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INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES · 2020 · IF 5.162

Relationship between gel properties and water holding of ovalbumin-carboxymethylcellulose electrostatic complex hydrogels

Wenfei Xiong,Ya Li,Bin Li,Fang Geng

The relationship between the water holding (WH) and gel properties of protein-based hydrogels is important for designing and regulating the texture and sensory properties of foods. Herein, the relation among WH and heat-set gel properties of ovalbumin (OVA)-carboxymethylcellulose (CMC) electrostatic complexes was explored. The results showed that the gels exhibited homogeneous and dense structure and good WH compared with pure OVA at pH 4.6, while Young's modulus decreased significantly ( P  < 0.05). This was closely related to the inhibition of the electrostatic interaction on the formation of large protein aggregates during heat treatment (90 °C, 30 min). Specially, the CMC1.2 (the degree of substitution was 1.2) with higher charge density showed stronger interference than CMC0.7 (the degree of substitution was 0.7) for the gel network structure and properties. Moreover, the addition of salt ions could enhance the gel strength. Meanwhile, the coarseness and microstructure pore size were also increased with enhancing of ionic strength , resulting in a significant decrease in the WH. The effective permeability coefficient (k 1 ) and water flux coefficient (k 2 ) of gels have a significant positive correlation with their network pore size, indicated that the regulation of WH of hydrogel mainly depended on controlling the pore size of its microstructure.

CAS / MDL: 9004-32-4
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FOOD HYDROCOLLOIDS · 2023 · IF 10.7

Heteroprotein complex coacervation of ovalbumin and lysozyme: Phase behavior, microstructure and processing properties

Zhaohui Yan,Jingbo Liu,Chenman Li,Jianqi Ren,Zhi Wang,Renzhao Zhang,Xuanting Liu

Egg white protein is a complex network system formed by the aggregation and interaction of multiple proteins, in which two oppositely charged proteins can induce the formation of heteroprotein complex coacervate (HPCC). This investigation aims to probe the complexation between ovalbumin (OVA) and lysozyme (LYS) via the heteroproteins phase diagram model, exploring the relationship between differential processing properties and complex state, protein molecular structure and intermolecular interactions. Results showed that the characteristic pH (pH c , pH ɸ1 , pH max , pH ɸ2 ) intensely relied on the protein ratios. Consequences of ζ-potential and the phase diagram manifested that OVA-LYS complex formation was predominantly triggered by electrostatic interactions. With the increasing OVA-LYS mixing ratio, the characteristic pH of the complex moved towards a higher pH value. By comparing the microphase structure of different phase regions induced by pH, we found that the protein structure unfolded at low pH, elevating the foaming and emulsifying capacity. Moreover, further increases in pH value brought on larger insoluble complex formation, which enhanced the foaming stability while decreased the emulsifying stability. Noteworthy, the coacervates obtained in the narrow range of pH 6.5–9.5 presented the strongest gel strength and highest water holding capacity , which was considered to be an efficacious way to regulate the gel properties of egg white protein. On the whole, the findings of this paper developed prominent insight for understanding the interaction between heteroproteins, which would lay a theoretical foundation for improving the quality and efficiency of functional egg powder and product development.

CAS / MDL: 3326-32-7 36877-69-7
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BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY · 2023 · IF 1.6

Sulfur dioxide derivatives aggravated ovalbumin-induced asthma through targeting TRPV1 and tight junctions

Zhou Liping,Lao Zishan,Fan Xinsheng,Hao Mengyang,Yang Yubing

This study aimed to investigate the effects of sulfur dioxide (SO2) derivatives on asthma induced by ovalbumin (OVA). Sprague Dawley rats were sensitized to and challenged with OVA and SO2 derivatives (NaHSO3 and Na2SO3, 1:3 M/M) to establish 28-day (short-term) and 42-day (long-term) asthma models. Exposure to SO2 derivatives aggravated asthma and hence, promoted lung injury in OVA-induced asthma. In addition, it upregulated the protein expression of TRPV1 and downregulated the expression of tight junctions (TJs). These changes were dose-dependent and were more pronounced in the presence of a high concentration of SO2 derivatives. In vitro, SO2 derivatives also increased the calcium influx and TRPV1 protein expression, and decreased TJ expression. Besides, no significant difference in the TJ expression was found between the WT and TRPV1−/- mice. The underlying mechanism might be related to regulating the effects of TRPV1 and TJs.

CAS / MDL: 60-31-1 7631-90-5
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Food & Function · 2018 ·Vol. 9 ·期 7 ·3788-3797 · IF 3.289

Enhancing the photostability and bioaccessibility of resveratrol using ovalbumin–carboxymethylcellulose nanocomplexes and nanoparticles

Wenfei Xiong,Cong Ren,Jing Li,Bin Li

The objective of this study was to investigate the impact of encapsulating resveratrol in ovalbumin (OVA)–carboxymethylcellulose (CMC) nanocomplexes or nanoparticles on its photostability and bioaccessibility. The nanocomplexes were formed by the electrostatic assembly between OVA and CMC, and the nanoparticles were fabricated through further heating the nanocomplexes at 90 °C for 30 min. The nanocomplexes and nanoparticles both presented a spherical morphology, and the nanoparticles exhibited larger average particle sizes and net zeta potential. The encapsulation efficiency and loading capacity were around 26% and 13 μg mg−1 for OVA/CMC nanocomplexes, and evidently increased to around 70% and 35 μg mg−1 for OVA/CMC nanoparticles, respectively. The major driving forces for resveratrol encapsulation were hydrogen bonding and hydrophobic interaction. Both the formulations could improve the photostability of trans-resveratrol when exposed to UV light, and the nanoparticles were more effective. Moreover, the release profile of resveratrol from the nanocapsules in the in vitro simulated gastrointestinal tract was greatly enhanced and could be well fitted using the Higuchi kinetic model and Korsmeyer–Peppas model, indicating a Fickian diffusion release mechanism. Compared to native resveratrol, the bioaccessibility of resveratrol embedded in nanocomplexes and nanoparticles was increased to 60% and 80%, respectively. These findings suggest that OVA/CMC nanocomplexes and nanoparticles have potential applications in the development of effective oral delivery systems of resveratrol as well as other lipophilic nutraceuticals into functional foods.

CAS / MDL: 9004-32-4
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JOURNAL OF DRUG DELIVERY SCIENCE AND TECHNOLOGY · 2015 · IF 0.476

Controlled release of a model protein drug ovalbumin from thiolated hyaluronic acid matrix

Jinping Du,Fazhao Fu,Xinyue Shi,Zongning Yin

The objectives of this work were to investigate the properties of the thiolated hyaluronic acid (HA) with different molecular weights (MWs) and to assess the effects of MW and dissolution medium on the release of ovalbumin from thiolated HA matrix tablets. Four HA-cysteine (HA-Cys) conjugates with increasing MWs (47, 101, 260 and 550 kDa) were synthesized. The resulting HA-Cys conjugates exhibited increased stability against hyaluronidase degradation, and such an effect became stronger with the increase of polymer MW. Swelling and erosion studies of HAs or HA-Cys conjugates based matrix tablets were performed in various media. We found that the water uptake capacity and erosion rate were strongly dependent on MW of HA, ionic strength and pH of the medium. Release studies showed that all investigated factors exerted effects on the drug release. Most of the release data based on HA matrix tablets followed super Case II transport but conformed to non-Fickian diffusion with HA-Cys conjugates. Taken together, this work managed to develop HA-Cys conjugates-based matrix tablets as controlled release systems for protein with tunable release rate through varying MWs of polymer.

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INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES · 2017 · IF 3.671

Effects of site-specific phosphorylation on the mechanical properties of ovalbumin-based hydrogels

Zhouyi Xiong,Meihu Ma,Guofeng Jin,Qi Xu

An efficient one-step grafting approach was developed to modify ovalbumin (OVA) by phosphorylation through selective reaction with the hydroxyl group of Ser and Thr residues present in OVA. The site-specific phosphorylated conjugates were characterized by Matrix-Assisted Laser Desorption Ionization-Time-of-Flight Mass Spectrometry (MALDI-TOF/MS) and the results indicated that the Ser residue could be more readily phosphorylated, and the typical phosphopeptides 264 LTEWTSSNVMEER 276 and 340 EVVGSAEAGVDAASVSEEFR 359 demonstrated the formation of monophosphoester. Moreover, 13 C NMR analysis showed that the βCH 2 of Ser acted as a hydroxyl donor to react with sodium tripolyphosphate (STPP), and the conjugates with variable phosphorylation sites could improve the weak network and the resulting poor mechanical properties of ovalbumin-based hydrogels. Furthermore, small-amplitude oscillatory measurements, creep recovery tests and texture profile analysis of hardness and stickiness indicated that phosphorylation can strengthen the intermolecular cross-linking of protein molecules and produce significant influence on the rheological behavior and texture properties, suggesting that a suitable conjugation site is essential for the best gelation properties at a different pH. The integrated results indicate that phosphorylation change significantly modify the viscoelastic and mechanical properties of OVA-based hydrogels by changing molecular dynamics upon heating.

CAS / MDL: 7758-29-4
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Foods · 2024 ·Vol. 13 ·期 8 ·1246 · IF 4.7

Enhancing Stability and Antioxidant Activity of Resveratrol-Loaded Emulsions by Ovalbumin–Dextran Conjugates

Wen Zhang,Lingli Meng,Xinyi Lv,Limin Wang,Pei Zhao,Jinrong Wang,Xinping Zhang,Jinyu Chen,Zijian Wu

A reliable strategy for improving the stability and shelf life of protein-stabilized systems is by covalently attaching the protein onto a polysaccharide. In this study, ovalbumin (OVA) was modified with dextran (DEX) of different molecular weights by the Maillard reaction, and was used to enhance the stability of emulsions loaded with resveratrol. The surface hydrophobicity, thermal stability, and FT-IR spectroscopy of the OVA–DEX conjugates were evaluated. The results showed that the surface hydrophobicity of OVA decreased, while the thermal stability of OVA was significantly improved after DEX covalent modification. The OVA–DEX1k-stabilized emulsion exhibited high encapsulation efficiency of resveratrol, with the value of 89.0%. In addition, OVA–DEX was considerably more effective in droplet stabilization against different environmental stresses (heat, pH, and ionic strength). After 28 days of storage at 25 °C, the OVA-stabilized emulsion showed faster decomposition of resveratrol, whereas the OVA–DEX-conjugate-stabilized emulsion had approximately 73% retention of resveratrol. Moreover, the antioxidant activity of resveratrol-loaded emulsions stabilized by OVA–DEX was higher during storage under different temperatures. These results proved that the OVA–DEX conjugates had the potential to form stable, food-grade emulsion-based delivery systems against environmental stresses, which strongly supports their potential in the field of food and biomedical applications.

CAS / MDL: 7727-21-1 28752-68-3
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Foods · 2024 ·Vol. 13 ·期 9 ·1336 · IF 4.7

Gut Microbiota-Derived Tryptophan Metabolites Alleviate Allergic Asthma Inflammation in Ovalbumin-Induced Mice

Hongchao Wang,Yuan He,Danting Dang,Yurong Zhao,Jianxin Zhao,Wenwei Lu

Asthma is a prevalent respiratory disease. The present study is designed to determine whether gut microbiota-derived tryptophan metabolites alleviate allergic asthma inflammation in ovalbumin (OVA)-induced mice and explore the effect and potential mechanism therein. Asthma model mice were constructed by OVA treatment, and kynurenine (KYN), indole-3-lactic acid (ILA), in-dole-3-carbaldehyde (I3C), and indole acetic acid (IAA) were administered by intraperitoneal injection. The percent survival, weight and asthma symptom score of mice were recorded. The total immunoglobulin E and OVA-specific (s)IgE in the serum and the inflammatory cytokines in the bronchoalveolar lavage fluid (BALF) were detected by the corresponding ELISA kits. The composition of the gut microbiota and tryptophan-targeted metabolism in mouse feces were analyzed using 16S rRNA gene sequencing and targeted metabolomics, respectively. The four tryptophan metabolites improved the percent survival, weight and asthma symptoms of mice, and reduced the inflammatory cells in lung tissues, especially I3C. I3C and IAA significantly (p< 0.05) downregulated the levels of OVA-IgE and inflammatory cytokines. KYN was observed to help restore gut microbiota diversity. Additionally, I3C, KYN, and ILA increased the relative abundance ofAnaeroplasma,Akkermansia, andRuminococcus_1, respectively, which were connected with tryptophan metabolic pathways. IAA also enhanced capability of tryptophan metabolism by the gut microbiota, restoring tryptophan metabolism and increasing production of other tryptophan metabolites. These findings suggest that tryptophan metabolites may modulate asthma through the gut microbiota, offering potential benefits for clinical asthma management.

CAS / MDL: 1821-52-9
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Frontiers in Immunology · 2024 · IF 5.7

Green carbon dots derived from Zingiberis Rhizoma Carbonisatum alleviate ovalbumin-induced allergic rhinitis

Long Zhou,Yingxin Yang,Tingjie Li,Yafang Zhao,Jinye Yuan,Chenxin He,Yan Huang,Jinyu Ma,Yue Zhang,Fang Lu,Jiaze Wu,Zijian Li,Hui Kong,Yan Zhao,Huihua Qu

Background: Allergic rhinitis (AR) affects up to 40% of the population, leading to significant healthcare expenditures. Current mainstream treatments, while effective, can lead to side effects and do not address the underlying immunological imbalances. Zingiberis Rhizoma Carbonisatum (ZRC), the partially charred product of Zingiberis Rhizoma (ZR), has been widely used clinically in China since ancient times to treat respiratory disorders.Methods: Inspired by the similarity between high-temperature pyrolysis and carbonization processing of herbal medicine, ZRC derived CDs (ZRC-CDs) were extracted and purified through several procedures. Then, the physicochemical characteristics of CDs were delineated through a suite of characterization methods. Moreover, our investigation zeroed in on elucidating the ameliorative impacts of CDs on ovalbumin-induced rat models alongside their underlying mechanisms.Results: ZRC-CDs with particle sizes ranging from 1.0 to 3.5 nm and rich surface functional groups. Additionally, we observed that ZRC-CDs significantly attenuated nasal symptoms and pathological damage in ovalbumin-induced AR rats, and modulated lipid metabolism and type 2 inflammatory responses. They also inhibit PI3K/AKT and JAK/STAT pathways, which are associated with metabolism and inflammation. Importantly, ZRC-CDs demonstrated high biocompatibility, underscoring their potential as a novel therapeutic agent.Conclusion: ZRC-CDs offer a promising alternative for AR treatment and could help facilitate broader clinical use of the ZRC. In addition, the exploration of the inherent bioactivity of CDs can help to broaden their biological applications.

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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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FOOD HYDROCOLLOIDS · 2026 · IF 13.8

Divalent cation-mediated regulation of the hierarchical structure and rheological properties of ovalbumin fibrils

Lifeng Wang,Yihan Zhang,Yuhang Gao,Rongcheng Li,Renfeng Gao,Xing Li,Yuxiang Gu

Mg²⁺, Zn²⁺, Ca²⁺ and Fe²⁺ increased antiparallel β-sheet content in preformed ovalbumin fibrils. • Cation treatment shortened apparent fibril contours and increased interfibrillar aggregation. • Divalent cations increased the viscosity and storage modulus of ovalbumin fibril dispersions. • Cation treatment reduced the zeta potential and apparent surface hydrophobicity of ovalbumin fibrils. • ITC showed relatively weak, ion-dependent association between divalent cations and preformed fibrils. Metal ions can regulate the structural organization and macroscopic properties of protein fibrillar assemblies. Although previous studies have extensively examined ion-mediated regulation of protein fibrillation, the effects of divalent cations on the hierarchical organization of preformed egg-protein fibrils remain poorly understood. In this study, OVA fibrils were prepared by heating the protein at pH 2.0 and 90 °C for 8 h, after which Mg 2+ , Zn 2+ , Ca 2+ , or Fe 2+ was added to evaluate the effect of each ion on the post-formation organization and properties of the preformed fibrils. Divalent-cation treatment caused ion-dependent changes in the secondary-structure distribution, colloidal properties, microscopic morphology, and rheological behavior of the preformed OVA fibrils. These changes were attributed to post-formation interfibrillar association, aggregation, and structural reorganization rather than enhanced fibril formation. All OVA fibril systems showed partial precipitation at 500 mM, indicating loss of colloidal stability rather than homogeneous hydrogel formation. ICP-MS revealed ion-dependent differences in apparent metal retention. Collectively, these findings demonstrated that divalent cations regulated the hierarchical organization and rheological properties of preformed OVA fibrils through ion-dependent post-formation structural reorganization, providing a basis for controlling the functionality of egg-protein fibrillar materials. Download: Download high-res image (340KB) Download: Download full-size image

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JOURNAL OF FOOD SCIENCE · 2026 ·Vol. 91 ·期 4 ·e71017 · IF 4.1

Synergistic Noncovalent Mulberry Polysaccharide–Ovalbumin Complexes for Enhanced Functional Properties and Pickering Emulsion Stability

Miaomiao Wang,Xinshuai Zhang,Weiwei Cheng,Erna Li,Xinyu Wei,Feng Xiao,Jialiang He,Baocheng Xu,Lili Liu

This study systematically investigated the non-covalent interaction mechanisms, structural characteristics, and functional properties of ovalbumin (OVA)–mulberry polysaccharide (MP) complexes under different pH and mixing ratios and further constructed pickering emulsions based on the optimized complex. The phase behavior of the OVA–MP system exhibited significant pH and ratio-dependent variations. As the pH decreased from 6.5 to 2.0, the turbidity of the system followed a “dissolution–aggregation–re-dissolution” pattern, with the maximum aggregation point (pH opt ) corresponding closely to the isoelectric point of OVA (pI ≈ 4.5). Spectroscopic analyses revealed that MP induced OVA conformational relaxation and hydrophobic exposure by reinforcing hydrogen bonding and electrostatic interactions. This process modulated the secondary structural order and hydrogen-bond network stability. Functionally, the OVA–MP complex exhibited significantly enhanced emulsifying activity, thermal stability, and foaming properties. Under the conditions of pH 6.0, volume ratio 2:1, and denaturation temperature ( T d ) 95.4°C, the comprehensive performance (ESI = 39.36 ± 0.33 min) was the best. Molecular dynamics (MD) simulations confirmed that OVA–MP binding was a thermodynamically spontaneous process (ΔG = –38.98 ± 0.89 kcal/mol), mainly driven by van der Waals and hydrogen-bonding interactions. The resulting O/W pickering emulsion displayed reduced droplet size, pronounced shear-thinning behavior, higher viscoelasticity (G′ > G″), and improved salt and storage stability. Overall, MP modulates OVA conformation and interfacial behavior through synergistic hydrogen bonding and electrostatic attraction, forming a structurally reinforced interface. These findings provide theoretical and technical insights into designing food-grade biopolymer emulsifiers and functional delivery systems with enhanced stability.

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