References
- Alves, R. C., Pimentel, F. B., Nouws, H. P. A., Marques, R. C. B., González-García, M. B., Oliveira, M. B. P. P., & Delerue-Matos, C. (2015). Detection of Ara h 1 (a major peanut allergen) in food using an electrochemical gold nanoparticle-coated screen-printed immunosensor. Biosensors and Bioelectronics, 64, 19–24. doi: https://doi.org/10.1016/j.bios.2014.08.026
- Beyer, K., Morrowa, E., Li, X.-M., Bardina, L., Bannon, G. A., Burks, A. W., & Sampson, H. A. (2001). Effects of cooking methods on peanut allergenicity. Journal of Allergy and Clinical Immunology, 107(6), 1077–1081. doi: https://doi.org/10.1067/mai.2001.115480
- Blanc, F., Vissers, Y. M., Adel-Patient, K., Rigby, N. M., Mackie, A. R., Gunning, A. P., … Mills, E. N. C. (2011). Boiling peanut Ara h 1 results in the formation of aggregates with reduced allergenicity. Molecular Nutrition & Food Research, 55(12), 1887–1894. doi: https://doi.org/10.1002/mnfr.201100251
- Bunyavanich, S., Rifas-Shiman, S. L., Platts-Mills, T. A. E., Workman, L., Sordillo, J. E., Gillman, M. W., … Litonjua, A. A. (2014). Peanut allergy prevalence among school-age children in a US cohort not selected for any disease. Journal of Allergy and Clinical Immunology, 134(3), 753–755. doi: https://doi.org/10.1016/j.jaci.2014.05.050
- Burks, A. W., Wood, R. A., Jones, S. M., Sicherer, S. H., Fleischer, D. M., Scurlock, A. M., … Sampson, H. A. (2015). Sublingual immunotherapy for peanut allergy: Long-term follow-up of a randomized multicenter trial. Journal of Allergy and Clinical Immunology, 135(5), 1240–1248.e3. doi: https://doi.org/10.1016/j.jaci.2014.12.1917
- Chen, Y., Tu, Z., Wang, H., Zhang, L., Sha, X., Pang, J., … Yang, W. (2016). Glycation of β-lactoglobulin under dynamic high pressure microfluidization treatment: Effects on IgE-binding capacity and conformation. Food Research International, 89, 882–888. doi: https://doi.org/10.1016/j.foodres.2016.10.020
- Du Toit, G., Katz, Y., Sasieni, P., Mesher, D., Maleki, S. J., Fisher, H. R., … Lack, G. (2008). Early consumption of peanuts in infancy is associated with a low prevalence of peanut allergy. Journal of Allergy and Clinical Immunology, 122(5), 984–991. doi: https://doi.org/10.1016/j.jaci.2008.08.039
- Guillon, B., Bernard, H., Drumare, M.-F., Hazebrouck, S., & Adel-Patient, K. (2016). Heat processing of peanut seed enhances the sensitization potential of the major peanut allergen Ara h 6. Molecular Nutrition & Food Research, 60(12), 2722–2735. doi: https://doi.org/10.1002/mnfr.201500923
- Hurlburt, B., McBride, J., Nesbit, J., Ruan, S., & Maleki, S. (2014). Purification of recombinant peanut allergen Ara h 1 and comparison of IgE binding to the natural protein. Foods (basel, Switzerland), 3(4), 642–657. doi: https://doi.org/10.3390/foods3040642
- Lee, A. J., Thalayasingam, M., & Lee, B. W. (2013). Food allergy in Asia: How does it compare? Asia Pacific Allergy, 3(1), 3. doi: https://doi.org/10.5415/apallergy.2013.3.1.3
- Liu, C.-Y., Tao, S., Xue, J.-Y., Zhang, H., Xue, W.-T., & Chen, F.-S. (2012). Identification and purification of a novel fish allergen from largemouth bass (Micropterus salmoides). Food and Agricultural Immunology, 25(1), 70–81. doi: https://doi.org/10.1080/09540105.2012.745122
- Long, F., Yang, X., Sun, J., Zhong, Q., Wei, J., Qu, P., & Yue, T. (2016). Effects of combined high pressure and thermal treatment on the allergenic potential of peanut in a mouse model of allergy. Innovative Food Science & Emerging Technologies, 35, 133–138. doi: https://doi.org/10.1016/j.ifset.2016.04.003
- Małgorzata, W., Konrad, P. M., & Zieliński, H. (2016). Effect of roasting time of buckwheat groats on the formation of Maillard reaction products and antioxidant capacity. Food Chemistry, 196, 355–358. doi: https://doi.org/10.1016/j.foodchem.2015.09.064
- Mattison, C. P., Dinter, J., Berberich, M. J., Chung, S.-Y., Reed, S. S., Le Gall, S., & Grimm, C. C. (2015). In vitro evaluation of digestive and endolysosomal enzymes to cleave CML-modified Ara h 1 peptides. Food Science & Nutrition, 3(4), 273–283. doi: https://doi.org/10.1002/fsn3.215
- Mills, E. N. C., Sancho, A. I., Rigby, N. M., Jenkins, J. A., & Mackie, A. R. (2009). Impact of food processing on the structural and allergenic properties of food allergens. Molecular Nutrition & Food Research, 53(8), 963–969. doi: https://doi.org/10.1002/mnfr.200800236
- Moghaddam, A. E., Hillson, W. R., Noti, M., Gartlan, K. H., Johnson, S., Thomas, B., … Sattentau, Q. J. (2014). Dry roasting enhances peanut-induced allergic sensitization across mucosal and cutaneous routes in mice. Journal of Allergy and Clinical Immunology, 134(6), 1453–1456. doi: https://doi.org/10.1016/j.jaci.2014.07.032
- Mondoulet, L., Paty, E., Drumare, M. F., AH-Leung, S., Scheinmann, P., Willemot, R. M., … Bernard, H. (2005). Influence of thermal processing on the allergenicity of peanut proteins. Journal of Agricultural and Food Chemistry, 53, 4547–4553 doi: https://doi.org/10.1021/jf050091p
- Niess, J.-H., Vissers, Y. M., Blanc, F., Skov, P. S., Johnson, P. E., Rigby, N. M., … Adel-Patient, K. (2011). Effect of heating and glycation on the allergenicity of 2S albumins (Ara h 2/6) from peanut. PLoS ONE, 6(8), e23998. doi: https://doi.org/10.1371/journal.pone.0023998
- Peng, X., Ren, C., & Guo, S. (2016). Particle formation and gelation of soymilk: Effect of heat. Trends in Food Science & Technology, 54, 138–147. doi: https://doi.org/10.1016/j.tifs.2016.06.005
- Perez-Riverol, A., Justo-Jacomini, D., Zollner, R., & Brochetto-Braga, M. (2015). Facing hymenoptera venom allergy: From natural to recombinant allergens. Toxins, 7(7), 2551–2570. doi: https://doi.org/10.3390/toxins7072551
- Rahaman, T., Vasiljevic, T., & Ramchandran, L. (2016). Effect of processing on conformational changes of food proteins related to allergenicity. Trends in Food Science & Technology, 49, 24–34. doi: https://doi.org/10.1016/j.tifs.2016.01.001
- Ramesh, M., Yuenyongviwat, A., Konstantinou, G. N., Lieberman, J., Pascal, M., Masilamani, M., & Sampson, H. A. (2016). Peanut T-cell epitope discovery: Ara h 1. Journal of Allergy and Clinical Immunology, 137(6), 1764–1771.e4. doi: https://doi.org/10.1016/j.jaci.2015.12.1327
- Rao, H., Tian, Y., Tao, S., Tang, J., Li, X., & Xue, W.-T. (2016). Key factors affecting the immunoreactivity of roasted and boiled peanuts: Temperature and water. LWT – Food Science and Technology, 72, 492–500. doi: https://doi.org/10.1016/j.lwt.2016.05.014
- Satitsuksanoa, P., Głobińska, A., Jansen, K., van de Veen, W., & Akdis, M. (2018). Modified allergens for immunotherapy. Current Allergy and Asthma Reports, 18(2), 3, doi: https://doi.org/10.1007/s11882-018-0766-x
- Sayers, R. L., Johnson, P. E., Marsh, J. T., Barran, P., Brown, H., & Mills, E. N. C. (2016). The effect of thermal processing on the behaviour of peanut allergen peptide targets used in multiple reaction monitoring mass spectrometry experiments. The Analyst, 141(13), 4130–4141. doi: https://doi.org/10.1039/c6an00359a
- Schmitt, D. A., Nesbit, J. B., Hurlburt, B. K., Cheng, H., & Maleki, S. J. (2010). Processing can alter the properties of peanut extract preparations. Journal of Agricultural and Food Chemistry, 58(2), 1138–1143. doi: https://doi.org/10.1021/jf902694j
- Shen, L.-L., Zhu, Q.-Q., Huang, F.-W., Xu, H., Wu, X.-L., Xiao, H.-F., … Liu, Z.-G. (2015). Effect of heat treatment on structure and immunogenicity of recombinant peanut protein Ara h 2.01. LWT – Food Science and Technology, 60(2), 964–969. doi: https://doi.org/10.1016/j.lwt.2014.10.044
- Sicherer, S. H., & Sampson, H. A. (2014). Food allergy: Epidemiology, pathogenesis, diagnosis, and treatment. Journal of Allergy and Clinical Immunology, 133(2), 291–307.e5. doi:10.1016/j.jaci.2013.11.020.
- Starkl, P. (2011). Heating affects structure, enterocyte adsorption and signalling, as well as immunogenicity of the peanut allergen Ara h 2. The Open Allergy Journal, 4(1), 24–34. doi: https://doi.org/10.2174/1874838401104010024
- Teodorowicz, M., Fiedorowicz, E., Kostyra, H., Wichers, H., & Kostyra, E. (2013). Effect of Maillard reaction on biochemical properties of peanut 7S globulin (Ara h 1) and its interaction with a human colon cancer cell line (Caco-2). European Journal of Nutrition, 52(8), 1927–1938. doi: https://doi.org/10.1007/s00394-013-0494-x
- Valenta, R., Campana, R., Focke-Tejkl, M., & Niederberger, V. (2016). Vaccine development for allergen-specific immunotherapy based on recombinant allergens and synthetic allergen peptides: Lessons from the past and novel mechanisms of action for the future. Journal of Allergy and Clinical Immunology, 137(2), 351–357. doi: https://doi.org/10.1016/j.jaci.2015.12.1299
- Vissers, Y. M., Iwan, M., Adel-Patient, K., Stahl Skov, P., Rigby, N. M., Johnson, P. E., … Wichers, H. J. (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 & Experimental Allergy, 41(11), 1631–1642. doi: https://doi.org/10.1111/j.1365-2222.2011.03830.x
- Wolz, M., & Kulozik, U. (2015). Thermal denaturation kinetics of whey proteins at high protein concentrations. International Dairy Journal, 49, 95–101. doi: https://doi.org/10.1016/j.idairyj.2015.05.008
- Wu, Z., Yan, F., Wei, X., Li, X., Tong, P., Yang, A., … Chen, H. (2015). Purification and recombinant expression of major peanut allergen Ara h 1. Preparative Biochemistry and Biotechnology, 45(5), 438–446. doi: https://doi.org/10.1080/10826068.2014.940972