COLLOIDS AND SURFACES A-PHYSICOCHEMICAL AND ENGINEERING ASPECTS
·
2025
·
IF 5.4
Yibang Zhang,Dong Chen,Yang Liu,Aisha Labaran Ammani,Atena Ahmadian,Aftab Ullah
Protein-lipid interactions are pivotal in various biological processes, including membrane trafficking, signal transduction, and cellular compartmentalization. This study investigates how fatty acid modification alters the physicochemical properties of ovalbumin (OVA) and its interactions with lipid bilayers, with implications for controlled release applications. We hypothesize that modifying OVA with different fatty acids will significantly alter its surface hydrophobicity and membrane affinity, thereby influencing its potential for targeted drug delivery. OVA was chemically modified with four fatty acids (myristic, palmitic, stearic, and oleic acids) using N-hydroxysuccinimide (NHS) esters. Surface hydrophobicity was assessed via 8-Anilino-1-naphthalenesulfonic acid ammonium (ANS) fluorescence assays, revealing that modifications increased hydrophobicity, particularly with longer fatty acid chains. Interactions with liposomes were characterized using dynamic light scattering (DLS) and zeta potential measurements, indicating enhanced liposome binding and altered bilayer properties due to fatty acid modifications. Quartz crystal microbalance with dissipation (QCM-D) analysis confirmed the insertion of fatty acid chains into the lipid bilayer. In vitro release experiments demonstrated that fatty acid modification significantly affected the release kinetics of OVA, with oleic acid-modified OVA showing the lowest cumulative release. Our findings highlight the role of fatty acid structure in modulating protein-lipid interactions and underscore the potential of fatty acid-modified OVA for developing targeted drug delivery systems. Future work will explore the underlying mechanisms and evaluate the therapeutic potential of these modified proteins in vivo.
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高影响因子
FOOD HYDROCOLLOIDS
·
2025
·
IF 12.4
Ying Liu,Haoyu Yu,Chenyang Fan,Min-hsiung Pan,Yi-shiou Chiou,Baomiao Ding
The study investigated the enhancement of ovalbumin (OVA) gel properties through the incorporation of liposomes (Lip) and clarified the mechanisms responsible for these improvements, with the aim of addressing limitations in water-holding capacity (WHC), gel strength, and stability commonly observed in native OVA systems. Lip was incorporated into OVA gels at various Lip-to-OVA ratios, and Lip-OVA gel properties were evaluated and analyzed. Results demonstrated that Lip-OVA gel WHC, strength and freeze-thaw stability were significantly improved with the Lip-to-OVA ratio increasing. SEM micrographs revealed a denser and more homogenous network structure in Lip-OVA gels compared to native OVA gels. FTIR and fluorescence spectroscopy indicated that hydrogen bonding, hydrophobic interactions, and protein conformational rearrangements were pivotal to gel enhancement. Surface hydrophobicity and contact angle measurements further confirmed increased exposure of hydrophobic groups and supported conformational rearrangement. The increase in free sulfhydryl content and the change in CD spectra indicated that OVA structure shifted towards a decrease in α-helix content and an increase in β-sheet content, leading to the unfolding of OVA and promoting intermolecular cross-linkage. The primary forces contributing to the improved gel structure were identified as hydrophobic interactions and disulfide bonding, with ionic and hydrogen bonds playing a supportive role. Furthermore, it was observed that the gel stabilization shifted toward hydrophobic interactions over disulfide bonding after incorporation with Lip. These findings provide mechanistic insight into how Lips modulate protein gel structure and function, offering a strategy to design protein-based gels with enhanced texture, stability, and potential for advanced food applications.
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PLoS One
·
2021
·Vol. 16
·期 1
·e0245207
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IF 3.24
Xiaoxiao Dong,Boye Li,Boyang Yu,Tian Chen,Qin Hu,Bo Peng,Wang Sheng
In the present study, we evaluated adjuvant potential of Poria cocos polysaccharide (PCP) on the Th1-type immune responses of C57/BL6 mice against ovalbumin (OVA). We first determined the effect of PCP on maturation of murine bone marrow derived dendritic cells (BMDCs), PCP significantly upregulated surface expression of MHCII, CD40, CD80, CD86 and enhanced production of IL-6 and IL-12p40. In addition, PCP affected receptor-mediated endocytosis, but not pinocytosis in BMDCs. Furthermore, OVA + PCP immunization induced specific cytotoxic CD8 + T cell killing of OVA (257–264) peptide pulsed cell. When mice were immunized subcutaneously in a week interval with OVA + PCP. Serum were collected for measuring OVA-specific antibody and splenocytes were harvested for analyzing CD69, IFN-γ ELISpot and cytokines production. The result indicated that OVA-specific IgG, IgG2a and IgG1 antibody levels in serum were significantly elevated by PCP compared with control. PCP increased OVA-specific IFN-γ-secreting CD8 + , CD4 + T cells, promoted CD8 + T cell proliferation and up-regulated Th-1 type (IFN-γ, IL-2) cytokine production. In conclusion, data suggest that PCP enhanced cellular immune response and possess potential as a vaccine adjuvant for Th1 immune response.
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PubMed
高影响因子
FOOD CHEMISTRY
·
2017
·
IF 4.529
Jin Feng,He Cai,Hua Wang,Chunyang Li,Songbai Liu
Conjugates of ovalbumin (OVA) with (+)-catechin (C), (−)-epigallocatechin (EGC) or (−)-epigallocatechin gallate (EGCG) were synthesized through a free-radical grafting approach. The covalent binding between OVA and catechins was confirmed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS). OVA-catechin conjugates were further characterized by a combination of steady-state fluorescence spectroscopy, differential scanning calorimetry (DSC), Fourier transform infrared (FTIR) spectroscopy and circular dichroism (CD) analyses. Results suggested that the conjugates contained less α-helix but more β-sheet secondary structure than OVA. The catechin-grafting reaction led to improved surface hydrophobicity and decreased tertiary conformation stability of OVA. Compared with that emulsified by OVA, fish oil emulsion coated by conjugates demonstrated smaller droplet size, better storage stability and less viscosity. Besides, conjugates inhibited the lipid oxidation in fish oil emulsion more effectively than OVA because of their higher antioxidant activity and interfacial accumulation.
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BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
·
2021
·Vol. 85
·期 8
·1809-1817
·
IF 2.043
Li Qiang,Zhai Chunmiao,Wang Guodong,Zhou Jia,Li Weiguang,Xie Liquan,Shi Zhanli
Ginsenoside Rh1 (Rh1) has anti-inflammatory effects in asthma mice, but the underlying mechanism remains unclear. BALB/c mice were sensitized and challenged with ovalbumin (OVA) to construct asthma model. Mice received Rh1 or tiotropium bromide 0.5 h before OVA challenge. Airway morphology and airway remodeling were assessed by HE staining and Masson's trichrome staining, respectively. Th1/Th2 cytokines in serum or broncho alveolar lavage fluid (BALF) were measured by ELISA kits. Rh1 significantly alleviated the lung resistance and airway resistance, and reduced the number of total inflammation cells, eosinophils, neutrophils, and lymphocytes in BALF of the asthmatic mice. The morphological changes and collagen deposition of airway were also reduced by Rh1 in asthmatic mice. The increase of Eotaxin, IL-4, IL-5, IL-13, and IL-33 and the decrease of IL-12 and IFN-γ in both BALF and serum of OVA exposed mice were reversed by Rh1. Rh1 attenuates OVA-induced asthma in the mice model by regulating Th1/Th2 cytokines balance.
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INTERNATIONAL IMMUNOPHARMACOLOGY
·
2025
·
IF 4.7
Longwei Yang,Wenhao Ge,Xi Lin,Ning Yu,Xiaodong Xu,Jianfa Zhang
Allergic asthma is an inflammatory airway disease in which mast cells play a key role in its pathogenesis. Riclinoctaose (Rios), an octasaccharide composed of glucose and galactose, has been reported to modulate macrophage polarization in renal ischemia-reperfusion injury. This study investigates the effects of nebulized Rios in an ovalbumin (OVA)-induced allergic asthma model. Nebulized Rios significantly reduced airway hyperresponsiveness (AHR), inflammatory cell infiltration, pulmonary fibrosis, and mucus production in OVA-treated mice. Additionally, Rios suppressed lung inflammatory cytokine production and protected against OVA-induced oxidative injury. In bronchoalveolar lavage fluid (BALF), Rios decreased the number of neutrophils and macrophages, as well as serum immunoglobulin E (IgE) and interleukin-4 (IL-4) levels. Metabolomics analysis using 1 H NMR showed significant changes in the lung metabolic profile of OVA-induced asthma mice, which were partially reversed by Rios treatment. Confocal laser microscopy (CLM) revealed that fluorescently labeled Rios specifically binds to mast cell membranes. In vitro, Rios reduced degranulation and inflammatory responses in mast cells RBL-2H3 following anti-Dinitrophenyl-Immunoglobulin E (anti-DNP-IgE) sensitization and anti-Dinitrophenyl-Bovine Serum Albumin (anti-DNP-BSA) stimulation. These results suggest that Rios has therapeutic potential for allergic asthma, likely through the modulation of mast cell degranulation and mediator release.
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高影响因子
FOOD HYDROCOLLOIDS
·
2025
·
IF 12.4
Yaping Liu,Chenxin Huang,Jiajie Wang,Xianchao Feng,Meihu Ma
Egg white proteins exhibit high thermal susceptibility to undesired aggregation, which limits their processing utility. In this study, the thermally regulated co-aggregation mechanism between ovotransferrin (OVT) and ovalbumin (OVA) was systematically investigated. Turbidity kinetics and particle size distribution results showed that the initial aggregation occurred at 55°C, induced by 4.3% disulfide cleavage and a 38.9% enrichment of β-sheet ( P < 0.05). Size exclusion chromatography results showed that this structural unfolding was mainly due to OVT molecules. The structurally activated OVT then specifically anchored the double cavities of OVA. Subsequently, upon heating at 60 - 65°C, the β-sheet reverted to the α-helix as detected by CD and FTIR spectroscopy, and the hydrophobic tyrosine and phenylalanine residues were reburied as detected by fluorescence spectroscopy, forming reversible metastable aggregates. At temperatures above 65°C, the larger heteroprotein complex (∼1.5 μm) emerged. ITC results showed that the co-aggregation was entropy-driven ( TΔS = +45.5 kJ/mol) with a stoichiometric ratio of 2:1 (OVT: OVA, n = 2.19 ± 0.12). Molecular docking and interaction force analyses revealed covalent disulfide bonds and multiple non-covalent bonds involved in this process. Notably, OVT acted as the aggregation initiator and governed the reverse aggregation, whereas OVA provided the structural backbone. These results provided a theoretical basis for the precise regulation of complex functional properties in the food industry.
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FOOD CHEMISTRY
·
2026
·
IF 10.4
Zenghong Xing,Xiaoyun Fei,Deming Gong,Guowen Zhang
Resveratrol (Res) is a bioactive compound with limited application in food and pharmaceuticals due to its poor solubility, low stability and limited bioavailability. To address these challenges, this study developed novel ovalbumin-proanthocyanidin‑sodium alginate (OVA-PC-SA) conjugate-based oleogels, and investigated the effect of conjugate concentration on the properties of oleogels and Res's delivery performance. Results indicated that oil binding capacity exceeded 99% at conjugate concentrations of 0.4–1.0%, and the hardness, gel strength and thermal stability of the oleogels were enhanced significantly with increasing conjugate concentration. All oleogels contained β-type crystals and exhibited superior oxidative stability compared to unstructured oil. At conjugate concentrations of 0.2% and 1.0%, the oleogels exhibited high encapsulation efficiencies (87.47% and 91.10%), loading capacities (99.10 and 102.23 mg/g), and significantly improved Res's in vitro bioaccessibility (80.53% and 85.06%) compared to Res-loaded oil (75.41%). The oleogels enhanced the controlled release of lipophilic bioactive substances, demonstrating their potential as effective carriers.
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CHEMBIOCHEM
·
2026
·Vol. 27
·期 1
·e202500945
·
IF 2.8
Min Huang,Jiayi Han,Hao Li,Junhao Lin,Qingbo Jiao,Zexing Cao,Qunfang Lei,Wenjun Fang,Gerui Ren,Zhijun Song,Ying Zheng,Ruibo Wu,Hujun Xie
Growing interest in sustainable nutrition has improved the importance of understanding the interactions between (-)-Epigallocatechin-3-gallate (EGCG), a polyphenol in green tea, and proteins for functional food development. In this study, we investigated the regulatory effects of EGCG on the aggregation behavior of zein, ovalbumin, and their complexes. The addition of EGCG at 100 μg mL −1 led to significant changes in particle sizes of zein, ovalbumin, and zein-ovalbumin complexes, increasing them from 215.6, 3485.3, and 2081.0 nm to 4822.3, 7857.0, and 5895.7 nm, respectively. The zeta potentials of these samples decreased from 8.4, −2.6, and 5.0 mV to −5.3, −0.66, and 2.13 mV, respectively, indicating a reduction in net surface charges and promotion of protein aggregation. UV–vis absorption spectroscopy revealed hyperchromic effects and blue shifts upon EGCG addition, suggesting conformational changes. Molecular dynamics simulations further revealed that EGCG contributed to the structural stabilization of both individual proteins and their complexes by reinforcing hydrophobic and electrostatic contacts at the molecular interface. These findings provide molecular-level insights into the regulatory role of EGCG in protein assembly and offer guidance for the rational design of plant-animal protein complexes with tailored functional properties for food applications. Graphical EGCG plays a significant regulatory role in protein aggregation behavior. EGCG interacts with protein molecules, promoting conformational changes and aggregation, particularly in systems involving zein and ovalbumin. This study highlights the potential application of EGCG in the development of functional foods.
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高影响因子
FOOD HYDROCOLLOIDS
·
2023
·
IF 10.7
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.
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FOOD CHEMISTRY
·
2022
·
IF 9.231
Na Xia,Chunqing Wang,Siming Zhu
In this study, ovalbumin (OVA) formed a complex with neohesperidin (NH) via a pH-shifting method. The NH-OVA complex self-assembled into NH-OVA nano-particles, which were then characterized and whose binding mechanism was evaluated by using multi-spectroscopic, thermodynamics, and molecular docking simulation methods. Fluorescence intensity decreased after OVA was complexed with NH. The binding constant of the OVA-NH complex was in the order of 6.32 × 10 5 M −1 suggesting that the complex is stable. Circular dichroism (CD) analysis showed that α -helix content increased, β-folding, β -turning, and irregular crimp content decreased after OVA and NH binding. Isothermal titration calorimetry results showed that hydrophobic interactions and hydrogen bonds made an important impact in the complex formation. The molecular docking results revealed that Van der Waals forces and hydrogen bonds contributed to the free binding energy of the complex. There were multiple possible surface binding sites between OVA with NH. The obtained results provide new insights into the interaction mechanism of OVA and NH, and as a vehicle for NH, the OVA has shown promising applications in functional foods.
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高影响因子
FOOD RESEARCH INTERNATIONAL
·
2022
·
IF 7.425
Yejun Zhong,Lei Yang,Ziyi Zhu,Hongyu Chen,Chengmei Liu,Taotao Dai,Er Sheng Gong
The protective effect of ovalbumin-flavonoids (naringenin, genistein, naringin, puerarin, and daidzein) hydrogels on the thrombolytic activity and stability of nattokinase were investigated. The results suggested that flavonoids promoted the gelation of ovalbumin solution, which was not able to form hydrogel at the same concentration upon heating. The nattokinase/ovalbumin-naringenin hydrogel had the strongest hardness and springiness. All nattokinase/ovalbumin-flavonoids hydrogels were more elastic than viscous. After in vitro digestion, the thrombolytic capacities of all nattokinase/ovalbumin-flavonoids hydrogels were significantly higher than that of free nattokinase. Moreover, nattokinase/ovalbumin-flavonoids hydrogels showed higher thermal and pH stability than free nattokinase. Fluorescence spectroscopy and molecular docking analysis revealed that the main interactions between nattokinase and daidzein, nattokinase and genistein were mainly hydrogen bond, while the main interactions between nattokinase and naringin, nattokinase and puerarin, nattokinase and naringenin were hydrophobic interaction. This research suggested that nattokinase/ovalbumin-flavonoids had great potential for applications in the treatment of thrombus.
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高影响因子
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