INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
·
2024
·
IF 7.7
Zhi-Wei Liu,Pan-Pan Tang,Yi-Xuan Zhang,Jun-Hu Cheng,Rana Muhammad Aadil,Xiu-Bin Liu
The impact of Dielectric-Barrier Discharge (DBD) plasma treatment on the prevention of heat-induced aggregation of Ovalbumin (OVA) and improvement in emulsification properties was investigated. Results highlighted the effective inhibition of thermal aggregation of OVA following exposure to plasma. Structural analysis revealed that the plasma-induced oxidation of sulfhydryl and intermolecular disulfide bonds played a pivotal role in inhibiting the thermal aggregation, considered by Sodium Dodecyl Sulfate Polyacrylamide Gel Electrophoresis (SDS-PAGE), multiplies spectroscopy, and analysis of dynamic exchange of sulfhydryl-disulfide bonds. Meanwhile, the oxidation of exposed hydrophobic sites due to plasma treatment resulted in the transformation of the OVA molecule's surface from hydrophobic to hydrophilic, contributing significantly to the aggregation inhibition. Additionally, compared to an untreated sample of OVA, almost one-fold increase in emulsifying ability (EAI) and 1.5-fold in emulsifying stability (ESI) was observed after 4 min of plasma treatment. These findings demonstrated that plasma treatment not only enhanced the thermal stability of OVA, but also improved its emulsification properties.
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
LANGMUIR
·
2018
·
IF 3.789
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
✓ 已验证
DOI
高影响因子
FOOD HYDROCOLLOIDS
·
2025
·
IF 12.4
Bin Ma,Haobo Jin,Qi Zeng,Yongguo Jin
Succinylation has attracted extensive research attention in regulating protein functional properties. As the second most abundant protein in egg white, the foaming and gelling properties of ovotransferrin (OVT) are crucial for its applications in the food industry. However, current research on the effects of succinylation on these properties of OVT remains limited. Herein, OVT was subjected to succinylation by different levels of succinic anhydride, with characterization conducted on native OVT (NOVT) and modified OVT (OVTA). Additionally, the effects of different degrees (OVTA1, OVTA2, and OVTA3) of succinylation on foaming ability and stability of OVT were evaluated. Concurrently, the regulatory mechanisms underlying succinylation-mediated modulation of OVT’s thermal aggregation behavior and thermal stability were investigated via visual observation, microstructural analysis, and microrheological measurements. The results showed that succinylation significantly improved the foaming ability and stability of OVT (for half-life, OVTA1 was 2.3-fold that of NOVT), and effectively enhanced the thermal stability of OVT (For melting temperature, OVTA3 was 32.6°C higher than NOVT), thereby inhibiting heat-induced aggregation. This study provides a theoretical foundation for elucidating the regulatory mechanisms of succinylation on OVT functional properties, offering important guidance for expanding OVT applications in food and related fields.
研究领域:
食品科学
·
蛋白质化学
·
分子修饰
·
功能食品
·
生物物理化学
✓ 已验证
产品关联
DOI
高影响因子
FOOD HYDROCOLLOIDS
·
2025
·
IF 12.4
Yutong Jiang,Xin Wen,Jiahui Guo,Hongyu Li,Zhanmei Jiang,Yun Chen
This study investigated how tea saponin (Ts), gypenoside (Gyp), mogroside V(Mog), glycyrrhizic acid (GA) and stevioside (STE) affected the heat-induced aggregates of α-lactalbumin (Ala), focusing on inhibition mechanisms of disulfide cross-linking and their impact on structural and physicochemical properties. SDS-PAGE and size exclusion chromatography (SEC) confirmed that saponins probably bound Ala monomers via hydrophobic forces and hydrogen bonds, inhibiting the formation of disulfide bonds in heat-induced Ala (H-Ala) and effectively decreasing polymer generation, with the inhibitory effect in the order of Gyp, GA, Ts, STE, Mog. LC-MS/MS analysis revealed that Ala (6), Ala (91), Ala (111) and Ala (120) were the most active sites for the disulfide crosslinking reaction in H-Ala. Specifically, the number of intramolecular disulfide cross-linked peptides of heat-induced Ala-Mog, Ala-STE, Ala-GA, Ala-Ts and Ala-Gyp complexes significantly decreased by 5, 6, 7, 8 and 10, respectively, compared with H-Ala. Notably, the heat-induced Ala-Gyp complex exhibited the highest absolute zeta potential, smallest particle size, lowest hydrophobicity, which correlated with its superior inhibition of aggregation. The study highlighted the potential of saponins as natural additives for the stabilization of heat-sensitive proteins during the thermal processing, offering new insights for food industry applications.
研究领域:
食品科学
·
分子生物学
·
生物物理化学
·
蛋白质工程
·
天然产物化学
✓ 已验证
产品关联
DOI
高影响因子
FOOD CHEMISTRY
·
2025
·
IF 9.8
Huijuan Yang,Feijia Xu,Haifeng Wang,Liting Ji,Qing Shen
Excessive sodium intake increases cardiovascular risks, driving demand for low-sodium meat products. Yet low-salt conditions (0.2 M NaCl) weaken the solubility and gelation capacity of pork myofibrillar proteins (MPs). This study investigated the mechanism by which ultrasound treatment (500 W, 20 kHz, 60 % amplitude) modulated the thermal aggregation behavior of low-salt pork MPs to enhance their gel properties. Changes in the secondary and tertiary structures of the modified MPs, along with their thermal aggregation behavior, were systematically characterized and comprehensively analyzed. Results showed that ultrasound treatment (500 W, 20 kHz, 60 % amplitude) significantly ( p < 0.05) improved the gel properties of low-salt MPs by effectively regulating their thermal aggregation. Specifically, 9 min ultrasound treatment induced disordering of the secondary structure, reduced particle size to 133.70 nm, increased free sulfhydryl group content to 7.21 × 10 −5 mol/g and elevated surface hydrophobicity to 81.49 %, thereby suppressing aggregate nucleation. At 50 °C, ordered aggregates formed through hydrophobic domains. Subsequently, at 80 °C, the gel network transitioned from a predominantly salt-bridge structure to one stabilized by covalent bonds, as confirmed by scanning electron microscopy. This approach provides an efficient strategy for developing low-salt pork products (e.g., sausages, hams) and facilitates the industrial production of healthier meat alternatives.
研究领域:
食品科学
·
蛋白质化学
·
肉品加工
·
分子构象
·
功能特性
·
非热加工技术
✓ 已验证
产品关联
DOI
PubMed
高影响因子
Journal of Materials Chemistry A
·
2025
·
IF 9.5
Hao Xiong,Bowen Li,Hongjie Qiu,Pengfei Liu,Kunyuan Zheng,Zening Lei,Peng Xiang,Xinyu Tan
Perovskite solar cells (PSCs) have attracted considerable research interest in recent decades due to their remarkable power conversion efficiencies. However, their thermal stability is remains one of the crucial challenges for commercial applications. Bathocuproine (BCP), widely employed as an interfacial buffer layer between the electron transport layer and the metal electrode, tends to undergo thermal aggregation at elevated temperatures, thereby compromising device stability. In this paper, the aggregation behavior of BCP under thermal stability test was investigated. It was proposed that introducing Polyethylenimine (PEIE) into BCP could inhibit its high-temperature aggregation. The -NH and -OH groups in PEIE can form hydrogen bonds with pyridine nitrogen in BCP. This interaction enables moderate π-π stacking between to exist within a wider temperature and improves the morphology and uniformity of the film. Concurrently, PEIE improves energy level alignment at the C60/BCP interface, facilitating more efficient electron extraction and transport. Moreover, the incorporation of PEIE remarkably suppresses the infiltration of Ag ions under continuous thermal conditions, which further boosts the thermal stability of the device. By utilizing the PEIE-modified BCP buffer layer, the resulting PSCs demonstrate a champion power conversion efficiency (PCE) of 25.83%. Even after 1000 hours operation under a relative humidity of 30%, it still maintains an efficiency of more than 85% demonstrating significantly enhanced stability. This work presents an innovative design strategy for developing PSCs with simultaneously enhanced efficiency and operational stability.
研究领域:
可再生能源
·
材料科学
·
光伏技术
·
纳米技术
·
化学工程
✓ 已验证
产品关联
DOI
高影响因子
危险品化学品经营许可证（带存储）