2021
DOI: 10.1016/j.foodchem.2020.128962
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Effects of heat treatment on the antigenicity, antigen epitopes, and structural properties of β-conglycinin

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Cited by 42 publications
(48 citation statements)
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“…It has been previously demonstrated that the accessibility of different antibodies to specific epitopes can be modified by partial unfolding, in the case of food allergens, having an effect on their sensitizing potential. 73 Similarly, heat denaturation of allergens has been reported to decrease the integrity of IgE epitopes, 74 evidencing the impact of structural alterations on antibody recognition. Thus, these results confirmed that binding of Bet v 1 to NSNPs resulted in efficient antibody recognition due to its well-folded state at the particle surface, while this state was compromised by the specific nanotopography of MSNPs.…”
Section: Resultsmentioning
confidence: 97%
“…It has been previously demonstrated that the accessibility of different antibodies to specific epitopes can be modified by partial unfolding, in the case of food allergens, having an effect on their sensitizing potential. 73 Similarly, heat denaturation of allergens has been reported to decrease the integrity of IgE epitopes, 74 evidencing the impact of structural alterations on antibody recognition. Thus, these results confirmed that binding of Bet v 1 to NSNPs resulted in efficient antibody recognition due to its well-folded state at the particle surface, while this state was compromised by the specific nanotopography of MSNPs.…”
Section: Resultsmentioning
confidence: 97%
“…The content levels of α‐helix and β‐turn will increased, while the β‐sheet structure decreases, the peak shapes had obviously changed, which indicated that the heating temperatures had significant effects on the secondary structures of the soybean glycinin, the results are consistent with Guohui Long's research (Long et al ., 2015). Some literatures have proved that changes in the secondary structure of proteins can lead to changes in the antigenicity of proteins (Xi & He, ; Li et al ., 2018; Li et al ., 2021). This suggested that the ultra‐high pressure combined with heat treatments changed the secondary structure of glycinin, so the epitopes on proteins were buried or exposed (Heydenreich et al ., 2012; Tong et al ., 2012; Bu et al ., 2015; Verhoeckx et al ., 2015; Yang et al ., 2015).…”
Section: Resultsmentioning
confidence: 99%
“…A large number of research results have confirmed that the three processing methods of heat treatments, ultra‐high‐pressure treatments and high pressure combined with heat treatments mainly reduced the sensitisation by changing the structures of the soybean allergenic proteins, destroying the allergen epitopes and losing the immunogenicity (Li et al ., 2012; Yang et al ., 2015; Zhou et al ., 2016; Xi & He, ; Bavaro et al ., 2018; Li et al ., 2018; Li et al ., 2021). This study chose to analyse the changes in the antigenicity and structural characteristics of glycinin following treatments in which ultra‐high‐pressure was combined with heat in order promote the development of hypoallergenic foods (Xi & He, ; Li et al ., 2021).…”
Section: Introductionmentioning
confidence: 99%
“…Therefore, IRE, independent of thermal effects, is a nonthermal ablation technique that only acts on the lipid bilayer of the cell membrane and has little effect on other molecules, such as membrane proteins and intracellular macromolecules (2,11). In contrast, cryoablation and thermal ablation lead to protein denaturation, resulting in changes in tumor antigenicity (81). One study collected and analyzed cell lysates of B16 melanoma cells after exposure to heat (50°C, 30 min), cold (−80°C, 30 min), and IRE (1,250 V/cm, 99 pulses, 50 ms pulses, 1 Hz interval).…”
Section: Characteristics Of the Immune Response In Tumors Induced By Ire Ire Induces A Much Stronger Immune Response Than Other Ablation mentioning
confidence: 99%