A.2nd 1992. Polysialylation: From bacteria to brains. Glycobiology 2 (1):5–23. doi:10.1093/glycob/2.1.5.
  • Urisu, A., Y. Kondo, and I. Tsuge. 2015. Hen’s egg allergy. Chemical Immunology and Allergy 101:124–30. doi:10.1159/000375416.
  • Usui, M., H. Tamura, K. Nakamura, T. Ogawa, M. Muroshita, H. Azakami, S. Kanuma, and A. Kato. 2004. Enhanced bactericidal action and masking of allergen structure of soy protein by attachment of chitosan through maillard-type protein-polysaccharide conjugation. Die Nahrung 48 (1):69–72. doi:10.1002/food.200300423.
  • Vagin, O., J. A. Kraut, and G. Sachs. 2009. Role of N-glycosylation in trafficking of apical membrane proteins in epithelia. American Journal of Physiology. Renal Physiology 296 (3):F459–F469. doi:10.1152/ajprenal.90340.2008.
  • Vanga, S. K., and V. Raghavan. 2017. 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.
  • Verhoeckx, K. C., Y. M. Vissers, J. L. Baumert, R. Faludi, M. Feys, S. Flanagan, C. Herouet-Guicheney, T. Holzhauser, R. Shimojo, N. van der Bolt, et al. 2015. Food processing and allergenicity. Food and Chemical Toxicology: An International Journal Published for the British Industrial Biological Research Association 80:223–40. doi:10.1016/j.fct.2015.03.005.
  • Villa, C., J. Costa, M. B. P. Oliveira, and I. Mafra. 2018. Bovine milk allergens: A comprehensive review. Comprehensive Reviews in Food Science and Food Safety 17 (1):137–64. doi:10.1111/1541-4337.12318.
  • Vissers, Y. M., F. Blanc, P. S. Skov, P. E. Johnson, N. M. Rigby, L. Przybylski-Nicaise, H. Bernard, J. M. Wal, B. Ballmer-Weber, L. Zuidmeer-Jongejan, et al. 2011. Effect of heating and glycation on the allergenicity of 2S albumins (Ara h 2/6) from peanut. PloS One 6 (8):e23998. doi:10.1371/journal.pone.0023998.
  • Vissers, Y. M., M. Iwan, K. Adel-Patient, P. Stahl Skov, N. M. Rigby, P. E. Johnson, P. Mandrup Müller, L. Przybylski-Nicaise, M. Schaap, J. Ruinemans-Koerts, et al. 2011. Effect of roasting on the allergenicity of major peanut allergens Ara h 1 and Ara h 2/6: The necessity of degranulation assays. Clinical and Experimental Allergy: Journal of the British Society for Allergy and Clinical Immunology 41 (11):1631–42. doi:10.1111/j.1365-2222.2011.03830.x.
  • Wal, J. M. 1998. Immunochemical and molecular characterization of milk allergens. Allergy 53 (46 Suppl):114–7. doi:10.1111/j.1398-9995.1998.tb04979.x.
  • Wal, J. M. 2002. Cow’s milk proteins/allergens. Annals of Allergy, Asthma & Immunology: Official Publication of the American College of Allergy, Asthma, & Immunology 89 (6 Suppl 1):3–10. doi:10.1016/s1081-1206(10)62115-1.
  • Wal, J. M. 2004. Bovine milk allergenicity. Annals of Allergy, Asthma & Immunology: Official Publication of the American College of Allergy, Asthma, & Immunology 93 (5 Suppl 3):S2–S11. doi:10.1016/s1081-1206(10)61726-7.
  • Wallowitz, M., W. R. Peterson, S. Uratsu, S. S. Comstock, A. M. Dandekar, and S. S. Teuber. 2006. Jug r 4, a legumin group food allergen from walnut (Juglans regia Cv. Chandler). Journal of Agricultural and Food Chemistry 54 (21):8369–75. doi:10.1021/jf061329s.
  • Wang, X. M., Y. H. Ye, Z. C. Tu, Y. M. Hu, H. Wang, and T. Huang. 2021. Mechanism of the reduced IgG/IgE binding abilities of glycated β-lactoglobulin and its digests through high-resolution mass spectrometry. Journal of Agricultural and Food Chemistry 69 (12):3741–50. doi:10.1021/acs.jafc.1c00205.
  • Watanabe, D., N. Adányi, K. Takács, A. Maczó, A. Nagy, É. Gelencsér, M. Pachner, K. Lauter, S. Baumgartner, and J. Vollmann. 2017. Development of soybeans with low P34 allergen protein concentration for reduced allergenicity of soy foods. Journal of the Science of Food and Agriculture 97 (3):1010–7. doi:10.1002/jsfa.7827.
  • Waugh, D. S. 2016. The remarkable solubility-enhancing power of Escherichia coli maltose-binding protein. Niezwykła zdolność MBP Escherichia coli do zwiększania rozpuszczalności innych białek. Postępy Biochemii 62 (3):377–82. doi:10.18388/pb.2016_41.
  • Wei, Z., and Q. Huang. 2019. Modification of ovotransferrin by maillard reaction: Consequences for structure, fibrillation and emulsifying property of fibrils. Food Hydrocolloids 97:105186. doi:10.1016/j.foodhyd.2019.105186.
  • Wei, B., K. Berning, C. Quan, and Y. T. Zhang. 2017. Glycation of antibodies: Modification, methods and potential effects on biological functions. mAbs 9 (4):586–94. doi:10.1080/19420862.2017.1300214.
  • Wei, Y., C. S. Han, J. Zhou, Y. Liu, L. Chen, and R. Q. He. 2012. D-ribose in glycation and protein aggregation. Biochimica et Biophysica Acta 1820 (4):488–94. doi:10.1016/j.bbagen.2012.01.005.
  • Wong, L., E. H. Tham, and B. W. Lee. 2019. An update on shellfish allergy. Current Opinion in Allergy and Clinical Immunology 19 (3):236–42. doi:10.1097/ACI.0000000000000532.
  • Wood, R. A. 2017. Oral immunotherapy for food allergy. Journal of Investigational Allergology & Clinical Immunology 27 (3):151–9. doi:10.18176/jiaci.0143.
  • Wu, X., M. Liu, L. Xia, H. Wu, Z. Liu, and X. Xu. 2013. Conjugation of functional oligosaccharides reduced in vitro allergenicity of β-lactoglobulin. Food and Agricultural Immunology 24 (4):379–91. doi:10.1080/09540105.2012.686990.
  • Wu, Y., Y. Lu, Y. Huang, H. Lin, G. Chen, Y. Chen, and Z. Li. 2022. Glycosylation reduces the allergenicity of turbot (Scophthalmus maximus) parvalbumin by regulating digestibility, cellular mediators release and Th1/Th2 immunobalance. Food Chemistry 382:132574. doi:10.1016/j.foodchem.2022.132574.
  • Xiang, J., F. Liu, B. Wang, L. Chen, W. Liu, and S. Tan. 2021. A literature review on Maillard reaction based on milk proteins and carbohydrates in food and pharmaceutical products: advantages, disadvantages, and avoidance strategies. Foods (Basel, Switzerland) 10 (9):1998. doi:10.3390/foods10091998.
  • Xu, L., Y. Gong, J. E. Gern, and J. A. Lucey. 2020. Influence of whey protein hydrolysis in combination with dextran glycation on immunoglobulin E binding capacity with blood sera obtained from patients with a cow milk protein allergy. Journal of Dairy Science 103 (2):1141–50. doi:10.3168/jds.2019-17187.
  • Xu, L., Y. Gong, J. E. Gern, S. Ikeda, and J. A. Lucey. 2018. Glycation of whey protein with dextrans of different molar mass: Effect on immunoglobulin E-binding capacity with blood sera obtained from patients with cow milk protein allergy. Journal of Dairy Science 101 (8):6823–34. doi:10.3168/jds.2017-14338.
  • Xu, Z. Z., G. Q. Huang, T. C. Xu, L. N. Liu, and J. X. Xiao. 2019. Comparative study on the Maillard reaction of chitosan oligosaccharide and glucose with soybean protein isolate. International Journal of Biological Macromolecules 131:601–7. doi:10.1016/j.ijbiomac.2019.03.101.
  • Yamamoto, S., N. Mikami, M. Matsuno, T. Hara, S. Odani, A. Suzuki, and T. Nishiumi. 2010. Effects of a high-pressure treatment on bovine gamma globulin and its reduction in allergenicity. Bioscience, Biotechnology, and Biochemistry 74 (3):525–30. doi:10.1271/bbb.90715.
  • Yang, C., F. Zhong, H. Douglas Goff, and Y. Li. 2019. Study on starch-protein interactions and their effects on physicochemical and digestible properties of the blends. Food Chemistry 280:51–8. doi:10.1016/j.foodchem.2018.12.028.
  • Yang, H., J. Min, X. Y. Han, X. Y. Li, J. W. Hu, H. Liu, M. J. Cao, and G. M. Liu. 2018. Reduction of the histamine content and immunoreactivity of parvalbumin in Decapterus maruadsi by a Maillard reaction combined with pressure treatment. Food & Function 9 (9):4897–905. doi:10.1039/c8fo01167b.
  • Yang, M., M. Tan, J. Wu, Z. Chen, X. Long, Y. Zeng, H. Cai, Y. Zhang, L. Geng, Y. Xiao, et al. 2019. Prevalence, characteristics, and outcome of cow’s milk protein allergy in Chinese infants: A population-based survey. JPEN. Journal of Parenteral and Enteral Nutrition 43 (6):803–8. doi:10.1002/jpen.1472.
  • Yang, Q., Y. Wang, M. Yang, X. Liu, S. Lyu, B. Liu, J. Liu, and T. Zhang. 2022. Effect of glycation degree on the structure and digestion properties of ovalbumin: A study of amino acids and peptides release after in vitro gastrointestinal simulated digestion. Food Chemistry 373 (Pt B):131331. doi:10.1016/j.foodchem.2021.131331.
  • Yang, S., Z. C. Tu, H. Wang, and T. Huang. 2020. The reduction in the immunoglobulin G and immunoglobulin E binding capacity of β-lactoglobulin via spray-drying technology. Journal of Dairy Science 103 (4):2993–3001. doi:10.3168/jds.2019-17322.
  • Yang, W., Z. Tu, H. Wang, L. Zhang, and Q. Song. 2018. Glycation of ovalbumin after high-intensity ultrasound pretreatment: Effects on conformation, immunoglobulin (Ig)G/IgE binding ability and antioxidant activity. Journal of the Science of Food and Agriculture 98 (10):3767–73. doi:10.1002/jsfa.8890.
  • Yang, W., Z. Tu, H. Wang, L. Zhang, S. Xu, C. Niu, H. Yao, and I. A. Kaltashov. 2017. Mechanism of reduction in IgG and IgE binding of β-lactoglobulin induced by ultrasound pretreatment combined with dry-state glycation: A study using conventional spectrometry and high-resolution mass spectrometry. Journal of Agricultural and Food Chemistry 65 (36):8018–27. doi:10.1021/acs.jafc.7b02842.
  • Yang, Y., G. Liu, Z. Tu, H. Wang, Y. Hu, J. Mao, and J. Zhang. 2020. Insight into the mechanism of reduced IgG/IgE binding capacity in ovalbumin as induced by glycation with monose epimers through liquid chromatography and high-resolution mass spectrometry. Journal of Agricultural and Food Chemistry 68 (22):6065–75. doi:10.1021/acs.jafc.0c01233.
  • Yang, Y., H. F. Yan, Y. X. Zhang, H. L. Chen, M. J. Cao, M. S. Li, M. L. Zhang, X. R. He, and G. M. Liu. 2020. Expression and epitope identification of myosin light chain isoform 1, an allergen in Procambarus clarkii. Food Chemistry 317:126422. doi:10.1021/acs.jafc.0c01233.
  • Yang, Z. H., C. Li, Y. Y. Li, and Z. H. Wang. 2013. Effects of Maillard reaction on allergenicity of buckwheat allergen Fag t 3 during thermal processing. Journal of the Science of Food and Agriculture 93 (6):1510–5. doi:10.1002/jsfa.5928.
  • Yoshino, K., K. Sakai, Y. Mizuha, A. Shimizuike, and S. Yamamoto. 2004. Peptic digestibility of raw and heat-coagulated hen’s egg white proteins at acidic pH range. International Journal of Food Sciences and Nutrition 55 (8):635–40. doi:10.1080/09637480412331350173.
  • Yousefi, R., L. Ferdowsi, Z. Tavaf, T. Sadeghian, A. M. Tamaddon, M. Moghtaderi, and Z. Pourpak. 2017. Evaluation of structure, chaperone-like activity and allergenicity of reduced glycated adduct of bovine β-casein. Protein and Peptide Letters 24 (1):46–55. doi:10.2174/0929866524666161121144025.
  • Yu, M., Y. Zhou, X. Wang, M. Xie, B. Zhang, H. Yu, and Z. Sun. 2021. Effect of ultrasonic pre-treatment on Ara h 1 in peanut sprouts. Ultrasonics Sonochemistry 75:105607. doi:10.1016/j.ultsonch.2021.105607.
  • Yu, W., D. M. H. Freeland, and K. C. Nadeau. 2016. Food allergy: Immune mechanisms, diagnosis and immunotherapy. Nature Reviews. Immunology 16 (12):751–65. doi:10.1038/nri.2016.111.
  • Yuan, F., I. Ahmed, L. Lv, Z. Li, Z. Li, H. Lin, H. Lin, J. Zhao, S. Tian, and J. Ma. 2018. Impacts of glycation and transglutaminase-catalyzed glycosylation with glucosamine on the conformational structure and allergenicity of bovine β-lactoglobulin. Food & Function 9 (7):3944–55. doi:10.1039/c8fo00909k.
  • 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.
  • Zaffran, V. D., S. Gupta, S. K. Sathe, and M. G. Roper. 2021. Effect of deglycosylation on immunoreactivity and in vitro pepsin digestibility of major cashew (Anacardium occidentale L.) allergen, Ana o 1. Journal of Food Science 86 (3):1144–52. doi:10.1111/1750-3841.15628.
  • Zhang, J., Y. Shen, J. Li, H. Li, and P. Si. 2020. Component-Resolved diagnostic study of egg allergy in northern Chinese children. BioMed Research International 2020:3831087. doi:10.1155/2020/3831087.
  • Zhang, M., Z. C. Tu, J. Liu, Y. M. Hu, H. Wang, J. H. Mao, and J. L. Li. 2021. The IgE/IgG binding capacity and structural changes of Alaska Pollock parvalbumin glycated with different reducing sugars. Journal of Food Biochemistry 45 (1):e13539. doi:10.1111/jfbc.13539.
  • Zhang, P., J. Gao, H. Che, W. Xue, and D. Yang. 2021. Molecular basis of IgE-mediated shrimp allergy and heat desensitization. Nutrients 13 (10):3397. doi:10.3390/nu13103397.
  • Zhang, Q., Y. Wang, and L. Fu. 2020. Dietary advanced glycation end-products: Perspectives linking food processing with health implications. Comprehensive Reviews in Food Science and Food Safety 19 (5):2559–87. doi:10.1111/1541-4337.12593.
  • Zhang, T., Y. Shi, Y. Zhao, G. Tang, B. Niu, and Q. Chen. 2018. Boiling and roasting treatment affecting the peanut allergenicity. Annals of Translational Medicine 6 (18):357. doi:10.21037/atm.2018.05.08.
  • Zhang, T., Y. Shi, Y. Zhao, J. Wang, M. Wang, B. Niu, and Q. Chen. 2019. Different thermal processing effects on peanut allergenicity. Journal of the Science of Food and Agriculture 99 (5):2321–8. doi:10.1002/jsfa.9430.
  • Zhang, W., Q. Zhu, T. Zhang, Q. Cai, and Q. Chen. 2016. Thermal processing effects on peanut allergen Ara h 2 allergenicity in mice and its antigenic epitope structure. Food Chemistry 212:657–62. doi:10.1016/j.foodchem.2016.06.036.
  • Zhang, Z., X. M. Li, Z. Li, and H. Lin. 2021. Investigation of glycated shrimp tropomyosin as a hypoallergen for potential immunotherapy. Food & Function 12 (6):2750–9. doi:10.1039/d0fo03039b.
  • Zhang, Z., X. M. Li, H. Xiao, A. Nowak-Wegrzyn, and P. Zhou. 2020. Insight into the allergenicity of shrimp tropomyosin glycated by functional oligosaccharides containing advanced glycation end products. Food Chemistry 302:125348. doi:10.1016/j.foodchem.2019.125348.
  • Zhang, Z., H. Xiao, and P. Zhou. 2019. Allergenicity suppression of tropomyosin from Exopalaemon modestus by glycation with saccharides of different molecular sizes. Food Chemistry 288:268–75. doi:10.1016/j.foodchem.2019.03.019.
  • Zhang, Z., H. Xiao, and P. Zhou. 2019. Glycation by saccharides of different molecular sizes affected the allergenicity of shrimp tropomyosin via epitope loss and the generation of advanced glycation end products. Food & Function 10 (11):7042–51. doi:10.1039/c9fo01547g.
  • Zhang, Z., H. Xiao, X. Zhang, and P. Zhou. 2019. Insight into the effects of deglycosylation and glycation of shrimp tropomyosin on in vivo allergenicity and mast cell function. Food & Function 10 (7):3934–41. doi:10.1039/c9fo00699k.
  • Zhao, Y. J., Q. F. Cai, T. C. Jin, L. J. Zhang, D. X. Fei, G. M. Liu, and M. J. Cao. 2017. Effect of Maillard reaction on the structural and immunological properties of recombinant silver carp parvalbumin. LWT 75:25–33. doi:10.1016/j.lwt.2016.08.049.

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