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JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY · 2024 · IF 5.7

Fucoidan-Mediated Covalent Modification Mitigates Allergenicity of Shrimp (Penaeus vannamei) in Mice via Enhanced Intestinal Barrier Function and Antigen Presentation Suppression

Qiaozhen Liu,Songyi Lin,Kexin Liu,Shuqi Jia,Shuya Wang,Na Sun

Covalent modification is an effective strategy for reducing the allergenicity of single allergens. However, due to the complexity of the food matrix, its application in hypoallergenic food production requires further exploration. The study showed that covalent modification of fucoidan decreased the specific antibody levels, inhibited Th2 cell differentiation, and reduced mast cell degranulation, suggesting that it significantly reduced the allergenicity of Penaeus vannamei. Further analysis showed that covalent modification not only up-regulated the intestinal tight junction proteins expression and improved intestinal mucus secretion but also restored intestinal microbial homeostasis by immunological and 16S rRNA gene sequencing. Additionally, covalent modification inhibited dendritic cell maturation and CD8+ T cell differentiation, thereby reducing antigen recognition and presentation, as determined by transcriptome and flow cytometry. Therefore, the covalent modification of fucoidan reduced shrimp allergenicity by enhancing intestinal barrier function and inhibiting antigen presentation. In conclusion, it is a potential strategy for processing hypoallergenic foods.

CAS / MDL: 60842-46-8
研究领域: 食品科学 · 免疫学 · 微生物学
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Food Chemistry-X · 2024 · IF 6.5

Coconut milk allergenicity: Insight into reducing the affinity of coconut globulin to immunoglobulin E by atmospheric cold plasma

Yang Chen,Yile Chen,Tian Li,Jiamei Wang,Weimin Zhang

Atmospheric cold plasma (ACP) presents a promising method for the sterilization of coconut milk and exhibits a modifying effect on coconut globulin (CG), the primary allergen in coconut milk. This study investigated the potential role of ACP treatment in mitigating the allergenic properties of coconut milk by examining changes in protein structure. ACP treatment induced structural alterations in CG, disrupting binding sites with immunoglobulin E (IgE). Consequently, this led to a reduction in the affinity between CG and IgE, evidenced by a decrease in K a from 2.17 × 10 4 /M to 0.64 × 10 4 /M, thereby diminishing IgE-mediated allergic reactions. The findings from allergenic and cellular models further corroborated that ACP treatment decreased the allergenicity of CG by 55.18%, while inhibiting degranulation and the release of allergic mediators. This study presents an innovative methodology for producing hypoallergenic coconut milk, thereby expanding the applicability of ACP technology within the food industry.

研究领域: 食品科学 · 过敏研究 · 等离子技术 · 蛋白质化学
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JOURNAL OF FOOD SCIENCE · 2021 ·Vol. 86 ·期 7 ·3014-3022 · IF 3.167

Effects of deglycosylation and the Maillard reaction on conformation and allergenicity of the egg ovomucoid

Junjie Ma,Jinru Zhou,Lerong Chen,Hong Zhang,Yanbo Wang,Linglin Fu

Ovomucoid (OVM), known as the major allergen in egg white, has gained increasing concerns in industrialized countries. Here, we found the deglycosylation and Maillard reaction with galactooligosaccharide (GOS) and fructooligosaccharide (FOS) can induce conformational transformation of OVM from other structures (β-turn, strang, and random coils) to α-helix. We also introduced an approach to reduce the allergenicity of Gallus domesticus OVM by Maillard reaction with GOS and FOS. However, the OVM glycated by mannosan (MOS) and deglycosylated OVM exhibited higher allergenicity than native OVM. Therefore, GOS and FOS, especially GOS, could be applied in the reduction of the potential allergenicity of OVM through glycation. Furthermore, these findings may provide new insights into the development of hypoallergenic egg products. Practical Application In this study, the allergenicity and conformation of OVM treated with deglycosylation and glycation (GOS, FOS, and MOS) were investigated. The results would provide a better understanding of the effects of deglycosylation and Maillard reaction with different reducing sugars on the molecular characteristics of OVM and further provide new insights into the development of hypoallergenic egg products.

研究领域: 食品科学 · 过敏学 · 化学
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JOURNAL OF FOOD SCIENCE · 2024 ·Vol. 89 ·期 12 ·9257-9270 · IF 3.2

Assessment of transglutaminase catalyzed cross-linking on the potential allergenicity and conformation of heterologous protein polymers

Guangliang Xing,Jia Liu,Ruohan Wang,Yitong Wu

Transglutaminase (TGase)-mediated cross-linking has gained significant attention due to its potential to reduce the allergenicity of food proteins. This study investigates the effects of TGase cross-linking on allergenicity and conformational modifications in a dual-protein system comprising soy protein isolate (SPI) and β-lactoglobulin (β-LG). The results showed that TGase cross-linking effectively decreased the allergenic potential of both SPI and β-LG, with a more pronounced reduction observed in the allergenicity of soy protein in the dual-protein system. SDS-PAGE analysis revealed that the 7S and 11S subunits of soy protein were more easily cross-linked than β-LG. Secondary structure analysis indicated that TGase treatment disrupted β-sheet structures, increased the content of random coils, and enhanced protein flexibility. Ultraviolet absorption and intrinsic fluorescence analyses confirmed these structural alterations, with TGase treatment exposing additional aromatic amino acids. A reduction in free sulfhydryl groups and altered intermolecular forces further corroborated the occurrence of cross-linking. These findings suggest that TGase-mediated cross-linking effectively reduced the allergenicity of SPI and β-LG by modifying their conformations, offering potential strategies for the development of hypoallergenic dual-protein food products. Practical Application This study has practical applications in the food industry to develop hypoallergenic food products, particularly those that combine soy and dairy proteins. By using TGase to cross-link these proteins, the allergenicity can be reduced, resulting in products that are safer for consumers with food allergies.

CAS / MDL: 9045-23-2
研究领域: 食品科学 · 过敏研究 · 蛋白质化学 · 生物技术
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INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES · 2023 · IF 8.2

Molecular structure, IgE binding capacity and gut microbiota of ovalbumin conjugated to fructose and galactose:A comparative study

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.

CAS / MDL: 57-48-7 59-23-4
研究领域: 食品科学 · 免疫学 · 微生物学
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LWT-FOOD SCIENCE AND TECHNOLOGY · 2020 · IF 4.006

Investigation of the mechanism underlying the influence of mild glycation on the digestibility and IgG/IgE-binding abilities of β-lactoglobulin and its digests through LC orbitrap MS/MS

Xu-mei Wang,Yun-hua Ye,Zong-cai Tu,Yue-ming Hu,Hui Wang,Cheng-yan He

This study aimed to investigate the mechanism underlying the influence of mild glycation on the digestibility and anaphylactic effect of β-lactoglobulin (βLG) and its digests through LC Orbitrap MS/MS. Three glycated sites were discovered after glycation with fructose, whereas only lysine47 (K47) was glycated with maltose . After digestion, the intrinsic fluorescence intensity decreased and red shifted, and the degree of hydrolysis (DH) values showed no significant difference among digests. βLG glycated with Fru showed the lowest IgG and IgE-binding abilities. Meanwhile, the IgG and IgE-binding abilities further decreased and showed no apparent difference among digests. These results were attributed to the proximity to the IgG-binding epitope, the high glycation degree of K47, and mild glycation. Therefore, mild glycation could reduce the anaphylaxis of proteins before digestion, but did not influence the anaphylactic effect of the digests.

CAS / MDL: 6363-53-7
研究领域: 食品科学 · 免疫学 · 蛋白质组学
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JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY · 2020 · IF 4.192

Effect of Ultrasound Treatment on Allergenicity Reduction of Milk Casein via Colloid Formation

Chong Wang,Qiang Xie,Yanbo Wang,Linglin Fu

Cow’s milk protein allergy, which occurs in approximately 5–10% of the population of infants and children, has become an important public food safety problem. As a major allergen in cow’s milk, the most abundant protein casein (CN) is considered to be potent in inducing food allergy. In recent years, ultrasound treatment has played a significant role in the field of colloidal particulate system. In this study, we found that ultrasound treatment dramatically decreased the diameter of a CN particle to less than 100 nm in the presence of Tween 80, producing colloidal casein (c-CN) with high transparency. The electrophoretic and transmission electron microscopy analysis showed that the advanced protein structure of CN changed significantly. In addition, the enzyme-linked immunosorbent assay with allergic sera showed that the immunoglobulin-E-binding capacity of c-CN was significantly decreased. In the meantime, the LAD2 mast cell line degranulation assay demonstrated that ultrasound treatment made CN hypoallergenic. The colloidal and hypoallergenic properties of c-CN were stably maintained for more than 30 days. Likewise, the allergenicity of fresh whole milk also decreased after ultrasound treatment. This work provided an effective way to reduce the allergenicity of milk allergen, which could be beneficial to the production of hypoallergenic cow’s milk.

CAS / MDL: 7365-45-9 9005-65-6
研究领域: 食品科学 · 免疫学
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FOOD CHEMISTRY · 2021 · IF 7.514

Insight into the mechanism of d-allose in reducing the allergenicity and digestibility of ultrasound-pretreated α-lactalbumin by high-resolution mass spectrometry

Dan Bu,Zong-cai Tu,Hui Wang,Yue-ming Hu,Qing Sun,Guang-xian Liu

The mechanism of d -allose in reducing the allergenicity and digestibility of ultrasound-pretreated α-lactalbumin (α-LA) was studied. The intensity reduction and peak red shift occurred in fluorescence spectra of glycated samples. Enzyme-linked immunosorbent assay and basophil degranulation analysis showed that d -allose significantly reduced the allergenicity of α-LA, and ultrasound-pretreated α-LA showed the lowest allergenicity after glycation. Compared with α-LA, the degree of hydrolysis decreased in glycated samples. Size-exclusion high-performance liquid chromatography showed that the glycated α-LA was resistant to digestive enzymes. The glycated sites and average degree of substitution per peptide molecule were determined using LC Orbitrap MS/MS. These results suggested that the masking of linear allergenic epitopes by glycation could reduce the allergenicity. Therefore, the combination of ultrasound pretreatment and glycation is a potential method to reduce protein allergenicity in food processing and provides a useful approach for the application of rare sugars in food processing.

研究领域: 食品科学 · 过敏学 · 质谱学
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Food Science and Human Wellness · 2023 · IF 7

Antarctic krill antioxidant peptides show inferior IgE-binding ability and RBL-2H3 cell degranulation

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.

CAS / MDL: 3317-61-1
研究领域: 食品科学 · 生物化学 · 免疫学
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JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE · 2023 · IF 4.1

Shedding light on the interaction of ovalbumin and resveratrol: structure, digestibility, transport, and allergenicity assessment of OVA–RES complexes

Xiaoqian Xu,Qiang Cao,Jin Yuan,Ping Tong,Xin Li,Anshu Yang,Zhihua Wu,Xiaohua Liu,Hongbing Chen,Jinyan Gao

BACKGROUND The interaction between food allergens and plant polyphenols has become a safe and effective management strategy to prevent food allergies. Ovalbumin (OVA) is the most abundant allergen in egg whites. Resveratrol (RES) is a plant polyphenol that is abundant in red grapes, berries, and peanuts, and has an anti-allergic effect on allergy-related immune cells. However, there is little information about the effect of RES on the allergenicity of OVA. In this study, the effect of RES on the allergenicity of OVA was investigated. RESULTS Molecular docking and spectroscopic studies indicated that the addition of RES changed the structure of OVA. The digestion and transfer rate of OVA–RES were effectively improved with an in vitro gastrointestinal digestion model and Caco-2 cell model, especially when the molar ratio of OVA–RES was 1:20. Meanwhile, the KU812 cell degranulation assay proved that the potential allergenicity was remarkably decreased while the molar ratios of OVA–RES were increased to 1:20. Furthermore, hydrogen bonds and van der Waals forces were the dominating forces to stabilize the OVA–RES complexes. CONCLUSION All the findings demonstrated that the potential allergenicity of OVA was reduced when interacting with RES, and RES can be a potential food material for preparing a hypoallergenic protein, especially for egg allergy. © 2023 Society of Chemical Industry.

CAS / MDL: 10102-40-6
研究领域: 食品科学 · 过敏研究 · 分子生物学 · 营养学
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FOOD RESEARCH INTERNATIONAL · 2025 · IF 8

Assessment of the effect of metal-phenolic networks on the IgE/IgG binding capacity and functional properties of whey protein isolates

Lidong Pang,Chen Chen,Shihang Li,Jia Shi,Yue Su,Xinyan Yang,Yujun Jiang

Whey protein isolate (WPI) is an important food ingredient, but its high allergenicity limit its application. Recently, metal–phenolic networks (MPNs) have been shown to be effective in modifying proteins. The aim of this study was to evaluate the effects of MPNs formed from (−)-epigallocatechin-3-gallate (EGCG) and Fe 3+ on the structure, antibody-binding capacity, and functional properties of WPI. The results showed that MPN modification significantly reduced the antibody-binding capacity of WPI with immunoglobulin E and IgG binding reduced by 76.40 % and 84.74 %, respectively. Multispectroscopy and liquid chromatography–tandem mass spectrometry analyses suggest that this reduction is due to the destruction of conformational epitopes and the masking of linear epitopes by MPNs. Additionally, the introduction of phenolic hydroxyl groups through MPN modification led to conformational unfolding of WPI and reduced surface hydrophobicity, thereby enhancing its antioxidant activity, hypoglycemic ability, and foaming properties. These improvements were more pronounced at higher doses. Specifically, at a dosage of 96 mM, the total antioxidant capacity is 44.01 % and the foaming properties are 104 %. This study provides new insights into the modification of WPI and offers a promising strategy for developing hypoallergenic foods products.

CAS / MDL: 148707-39-5
研究领域: 食品科学 · 过敏研究 · 蛋白质化学 · 生物功能特性 · 纳米技术
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JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY · 2025 · IF 6.2

Molecular Mechanism of Glycation Structure-Mediated Immune Recognition and Sensitization by Typical Milk Allergens

Qiaozhi Zhang,Youliang Song,Yuhao Jiang,Aiqian Ye,Zhongshan Gao,Kan Jiang,Linglin Fu

This study examines how α-dicarbonyl compounds─methylglyoxal (MGO) and glyoxal (GO)─affect the structure and allergenicity of β-lactoglobulin (β-LG) and α-casein (α-CN) during thermal processing. Glycation-induced changes were analyzed using SDS-PAGE, circular dichroism, and HPLC-MS/MS, while advanced glycation end-products (AGEs) were quantified via UHPLC-QqQ-MS/MS. Results showed that GO was more reactive than MGO, modifying Lys/Arg residues and increasing AGEs in a temperature- and concentration-dependent manner. Glycation reduced the IgE-binding capacity of β-LG but enhanced that of α-CN. In vitro studies revealed that glycated β-LG disrupted Caco-2 monolayer integrity and was more efficiently internalized by bone marrow-derived dendritic cells (BMDCs), upregulating costimulatory factors including CD80, CD86, and CD103. Transcriptomic analysis of monocyte-derived dendritic cells linked glycated β-LG to IL-17, the Toll-like receptor, and NF-κB pathways. Further pathway inhibition experiments demonstrated that the TLR4/NF-κB axis is an important contributor to BMDC maturation and inflammatory cytokine production induced by glycated β-LG. These findings demonstrate that MGO and GO alter the conformational structures and IgE-binding epitopes of milk allergens during heating, differentially modulating their allergenicity. This study provides mechanistic insights into how thermal processing affects the allergenic properties of food allergens, offering new strategies for food safety evaluation and allergy control.

研究领域: 食物过敏 · 分子免疫学 · 食品化学 · 结构生物学 · 细胞生物学 · 分子机制
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