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ovalbumin
Food Bioscience · 2026 · IF 5.9

Curcumin cellular delivery based on assembly of clover shaped trityl polyethylene glycols with ovalbumin

Zhe Zheng,Songbai Liu

Novel curcumin (Cur) cellular delivery system based on assembly of clover shaped trityl polyethylene glycol (TrPEG) with heat denatured ovalbumin (OVA) through hydrophobic interactions was developed in this study. TrPEGs of different degree polymerization (n = 3, 6, 9) were prepared by the coupling of trityl chloride and PEGs under the optimized condition, and the structures were verified by NMR and MS measurements. The excellent amphiphilic and biocompatible TrPEG-9 demonstrated marvelous selective binding capability with the denatured OVA and stabilization of the assembled particles through the clover shaped head. Introduction of TrPEG-9 (EG) with OVA significantly enhanced encapsulation efficiency (83 %) of Cur and afforded uniform compact nanoparticles (63 nm). Evaluation by Saccharomyces cerevisiae model revealed effectively promoted Cur cellular delivery and significantly reactive oxygen species (ROS) reduction capacity of EG-OVA-Cur, and clathrin-mediated endocytosis and macropinocytosis cellular uptake followed by intracellular vacuolar trafficking. This assembled system has great potential for cellular delivery of nutraceutical and biomedical bioactives.

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INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES · 2026 · IF 8.7

Ovalbumin–peanut protein isolate emulsion gels for enhanced co-delivery of curcumin and quercetin

Meiyu Zhou,Jinxin Wang,Weiwei Cheng,Erna Li,Feng Xiao,Jialiang He,Lili Liu,Baocheng Xu

A Dual-Synergy strategy integrates supramolecular co-assembly with heterogeneous protein networks for efficient delivery. • DFT and IGMH analyses reveal π–π and C–H···π interactions drive Cur–Que co-assemblies’ synergistic antioxidant activity. • Cur/Que. co-assemblies reinforce the OVA/PPI network via extensive non-covalent interactions, elevating T peak to 91.21°C. • The composite gel restricts lipid digestion and boosts Cur and Que in vitro bioavailability to 58.96% and 63.17%. Hydrophobic phytochemicals often show limited solubility and low bioaccessibility during digestion, which restricts their use in functional food systems. In this study, a protein-based emulsion gel was developed by embedding a curcumin–quercetin supramolecular co-assembly within a composite network formed from ovalbumin and peanut protein isolate. The curcumin–quercetin co-assembly at a 5:5 ratio showed the strongest synergistic antioxidant activity, with a combination index of 0.598. Density functional theory calculations and independent gradient model analysis based on Hirshfeld partition indicated that π–π stacking and C–H···π interactions stabilized the co-assembled structure, modulated frontier orbital energy levels, reduced the energy gap, and increased electrophilicity, thereby enhancing radical-scavenging activity. The ovalbumin–peanut protein isolate composite at a 5:5 ratio formed a well-developed gel network and generated nanoscale embedded structures of approximately 779 nm through electrostatic and hydrophobic interactions. Incorporation of 1% curcumin–quercetin co-assembly resulted in encapsulation efficiencies above 97% for both phytochemicals. It also increased the storage modulus by 77.5% and improved water-holding capacity to 82.15%. Low-field nuclear magnetic resonance analysis showed a higher proportion of bound water, while the thermal transition temperature increased from 81.83 to 91.21 °C. These results indicate that the co-assemblies served as active crosslinking domains within the protein network through hydrogen bonding and hydrophobic interactions. During simulated digestion, the integrated co-assembly gel system delayed lipid digestion, with a free fatty acid release of approximately 58.55%, and increased the bioaccessibility of curcumin and quercetin to 58.96% and 63.17%, respectively. This study reveals how molecular co-assembly and protein gel structuring jointly improve the stability and delivery performance of hydrophobic phytochemicals, providing a basis for designing nutrient-dense functional food delivery systems.

✓ 已验证 DOI PubMed 高影响因子
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JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY · 2023 · IF 6.1

Mechanism of Targeted Regulation of Ovalbumin Epitopes by Pulsed Electric Field-Assisted Alcalase Treatment

Yinli Li,Jie Ding,Liu Dong,Na Sun,Songyi Lin

Egg is one of the eight major food allergens, and ovalbumin (OVA) is the most abundant allergenic protein in eggs. In this study, the effects of pulsed electric field (PEF)-assisted Alcalase hydrolysis on the spatial conformation and potential allergenicity of OVA were studied, and the mechanism of its inhibiting allergic reactions effect was revealed. PEF-assisted Alcalase hydrolysis increased the degree of hydrolysis, surface hydrophobicity, and free sulfhydryl group content. Moreover, the reduction in the α-helix content, fluorescence intensity, and disulfide bond content suggested that PEF promoted the OVA hydrolysis by Alcalase. Additionally, enzyme-linked immunosorbent assay data indicated that PEF-assisted Alcalase hydrolysis hindered OVA binding to immunoglobulins E and G1. Finally, based on bioinformatics combined with mass spectrometry, PEF-assisted Alcalase reduced OVA-induced allergic reactions by destroying epitopes in OVA. Overall, PEF technology further destroyed the epitopes of allergens by targeting the binding sites of substrates and enzymes to improve the affinity of enzymes and substrates, reducing allergic reactions.

CAS / MDL: 69-78-3 643-79-8
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INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES · 2021 · IF 6.953

Molecular structure modification of ovalbumin through controlled glycosylation with dextran for its emulsibility improvement

Yimei Zheng,Yu Chang,Biying Luo,Hui Teng,Lei Chen

Ovalbumin (OVA) is a high nutritious protein, but the poor emulsibility limited its application. The present study glycosylated OVA with dextran (Dex) by controlled wetheating (60–90 °C for 3 h). Temperature was an inductive factor for glycosylation degree (DG and browning intensity), and higher temperature could accelerate the reaction. Variations in molecular structure of OVA were analyzed by SDS-PAGE, FTIR, fluorescence spectroscopy and UV spectroscopy, which verified successes in the generation of glycoconjugate with more flexible structure. Emulsifying activity index (EAI) and emulsion stability index (ESI) for the emulsion of OVA-Dex glycoconjugates were significantly enhanced with the increasing of glycosylation temperature. Moreover, confocal laser scanning results revealed that the emulsion exhibited smaller size and more uniform distribution, and slower transmission profiles were checked by LUMiSizer centrifugal analysis as well, confirming the emulsibility improvement of OVA. Thus, controlled glycosylation reaction is an available method to improve the emulsifying properties of OVA.

CAS / MDL: 9048-71-9 9004-54-0
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CHEMICAL PHYSICS · 2020 · IF 1.771

Structural transitions of ovalbumin/κ-carrageenan complexes under the effects of pH and composition

Zhizhuo Lu,Lihong Wang,Hujun Xie,Qunfang Lei,Wenjun Fang,Xiaoxing Lu

Colloid particles consisting of biopolymers such as proteins and polysaccharides have been widely used as food or drug components. Here we investigate the interactions and structures in aqueous mixtures of ovalbumin (OVA) and κ-carrageenan (CRG) to unravel the complexation mechanism. The pH titration results for the OVA/CRG system (0.025%:0.025% by mass) indicate the structural transition of the OVA/CRG complexes happens during acidification. Significant accumulation of insoluble OVA/CRG complex coacervates with OVA packed in the hydrophobic structures formed by CRG occurs when pH is lower than the isoelectric point of OVA. The highest turbidity is reached at pH = 3.0 because of the strongest electrostatic attraction, and further deceasing pH leads to the dissociation of complex coacervates. Composition and ionic strength show significant effects on turbidity and aggregates formation by tuning electrostatic interactions between N–H + of –NH 3 + on OVA and S–O − of –SO 3 − on CRG.

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JOURNAL OF MATERIALS SCIENCE · 2021 ·Vol. 56 ·期 34 ·19283-19295 · IF 4.22

Biocompatible mesoporous polymeric ionic liquid with high adsorption capacity for selective isolation of ovalbumin

Qi Shoujing,Zhang Chunyu,Hu Zhengjie,Chen Xuwei

Ionic liquids are becoming widely applied in the extraction/separation of biological molecules. In this study, the solidification of ionic liquid 1-hydroxyethyl-3-vinylimidazole chloride ([HVIM]Cl) was achieved via one-pot free radical copolymerisation with divinylbenzene (DVB) as a cross-linking reagent, giving a mesoporous hydrophilic polymeric ionic liquid (PIL). Mesoporous PIL possesses a large surface area of 328.32 m 2 ·g −1 and a high pore volume of 0.45 cm 3 ·g −1 . Owing to hydrophilic interactions and π–π stacking interactions, the PIL adsorbs ovalbumin (Ova) selectively with a theoretical maximum adsorption capacity of 2468.0 mg·g −1 , and this Ova adsorption fit the Langmuir model well. The captured Ova was efficiently recovered using sodium dodecyl sulphate (0.4%, m·v −1 ) with an elution efficiency of 94.7%. Circular dichroism spectra indicated that the adsorption-elution process caused no conformational changes in Ova, indicating that the prepared PIL is highly biocompatible. The practicability of this mesoporous PIL was well demonstrated by the selective adsorption of Ova from protein mixtures and the efficient isolation of Ova from chicken egg white. Graphical abstract

CAS / MDL: 78-67-1 288-32-4 77-86-1
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INTERNATIONAL JOURNAL OF FOOD PROPERTIES · 2020 · IF 1.808

Enzymolysis kinetics and structural-functional properties of high-intensity ultrasound-assisted alkali pretreatment ovalbumin

Lili Liu,Weiming Hao,Xiaoning Dai,Yang Zhu,Ke Chen,Xiaopan Yang

This research investigated the enzymolysis kinetics of high-intensity ultrasound (HIU)-assisted alkali pretreatment Ovalbumin (OVA) through using Alcalase, and its structural and functional properties. The structural characteristics of OVA were performed with sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), surface hydrophobicity, Fourier Transform Infrared, and differential scanning calorimetry. SDS-PAGE analysis indicated that the pretreatment sample showed proportion of lower molecular mass components (14.3–20.1 kDa). There was an increase in the intensity of fluorescence spectrum and changes in functional groups after the pretreatment on OVA compared with the control (without treatment), which might be the reason for the significantly enhancing efficiency of the enzymatic hydrolysis. The thermal denaturation temperature of enzymatic hydrolysis of OVA after pretreatment was 95.1°C, which was 17.5°C higher than that of control. As compared to OVA (control), the enzymatic hydrolysis with HIU-assisted alkali pretreatment was found to significantly improve protein solubility, emulsifying properties, foaming ability (FA) and foam stability, oil, and water absorption capacity (WAC). Especially emulsifying activity index, FA, WAC, and oil absorption capacity were increased by 228.7%, 88.5%, 102.6%, and 67.4%, respectively (P< 0.05). A simplified kinetic equation for the enzymolysis model was deduced to successfully describe the enzymatic hydrolysis of pretreated OVA. The results proved the effects of the pretreatment on the substrate enhanced the enzymolysis process and this influence had relation to the structure changes. Furthermore, the enzymatic hydrolysis process for other proteins demonstrated the applicability of the model.

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FOOD HYDROCOLLOIDS · 2019 · IF 5.839

Pomegranate seed oil stabilized with ovalbumin glycated by inulin: Physicochemical stability and oxidative stability

Bing Hu,Kangping Wang,Lingyu Han,Bin Zhou,Jixin Yang,Shugang Li

Pomegranate seed oil is rich of conjugated fatty acids which are highly appealing for a variety of applications in food industry. In this research, ovalbumin (OVA) and ovalbumin-inulin glycoconjugates with different Maillard reaction times were used to stabilize pomegranate seed oil emulsions and their impact on physicochemical stability and oxidative stability of the products was investigated. The OVA-inulin glycoconjugate produced on 10th day of Maillard reaction has exhibited significantly higher conjugation efficiency, lower surface hydrophobicity and lower surface tension than other glycoconjugates . The secondary conformation of OVA and conjugates determined by far-UV circular dichroism spectroscopy has remarkably changed. The reduction in intensity of Trp-fluorescence observed in glycated proteins with inulin indicated that the glycation affected partially the side chains of protein in tertiary structure through the Maillard reaction without great disruption of native structure. The emulsion stabilized by OVA-inulin glycoconjugate obtained by 10 days Maillard reaction has shown the best physicochemical stability. Compared with the OVA emulsion, the oxidative stability of the glycated OVA emulsion system was significantly improved (p < 0.05). Fatty acid profile results also confirmed that OVA-inulin glycoconjugates were able to prevent the pomegranate seed oil from oxidation . It is suggested that the inulin attached to OVA by glycation played a vital role in physicochemical stability and oxidative stability of pomegranate seed oil emulsions.

CAS / MDL: 1898-66-4
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FOOD HYDROCOLLOIDS · 2018 · IF 5.089

Fabrication of ovalbumin/κ-carrageenan complex nanoparticles as a novel carrier for curcumin delivery

Hujun Xie,Chuyue Xiang,Yang Li,Lihong Wang,Yutong Zhang,Zhijun Song,Xiangjuan Ma,Xiaoxing Lu,Qunfang Lei,Wenjun Fang

Natural biopolymers are biocompatible and biodegradable, and have been a focus on the research of biologically active carrier materials. In this manuscript, the nanoparticles of ovalbumin/ κ -carrageenan (OVA-CRG) complex were fabricated to encapsulate and protect curcumin under moderate conditions, forming the ovalbumin/ κ -carrageenan/curcumin (OVA-CRG-CUR) complex nanoparticles. The OVA-CRG complex nanoparticles show good curcumin entrapping performance, and the addition of curcumin does not affect the emulsifying stability (ES) and emulsifying activity (EA) of OVA-CRG complex nanoparticles. The maximum ES of OVA-CRG-CUR is reached at 36 h with the value of 84.6 min, and the maximum EA is reached at 48 h with the value of 74.2 m 2 /g. The encapsulated curcumin demonstrates high antioxidation activity, while its thermal and light stabilities of curcumin are both increased. The release behavior of curcumin is further studied in simulated gastric and intestinal fluids. The lower release rate of curcumin in simulated gastric fluid with the final value of 12.9% after 3 h indicates that the OVA-CRG complex nanoparticles are good carriers for improving the stability of curcumin in acidic environment, and are able to enhance the bioavailability of curcumin by a gradual release in intestine. Present researches elucidate that proteins-polysaccharides complex nanoparticles are feasible to solubilize and protect sensitive amphiphilic bioactive compounds and have extensive potential in food and medicinal applications.

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FOOD CHEMISTRY · 2024 · IF 8.5

Cold plasma for enhancing covalent conjugation of ovalbumin-gallic acid and its functional properties

Chang Liu,Pan-Pan Tang,Xiu-Bin Liu,Jun-Xiang Liu,Xiao-Hong Pan,Rana Muhammad Aadil,Jun-Hu Cheng,Zhi-Wei Liu

The utilization of cold plasma (CP) treatment to promote covalent conjugation of ovalbumin (OVA) and gallic acid (GA), as well as its functionality, were investigated. Results demonstrated that CP significantly enhanced the covalent grafting of OVA and GA. The maximum conjugation of GA, 24.33 ± 2.24 mg/g, was achieved following 45 s of CP treatment. Covalent conjugation between GA and OVA were confirmed through analyses of total sulfhydryl (-SH) group, Fourier transform infrared (FTIR) spectroscopy, and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Unfolding of the OVA molecule occurred upon conjugation with GA, as evidenced by multiple spectroscopy analyses. Additionally, conjugation with GA resulted in significant improvements in the antioxidant activity and emulsifying properties of OVA. This study demonstrated that CP is a robust and sustainable technique for promoting the covalent conjugate of polyphenols and proteins, offering a novel approach to enhance the functional properties of proteins.

CAS / MDL: 69-78-3
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Food Chemistry-X · 2024 · IF 6.5

Effect of glycation with three polysaccharides on the structural and emulsifying properties of ovalbumin

Yaxue Hu,Qiqi Bian,Lijia Chen,Xichang Wang,Jian Zhong

Herein, three types of ovalbumin (OA)-polysaccharide conjugates were prepared with three polysaccharides (XG: xanthan gum; GG: guar gum; KGM: konjac glucomannan) for the fish oil emulsion stabilization. The glycation did not change the spectra bands and secondary structure percentages of OA, whereas it decreased the molecular surface hydrophobicity of OA. The initial emulsion droplet sizes were dependent on the polysaccharide types, OA preparation concentrations, polysaccharide: OA mass ratios, and glycation pH. The emulsion stability was mainly dependent on the polysaccharide types, polysaccharide: OA mass ratios, and glycation pH. However, it was minorly dependent on the OA preparation concentrations. The emulsions stabilized by conjugates with high polysaccharide: OA mass ratios (e.g., ≥3:5 for OA-GG) or appropriate glycation pH (e.g., 5.0–6.1 for OA-XG) showed no obvious creaming during the room temperature storage. This work provided basic knowledge on the structural modification and functional application of a protein.

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EXPERIMENTAL ANIMALS · 2023 · IF 2.4

Lonicerin alleviates ovalbumin-induced asthma of mice via inhibiting EZH2/NF-κB signaling pathway

Rui DAI,Yun XIANG,Rui FANG,Hai-Han ZHENG,Qing-Song ZHAO,Yan WANG

Asthma is the most common chronic disease in the respiratory system of children caused by abnormal immunity that responses to common antigens. Lonicerin exerts anti-inflammatory activity in other inflammatory models through targeting enhancer of zeste homolog 2 (EZH2) that is related to asthma. We sought to explore the role and mechanism of lonicerin in regulating allergic airway inflammation. Mice were intraperitoneally injected 10 μg ovalbumin (OVA) on postnatal day 5 (P5) and P10, and then inhaled 3% aerosolized OVA for 10 min every day on P18–20, to establish asthmatic mice model. Lonicerin (10 or 30 mg/kg) was given to mice by intragastric administration on P16–P20. Notably, the administration of lonicerin amended infiltration of inflammatory cells and mucus hypersecretion. OVA-specific IgE level, inflammatory cell count and inflammatory cytokines in asthmatic mice were reduced after lonicerin treatment. Moreover, it suppressed the activity of EZH2 and activation of nuclear factor-kappa B (NF-ĸB) as evidenced by decreasing tri-methylation of histone H3 at lysine 27 and reducing nuclear translocation of NF-κB p65. In a word, Lonicerin may attenuate asthma by inhibiting EZH2/NF-κB signaling pathway.

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