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FOOD HYDROCOLLOIDS · 2024 · IF 11

How the ovalbumin modulates the conformation of zein through protein-protein interactions

Hujun Xie,Hao Li,Lei Liu,Xinpei Cai,Tianrong Wang,Qingbo Jiao,Nan Lv,Min Huang,Ruibo Wu,Zexing Cao,Qunfang Lei,Wenjun Fang,Gerui Ren

Under the prevailing trend of transitioning from animal proteins to plant protein-based substitutes, the interaction between these two protein sources is of paramount importance. In this work, zein as a representative plant protein, the influence of animal protein ovalbumin on the conformation and physicochemical properties of zein was explored through experiments and theoretical calculations. Dynamic light scattering and transmission electron microscopy showed that the formation of Zein-Ovalbumin complexes, and significant fluorescence quenching occurred between zein and ovalbumin. The results of UV indicated that the microenvironment surrounding the protein residues was influenced by the changes of protein conformation. The secondary structure of zein was regulated by ovalbumin according to the results of circular dichroism spectroscopy. The determination of surface hydrophobicity and zeta-potential indicated that protein-protein interactions affected the exposure of hydrophobic groups and the strength of surface charges. Fourier transform infrared spectroscopy and dissociation experiments identified that the main driving forces to yield Zein-Ovalbumin complexes were hydrophobic, hydrogen bonding, and electrostatic interactions. The results of molecular dynamics simulations suggested that the increased interaction strength between zein and ovalbumin led to a tighter complex structure with a binding free energy of −32.4 kcal/mol. This study proposed a method to regulate the structural and functional properties of plant proteins through protein-protein interactions.

研究领域: 食品科学 · 生物化学
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LANGMUIR · 2018 · IF 3.789

Specific Ion Effects on Protein Thermal Aggregation from Dilute Solutions to Crowded Environments

Shuling Li,Shuji Ye,Guangming Liu

We have investigated specific ion effects on protein thermal aggregation from dilute solutions to crowded environments. Ovalbumin and poly(ethylene glycol) have been employed as the model protein and crowding agent, respectively. Our studies demonstrate that the rate-limiting step of ovalbumin thermal aggregation is changed from the aggregation of unfolded protein molecules to the unfolding of the protein molecules, when the solution conditions are varied from a dilute solution to a crowded environment. The specific ion effects acting on the thermal aggregation of ovalbumin generated by kosmotropic and chaotropic ions are different. The thermal aggregation of ovalbumin molecules is promoted by kosmotropic anions in dilute solutions via an increase in protein hydrophobic interactions. In contrast, ovalbumin thermal aggregation is facilitated by chaotropic ions in crowded environments through accelerated unfolding of protein molecules. Therefore, there are distinct mechanisms causing the ion specificities of protein thermal aggregation between dilute solutions and crowded environments. The ion specificities are dominated by ion-specific hydrophobic interactions between protein molecules and ion-specific unfolding of protein molecules in dilute solutions and crowded environments, respectively.

研究领域: 生物化学 · 分子生物学
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FOOD HYDROCOLLOIDS · 2024 · IF 11

Comparative analysis of carrageenan/ovalbumin and carrageenan oligosaccharide/ovalbumin complexes

Hujun Xie,Qing Cao,Yingying Jiang,Yingying Pan,Sihan Chen,Qingbo Jiao,Gerui Ren,Di Wu,Min Huang

The saccharides ι-carrageenan (ι-CG) and ι-carrageenan oligosaccharides (ι-CO) exhibit different molecular chain lengths and charge intensities, which are pivotal determinants of their interactions with ovalbumin (OVA). This study investigated the interaction mechanisms between OVA and ι-CG as well as between OVA and ι-CO using experimental methods and molecular docking. The results of zeta potential showed that the strongest electrostatic interaction occurred at an OVA/ι-CG ratio of 100:13 (−1.59 ± 0.41 mV) and an OVA/ι-CO ratio of 100:10 (−1.32 ± 0.30 mV). The OVA/ι-CG complexes showed higher turbidity (1.63 ± 0.08 cm −1 ). Furthermore, Fourier transform infrared spectroscopy showed that ι-CG significantly altered the secondary structure of OVA, whereas ι-CO did not affect it. Fluorescence spectroscopy also verified the interactions in the OVA/ι-CG and OVA/ι-CO complexes. Both complexes exhibited shear-thinning behaviour; the largest storage modulus ( G ′) and loss modulus ( G ″) were observed at 100:13 and 100:10 ratios for OVA/ι-CG OVA/ι-CO samples, respectively. ι-CG induced OVA to form more loosely clumped aggregates, whereas OVA and ι-CO formed compact granular aggregates when observed using confocal scanning laser microscopy. Molecular docking results showed that more salt bridges were formed between ι-CG and OVA than between ι-CO and OVA. A schematic model was established to elucidate the effects of ι-CG and ι-CO on OVA. This study provides instructions for designing innovative food systems based on different charge intensities and chain lengths of saccharides.

研究领域: 食品科学 · 生物化学
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CHEMISTRY & BIODIVERSITY · 2019 ·Vol. 17 ·期 1 ·e1900436 · IF 1.449

Preparation of Boronic Acid-Functionalized Silica Nanocomposites for Selective Enrichment of Glycoproteins

Peng Yang,Zeng-Lian Tian,Li-Ping Xie,Lin Su,Jun-Yi He,Yan-Ping Wu,Wei-Hua Jia

A facile method was developed for synthesis of boronic acid-functionalized silica nanocomposites (SiO 2 -BA) by ‘thiol-ene’ click reaction, where silica nanoparticles were synthesized by using tetraethoxysilane (TEOS) and γ -mercaptopropyl trimethoxysilane ( γ -MPTS) as precursors. The morphology and structure properties of the resultant SiO 2 -BA were characterized by transmission electronic microscopy (TEM), Fourier transform infrared spectroscopy (FT-IR), and Brunner-Emmet-Teller measurements (BET). The adsorption behavior of the SiO 2 -BA for glycoproteins was evaluated. Under the optimized conditions, the SiO 2 -BA exhibited higher adsorption capacity towards glycoproteins (ovalbumin, OVA, 7.64 μmol/g) than non-glycoproteins (bovine serum albumin, BSA, 0.83 μmol/g). In addition, the practicality of the SiO 2 -BA was further assessed by selective enrichment of glycoproteins from egg white samples. Graphical

CAS / MDL: 78-67-1
研究领域: 分析化学 · 生物化学
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ACS Applied Polymer Materials · 2023 · IF 5

Double-Network Protein Hydrogels as Flexible Pressure Sensors for Contactless Delivery

Anbo Zheng,Yuxiang Qin,Qing Xia,Xueshuo Zhang,Yanxu Chen

To meet the growing demand for sustainable development and ecofriendliness, hydrogels based on biopolymers have attracted widespread attention for developing flexible pressure sensors. Natural globular proteins exhibit great potential for developing biobased pressure sensors owing to their advantages of high water solubility, easy gelation, biocompatibility, and low production cost. However, realizing globular protein hydrogel-based sensors with interfacial and bulk toughness for pressure sensing and use in wearable devices remains a challenge. This study focuses on developing a high-performance flexible pressure sensor based on a biobased protein hydrogel. Consequently, a flexible protein/polyacrylamide (PAM) hydrogel with a featured double-network (DN) structure linked covalently with hydrogen bonds was first synthesized via a one-pot method based on natural ovalbumin (OVA). The unique DN structure of the as-synthesized OVA/PAM hydrogel affords excellent mechanical performance, flexibility, and adhesion properties. The mechanical properties of the DN hydrogel were enhanced after further cross-linking with Fe3+ and treatment with glycerol. Subsequently, the flexible pressure sensor was constructed by sandwiching a microstructured OVA/PAM dielectric layer between two flexible silver nanowire electrodes. The obtained sensor exhibits a high sensitivity of 2.9 kPa–1 and a short response time of 18 ms, ensuring the ability to monitor physiological signals. Based on its excellent performance, the fabricated sensor was used for monitoring the signals obtained using practical applications such as wrist bending, finger knocking, stretching, international Morse code, and pressure distribution. Particularly, we implemented a contactless delivery system using the fabricated OVA-based pressure sensors linked to unmanned vehicles and global positioning systems, providing a solution for low-risk commodity distribution during Coronavirus disease 2019 (COVID-19).

研究领域: 材料科学 · 生物医学工程 · 可持续发展技术
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Scientific Reports · 2020 ·Vol. 10 ·期 1 ·1-9 · IF 3.998

Improving emulsion stability based on ovalbumin-carboxymethyl cellulose complexes with thermal treatment near ovalbumin isoelectric point

Li Zhenshun,Kuang Hairui,Yang Jinchu,Hu Jie,Ding Baomiao,Sun Weiqing,Luo Yangchao

Ovalbumin (OVA) is an important protein emulsifier. However, it is unstable near the isoelectric point pH, which limits its applications in the food industry. Polysaccharides may be explored to tackle this challenge by improving its pH-dependent instability. In this work, carboxymethyl cellulose (CMC) was used as a model polysaccharide to mix with OVA near its isoelectric point (pH 4.7) with subsequent mild heating at 60 °C for 30 min. The molecular interactions between OVA and CMC were comprehensively studied via a series of characterizations, including turbidity, zeta potential, intrinsic fluorescence, surface hydrophobicity, circular dichroism (CD) spectra and Fourier transform infrared spectroscopy (FTIR). The droplet sizes of the emulsions prepared by OVA-CMC were measured to analyze emulsifying property and stability. The results indicated that free OVA was easily aggregated due to loss of surface charges, while complexing with CMC significantly inhibited OVA aggregation before and after heating owing to the strong electrostatic repulsion. In addition, OVA exposed more hydrophobic clusters after heating, which resulted in the growth of surface hydrophobicity. Altogether, the heated OVA-CMC complexes presented the best emulsifying property and stability. Our study demonstrated that complexing OVA with CMC not only greatly improved its physicochemical properties but also significantly enhanced its functionality as a food-grade emulsifying agent, expanding its applications in the food industry, as development of emulsion-based acidic food products.

CAS / MDL: 9004-32-4
研究领域: 食品科学 · 生物化学
✓ 已验证 产品关联 DOI PubMed 高影响因子
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INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES · 2026 · IF 8.7

Insight into heat-stressed ovalbumin covalently modified by resveratrol: Impact on the in vitro and in vivo immunological function of ovalbumin

Ping Yang,Caiying Yang,Xiaoqian Xu,Jinyan Gao,Hongbing Chen,Ping Tong

Covalent modification of RES under heat stress reduced the allergenicity of OVA. • HOVA-RES enhanced the digestibility and cellular transport capacity of OVA in vitro. • HOVA-RES obviously decreased the levels of specific antibodies and mMCP-1 in mice. • HOVA-RES significantly reduced the secretion of Th2-type cytokines. • HOVA-RES modulated the composition and diversity of the intestinal flora of mice. Heat stress (H) and covalent modification with resveratrol (RES) can significantly change the conformation of ovalbumin (OVA) and improve its processing properties, however, whether HOVA-RES affects the immunological function of OVA is still unclear. In this study, the effect of HOVA-RES on the digestion, transport, immune cell responsiveness, and allergenicity of OVA were investigated using the in vitro and in vivo models. Results showed that HOVA-RES enhanced the digestion and cellular transporter capacity of OVA, and the transported productions inhibited histamine and β-HEX release in the degranulation reaction of KU812 cells. In addition, HOVA-RES significantly reduced the OVA-specific IgE, IgG, IgG1, and mMCP-1 levels in mice sera. It also resulted in decreased secretion of Th2-type cytokines (IL-4, IL-5, and, IL-13) and reduced intestinal tissue damage. Moreover, HOVA-RES modulated the composition and diversity of the intestinal flora in OVA-sensitized mice, altered the abundance of dominant genera, and improved the intestinal microecology. Therefore, HOVA-RES covalent conjugation can improve the in vivo and in vitro immunological functions of OVA, especially significantly reduce its allergenicity, which provides a new direction to develop hypoallergenic products. Download: Download high-res image (132KB) Download: Download full-size image

CAS / MDL: 10102-40-6
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BIOSENSORS & BIOELECTRONICS · 2024 · IF 10.7

Biomimetic gastric microtissue electrochemical biosensors for ovalbumin detection

Donglei Jiang,Zeng Feng,Hui Jiang,Xinyue Xiang,Lifeng Wang

An innovative integrated three-dimensional (3D) bioprinted gastric microtissue electrochemical biosensor was developed in this study for the detection of allergen ovalbumin (OVA). In this system, OVA triggers the release of histamine from gastric microtissue, which then undergoes a redox reaction on the electrode surface, leading to an increase in the peak current. Gelatin methacrylate hydrogel serves as a scaffold for the 3D culture of RBL-2H3 and PC-12 cells for partially restoring allergic reactions in the human body in vitro. Furthermore, gold nanoparticle-modified anodized aluminum oxide sieves macromolecular substances and facilitates sensor nano-analysis. Composites of cerium-based organometallic framework, MnO 2 , and gold nanoparticles significantly enhanced the sensitivity of the screen-printed carbon electrode. Under optimal experimental conditions, the detection limit for OVA was 0.042 μg/mL, with a linear range of 0.1–10.0 μg/mL. The fabricated sensor demonstrated high sensitivity, reliability, and simplicity, showcasing its broad potential for allergen detection applications.

研究领域: 生物工程 · 分析化学 · 材料科学 · 生物技术
✓ 已验证 产品关联 DOI PubMed 高影响因子
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Food Chemistry-X · 2024 · IF 6.5

Emulsification properties of ovalbumin-fucoidan (OVA-FUC) binary complexes

Xiefei Li,Yingmei Wu,Wenshan Duan,Lei Chen,Lujie Cheng,Junmei Liu,Yan Zhou,Chao Ai,Xin Li,Qun Huang

The poor thermal stability and emulsifying properties of ovalbumin (OVA) limit its functional performance, but these limitations may be overcome by forming binary complexes. We prepared binary complexes of OVA and fucoidan (FUC) through electrostatic self-assembly and investigated the emulsifying properties of the complex by measuring the particle size, interfacial membrane thickness, zeta potential, and stability of the emulsion prepared with camellia oil and the complex. The OVA-FUC emulsions have a thicker interfacial membrane, lower mobility, higher viscosity, and better stability compared with the OVA emulsions. The emulsion prepared with 1.5 % OVA-FUC remained stable and homogeneous during storage. They tended to become unstable with freeze–thaw, but the oil encapsulated did not leak after coalescence occurred. With the addition of Ca 2+ , the OVA-FUC emulsion will be converted into a gel state. These findings indicate that OVA-FUC binary complexes can be used to prepare high-performance emulsions with great potential for development.

CAS / MDL: 2438-80-4
研究领域: 食品科学 · 胶体与表面化学
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CHEMBIOCHEM · 2019 ·Vol. 21 ·期 6 ·865-873 · IF 2.641

Injectable Ovalbumin-Based Composite Implant for Photothermal Tumor Therapy

Jing Zhang,Xiao An,Yuting Zheng,Yongkang Chen,Chenyao Wu,Shige Wang

Graphical Hardboiled : A multifunctional hydrogel implant based on ovalbumin has been designed that can simultaneously deliver a photothermal transducing agent (polydopamine) and a chemotherapeutic (doxorubicin) and/or a contrast agent (iohexol) to tumors. It is anticipated that the multifunctional implant, not showing obvious toxicity to healthy tissue, could be a promising system for synergistic cancer treatment. Polymeric hydrogels with three-dimensional network structures have found tremendous applications in biomedicine. Herein, we report the synthesis of a multifunctional implant based on ovalbumin (OVA) as a carrier capable of synergistically delivering a photothermal transducing agent (polydopamine, PDA) to tumors. The formation of PDA was achieved by utilizing the basicity of OVA, whereas the formation of the hydrogel implant was achieved through the in vitro/in vivo near-infrared (NIR) laser-induced hyperthermia of PDA. The as-prepared PDA@OVA implant exhibits high photothermal conversion efficiency (38.7 %). Once implanted in vivo, the OVA-based implant shows great versatility in the treatment of malignant tumors. Furthermore, a chemotherapeutic (doxorubicin, DOX) and a contrast agent (iohexol), dispersed in the OVA solution in advance, can also be firmly entrapped in the hydrogel along with the hydrogel formation. It is anticipated that the multifunctional OVA-based implant, not showing any obvious toxicity to healthy tissue, could be a promising system for synergistic cancer treatment.

研究领域: 生物医学 · 肿瘤学 · 材料科学
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JOURNAL OF PHYSICAL CHEMISTRY B · 2026 · IF 3.2

Magnesium Ion-Regulated Aggregation Mechanism of Zein–Ovalbumin Complexes

Min Huang,Yuanru Xu,Hao Li,Qingbo Jiao,Gerui Ren,Zexing Cao,Ruibo Wu,Ying Zheng,Qunfang Lei,Wenjun Fang,Hujun Xie

Metal ions can influence protein aggregation behavior through interactions with proteins during food processing, and a deeper understanding of these regulatory mechanisms is crucial for improving the structure and stability of food systems. In this study, the effect of Mg2+ on the aggregation behavior of Zein, Ovalbumin, and Zein–Ovalbumin complexes during thermal treatment was discussed using an aggregation kinetic model, and the relationship between protein conformational changes and protein aggregation behavior was revealed by combining theory with experiments. After the addition of Mg2+, the aggregation of Zein and Zein–Ovalbumin complexes was inhibited, while the aggregation of Ovalbumin was enhanced. The exposure of hydrophobic and free –SH groups of proteins was determined, thereby regulating the aggregation behavior of complexes. The thermal stability of protein complexes was also enhanced by electrostatic and hydrogen-bonding interactions between Zein and Ovalbumin, which was further validated via Fourier transform infrared spectroscopy and molecular dynamics simulation. Mg2+ reduced the binding free energy between proteins within the Zein–Ovalbumin complexes through the electrostatic shielding effect, thereby affecting the energy contributions of key residues. This study provides valuable mechanistic insights for strategically utilizing metal ions such as Mg2+ to regulate protein aggregation and optimize functional properties of complex proteins.

✓ 已验证 产品关联 DOI PubMed 高影响因子
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JOURNAL OF ELECTROANALYTICAL CHEMISTRY · 2026 · IF 4.1

Polyethyleneimine-modified electrospun SnC for the detection of ovalbumin

Haoxiang Wang,Yuyang He,Ruoyu Wang,Mengqi Lu,Dongpo Xu

Based on the electrostatic spinning process, a boronic acid-functionalized electrochemical sensor was designed. Polyethylenimine (PEI) was introduced into the electrospinning solution, which promoted the formation of fine particulate coatings from tin hydrolysis products. These particles were effectively anchored onto the nanofiber surfaces, resulting in a unique morphology that significantly increases the active sensing area. Boronic Acid Bonds Grafted onto Material Surfaces can effectively capture substances containing vicinal diols. By combining with molecular imprinting (MIP) which features specific imprinted cavities, this approach enables the capture of OVA. The blocking of these cavities leads to a change in the current response, thus achieving detection. The sensor demonstrates excellent selectivity and sensitivity, with a detection limit of 1.3 fg/mL. It can be applied to detect OVA in egg-free bread, showcasing certain practical detection capabilities.

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