Cited by 37

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

Characterization of physicochemical and immunogenic properties of allergenic proteins altered by food processing: a review

Zhou, Enning, Li, Qiangqiang, Zhu, Dan, Chen, Gang, Wu, Liming·2024·Food Science and Human Wellness

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.26599/fshw.2022.9250095

Cites

2 of 2 references verified0 citation errors · 0 not checkable

Statistics

Figures

Image 1
CC-BY-NC-ND · From the PDF
Figure 1 Number of publications and citations identified in the literature survey (2007 to mid-2022) on Web of Science with 'food' AND 'allergen' in the topic (A). The specific foods studied in the retrieved articles published from 2007 to mid-2022 (B).
Figure 1 Number of publications and citations identified in the literature survey (2007 to mid-2022) on Web of Science with 'food' AND 'allergen' in the topic (A). The specific foods studied in the retrieved articles published from 2007 to mid-2022 (B).CC-BY-NC-ND · From the PDF
Figure 2 The sensitization mechanism of a food allergen and the desensitization mechanism of an allergen-polyphenol copolymer during an IgE-mediated allergy reaction.
Figure 2 The sensitization mechanism of a food allergen and the desensitization mechanism of an allergen-polyphenol copolymer during an IgE-mediated allergy reaction.CC-BY-NC-ND · From the PDF
Figure 3 Applicability of different processing techniques to various foods for allergenicity reduction. A checkmark indicates a valid effect on allergenicity reduction; an x indicates an invalid effect on allergenicity reduction.
Figure 3 Applicability of different processing techniques to various foods for allergenicity reduction. A checkmark indicates a valid effect on allergenicity reduction; an x indicates an invalid effect on allergenicity reduction.CC-BY-NC-ND · From the PDF

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Show all 2 references

Research works printed but not linked: 135

  1. R. Valenta. Food allergies: the basics. 2015, 148(6): 1120-1131. · DOI · Paper page
  2. A. Cianferoni. Non-IgE mediated food allergy. 2020, 16(2): 95-105. · DOI
  3. T.W. Jimenez-Rodriguez. Anaphylaxis in the 21 st century: phenotypes, endotypes, and biomarkers. 2018, 11: 121-142. · DOI
  4. C. Kanagaratham. IgE and IgG antibodies as regulators of mast cell and basophil functions in food allergy. 2020, 11: 603050. · DOI
  5. J.P. Lopes. Food allergy: epidemiology, pathogenesis, diagnosis, prevention, and treatment. 2020, 66: 57-64. · DOI
  6. J. Costa. Are physicochemical properties shaping the allergenic potency of plant allergens?. 2022, 62(1): 37-63. · DOI
  7. J. Costa. Are physicochemical properties shaping the allergenic potency of animal allergens?. 2022, 62(1): 1-36. · DOI
  8. A. Cavazza. A spotlight on analytical prospects in food allergens: from emerging allergens and novel foods to bioplastics and plant-based sustainable food contact materials. 2022, 388: 132951. · DOI
  9. Y. Zhang. Effects of heating, autoclaving and ultra-high pressure on the solubility, immunoreactivity and structure of major allergens in egg. 2017 · DOI
  10. S.J. Maleki. The effects of roasting on the allergenic properties of peanut proteins. 2000, 106(4): 763-768. · DOI
  11. F.J. Moreno. Gastrointestinal digestion of food allergens:effect on their allergenicity. 2007, 61(1): 50-60. · DOI
  12. K.C.M. Verhoeckx. Food processing and allergenicity. 2015, 80: 223-240. · DOI · Paper page
  13. S.K. Vanga. Review of conventional and novel food processing methods on food allergens. 2017, 57(10): 2077-2094. · DOI
  14. T. Rahaman. Effect of processing on conformational changes of food proteins related to allergenicity. 2016, 49: 24-34. · DOI
  15. F.G. Chizoba Ekezie. Effects of nonthermal food processing technologies on food allergens: a review of recent research advances. 2018, 74: 12-25. · DOI
  16. B. Cabanillas. Effects of daily food processing on allergenicity. 2019, 59(1): 31-42. · DOI
  17. X. Dong. Critical reviews and recent advances of novel non-thermal processing techniques on the modification of food allergens. 2021, 61(2): 196-210. · DOI
  18. N. Stănciuc. Structural and antigenic properties of thermally treated gluten proteins. 2018, 267: 43-51. · DOI
  19. B. Tao. Extended boiling of peanut progressively reduces IgE allergenicity while retaining T cell reactivity. 2016, 46(7): 1004-1014. · DOI
  20. B.X. Deng. Using short-wave infrared radiation to improve aqueous enzymatic extraction of peanut oil: evaluation of peanut cotyledon microstructure and oil quality. 2018, 120(2). · DOI
  21. S.J. Maleki. The major peanut allergen, Ara h 2, functions as a trypsin inhibitor, and roasting enhances this function. 2003, 112(1): 190-195. · DOI
  22. S. Jiang. Effect of different thermal processing treatments on allergenicity of walnut proteins. 2018, 39: 94-99. · DOI
  23. G.M. Liu. Effects of boiling on the IgE-binding properties of tropomyosin of shrimp ( Litopenaeus vannamei ). 2010, 75(1): T1-T5. · DOI
  24. M. Besler. Stability of food allergens and allergenicity of processed foods. 2001, 756(1): 207-228. · DOI
  25. S. Dhakal. Effect of high pressure processing on the immunoreactivity of almond milk. 2014, 62: 215-222. · DOI
  26. T. Jacob. Food processing does not abolish the allergenicity of the carrot allergen Dau c 1: influence of pH, temperature, and the food matrix. 2020, 64(18): 2000334. · DOI
  27. J. Wang. Effect of microwave processing on the nutritional properties and allergenic potential of kiwifruit. 2022, 401: 134189. · DOI
  28. X. Dong. Impact of microwave processing on the secondary structure, in-vitro protein digestibility and allergenicity of shrimp( Litopenaeus vannamei ) proteins. 2021, 337: 127811. · DOI
  29. J. Leszczynska. The effect of microwave treatment on the immunoreactivity of gliadin and wheat flour. 2003, 217: 387-391. · DOI
  30. K.S. Varghese. Technology, applications and modelling of ohmic heating: a review. 2014, 51(10): 2304-2317. · DOI
  31. H. Jaeger. Opinion on the use of ohmic heating for the treatment of foods. 2016, 55: 84-97. · DOI
  32. R.N. Pereira. Influence of ohmic heating on the structural and immunoreactive properties of soybean proteins. 2021, 148: 111710. · DOI
  33. R.N. Pereira. Effects of ohmic heating on the immunoreactivity of β -lactoglobulin a relationship towards structural aspects. 2020, 11(5): 4002-4013. · DOI
  34. S. Naik. Ultrasonic treatment: a cohort review on bioactive compounds, allergens and physico-chemical properties of food. 2021, 4: 470-477. · DOI
  35. Z. Zhang. Conformation stability, in vitro digestibility and allergenicity of tropomyosin from shrimp ( Exopalaemon modestus ) as affected by high intensity ultrasound. 2017, 245: 997-1009. · DOI
  36. M. Yu. Preparation of resveratrol-enriched and poor allergic protein peanut sprout from ultrasound treated peanut seeds. 2016, 28: 334-340. · DOI
  37. H. Li. Reduction of major peanut allergens Ara h 1 and Ara h 2, in roasted peanuts by ultrasound assisted enzymatic treatment. 2013, 141(2): 762-768. · DOI
  38. X. Dong. Effects of high-intensity ultrasound processing on the physiochemical and allergenic properties of shrimp. 2020, 65: 102441. · DOI
  39. J. Wang. Influence of high-intensity ultrasound on the IgE binding capacity of Act d 2 allergen, secondary structure, and in-vitro digestibility of kiwifruit proteins. 2021, 71: 105409. · DOI
  40. R. Meyer-Pittroff. Specific immuno-modulation and therapy by means of high pressure treated allergens. 2007, 27(1): 63-67. · DOI
  41. A. Fernández. IgE binding capacity of apple allergens preserved after high pressure treatment. 2009, 29(4): 705-712. · DOI
  42. F.A. Husband. High-pressure treatment reduces the immunoreactivity of the major allergens in apple and celeriac. 2011, 55(7): 1087-1095. · DOI
  43. N. Kleber. Antigenic response of bovine β -lactoglobulin influenced by ultra-high pressure treatment and temperature. 2007, 8(1): 39-45. · DOI
  44. K.J. Hong. Aspergillus oryzae GB-107 fermentation improves nutritional quality of food soybeans and feed soybean meals. 2004, 7(4): 430-435. · DOI · Paper page
  45. Y.S. Song. Immunoreactivity reduction of soybean meal by fermentation, effect on amino acid composition and antigenicity of commercial soy products. 2008, 108(2): 571-581. · DOI
  46. A. Yang. Degradation of major allergens and allergenicity reduction of soybean meal through solid-state fermentation with microorganisms. 2018, 9(3): 1899-1909. · DOI
  47. S. Yin. A combined proteomic and metabolomic strategy for allergens characterization in natural and fermented brassica napus bee pollen. 2022, 9. · DOI
  48. N.U. Sruthi. Impacts of cold plasma treatment on physicochemical, functional, bioactive, textural, and sensory attributes of food: a comprehensive review. 2022, 368: 130809. · DOI
  49. S.W. Ng. The effect of atmospheric cold plasma treatment on the antigenic properties of bovine milk casein and whey proteins. 2021, 342: 128283. · DOI
  50. F. Sun. Effects of cold jet atmospheric pressure plasma on the structural characteristics and immunoreactivity of celiac-toxic peptides and wheat storage proteins. 2020, 21(3). · DOI
  51. H. Venkataratnam. Impact of cold plasma processing on major peanut allergens. 2020, 10(1): 17038. · DOI
  52. N.M. Coutinho. Cold plasma processing of milk and dairy products. 2018 · DOI
  53. F.C. Ekezie. Altering the IgE binding capacity of king prawn ( Litopenaeus vannamei ) tropomyosin through conformational changes induced by cold argon-plasma jet. 2019, 300: 125143. · DOI
  54. E.G. Alves Filho. Cold plasma processing effect on cashew nuts composition and allergenicity. 2019, 125: 108621. · DOI
  55. F. Cardona. Benefits of polyphenols on gut microbiota and implications in human health. 2013, 24(8): 1415-22. · DOI
  56. M.S. Swallah. Antioxidant potential overviews of secondary metabolites (polyphenols) in fruits. 2020, 2020: 9081686. · DOI
  57. H. Shakoor. Immunomodulatory effects of dietary polyphenols. 2021, 13(3). · DOI
  58. W. He. Function, digestibility and allergenicity assessment of ovalbumin–EGCG conjugates. 2019, 61: 103490. · DOI
  59. A.M. Mileo. Polyphenols: immunomodulatory and therapeutic implication in colorectal cancer. 2019, 10. · DOI
  60. T.G. Pan. Food allergenic protein conjugation with plant polyphenols for allergenicity reduction. 2022, 43: 36-42. · DOI
  61. T. Zhang. Changes in allergenicity of ovalbumin in vitro and in vivo on conjugation with quercetin. 2020, 68(13): 4027-4035. · DOI
  62. X. Lin. A new method to reduce allergenicity by improving the functional properties of soybean 7S protein through covalent modification with polyphenols. 2022, 373: 131589. · DOI
  63. X. Pi. A review on polyphenols and their potential application to reduce food allergenicity. 2022 · DOI
  64. X. Wu. Reducing the allergenic capacity of β -lactoglobulin by covalent conjugation with dietary polyphenols. 2018, 256: 427-434. · DOI
  65. W. He. Covalent conjugation with(–)-epigallo-catechin 3-gallate and chlorogenic acid changes allergenicity and functional properties of Ara h 1 from peanut. 2020, 331: 127355. · DOI
  66. A.O. Lasekan. Effects of buffer additives and thermal processing methods on the solubility of shrimp ( Penaeus monodon ) proteins and the immunoreactivity of its major allergen. 2016, 200: 146-153. · DOI
  67. H. Yang. Induction of oral tolerance by gamma-irradiated ovalbumin administration. 2016, 36(1): 14-18. · DOI
  68. X. Meng. Characterization of the potential allergenicity of irradiated bovine α -lactalbumin in a BALB/c mouse model. 2016, 97: 402-410. · DOI
  69. A. Guan. The effect of electron beam irradiation on IgG binding capacity and conformation of tropomyosin in shrimp. 2018, 264: 250-254. · DOI
  70. Z. Zhang. Conformation, allergenicity and human cell allergy sensitization of tropomyosin from exopalaemon modestus: effects of deglycosylation and Maillard reaction. 2019, 276: 520-527. · DOI
  71. L. Xu. 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. 2018, 101(8): 6823-6834. · DOI
  72. R.K. Gupta. Glycation of clinically relevant chickpea allergen attenuates its allergic immune response in Balb/c mice. 2017, 235: 244-256. · DOI
  73. A. Bugajska-Schretter. Purification, biochemical, and immunological characterisation of a major food allergen: different immunoglobulin E recognition of the apo- and calcium-bound forms of carp parvalbumin. 2000, 46(5): 661-669. · DOI
  74. L.K. Creamer. Effect of sodium dodecyl sulfate and palmitic acid on the equilibrium unfolding of bovine beta-lactoglobulin. 1995, 34(21): 7170-7176. · DOI
  75. K.J. Gong. Emulsifying properties and structure changes of spray and freeze-dried peanut protein isolate. 2016, 170: 33-40. · DOI
  76. G. Bulaj. Formation of disulfide bonds in proteins and peptides. 2005, 23(1): 87-92. · DOI
  77. M.A.B. Siddique. Effect of pulsed light treatment on structural and functional properties of whey protein isolate. 2016, 87: 189-196. · DOI
  78. H. Liu. Effects of high hydrostatic pressure on the conformational structure and gel properties of myofibrillar protein and meat quality: a review. 2021, 10(8): 1872. · DOI
  79. H. Xu. Effect of chlorogenic acid covalent conjugation on the allergenicity, digestibility and functional properties of whey protein. 2019, 298: 125024. · DOI
  80. T. Li. Effects of heat treatment on the antigenicity, antigen epitopes, and structural properties of β -conglycinin. 2021, 346: 128962. · DOI
  81. D. Croote. Food allergen detection by mass spectrometry: the role of systems biology. 2016, 2(1): 16022. · DOI
  82. L.N. Willison. Conformational epitope mapping of Pru du 6, a major allergen from almond nut. 2013, 55(3): 253-263. · DOI
  83. Q. Zhang. Epitope mapping of a 95 kDa antigen in complex with antibody by solution-phase amide backbone hydrogen/deuterium exchange monitored by fourier transform ion cyclotron resonance mass spectrometry. 2011, 83(18): 7129-7136. · DOI
  84. J.A. Sealey-Voyksner. Novel aspects of quantitation of immunogenic wheat gluten peptides by liquid chromatography–mass spectrometry/mass spectrometry. 2010, 1217(25): 4167-4183. · DOI
  85. Y. Zhu. Effects of ultrasonic and microwave processing on avidin assay and secondary structures of egg white protein. 2018 · DOI
  86. L. Fu. Maillard reaction with ribose, galacto-oligosaccharide or chitosan-oligosaccharide reduced the allergenicity of shrimp tropomyosin by inducing conformational changes. 2019, 274: 789-795. · DOI
  87. H.M. Farrell. Secondary structural studies of bovine caseins: temperature dependence of β -casein structure as analyzed by circular dichroism and FTIR spectroscopy and correlation with micellization. 2001, 15(4): 341-354. · DOI
  88. M. Carbonaro. Secondary structure of food proteins by Fourier transform spectroscopy in the mid-infrared region. 2010, 38(3): 679-690. · DOI
  89. S.K. Vanga. Effect of thermal and high electric fields on secondary structure of peanut protein. 2016, 19(5-8): 1259-1271. · DOI
  90. J. Yao. Effect of sodium alginate with three molecular weight forms on the water holding capacity of chicken breast myosin gel. 2018, 239: 1134-1142. · DOI
  91. J. Kong. Fourier transform infrared spectroscopic analysis of protein secondary structures. 2010, 39(008): 549-559. · DOI
  92. T.F. Kumosinski. Quantitation of the global secondary structure of globular proteins by FTIR spectroscopy: comparison with X-ray crystallographic structure. 1996, 43(2): 199-219. · DOI
  93. Y. Lu. Effect of covalent Interaction with chlorogenic acid on the allergenic capacity of ovalbumin. 2018, 66(37): 9794-9800. · DOI
  94. Z. Jia. Effect of covalent modification by(–)-epigallocatechin-3-gallate on physicochemical and functional properties of whey protein isolate. 2016, 66: 305-310. · DOI
  95. J. Xi. High hydrostatic pressure (HHP) effects on antigenicity and structural properties of soybean β -conglycinin. 2018, 55(2): 630-637. · DOI
  96. L. Jiang. Covalent conjugates of anthocyanins to soy protein: unravelling their structure features and in vitro gastrointestinal digestion fate. 2019, 120: 603-609. · DOI
  97. M. Liang. Interaction between lysozyme and procyanidin: multilevel structural nature and effect of carbohydrates. 2013, 138(2): 1596-1603. · DOI
  98. F. Xue. Physicochemical properties of soy protein isolates-cyanidin-3-galactoside conjugates produced using free radicals induced by ultrasound. 2020, 64: 104990. · DOI
  99. P.O. Tsvetkov. Plasmatic signature of disease by differential scanning calorimetry (DSC). 2019, 1964: 45-57. · DOI
  100. L. Tuppo. Detection of allergenic proteins in foodstuffs: advantages of the innovative multiplex allergen microarray-based immunoassay compared to conventional methods. 2022, 11(6): 878. · DOI
  101. J. Courtois. Detection of wheat allergens using 2D western blot and mass spectrometry. 2020, 178: 112907. · DOI
  102. M. Citartan. Aptamers as the powerhouse of dot blot assays. 2021, 232: 122436. · DOI
  103. M. Zhang. Advanced DNA-based methods for the detection of peanut allergens in processed food. 2019, 114: 278-292. · DOI
  104. S. Cau. Detection of celery ( Apium graveolens ) allergen in foods of animal and plant origin by droplet digital PCR assay. 2021, 130: 108407. · DOI
  105. E. Iniesto. Real time PCR to detect hazelnut allergen coding sequences in processed foods. 2013, 138(2): 1976-1981. · DOI
  106. Y. Shen. Biosensors for rapid detection of Salmonella in food: a review. 2021, 20(1): 149-197. · DOI
  107. J. Zhou. Surface plasmon resonance (SPR) biosensors for food allergen detection in food matrices. 2019, 142: 111449. · DOI
  108. A. Angulo-Ibáñez. Electrochemical tropomyosin allergen immunosensor for complex food matrix analysis. 2019, 1079: 94-102. · DOI
  109. I. Manea. Overview of food allergy diagnosis. 2016, 89(1): 5-10. · DOI
  110. G.S. Ladics. Review of animal models designed to predict the potential allergenicity of novel proteins in genetically modified crops. 2010, 56(2): 212-224. · DOI
  111. A. Yang. Screening of anti-allergy Lactobacillus and its effect on allergic reactions in BALB/c mice sensitized by soybean protein. 2021, 87: 104858. · DOI
  112. M. Milovanovic. Interleukin-17A promotes IgE production in human B cells. 2010, 130(11): 2621-2628. · DOI
  113. H. Zhang. Subsets of regulatory T cells and their roles in allergy. 2014, 12: 125. · DOI
  114. S. Benedé. Applications of mouse models to the study of food allergy. 2021, 2223: 1-17. · DOI
  115. B. Gonipeta. Mouse models of food allergy: How well do they simulate the human disorder?. 2015, 55(3): 437-452. · DOI
  116. X. Liu. Oral allergy syndrome and anaphylactic reactions in BALB/c mice caused by soybean glycinin and β -conglycinin. 2008, 38(2): 350-356. · DOI
  117. B. Gonipeta. An adjuvant-free mouse model to evaluate the allergenicity of milk whey protein. 2009, 92(10): 4738-4744. · DOI
  118. B. Gonipeta. Long-term characteristics of hazelnut allergy in an adjuvant-free mouse model. 2010, 152(3): 219-225. · DOI
  119. D. Dunkin. Allergic sensitization can be induced via multiple physiologic routes in an adjuvant-dependent manner. 2011, 128(6): 1251-1258.e2. · DOI
  120. F. Erdő. Evaluation of intranasal delivery route of drug administration for brain targeting. 2018, 143: 155-170. · DOI
  121. W. Al Bakri. Overview of intranasally delivered peptides: key considerations for pharmaceutical development. 2018, 15(10): 991-1005. · DOI
  122. D.I. Kim. Comparison of asthma phenotypes in OVA-induced mice challenged via inhaled and intranasal routes. 2019, 19(1): 241. · DOI
  123. Y. Wang. The comparation of intraperitoneal injection and nasal-only delivery allergic rhinitis model challenged with different allergen concentration. 2019, 33(2): 145-152. · DOI
  124. S. Wavrin. Influence of the route of exposure and the matrix on the sensitisation potency of a major cows’ milk allergen. 2015, 5(1): 3. · DOI
  125. B. Keshavarz. Matrix effect on food allergen detection – a case study of fish parvalbumin. 2019, 274: 526-534. · DOI
  126. A. Achouri. Thermal processing, salt and high pressure treatment effects on molecular structure and antigenicity of sesame protein isolate. 2013, 53(1): 240-251. · DOI
  127. C. Yamada. Degradation of soluble proteins including some allergens in brown rice grains by endogenous proteolytic activity during germination and heat-processing. 2014, 69(10): 1877-1883. · DOI
  128. M. Zeece. Effect of high-pressure treatment on in-vitro digestibility of β -lactoglobulin. 2008, 9(1): 62-69. · DOI
  129. S.L. Bavaro. Effect of thermal/pressure processing and simulated human digestion on the immunoreactivity of extractable peanut allergens. 2018, 109: 126-137. · DOI
  130. X. Pi. Effects of fermentation with Bacillus natto on the allergenicity of peanut. 2021, 141: 110862. · DOI
  131. Y. Tao. Enhancement of food processes by ultrasound: a review. 2015, 55(4): 570-594. · DOI
  132. X. Pi. Recent advances in alleviating food allergenicity through fermentation. 2022, 62(26): 7255-7268. · DOI
  133. M. Pan. Irradiation technology: an effective and promising strategy for eliminating food allergens. 2021, 148: 110578. · DOI
  134. Y. Yao. Release and conformational changes in allergenic proteins from wheat gluten induced by high hydrostatic pressure. 2022, 368: 130805. · DOI
  135. F. Liu. A comparative study of covalent and non-covalent interactions between zein and polyphenols in ethanol-water solution. 2017, 63: 625-634. · DOI

Cited by

Sorted by citations

Metadata

Authors
Zhou, E., Li, Q., Zhu, D., Chen, G., & Wu, L.
Venue
Food Science and Human Wellness
Published
2024-05
Volume
13
Issue
3
Pages
1135-1151
ISSN
  • 2097-0765
  • 2213-4530
Cited by
37
References
2
Language
en

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review