Mechanism on the Allergenicity Changes of α-Lactalbumin Treated by Sonication-Assisted Glycation during <i>In Vitro</i> Gastroduodenal Digestion

Wang, Xumei; Tu, Zong–cai; Ye, Yun‐Hua; Liu, Guangxian; Wang, Hui; Hu, Yueming

doi:10.1021/acs.jafc.1c02205

Cited by 19 publications

(21 citation statements)

References 36 publications

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“…A recent study showed that sonication combined with glycation only caused a small decrease in OVA digestibility under simulated gastric and small intestine conditions but that OVA‐specific IgG and IgE levels were exceedingly low after digestion (W. Yang et al., 2021). Similar phenomena were found in sonication‐assisted glycated α‐lactalbumin (X. Wang, Tu, Ye, et al., 2021), which can be attributed to the shielding effect of the linear epitopes caused by the greater degree of glycation. The allergenicity of β‐lactoglobulin was also significantly reduced by ultrasound combined with glycation modification and subsequent digestion.…”

Section: Food Processing Influences Digestion and Allergenicity Of Fo...supporting

confidence: 72%

Gastrointestinal fate of food allergens and its relationship with allergenicity

Sun

Liu

et al. 2022

Comp Rev Food Sci Food Safe

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Food allergens are closely related to their gastrointestinal digestion fate, but the changes in food allergens during digestion and related mechanisms are quite complicated. This review presents in detail digestion models for predicting allergenicity, the fates of food allergens in oral, gastric and duodenal digestion, and the applications of digestomics in mapping IgE-binding epitopes of digestion-resistant peptides. Moreover, this review highlights the structure-activity relationships of food allergens during gastrointestinal digestion. Digestion-labile allergens may share common structural characteristics, such as high flexibility, rendering them easier to be hydrolyzed into small fragments with decreased or eliminated allergenicity. In contrast, the presence of disulfide bonds, tightly wound α-helical structures, or hydrophobic domains in food allergens helps them resist gastrointestinal digestion, stabilizing IgEbinding epitopes, thus maintaining their sensitization. In rare cases, digestion leads to increased allergenicity due to exposure of new epitopes. Finally, the action of the food matrix and processing on the digestion and allergenicity of food allergens as well as the underlying mechanisms was overviewed. The food matrix can directly act on the allergen by forming complexes or new epitopes to affect its gastrointestinal digestibility and thereby alter its allergenicity or indirectly affect the allergenicity by competing for enzymatic cleavage or influencing gastrointestinal pH and microbial flora. Several processing techniques attenuate the allergenicity of food proteins by altering their conformation to improve susceptibility to degradation by digestive enzymes. Given the complexity of food components, the food itself rather than a single allergen should be used to obtain more accurate data for allergenicity assessment.

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Section: Food Processing Influences Digestion and Allergenicity Of Fo...supporting

confidence: 72%

Gastrointestinal fate of food allergens and its relationship with allergenicity

Sun

Liu

et al. 2022

Comp Rev Food Sci Food Safe

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“…As the leading pediatric food allergy, the peanut (Arachis hypogaea L.) allergy (PA) can cause anaphylaxis, and its prevalence has increased dramatically. , Although it is lifelong in most instances, disease-modifying treatments for the PA are lacking . Many attempts have been made to reduce the potential allergenicity of peanut allergens. − Previous studies have shown that the allergenicity can be changed by altering the structure and other physicochemical properties of food allergens. − …”

Section: Introductionmentioning

confidence: 99%

Effect of Processing on the Structure and Allergenicity of Peanut Allergen Ara h 2 Roasted in a Matrix

Chang

Zhou

Zhang

et al. 2022

J. Agric. Food Chem.

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Peanut allergy is the leading pediatric food allergy. Many attempts have been made to reduce its allergenicity by processing. After roasting, Ara h 2 and its derivatives in the matrix were isolated by immunoaffinity chromatography (IAC). The structure and allergenicity of Ara h 2 were analyzed by circular dichroism, mass spectrometry (MS), western blotting, the enzymelinked immunoassay, and cell modeling. Our results showed that a large portion of Ara h 2 was fragmented and cross-linked. Ara h 2 monomers accounted for only 13% of the total proteins after IAC purification. In addition, the structure of Ara h 2 changed after roasting. In addition to methylation and oxidation modification, the disulfide bonds of Ara h 2 were found to be rearranged after roasting. In the conformational structure of Ara h 2, the content of the α-helix decreased from 27.1 to 21.6% after roasting, while the content of the random coil increased from 29.1 to 34.3%. Six cleavage sites of trypsin were exposed, while three were covered. In terms of allergenicity, most of the cross-linking products were not recognized by patients' sera. Only one faint band around 40 kDa was observed in our blotting. For Ara h 2 monomers, roasting enhanced their IgE binding capacity and ability to stimulate the degranulation of basophils. The potential allergenicity increase of Ara h 2 monomers did not reflect the allergenicity change of Ara h 2 in the matrix due to the amount and property of its derivatives after roasting.

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“…SS treatment, particularly at high temperatures and long processing times, could induce the OVM aggregation, increase surface hydrophobicity, modify the functional groups and amino acids in OVM. These phenomena disrupted and buried some allergen epitopes and made it difficult for the combination of antibodies and antigens [ 14 , 15 ]. Therefore, the allergenicity of OVM was decreased and the anaphylactic reaction in the KU812 cell was inhibited.…”

Section: Resultsmentioning

confidence: 99%

“…The IgG and IgE-binding abilities of the OVM samples were estimated with indirect competitive ELISA according to our previous report [ 14 ]. Rabbit anti-OVM IgG serum and human anti-OVM IgE serum were used to determine IgG-binding ability and IgE-binding ability, respectively.…”

Section: Methodsmentioning

confidence: 99%

Effects of Superheated Steam Treatment on the Allergenicity and Structure of Chicken Egg Ovomucoid

Wen

et al. 2022

Foods

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The aim of this study was to explore the effects of an emerging and efficient heating technology, superheated steam (SS), on the allergenicity and molecular structure of ovomucoid (OVM). OVM was treated with 120–200 °C of SS for 2 to 10 min. The allergenicity (IgG/IgE binding abilities and cell degranulation assay) and molecular structure (main functional groups and amino acids modification) changes were investigated. The IgG-binding ability of OVM decreased and the releases of β-hex and TNF-γ were inhibited after SS treatment, indicating that the protein allergenicity was reduced. Significant increases in oxidation degree, free SH content and surface hydrophobicity were observed in SS-treated OVM. The protein dimer and trimer appeared after SS treatment. Meanwhile, obvious changes occurred in the primary structure. Specifically, serine can be readily modified by obtaining functional groups from other modification sites during SS treatment. Moreover, the natural OVM structure which showed resistance to trypsin digestion was disrupted, leading to increased protein digestibility. In conclusion, SS-induced OVM aggregation, functional groups and amino acids modifications as well as protein structure alteration led to reduced allergenicity and increased digestibility.

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Mechanism on the Allergenicity Changes of α-Lactalbumin Treated by Sonication-Assisted Glycation during In Vitro Gastroduodenal Digestion

Cited by 19 publications

References 36 publications

Gastrointestinal fate of food allergens and its relationship with allergenicity

Gastrointestinal fate of food allergens and its relationship with allergenicity

Effect of Processing on the Structure and Allergenicity of Peanut Allergen Ara h 2 Roasted in a Matrix

Effects of Superheated Steam Treatment on the Allergenicity and Structure of Chicken Egg Ovomucoid

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