FOOD CHEMISTRY
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2021
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IF 7.514
Xin Qi,Duoxia Xu,Jinjin Zhu,Shaojia Wang,Jingwei Peng,Wei Gao,Yanping Cao
In this study, the interaction of ovalbumin with lutein dipalmitate and the effect of ovalbumin on marigold lutein esters extracts were investigated. Lutein dipalmitate quenched the fluorescence of ovalbumin by static quenching. Binding and thermodynamic parameters proved that lutein dipalmitate bound to ovalbumin spontaneously by van der Waals force and hydrogen bond, and the complex stoichiometry was 1:1. Through three-dimensional fluorescence spectroscopy, Fourier transform infrared spectroscopy and circular dichroism experiments, the conformation of ovalbumin was unfolded, and alteration in the ovalbumin secondary structure induced by lutein dipalmitate was observed. The results of transmission electron microscopy and particle size revealed that there were spherical and nano-sized aggregates in the ovalbumin-lutein dipalmitate system, indicating the lutein dipalmitate not only could bind to ovalbumin at molecular level, but also promote the aggregation of ovalbumin. Additionally, the addition of ovalbumin had a positive effect on the stability of marigold lutein esters extracts.
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高影响因子
FOOD CHEMISTRY
·
2026
·
IF 10.4
Yitong Wang,Rui Wang,Qiaoying Guo,Xiaoqian Xu,Hui Teng,Lei Chen,Yanan Zhao
Hydrogen bonding and hydrophobic interactions were the major forces involved in the OVA-FUC complex. • The formation of the OVA-FUC complex resulted in enhanced emulsifying properties compared to individual OVA or FUC. • The galangin-loaded emulsion based on the OVA-FUC complex possessed potent antioxidant activity. • Galangin-loaded emulsion potentiates the oxidative stress resistance of Caenorhabditis . The effective delivery of hydrophobic bioactive compounds remains a major challenge in functional food and nutraceutical applications because of their poor aqueous solubility, limited physicochemical stability, and insufficient bioavailability. In this study, ovalbumin-fucoidan (OVA-FUC) complexes were constructed as food-grade stabilizers to develop galangin (GAL)-loaded emulsions with improved stability and antioxidant efficacy. The interaction mechanism, emulsion stability, and antioxidant activity were evaluated using structural characterization, interfacial analysis, storage tests, chemical antioxidant assays, and an ethanol-induced oxidative stress model in Caenorhabditis elegans . Results showed that OVA and FUC formed complexes mainly through hydrogen bonding and hydrophobic interactions. The 1-1 OVA-FUC complex exhibited the most favorable interfacial behavior and produced emulsions with superior storage stability. The GAL-loaded emulsion showed strong ABTS radical-scavenging activity (74.33 ± 7.60%) and effectively reduced ROS, lipofuscin, and MDA levels while increasing glutathione content and improving locomotor activity in C. elegans. These findings reveal that controlled OVA-FUC interactions can optimize interfacial assembly and emulsion stability, offering a practical strategy to improve the functional delivery of hydrophobic antioxidants in food systems. Download: Download high-res image (200KB) Download: Download full-size image
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FOOD RESEARCH INTERNATIONAL
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2026
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IF 8
Kaili Wang,Xu Zhao,Tong Zhang,Sijia Yang,Sufang Duan,Aili Li,Lu Li
Food allergy (FA) is characterized by an imbalance in T helper cell responses, specifically a dysregulation of the Th17 and Treg cells. While bovine milk exosomes (BMEs) are known to possess immunomodulatory properties, their role in modulating Th17/Treg balance in FA remains unclear. This study aimed to investigate whether BMEs could alleviate FA by restoring Th17/Treg balance and to identify the key miRNA mediators involved, particularly focusing on the STAT signaling pathway. An OVA-sensitized mouse model of FA was established. Mice were treated with varying doses of BMEs. Symptoms, immune parameters, cytokine levels, and relevant signaling pathways were assessed. High-throughput sequencing and bioinformatics were used to identify miRNA candidates. Functional validation was performed using gain- and loss-of-function experiments in splenic lymphocytes. The results showed that BMEs administration significantly alleviated FA symptoms in a dose-dependent manner, restored Th17/Treg balance, and suppressed STAT3/p-STAT3/RORγt activation. High-throughput sequencing revealed miR-320a as a key BME-derived miRNA that targets the STAT pathway. Functional experiments demonstrated that miR-320a overexpression in OVA-sensitized lymphocytes significantly reduced specific antibody production, promoted Treg cell differentiation, and downregulated the STAT3/p-STAT3/RORγt pathway. Conversely, miR-320a knockdown yielded opposing effects, exacerbating the allergic response. BMEs alleviate FA by delivering miR-320a, which targets the STAT3/RORγt axis and corrects Th17/Treg imbalance. These findings reveal a novel cross-species regulatory mechanism of BMEs and support their potential as a natural intervention strategy for FA.
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FOOD CHEMISTRY
·
2023
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IF 8.8
Quanshou Feng,Zehu Xie,Hongze Liang,Chuan-Fan Ding,Yinghua Yan
Ovalbumin (OVA) is an important protein source in our daily life. Unfortunately, the food safety problem has become more and more serious, such as protein allergy and contaminated protein. Therefore, it is necessary to detect vital proteins efficiently and rapidly. Mass spectrometry (MS) is a powerful tool for the detection of proteins. Herein, dual amino acids functionalized covalent organic frameworks containing disulfide covalent bonds ( [email protected] [email protected] , where G is glutathione and C is cysteine) were facilely prepared for OVA enrichment through hydrophilic interaction liquid chromatography (HILIC) under physiological pH. The results showed that [email protected] [email protected] had displayed sensitive detection (0.1 fmol), good selectivity (OVA: BSA = 1:100), adsorption capacity (311 mg/g), stability, reproducibility, linearity, LOQ level (42 μg/mL) and recovery ratio (64.83 %) for OVA. [email protected] [email protected] also demonstrated satisfactory purification ability in the enrichment of egg white, indicating that [email protected] [email protected] had great potential in the enrichment of protein from complex samples.
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JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
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2022
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IF 5.895
Bing Han,Yu Ma,Yixiang Liu
This study aimed to determine whether fucoxanthin alleviated ovalbumin (OVA)-induced food allergy (FA) and explored the possible mechanisms. The results indicated that supplementation with fucoxanthin at 10.0–20.0 mg/kg per day for 7 weeks inhibited food anaphylaxis and the production of immunoglobulin (Ig) E, IgG, histamine, and related cytokines while alleviating allergic symptoms in sensitized mice. Fucoxanthin enhanced the intestinal epithelial barrier by up-regulating tight junction (TJ) protein expression and promoting regenerating islet-derived protein III-gamma (RegIIIγ) and secretory IgA (sIgA) secretion. In addition, fucoxanthin induced the secretion of anti-inflammatory factors (interleukin (IL)-10 and transforming growth factor β (TGF-β)) by regulatory T (Treg) cells and decreased the pro-inflammatory factor levels (IL-4, tumor necrosis factor-α (TNF-α), IL-17, and IL-1β), ameliorating intestinal inflammation. Compared with the model group, beneficial bacteria, such as Lactobacillaceae, increased in the intestinal flora, while pathogenic bacteria like Helicobacteraceae, Desulfovibrionaceae, and Streptococcaceae decreased. Therefore, fucoxanthin may effectively prevent FA by enhancing the intestinal epithelial barrier and reshaping the intestinal flora.
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JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
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2022
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IF 5.895
Qiaozhi Zhang,Zhijie Huang,Huatao Li,Congnan Cen,Ruixing Zheng,Cao Lili,Shufen Zhang,Yanbo Wang,Linglin Fu
As a complex reaction, biological consequences of the Maillard reaction (MR) on dietary proteins need to be deciphered. Despite previous studies on the structural and antigenic properties of ovalbumin (OVA) by MR, associated changes induced by specific MR intermediates and their downstream products are largely unknown. This study focused on the impacts of glycation by α-dicarbonyl compounds (α-DCs), intermediates of MR and precursors of advanced glycation end-products (AGEs), on the structural and IgE-binding properties of ovalbumin (OVA) under simulated heating. Methylglyoxal (MGO), glyoxal (GO), and butanedione (BU) were selected as typical α-DCs to generate glycated OVA with different AGE-modifications (AGE-Ms). The results showed that reactions between OVA and α-DCs generated OVA-AGE with various degrees of modification and conformational unfolding, and the reactivity of α-DCs followed the order GO > MGO > BU. Depending on the precursor type, the levels of 10 specific AGEs were verified, and the amounts of total AGEs increased with heating temperature and α-DC dosage. Compared to native OVA, glycated OVA showed reduced IgE-binding levels but with sRAGE-binding ligands, the extent of which was associated with the contents of total AGEs and Nε-carboxymethyllysine, and changes in certain protein conformational structures. High-resolution mass spectrometry further identified different AGE-Ms on the Lys and Arg residues of OVA, confirming variations in the glycation sites and their associations with the immunoreactive epitopes of OVA under different conditions.
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Applied Sciences-Basel
·
2021
·Vol. 11
·期 24
·11815
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IF 2.679
Meiwen Lv,Xiukang Wang,Noman Walayat,Zhongli Zhang,Muhammad Hamzah Saleem,Asad Nawaz,Rana Muhammad Aadil,Shakeel Ahmed,Mario J. Simirgiotis,José M. Lorenzo,Basit Latief Jan
This study aimed to analyze the cryoprotective effect of a ovalbumin (OVA) and β-cyclodextrin (βCD) mixture (3:1, OVA/βCD) on the structure, rheology and gelling properties of myofibrillar proteins (MPs) during 90 days of frozen storage. A mixture of OVA/βCD at different concentrations (0, 2, 4, and 6%) was added to MPs and stored at −18 °C for 90 days. The addition of OVA/βCD significantly decreased the sulfhydryl contents while it increased the surface hydrophobicity, which was closely connected with tertiary structural changes. Circular dichroism analysis showed that the addition of OVA/βCD enhanced the stability of the secondary structure by inhibiting the decline in the α-helix. Rheological properties analysis indicated that 6% OVA/βCD treatment showed better storage modulus (G’) and loss modulus (G”). In addition, treatment of OVA/βCD showed better gel forming properties than the control group (0%), helping to form a homogeneous and denser gel network. The results proved that 6% OVA/βCD could be act as a promising cryoprotectant, which can improve the structure and gel behavior ofCulter alburnusMPs during frozen storage. Moreover, OVA/βCD could be a potential alternative to conventional cryoprotectants at the industrial level to increase the economic and commercial values of seafood products.Keywords:myofibrillar proteins;ovalbumin;β-cyclodextrin;cryoprotectant;frozen storage
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JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE
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2023
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IF 4.1
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.
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FOOD HYDROCOLLOIDS
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2020
·
IF 7.053
Chuyue Xiang,Jian Gao,Haoxin Ye,Gerui Ren,Xiangjuan Ma,Hujun Xie,Sheng Fang,Qunfang Lei,Wenjun Fang
Vitamin D 3 (VD 3 ) is a fat-soluble vitamin and easily degraded under acidic conditions, which will greatly reduce its bioavailability. The use of complexes formed by protein-polysaccharide to control release and protect active compounds has become a feasible way in the food field. In this work, ovalbumin (OVA) and high methoxyl pectin (PEC) were applied to fabricate OVA-PEC nanocomplexes to encapsulate and protect VD 3 . The encapsulation efficiency of VD 3 by OVA-PEC complexes could reach to 96.37%, and the storage stability of VD 3 was obviously improved after encapsulation. The in vitro simulated gastrointestinal experiments combined with SEM and SDS-PAGE were employed to observe the digestive behavior of OVA-PEC-VD 3 nanocomplexes. A small amount of VD 3 is released from OVA-PEC-VD 3 nanocomplexes in simulated gastric fluid, while a large amount of VD 3 is released in simulated intestinal fluid. The sustained release kinetic of VD 3 from OVA-PEC-VD 3 nanocomplexes was consistent with the law of Higuchi model. The preliminary molecular mechanism for VD 3 encapsulation by OVA-PEC complexes was also investigated, and the formation of OVA-PEC-VD 3 nanocomplexes is ascribed to the electrostatic interactions, hydrogen bonding and hydrophobic interactions among OVA, PEC and VD 3 . The results demonstrated that protein-polysaccharide complexes can effectively encapsulate VD 3 and achieve the goal of sustained release in the simulated gastrointestinal tract, which have potential applications in food and medicine.
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FOOD CHEMISTRY
·
2018
·
IF 4.946
Yang Chen,Zong-cai Tu,Hui Wang,Guang-xian Liu,Zi-wei Liao,Lu Zhang
In general, the reducing sugars were extensively utilized as additives to prevent denaturation and inactivation during the freeze-drying process. However, different additives have unequal protective effects on the protein conformation. To evaluate the mechanism of protection the protein structure using different additives in the freeze-drying process, the glycated sites and degree of substitution per peptide (DSP) of each site were investigated by LC-Orbitrap MS. We found that the ovalbumin that was supplemented with ribose and then lyophilized (R-oval) have the highest extent of glycation modification. K227 was the most reactive glycated site in R-Oval, with a DSP of 0.83. The ovalbumin that was supplemented with lactose and then lyophilized (L-Oval) have the lowest degree of glycation, and K227 did not undergo the glycation reaction. It was hypothesized that the order impact of different additives on protection of the protein conformation were lactose > galactose > ribose during the freeze-drying process.
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COLLOIDS AND SURFACES B-BIOINTERFACES
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2017
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IF 3.887
Zhouyi Xiong,Meihu Ma
To improve the interfacial properties, a phosphorylation modification of OVA was performed through dry-heating at three different pH values (5.0, 7.0 and 9.0) in the presence of sodium tripolyphosphate. X-ray photoelectron and Raman spectroscopies confirmed that phosphate groups were successfully grafted onto the ovalbumin backbone through covalent interaction to form O P bond. Additionally, 23, 21 and 18 phosphorylation sites were identified in the OVA that had been phosphorylated at pH 5.0, 7.0 and 9.0 (P-OVA5, P-OVA7 and P-OVA9) respectively by MALDI-TOF mass spectroscopy. More phosphorylated peptides and possible phosphorylation sites were found here than in previous studies with the reaction time reduced to 12 h. As a result, the iso-electric point (pI) of P-OVA shifted to lower pH, improving the stability of the P-OVA-included system over a wider pH range. The dynamic interfacial tension, which depends on the phosphorylation-induced conformational change, was explored by Fourier-transform Raman and circular dichroism spectroscopies, and the equilibrium interfacial tension decreased from 17.359 mNm −1 for natural OVA (N-OVA) to 15.969 mNm −1 for P-OVA9. Furthermore, P-OVA was applied to O/W emulsions, resulting in a narrower size distribution with a smaller particle size in P-OVA-stabilized emulsions than in N-OVA-stabilized emulsions. The increase rate of mean particle diameter after 60-min storage decreased from 72.37% for N-OVA to 7.97% for P-OVA5, implying a significant improvement of emulsion stability by preventing aggregation and coalescence. The results from this work demonstrated that the natural biopolymer can be applied to O/W emulsions by enhancing interfacial properties with phosphorylation.
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高影响因子
FOOD CHEMISTRY
·
2021
·
IF 7.514
Long Sheng,Qiao Liu,Wanyi Dong,Zhaoxia Cai
In this paper, the effects of ultrasonic assisted glycosylation on the gel properties of ovalbumin (OVA) were studied. The molecular characteristics of native ovalbumin, heated ovalbumin, traditional glycosylated ovalbumin, ultrasonic ovalbumin and ultrasonic assisted glycosylated ovalbumin were compared. The lowest free amino group content and the highest browning intensity indicated that ultrasonic can facilitate the Maillard reaction. The gel hardness of ultrasonic glycosylation and the traditional heating glycosylation groups individually increased to 653.2 and 526.9 g compared with the control (344.9 g). The transformation of protein structure was confirmed by FTIR and fluorescence spectrum, which prompted negatively charged groups to reach the protein surface and form more disulfide bond in sOVA-X gel. The interaction between the water and the protein was strengthened, thereby increasing the water holding capacity. These results supplied a theoretical basis for the application of ultrasonic to improve protein properties.
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