Exploration of Foods and Foodomics

Table 3. Summary of processing effects on food allergen structure and immunogenicity.

Food/Allergen	Processing method	Allergenicity outcome	Evidence type	MD insights	Reference
Peanut (Ara h 1, 2, 6)	Roasting	Increased—Maillard reaction stabilizes epitopes	In vitro (IgE-binding, SDS-PAGE)	RMSD increases confirm thermal destabilization	[44, 46]
Peanut (Ara h 1)	Boiling/Frying	Reduced—protein leaching and denaturation	In vitro (IgE-binding assays)	-	[46]
Peanut (Ara h 1)	Thermal denaturation	Reduced IgE-binding ability	In vitro (IgE-binding, SDS-PAGE)	-	[46]
Shrimp (tropomyosin)	Microwave/Cooking	Altered secondary structure; variable outcome	In vitro (immunoassay)	Turn structure reduction noted; β-sheet content increased with prolonged ultrasound treatment (FTIR)	[54, 73]
Kiwifruit (Act d 2)	Oscillating electric field	Reduced—α-helix/turn unfolding	In vitro	MD confirms α-helix/turn disruption	[57]
Cod parvalbumin (Gad m 1)	HHP + temperature	Structural unfolding achieved; allergenicity unchanged	Ex vivo (patient sera)	-	[60]
Silver carp protein	HHP	Secondary structure altered; allergenicity unchanged	In vitro (IgE-binding, structural)	-	[61]
Largemouth bass	HHP (400 MPa, 15 min)	A new 21 kDa allergenic band emerged	In vitro	SASA metrics explain epitope exposure variability	[59]
Soy (β-conglycinin, SPI)	HHP (400 MPa)	Epitope exposure increased, then decreased	In vitro (fluorescence)	MD shows aromatic residue exposure at 400 MPa	[55]
Crayfish (tropomyosin)	HHP + chlorogenic acid	Reduced—linear epitopes obscured	In vitro	-	[65]
Pompano fish (parvalbumin)	DPCD (15 MPa, 30 min, 50°C)	Reduced 39–41%—conformational epitope disruption	In vitro (ELISA, Western blot)	-	[66]
β-Lactoglobulin	MGO glycation	Variable—epitopes masked or revealed	In vitro	MD predicts glycation-induced epitope accessibility changes	[64]
Milk proteins	Enzymatic hydrolysis	Reduced—antigenic epitopes disrupted	In vitro	-	[68]
Pistachio	Steam roasting	Reduced IgE-binding and solubility	In vitro (competitive ELISA, Western blot)	-	[69]
Parvalbumin (fish)	Simulated gastric digestion	Partially resistant after 120 min	In vitro	MD models gastric enzyme interactions at the molecular level	[43, 45]
Cashew/Pistachio	Thermal processing	Dual effect—existing epitopes removed, new ones formed	In vitro (IgE-binding)	-	[49]

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DPCD: dense-phase carbon dioxide; HHP: high hydrostatic pressure; IgE: immunoglobulin E; MD: molecular dynamics; MGO: methylglyoxal; RMSD: root mean square deviation; SASA: solvent-accessible surface area; SPI: soy protein isolate.

Declarations

Acknowledgments

During the preparation of this work, the authors used PaperPal Advanced AI for grammar and clarity checking. Elicit for literature search, and Claude (Anthropic) for manuscript revision and structural reorganization. After using these tools, the authors reviewed and edited the content as needed and take full responsibility for the content of the publication.

Author contributions

PS: Conceptualization, Methodology, Supervision, Resources, Project administration, Formal analysis, Writing—review & editing, Visualization. YW: Investigation, Software, Writing—original draft, Visualization. VR: Supervision, Funding acquisition, Resources, Formal analysis, Project administration, Conceptualization. The authors have read and approved the submitted version.

Conflicts of interest

The authors declare no conflicts of interest in this manuscript.

Ethical approval

Not applicable.

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Availability of data and materials

As a narrative review of previously published literature, this study generated or analyzed no new data.

Funding

This work was supported by the Natural Sciences and Engineering Research Council of Canada (NSERC). The funder(s) had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.

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References

Sampson HA, Burks AW. Mechanisms of food allergy. Annu Rev Nutr. 1996;16:161–77. [DOI] [PubMed]

Sampson HA, O’Mahony L, Burks AW, Plaut M, Lack G, Akdis CA. Mechanisms of food allergy. J Allergy Clin Immunol. 2018;141:11–9. [DOI] [PubMed]

He S, Zhang H, Gao P. Actions of allergens and mediators in allergy. Mediators Inflamm. 2014;2014:207345. [DOI] [PubMed] [PMC]

Nosbaum A, Vocanson M, Rozieres A, Hennino A, Nicolas JF. Allergic and irritant contact dermatitis. Eur J Dermatol. 2009;19:325–32. [DOI] [PubMed]

Untersmayr E, Jensen-Jarolim E. Mechanisms of type I food allergy. Pharmacol Ther. 2006;112:787–98. [DOI] [PubMed]

Yang Y, He X, Li F, He S, Liu M, Li M, et al. Animal-derived food allergen: A review on the available crystal structure and new insights into structural epitope. Compr Rev Food Sci Food Saf. 2024;23:e13340. [DOI] [PubMed]

Yu W, Freeland DMH, Nadeau KC. Food allergy: immune mechanisms, diagnosis and immunotherapy. Nat Rev Immunol. 2016;16:751–65. [DOI] [PubMed] [PMC]

So T, Ito H, Hirata M, Ueda T, Imoto T. Contribution of conformational stability of hen lysozyme to induction of type 2 T-helper immune responses. Immunology. 2001;104:259–68. [DOI] [PubMed] [PMC]

Thomas K, Herouet-Guicheney C, Ladics G, Bannon G, Cockburn A, Crevel R, et al. Evaluating the effect of food processing on the potential human allergenicity of novel proteins: international workshop report. Food Chem Toxicol. 2007;45:1116–22. [DOI] [PubMed]

10.

Bøgh KL, Madsen CB. Food Allergens: Is There a Correlation between Stability to Digestion and Allergenicity? Crit Rev Food Sci Nutr. 2016;56:1545–67. [DOI] [PubMed]

11.

Jenkins JA, Breiteneder H, Mills EN. Evolutionary distance from human homologs reflects allergenicity of animal food proteins. J Allergy Clin Immunol. 2007;120:1399–405. [DOI] [PubMed]

12.

Tsai CL, Perng K, Hou YC, Shen CJ, Chen IN, Chen YT. Effect of species, muscle location, food processing and refrigerated storage on the fish allergens, tropomyosin and parvalbumin. Food Chem. 2023;402:134479. [DOI] [PubMed]

13.

Vanga SK, Raghavan V. Processing effects on tree nut allergens: A review. Crit Rev Food Sci Nutr. 2017;57:3794–806. [DOI] [PubMed]

14.

Bannon GA. What makes a food protein an allergen? Curr Allergy Asthma Rep. 2004;4:43–6. [DOI] [PubMed]

15.

Dong X. Effects of Ultrasound and Microwave Processing on Physicochemical and Allergenic Properties of Shrimp [dissertation]. McGill University; 2020.

16.

Zeng J, Ma F, Zhai L, Du C, Zhao J, Li Z, et al. Recent advance in sesame allergens: Influence of food processing and their detection methods. Food Chem. 2024;448:139058. [DOI] [PubMed]

17.

Shoji M, Adachi R, Akiyama H. Japanese Food Allergen Labeling Regulation: An Update. J AOAC Int. 2018;101:8–13. [DOI] [PubMed]

18.

Stone WE, Yeung JM. Principles and Practices for Allergen Management and Control in Processing. In: Allergen Management in the Food Industry. Hoboken: Wiley; 2010. pp. 145–65. [DOI]

19.

Reese I, Holzhauser T, Schnadt S, Dölle S, Kleine-Tebbe J, Raithel M, et al. Allergen and allergy risk assessment, allergen management, and gaps in the European Food Information Regulation (FIR): Are allergic consumers adequately protected by current statutory food safety and labelling regulations? Allergo J Int. 2015;24:180–4. [DOI] [PubMed] [PMC]

20.

Mills EN, Valovirta E, Madsen C, Taylor SL, Vieths S, Anklam E, et al. Information provision for allergic consumers--where are we going with food allergen labelling? Allergy. 2004;59:1262–8. [DOI] [PubMed]

21.

Ghaly AE, Ramakrishnan VV, Brooks MS, Budge SM, Dave D. Fish Processing Wastes as a Potential Source of Proteins, Amino Acids and Oils: A Critical Review. J Microbial Biochem Technol. 2013;5:107–29. [DOI]

22.

Vanga SK, Singh A, Raghavan V. Review of conventional and novel food processing methods on food allergens. Crit Rev Food Sci Nutr. 2017;57:2077–94. [DOI] [PubMed]

23.

Verhoeckx KCM, Vissers YM, Baumert JL, Faludi R, Feys M, Flanagan S, et al. Food processing and allergenicity. Food Chem Toxicol. 2015;80:223–40. [DOI] [PubMed]

24.

Jiang X, Rao Q. Effect of Processing on Fish Protein Antigenicity and Allergenicity. Foods. 2021;10:969. [DOI] [PubMed] [PMC]

25.

Elsayed S, Aas K, Sletten K, Johansson SG. Tryptic cleavage of a homogeneous cod fish allergen and isolation of two active polypeptide fragments. Immunochemistry. 1972;9:647–61. [DOI] [PubMed]

26.

Dijkema D, Emons JAM, Van de Ven AAJM, Oude Elberink JNG. Fish Allergy: Fishing for Novel Diagnostic and Therapeutic Options. Clin Rev Allergy Immunol. 2022;62:64–71. [DOI] [PubMed] [PMC]

27.

Kuehn A, Swoboda I, Arumugam K, Hilger C, Hentges F. Fish allergens at a glance: variable allergenicity of parvalbumins, the major fish allergens. Front Immunol. 2014;5:179. [DOI] [PubMed] [PMC]

28.

Houhoula D, Dimitriou P, Mengjezi G, Kyrana V, Lougovois V. Quantification of parvalbumin in commercially important Mediterranean seafood species using real time PCR. Czech J Food Sci. 2015;33:143–7. [DOI]

29.

Sicherer SH, Sampson HA. Food allergy: A review and update on epidemiology, pathogenesis, diagnosis, prevention, and management. J Allergy Clin Immunol. 2018;141:41–58. [DOI] [PubMed]

30.

Suther C, Moore MD, Beigelman A, Zhou Y. The Gut Microbiome and the Big Eight. Nutrients. 2020;12:3728. [DOI] [PubMed] [PMC]

31.

Kris-Etherton PM, Harris WS, Appel LJ; American Heart Association. Nutrition Committee. Fish consumption, fish oil, omega-3 fatty acids, and cardiovascular disease. Circulation. 2002;106:2747–57. [DOI] [PubMed]

32.

Kobayashi A, Tanaka H, Hamada Y, Ishizaki S, Nagashima Y, Shiomi K. Comparison of allergenicity and allergens between fish white and dark muscles. Allergy. 2006;61:357–63. [DOI] [PubMed]

33.

Kuehn A, Hilger C, Lehners-Weber C, Codreanu-Morel F, Morisset M, Metz-Favre C, et al. Identification of enolases and aldolases as important fish allergens in cod, salmon and tuna: component resolved diagnosis using parvalbumin and the new allergens. Clin Exp Allergy. 2013;43:811–22. [DOI] [PubMed]

34.

Sun Y, Luo Y, Chen J, Liu X, Gao J, Xie Y, et al. Fish Allergy: A Review of Clinical Characteristics, Mechanism, Allergens, Epitopes, and Cross-Reactivity. ACS Food Sci Technol. 2024;4:304–15. [DOI]

35.

González-Fernández J, Veleiro B, Daschner A, Cuéllar C. Are fish tropomyosins allergens? Ann Allergy Asthma Immunol. 2016;116:74–6.e5. [DOI] [PubMed]

36.

Liu R, Holck AL, Yang E, Liu C, Xue W. Tropomyosin from tilapia (Oreochromis mossambicus) as an allergen. Clin Exp Allergy. 2013;43:365–77. [DOI] [PubMed]

37.

González-Fernández J, Alguacil-Guillén M, Cuéllar C, Daschner A. Possible Allergenic Role of Tropomyosin in Patients with Adverse Reactions after Fish Intake. Immunol Invest. 2018;47:416–29. [DOI] [PubMed]

38.

Faber MA, Pascal M, El Kharbouchi O, Sabato V, Hagendorens MM, Decuyper II, et al. Shellfish allergens: tropomyosin and beyond. Allergy. 2017;72:842–8. [DOI] [PubMed]

39.

Ruethers T, Taki AC, Karnaneedi S, Nie S, Kalic T, Dai D, et al. Expanding the allergen repertoire of salmon and catfish. Allergy. 2021;76:1443–53. [DOI] [PubMed]

40.

Awuah GB, Ramaswamy HS, Economides A. Thermal processing and quality: Principles and overview. Chem Eng Process. 2007;46:584–602. [DOI]

41.

Boye J, Ma CY, Harwalkar V. Thermal Denaturation and Coagulation of Proteins. In: Damodaran S, Paraf A, editors. Food Proteins and their Applications. 1st Edition. CRC Press; 1997. pp. 25–56. [DOI]

42.

Davis PJ, Williams SC. Protein modification by thermal processing. Allergy. 1998;53:102–5. [DOI] [PubMed]

43.

Astwood JD, Leach JN, Fuchs RL. Stability of food allergens to digestion in vitro. Nat Biotechnol. 1996;14:1269–73. [DOI] [PubMed]

44.

Cabanillas B, Novak N. Effects of daily food processing on allergenicity. Crit Rev Food Sci Nutr. 2019;59:31–42. [DOI] [PubMed]

45.

Koidl L, Gentile SA, Untersmayr E. Allergen Stability in Food Allergy: A Clinician’s Perspective. Curr Allergy Asthma Rep. 2023;23:601–12. [DOI] [PubMed] [PMC]

46.

Meng S, Li J, Chang S, Maleki SJ. Quantitative and kinetic analyses of peanut allergens as affected by food processing. Food Chem X. 2019;1:100004. [DOI] [PubMed] [PMC]

47.

Villa C, Costa J, Mafra I. Sesame as a source of food allergens: clinical relevance, molecular characterization, cross-reactivity, stability toward processing and detection strategies. Crit Rev Food Sci Nutr. 2024;64:4746–62. [DOI] [PubMed]

48.

Sanchiz A, Cuadrado C, Dieguez MC, Ballesteros I, Rodríguez J, Crespo JF, et al. Thermal processing effects on the IgE-reactivity of cashew and pistachio. Food Chem. 2018;245:595–602. [DOI] [PubMed]

49.

Cuadrado C, Cheng H, Sanchiz A, Ballesteros I, Easson M, Grimm CC, et al. Influence of enzymatic hydrolysis on the allergenic reactivity of processed cashew and pistachio. Food Chem. 2018;241:372–9. [DOI] [PubMed]

50.

Khan MU, Lin H, Ahmed I, Chen Y, Zhao J, Hang T, et al. Whey allergens: Influence of nonthermal processing treatments and their detection methods. Compr Rev Food Sci Food Saf. 2021;20:4480–510. [DOI] [PubMed]

51.

Khan MU, Ahmed I, Lin H, Li Z, Costa J, Mafra I, et al. Potential efficacy of processing technologies for mitigating crustacean allergenicity. Crit Rev Food Sci Nutr. 2019;59:2807–30. [DOI] [PubMed]

52.

Smith A, Raghavan V. Molecular Dynamics Simulation of the Thermal Treatment of the Ara h 6 Peanut Protein. Processes. 2025;13:434. [DOI]

53.

Smith A, Raghavan V. Statistical Analysis of the Effect of Simulation Time on the Results of Molecular Dynamics Studies of Food Proteins: A Study of the Ara h 6 Peanut Protein. Processes. 2025;13:581. [DOI]

54.

Dong X, Wang J, Raghavan V. Impact of microwave processing on the secondary structure, in-vitro protein digestibility and allergenicity of shrimp (Litopenaeus vannamei) proteins. Food Chem. 2021;337:127811. [DOI]

55.

Dehnad D, Emadzadeh B, Ghorani B, Assadpour E, Yang N, Jafari SM. The influence of high hydrostatic pressure on different properties of legume proteins with an emphasis on soy proteins; a comprehensive review. Food Hydrocoll. 2024;146:109188. [DOI]

56.

Dong X. Impacts of Advanced Processing Techniques on the Physicochemical, Structural, and Allergenic Properties of Atlantic Cod [dissertation]. Montreal: McGill University; 2024.

57.

Wang J, Wang J, Kranthi Vanga S, Raghavan V. Influence of high-intensity ultrasound on the IgE binding capacity of Act d 2 allergen, secondary structure, and In-vitro digestibility of kiwifruit proteins. Ultrason Sonochem. 2021;71:105409. [DOI]

58.

Yaghoubi Naei V, Sankian M, Moghadam M, Farshidi N, Ayati SH, Hamid F, et al. The Influence of Gamma Radiation Processing on the Allergenicity of Main Pistachio Allergens. Rep Biochem Mol Biol. 2019;7:150–5. [PubMed] [PMC]

59.

Liu CY, Tao S, Liu R, Chen FS, Xue WT. Is high pressure treatment able to modify the allergenicity of the largemouth bass allergens? High Pressure Res. 2012;32:551–6. [DOI]

60.

Somkuti J, Bublin M, Breiteneder H, Smeller L. Pressure-temperature stability, Ca2+ binding, and pressure-temperature phase diagram of cod parvalbumin: Gad m 1. Biochemistry. 2012;51:5903–11. [DOI] [PubMed]

61.

Liu R, Xue W. High-pressure treatment with silver carp (Hypophthalmichthys molitrix) protein and its allergic analysis. High Pressure Res. 2010;30:438–42. [DOI]

62.

Ma X, Liang R, Xing Q, Lozano-Ojalvo D. Can food processing produce hypoallergenic egg? J Food Sci. 2020;85:2635–44. [DOI] [PubMed]

63.

Rahaman T, Vasiljevic T, Ramchandran L. Effect of processing on conformational changes of food proteins related to allergenicity. Trends Food Sci Technol. 2016;49:24–34. [DOI]

64.

Ge X, Qu X, Xie C, Zang J, Wu W, Lv L. The influence on the structure and allergenicity of milk β-lactoglobulin by methylglyoxal during thermal processing. Food Res Int. 2024;196:115043. [DOI] [PubMed]

65.

Liu G, Luo J, Xiong W, Meng T, Zhang X, Liu Y, et al. Chlorogenic acid alleviates crayfish allergy by altering the structure of crayfish tropomyosin and upregulating TLR8. Food Chem. 2024;443:138614. [DOI] [PubMed]

66.

Qiu H, Duan W, Hu W, Wei S, Liu Y, Sun Q, et al. Insight into the allergenicity and structure changes of parvalbumin from Trachinotus ovatus induced by dense-phase carbon dioxide. Int J Biol Macromol. 2024;260:129582. [DOI] [PubMed]

67.

Lv L, Qu X, Yang N, Ahmed I. The conformational structural change of β-lactoglobulin via acrolein treatment reduced the allergenicity. Food Chem X. 2021;10:100120. [DOI] [PubMed] [PMC]

68.

Zeng J, Wang Q, Yi H, Chen C, Du C, Xiong G, et al. Recent insights in cow’s milk protein allergy: Clinical relevance, allergen features, and influences of food processing. Trends Food Sci Technol. 2025;156:104830. [DOI]

69.

Noorbakhsh R, Mortazavi SA, Sankian M, Shahidi F, Maleki SJ, Nasiraii LR, et al. Influence of processing on the allergenic properties of pistachio nut assessed in vitro. J Agric Food Chem. 2010;58:10231–5. [DOI] [PubMed]

70.

Zhang Y, Wu Z, Li K, Li X, Yang A, Tong P, et al. Allergenicity assessment on thermally processed peanut influenced by extraction and assessment methods. Food Chem. 2019;281:130–9. [DOI] [PubMed]

71.

Yang J, Kumar N, Kuang H, Song J, Li Y. Changes of digestive stability and potential allergenicity of high hydrostatic pressure-treated ovalbumin during in vitro digestion. Food Chem. 2025;473:142962. [DOI] [PubMed]

72.

Zhu Y, Vanga SK, Wang J, Raghavan V. Impact of food processing on the structural and allergenic properties of egg white. Trends Food Sci Technol. 2018;78:188–96. [DOI]

73.

Dong X, Wang J, Raghavan V. Effects of high-intensity ultrasound processing on the physiochemical and allergenic properties of shrimp. Innov Food Sci Emerg Technol. 2020;65:102441. [DOI]

74.

Smith A. Effect of Simulation Time on Molecular Dynamics Simulations of Food Proteins: A Study of the Ara H6 Peanut Protein [dissertation]. McGill University; 2023.

75.

Dong X, Wang J, Raghavan V. Critical reviews and recent advances of novel non-thermal processing techniques on the modification of food allergens. Crit Rev Food Sci Nutr. 2021;61:196–210. [DOI] [PubMed]

76.

Liu W, Yang Q, Wang Z, Wang J, Min F, Yuan J, et al. Quantitative food allergen risk assessment: Evolving concepts, modern approaches, and industry implications. Compr Rev Food Sci Food Saf. 2025;24:e70132. [DOI] [PubMed]

77.

Barshow SM, Kulis MD, Burks AW, Kim EH. Mechanisms of oral immunotherapy. Clin Exp Allergy. 2021;51:527–35. [DOI] [PubMed] [PMC]

78.

Dong X, Raghavan V. A comprehensive overview of emerging processing techniques and detection methods for seafood allergens. Compr Rev Food Sci Food Saf. 2022;21:3540–57. [DOI] [PubMed]

79.

Maleki SJ, Kopper RA, Shin DS, Park CW, Compadre CM, Sampson H, et al. Structure of the major peanut allergen Ara h 1 may protect IgE-binding epitopes from degradation. J Immunol. 2000;164:5844–9. [DOI] [PubMed]

80.

Chapman M, Pomés A, Aalberse R. Molecular Biology of Allergens: Structure and Immune Recognition. In: Pawankar R, Holgate ST, Rosenwasser LJ, editors. Allergy Frontiers: Epigenetics, Allergens and Risk Factors. Vol. 1. Tokyo: Springer; 2009. pp. 265–89. [DOI]

81.

Wang T, Zhang L, Raghavan V, Liu Y, Wang J. Analysis of epitopes and structural responses in egg allergen Gal d 1 using bioinformatic tools and molecular dynamics simulation. Curr Res Food Sci. 2025;10:101048. [DOI] [PubMed] [PMC]

82.

Polenta GA. Towards the Quantitative Management of Food Allergens in the Food Industry. Curr Food Sci Technol Rep. 2023;1:99–107. [DOI]