Food Science and Human Wellness
·
2023
·
IF 7
Linglin Fu,Rongrong Wang,Jinru Zhou,Chong Wang,Yanbo Wang
N -glycans in many proteins are of great concern because of their strong association with food allergies. Triticum aestivum (bread wheat), a major food crop, is known as one of the “Big Eight” allergenic groups. However, little research has been done about N -glycans in wheat glycoproteins. In this study, a soluble wheat glycoprotein was purified from wheat and further identified as globulin-1 S allele (GSA). The wheat GSA displayed significant IgE-binding activity. Moreover, one N -glycosylation site and 6 kinds of N -glycans were identified by mass spectrometry, including 3 high mannose types and 3 complex types. Furthermore, the IgE-binding activity of wheat GSA is proved to be reduced by the removal of N -glycan, thermal treatment (temperatures > 80 °C), and strong acidic treatment (pH 3.0). These findings would provide a better understanding of the effects of N -glycosylation, thermal treatment, and acidic treatment on the molecular characteristics of GSA, and further provide new insights into the development of hypoallergenic wheat products.
研究领域:
食品科学
·
植物生物学
·
免疫学
✓ 已验证
DOI
高影响因子
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
·
2023
·
IF 8.2
Ji-hua Mao,Kai Zhang,Ying-fei He,Jun Liu,Yan-hong Shao,Zong-cai Tu
Ovalbumin (OVA) was modified by fructose (Fru) and galactose (Gal) to study the structure, IgG/IgE binding capacity and effects on human intestinal microbiota of the conjugated products. Compared with OVA-Fru, OVA-Gal has a lower IgG/IgE binding capacity. The reduction of OVA is not only associated with the glycation of R84, K92, K206, K263, K322 and R381 in the linear epitopes, but also with conformational epitope changes, manifested as secondary and tertiary structural changes caused by Gal glycation. In addition, OVA-Gal could alter the structure and abundance of gut microbiota at phylum, family, and genus levels and restore the abundance of bacteria associated with allergenicity , such as Barnesiella , Christensenellaceae_R-7_group , and Collinsela , thereby reducing allergic reactions. These results indicate that OVA-Gal glycation can reduce the IgE binding capacity of OVA and change the structure of human intestinal microbiota. Therefore, Gal glycation may be a potential method to reduce protein allergenicity.
研究领域:
食品科学
·
免疫学
·
微生物学
✓ 已验证
产品关联
DOI
PubMed
高影响因子
Food Bioscience
·
2024
·
IF 4.8
Caiying Yang,Ying Zhang,Xiaoya Zhou,Zhihua Wu,Jinyan Gao,Hongbing Chen,Ping Tong
Allergen modification is a novel strategy for preventing and treating food allergy. Resveratrol (RES) can be used as a modifying ligand for allergens, but the interaction mechanism between RES and allergens is still not detailed, and the ramifications of this interaction on the structure, epitope and allergenicity of allergens are also lacking a clear explanation. In addition, the application of heat can promote protein structure to unfold and expose more binding sites to facilitate interaction. Therefore, in this study, ovalbumin (OVA) was selected as the allergen model and was heated to expose more binding sites. The effects of the interaction between RES and heat-stressed ovalbumin (HOVA) on allergen structure, epitope and allergenicity were investigated by combining routine experimental analysis and computer simulation. Results showed heat stress at 323 K for 15 min could better unfold the molecular structure of OVA. On this basis, the interaction between RES and OVA was strengthened, which showed a static quenching of the ground state complex with binding affinity of 1.25 × 10 6 L/mol. The binding of RES induced the variation of protein microenvironment, and the overall structure tended to disordered direction. Computer simulation had shown RES could directly act on the IgE epitope region (AA251-260) of the OVA. The allergenicity evaluation experiment further indicated the combination of RES alleviated the IgE binding capacity of HOVA. These findings are helpful to further study the mechanism of RES ligand modification to change food allergy.
研究领域:
食品科学
·
过敏反应
·
生物化学
·
分子生物学
✓ 已验证
产品关联
DOI
高影响因子
FOOD CHEMISTRY
·
2020
·
IF 6.306
Jing-jing Zhang,Zong-cai Tu,Hui Wang,Yue-ming Hu,Peng-cheng Du,Yi-peng Yang
In this work, the mechanism of the effect of lipid oxidation on the IgG/IgE binding ability of ovalbumin (OVA) was investigated via the peroxyl radicals produced by 2, 2′-azobis (2-amidinopropane) dihydrochloride to simulate lipid oxidation. Results showed that the structure of OVA unfolded partially with an increase in oxidation degree, leading to the exposure of the allergenic epitopes and increasing the IgG/IgE binding ability of OVA. Nine oxidation sites were found on the α-helix, and these sites may unwind the α-helix and expose the allergenic epitopes on the OVA surface, leading to antibody recognition and combination. Consequently, the IgG/IgE binding ability of OVA was increased. In conclusion, the allergenic capacity of OVA can be promoted by modifying peroxyl radical oxidation in processing egg products.
研究领域:
食品科学
·
免疫学
✓ 已验证
产品关联
DOI
PubMed
高影响因子
FOOD CHEMISTRY
·
2023
·
IF 8.8
Enning Zhou,Weiwei Wang,Xiaofeng Xue,Pianpian Wang,Fan Wu,Liming Wu,Qiangqiang Li
Bee pollen is a byproduct of pollination, which is a necessary process to produce foods. However, bee pollen can induce significant food-borne allergies. We previously identified a bee pollen-derived pan-allergen in the profilin family, Bra c p. Herein, we aimed to reduce Bra c p allergenicity via protein oxidation with hydrogen peroxide and explore the changes induced. Ion-mobility mass spectrometry revealed aggregation of the oxidized product; we also found irreversible sulfonation of the free sulfhydryl group of the Bra c p Cys98 residue to a more stable cysteine derivative. A significant proportion of the α-helices in Bra c p were transformed into β-sheets after oxidation, masking the antigenic epitopes. An immunoassay demonstrated that the IgE-binding affinity of Bra c p was decreased in vitro after oxidation. To our knowledge, this is the first report describing the application of protein oxidation to reduce the allergenicity of profilin family member in foods.
研究领域:
过敏反应
·
免疫学
·
蛋白质化学
·
食品科学
✓ 已验证
产品关联
DOI
PubMed
高影响因子
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
·
2024
·
IF 5.7
Ze Yun,Jiahao Li,Wenyue Zhu,Xin Yuan,Jiajia Zhao,Minjie Liao,Lingjun Ma,Fang Chen,Xiaosong Hu,Junfu Ji
Allergenicity of soybean 7S protein (7S) troubles many people around the world. However, many processing methods for lowering allergenicity is invalid. Interaction of 7S with phenolic acids, such as chlorogenic acid (CHA), to structurally modify 7S may lower the allergenicity. Hence, the effects of covalent (C-I, periodate oxidation method) and noncovalent interactions (NC-I) of 7S with CHA in different concentrations (0.3, 0.5, and 1.0 mM) on lowering 7S allergenicity were investigated in this study. The results demonstrated that C-I led to higher binding efficiency (C-0.3:28.51 ± 2.13%) than NC-I (N-0.3:22.66 ± 1.75%). The C-I decreased the α-helix content (C-1:21.06%), while the NC-I increased the random coil content (N-1:24.39%). The covalent 7S–CHA complexes of different concentrations had lower IgE binding capacity (C-0.3:37.38 ± 0.61; C-0.5:34.89 ± 0.80; C-1:35.69 ± 0.61%) compared with that of natural 7S (100%), while the noncovalent 7S–CHA complexes showed concentration-dependent inhibition of IgE binding capacity (N-0.3:57.89 ± 1.23; N-0.5:46.91 ± 1.57; N-1:40.79 ± 0.22%). Both interactions produced binding to known linear epitopes. This study provides the theoretical basis for the CHA application in soybean products to lower soybean allergenicity.
研究领域:
食品科学
·
过敏研究
·
生物化学
✓ 已验证
产品关联
DOI
PubMed
高影响因子
FOOD CHEMISTRY
·
2022
·
IF 9.231
Xu-mei Wang,Zong-cai Tu,Yun-hua Ye,Guang-xian Liu,Yue-ming Hu,Hui Wang
This study aimed to isolate and evaluate the allergenicity of glycated α-lactalbumin (ALA) digestive products and identify its allergenic peptides. The digestive products of native-, alone glycated- and ultrasound-assisted glycated ALA (ALA-D, ALA-gal-D, 100ALA-gal-D) were isolated into three fractions (F1, F2 and F3). High-resolution mass spectrometry showed that the digestion-resistant peptides of F2 and F3 mainly distributed in amino acid sequence (AA) 25–31, AA32-53, AA40-53, AA54-60, AA80-90, AA94-104. The allergenicity of the three fractions of glycated ALA was lower than that in ALA-D, indicating glycation of ALA could indeed reduce its allergenicity after digestion. Furthermore, most fractions isolated from high glycation-degree ALA had the lowest allergenicity. The IgG/IgE binding abilities of synthesized peptides indicated that AA94-104 firstly identified by us embodied the strongest allergenicity and might be the potential allergenic peptide. This will provide a theory for preparing hypoallergenic products based on the identified allergenic peptides.
研究领域:
食品科学
·
过敏学
·
蛋白质组学
✓ 已验证
产品关联
DOI
PubMed
高影响因子
LWT-FOOD SCIENCE AND TECHNOLOGY
·
2024
·
IF 6
Yiling Zhou,Yaru Liao,Jing Bai,Xinlei Xia,Zhihua Wu,Xin Li,Ping Tong,Hongbing Chen,Anshu Yang
This study aimed to investigate the effects of active soybean isoflavones on the structure and potential allergenicity of glycinin, a major allergen, in soybean. The interaction mechanism between two active soybean isoflavones, namely, genistein (Gen) and daidzein (Dai), and glycinin were investigated using a series of spectral techniques. The structure of the isoflavone-glycinin complexes was characterized by SDS-PAGE and spectral techniques. In addition, the potential allergenicity of the isoflavone-glycinin complexes and their digestion products in vitro was measured via Western blot and enzyme-linked immunosorbent assay. Results showed that Gen and Dai effectively quenched the intrinsic fluorescence of glycinin largely through static quenching. Dai interacted with glycinin through hydrogen bonding and van der Waals forces, while Gen relied on hydrophobic interactions with glycinin. Furthermore, the neutral complex of daidzein-glycinin (Dai-G) exhibited weaker IgE binding ability compared with the glycinin samples. These findings provided new insights into the molecular mechanisms that underlay the immunomodulatory effects of soybean isoflavones and their potential applications in food allergy prevention and management.
CAS / MDL:
研究领域:
食品科学
·
过敏与免疫学
·
分子生物学
✓ 已验证
产品关联
DOI
高影响因子
JOURNAL OF FOOD SCIENCE
·
2025
·Vol. 90
·期 8
·e70432
·
IF 3.4
Qin Geng,David Julian McClements,Taotao Dai,Wenlong Zhou,Zhihua Wu,Hongbing Chen
The molecular structure and surface properties of peanut proteins are altered by their non-covalent interactions with food polyphenols, which alter their allergenicity. In our research, the interactions between the critical peanut allergen (Ara h 2) and a model polyphenol (tannic acid [TA]) were studied utilizing experimental (spectroscopy and calorimetry) and molecular docking methods. Ultraviolet (UV) and circular dichroism (CD) spectroscopy analysis indicated that the microenvironment polarity and secondary/tertiary structure of Ara h 2 were changed due to its interaction with TA. Specifically, degree of molecular disorder increased, and the surface hydrophobicity of the polypeptide decreased after Ara h 2 interacted with TA. Analysis using fluorescence quenching, isothermal titration calorimetry, and molecular docking showed that the main non-covalent interactions were hydrogen bond formation between the Ara h 2 and TA. Binding site analysis using molecular docking indicated that the TA may have interacted with specific amino acids in the polypeptide chain, including Lys 31, Arg 34, Asp 35, Trp 44, Ser 54, Arg 59, Arg 60, Arg 122, Glu 123, and Gln 130. These amino acids are known to be part of the IgE epitope regions of Ara h 2, and so TA binding might be expected to impact peanut protein allergenicity. Indeed, an enzyme-linked immunosorbent assay (ELISA) study indicated that the IgE binding capacity of Ara h 2 was reduced after interacting with TA in a dose-dependent manner. This study enriches the understanding of the interactions between peanut protein allergens and small-molecule nutrients and provides a method for reducing the potential allergenicity of Ara h 2. Practical applications Employing the plant polyphenols as a means to modulate the activity of food allergens could potentially offer a breakthrough in managing food allergies. The strategic non-covalent binding of polyphenols, exemplified by TA, to the peanut allergen Ara h 2, may effectively lower its capacity to trigger allergic reactions, thereby offering an approach to mitigating peanut sensitization risks. The study examined the alterations in the structure and allergenic properties of Ara h 2 following its interaction with TA. This investigation was poised to accelerate the identification of TA's potential to inhibit peanut-induced allergic responses through allergen binding.
研究领域:
食品科学
·
过敏研究
·
分子生物学
·
生物化学
·
免疫学
·
结构生物学
✓ 已验证
产品关联
DOI
PubMed
高影响因子
FOOD HYDROCOLLOIDS
·
2025
·
IF 12.4
Lidong Pang,Shihang Li,Chen Chen,Jia Shi,Yue Su,Xinyan Yang,Yujun Jiang
Polyphenol-modified proteins have been extensively studied, but the long processing time limits their application. This study aims to evaluate the effects of ultrasonic-assisted treatment (UAT) at 0 W (no ultrasound) and 650 W, as well as heat-assisted treatment (HAT) at 25 °C (no heat) and 80 °C, on the physicochemical, structural, antibody-binding capacity and functional properties of whey protein isolate (WPI)-(−)-epigallocatechin gallate (EGCG) conjugates. The results showed that the immunoglobulin E (IgE) binding capacity of WPI-EGCG conjugate prepared by UAT (U650-E) and WPI-EGCG conjugate prepared by HAT (H80-E) was significantly reduced in comparison with the corresponding conjugates without ultrasound-assisted and without heat-assisted. Notably, H80-E exhibits the lowest IgE binding capacity (42.40 %) and demonstrates superior performance in terms of antioxidant capacity, α-glucosidase inhibitory activity, solubility, and emulsifying properties. This is attributed to the effects of heat treatment on the structure of WPI and the binding sites between WPI and EGCG. In addition, the reduction in IgE binding capacity of H80-E can be attributed to the disruption of conformational epitopes and the masking of critical linear epitopes by both heat treatment and the presence of EGCG. However, the foaming characteristics of H80-E were observed to be less favorable compared to those of U650-E, which can be attributed to the decreased surface hydrophobicity and diminished free sulfhydryl group content exhibited by H80-E. This study demonstrates that WPI-EGCG conjugates prepared by HAT have more potential for application in hypoallergenic or functional foods.
研究领域:
食品科学
·
免疫学
·
生物化学
✓ 已验证
产品关联
DOI
高影响因子
Food Science and Human Wellness
·
2023
·
IF 7
Jie Ding,Chunyan Zhu,Pengfei Jiang,Libo Qi,Na Sun,Songyi Lin
Enzymatic hydrolysis, isolation, and purification might make a great deal of difference in antioxidant activity and antigenicity of peptide components. This study aimed to isolate and purify antioxidant peptide components from Antarctic krill and evaluate their allergenicity of them. Electron paramagnetic resonance (EPR) spectroscopy results indicated 3 10 kDa Antarctic krill hydrolysates (AKHs) had higher DPPH and · OH radical scavenging rates. And the second component (N2-2) purified 3 10 kDa hydrolysate showed better ability to scavenge DPPH and · OH radicals ( P < 0.05), which were (47.43 ± 2.18)% and (34.33 ± 1.25)%, respectively. Additionally, indirect-ELISA results revealed that N2-1 had a weaker ability to bind specific IgE and that N2-2 had a lower binding capability to specific IgG1 ( P < 0.05). And N2-2 had a higher EC 50 value of (5.29 ± 0.95) ng/mL ( P < 0.05) in cell degranulation assay, which was about 13.80 times that of Antarctic krill. Therefore, N2-2 might be the potential source of the antioxidant peptides with lower allergenicity.
研究领域:
食品科学
·
生物化学
·
免疫学
✓ 已验证
产品关联
DOI
高影响因子
FOOD CHEMISTRY
·
2024
·
IF 8.5
Fukai Li,Enning Zhou,Min Wang,Fei Pan,Jian Zhou,Mengrui Yang,Tongtong Wang,Liang Li,Liming Wu,Qiangqiang Li
Reducing the allergenicity of edible insects is crucial for the comprehensive utilization of insect resources. Phospholipase A2 (PLA2) exists in various edible insects and mammalian tissues, which can cause serious allergic reactions. Herein, we constructed a magnetic nanocomposite with photo/chemical synergistic capability to mitigate the allergenicity of PLA2. The formation of prepared nanocomposite was systematically confirmed using various techniques. The nanocomposite exhibited uniform diameters, abundant functional groups, excellent magnetic capabilities. An effective photo/chemical method was established to reduce the allergenicity of PLA2 in vitro. The feasibility of the method was demonstrated through circular dichroism, fluorescence spectrum and IgE-binding analysis. The allergenicity and IgE-binding effect of PLA2 were significantly reduced due to conformational changes after nanomaterial treatment. These results demonstrate the sensitivity and effectiveness a strategy for reducing PLA2 allergenicity, providing a basis for development of nanomaterials to reduce the risk of novel food allergies in response to edible insect products.
研究领域:
纳米技术
·
过敏学
·
食品科学
·
材料科学
✓ 已验证
产品关联
DOI
PubMed
高影响因子
危险品化学品经营许可证（带存储）