Journal of Food Measurement and Characterization
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2024
·Vol. 18
·期 12
·9856-9866
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IF 2.9
Zhang Maoying,Quan Fan,Zhang Jing,Feng Wanli,Zou Xianfeng
This study aims to covalently couple black soybean 7S globulin with polysaccharides via the Maillard reaction to enhance the solubility and emulsifying properties of black soybean 7S globulin. After glycosylation modification, the solubility of the modified product is significantly higher than that of natural black soybean 7S globulin (7S). When the pH is above 4, the solubility of the 7S globulin coupled with 20 kDa molecular weight glucan is notably higher compared to other polysaccharides. Among the glycosylation products, the 7S globulin coupled with 100 kDa molecular weight glucan exhibits the best emulsification properties, reaching 72.22 m²/g. Its emulsifying properties and stability are improved by 446.98% and 223.30%, respectively, compared to the native black soybean 7S globulin. The contact angle of the black soybean 7S globulin is 69.93 ± 1.4°, while the glycosylated product with gum arabic shows the most significant change, decreasing to 51.65 ± 1.43°, indicating an increase in hydrophilicity.
研究领域:
食品科学
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生物化学
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高影响因子
FOOD CHEMISTRY
·
2025
·
IF 9.8
Yan Xu,Jialu Shi,Xin Wang,Yue Wang,Yongxin Zhao,Vijaya Raghavan,Jin Wang
Punicalagin (PUN) is the predominant polyphenol in pomegranate peels, and it has antioxidant property. This study aimed to explore the potential of PUN binding in reducing the allergenicity of soybean protein 7S (a major soy allergen). Ultrasound pretreatment (U7S) was used to enhance the availability of PUN binding sites. After PUN binding, the U7S conformation became more disordered, and the surface hydrophobicity was reduced. The molecular docking results indicated that the formation of the U7S-PUN complexes mainly depended on hydrogen bonding interactions. The phenolic hydroxyl group from PUN endowed U7S with high antioxidant properties, which were retained after digestion in the gastrointestinal tract. At a molar ratio of 1:50, U7S-PUN complexes reduced the IgG binding capacity by approximately 58.05 % and increased the rate of degranulation inhibition to about 35.87 %. This research offers a theoretical foundation for the use of PUN in the production of hypoallergenic plant-based protein products.
研究领域:
食品科学
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免疫学
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生物化学
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DOI
PubMed
高影响因子
LWT-FOOD SCIENCE AND TECHNOLOGY
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2025
·
IF 6.6
Rongxue Zhou,Yuan Zhao,Linfan Shi,Zhongyang Ren,Wuyin Weng
The effect of 7S/11S ratio on the physicochemical properties of soy protein isolate (SPI) and SPI-linoleic acid (LA) films was studied. The apparent viscosity in the film-forming solution and the oil droplet size in the film-forming emulsion increased with increasing 11S globulin ratio. The oil droplets in the SPI-LA films increased in number and floated to the surface when the 7S/11S ratio was 2:6. The tensile strength (TS) and elongation at break (EAB) of 7S globulin films were 9.45 MPa and 94.51%, respectively. The increase in the 11S globulin ratio increases the TS of SPI and SPI-LA films; however, their EAB did not change. As the 7S/11S ratio decreased, the water vapor transmittance of the SPI films and the SPI-LA films decreased, but their glass transition temperature and transparency values increased. The proportion of hydrogen bonds and non-disulfide covalent bonds in the SPI films and the SPI-oil films reduced with the increase in the 11S globulin ratio, whereas that of disulfide bonds and hydrophobic interactions increased. This study clarified the effect of 7S/11S ratio on the properties of SPI and SPI-LA films, providing the theoretical guidance for selecting suitable SPI for the preparation of edible films.
研究领域:
食品科学
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生物化学
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DOI
高影响因子
COLLOIDS AND SURFACES A-PHYSICOCHEMICAL AND ENGINEERING ASPECTS
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2022
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IF 5.518
Jing He,Zhengli Peng,Jinxian Yang,Laixin Dai,Zan Hua,Lianwei Li
In the past decade, there is a number of studies focusing on the interactions between methylcellulose and ions/surfactants, whereas in real food and material systems, methylcellulose is widely co-existing with natural macromolecules such as polysaccharides and proteins, but their interplay has been scarcely studied so far. In this work, by selecting soy 7S globulin as a model protein, we have investigated the interplay between methylcellulose and soy 7S globulin in aqueous solutions, and its influence on the thermo-responsive behavior of methylcellulose chains. By combining particle sizing, isothermal titration calorimetry and cloud point measurements, it is observed that the addition of 7S globulin induces the formation of 7S globulin-methylcellulose aggregates, mainly driven by the weak hydrophobic force (∼ 0.03 kJ/mol) at T = 25 °C, and facilitated the formation of 7S globulin-methylcellulose fibrils aggregates at T = 50 – 70 °C, which shows thermo-responsive behavior. Atomic force microscopy and rheology results signify that the 7S globulin probably acted as multi-site centers to bridge fibrils together and eventually formed large spherical aggregates covered with reticular fibrous structures, along with the decrease in the modulus of 7S globulin-methylcellulose gel network, which is due to the heterogeneous distribution of aggregates and poor continuity of network. This study not only reveals the influence of 7S globulin on the thermo-responsive behavior of methylcellulose but also lays a foundation for further optimizing the performance of the 7S globulin-methylcellulose system in real food and material systems.
研究领域:
食品科学
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材料科学
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生物化学
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DOI
高影响因子
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
·
2024
·
IF 5.7
Ze Yun,Jiahao Li,Wenyue Zhu,Xin Yuan,Jiajia Zhao,Minjie Liao,Lingjun Ma,Fang Chen,Xiaosong Hu,Junfu Ji
Allergenicity of soybean 7S protein (7S) troubles many people around the world. However, many processing methods for lowering allergenicity is invalid. Interaction of 7S with phenolic acids, such as chlorogenic acid (CHA), to structurally modify 7S may lower the allergenicity. Hence, the effects of covalent (C-I, periodate oxidation method) and noncovalent interactions (NC-I) of 7S with CHA in different concentrations (0.3, 0.5, and 1.0 mM) on lowering 7S allergenicity were investigated in this study. The results demonstrated that C-I led to higher binding efficiency (C-0.3:28.51 ± 2.13%) than NC-I (N-0.3:22.66 ± 1.75%). The C-I decreased the α-helix content (C-1:21.06%), while the NC-I increased the random coil content (N-1:24.39%). The covalent 7S–CHA complexes of different concentrations had lower IgE binding capacity (C-0.3:37.38 ± 0.61; C-0.5:34.89 ± 0.80; C-1:35.69 ± 0.61%) compared with that of natural 7S (100%), while the noncovalent 7S–CHA complexes showed concentration-dependent inhibition of IgE binding capacity (N-0.3:57.89 ± 1.23; N-0.5:46.91 ± 1.57; N-1:40.79 ± 0.22%). Both interactions produced binding to known linear epitopes. This study provides the theoretical basis for the CHA application in soybean products to lower soybean allergenicity.
研究领域:
食品科学
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过敏研究
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生物化学
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DOI
PubMed
高影响因子
LWT-FOOD SCIENCE AND TECHNOLOGY
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2022
·
IF 6.056
Nannan Chen,Baoyan Yang,Ying Wang,Ning Zhang,Ying Li,Chaoying Qiu,Yong Wang
Flaxseed protein contains mainly 11S globulin (FG). It suffers significant aggregation upon heating, ionic strength and pH variation which hinders its application in food products. This study aims at improving the colloidal stability of FG by fabricating a flaxseed 11S globulin-soy 7S globulin (SG) complex and exploring its potential application in stabilizing emulsion. Results showed that SG could limit the thermal aggregation of FG by forming a stable FG-SG complex above 80 °C at neutral pH. Increasing temperature and heating time would promote the exposure of hydrophobic sites and facilitate the complexation that was irreversible. The complex showed enhanced stability against ionic strength and pH variation and was able to stabilize high internal phase emulsion (HIPE) with oil volume fraction up to 85% by a minimal protein concentration of 20 g/L which however could not be achieved solely by flaxseed 11S globulin. The HIPEs showed long term stability in a wide range of pH and ionic strength. This study paves way for enhancing the functionalities of oilseed 11S globulin simply through thermal induced complexation with 7S globulin from another plant source.
研究领域:
食品科学
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蛋白质化学
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胶体科学
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DOI
高影响因子
Foods
·
2023
·Vol. 12
·期 14
·2650
·
IF 5.2
Wenhui Li,Qiongling Chen,Xiaowen Wang,Zhenjia Chen
To investigate the impact of frozen storage conditions on the physicochemical properties of soybean protein and explore the underlying mechanisms, this study focused on soybean isolate (SPI), ß-soybean companion globulin (7S), and soybean globulin (11S). The protein solutions were prepared at a concentration of 2% and subjected to freezing for 1 and 5 days. Subsequently, the protein content, physicochemical properties, secondary structure, sulfhydryl content, and chemical interaction forces were assessed and analyzed using UV spectrophotometry, Zeta potential measurements, SDS-PAGE, Fourier infrared spectroscopy, and endogenous fluorescence photoemission spectroscopy. The obtained results revealed that the solubility and total sulfhydryl content of SPI, 7S, and 11S exhibited a decreasing trend with prolonged freezing time. Among them, 11S demonstrated the largest decrease in solubility and total sulfhydryl content, followed by SPI, and 7S the least. During freezing, the aromatic amino acids of SPI, 7S, and 11S molecules were exposed, leading to increased hydrophobicity, protein aggregation, and particle size enlargement, and the structure of the protein changed from disordered structure to ordered structure. After freezing, the polarity of the microenvironment of SPI, 7S, and 11S increased, and their maximum fluorescence emission wavelengths were red-shifted. Notably, the largest red shift of SPI was from 332 nm to 335 nm. As freezing time increased, the contribution of hydrogen bonding increased, while the contribution of hydrophobic interactions decreased. This indicates that freezing affects the hydrophobic interactions, hydrogen bonding, and other chemical forces of the protein. The growth of ice crystals leads to the unfolding of protein molecular chains, exposure of internal hydrophobic groups, enhancement of hydrophobicity, and alters the secondary structure of the protein.Keywords:different freezing time;soybean isolate protein;7S;11S
研究领域:
食品科学
·
蛋白质化学
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DOI
PubMed
高影响因子
FOOD RESEARCH INTERNATIONAL
·
2026
·
IF 8.8
Wei Wan,Xiaokang Na,Ming Du,Jianyu Zhu,Beiwei Zhu,Chao Wu
7S and 11S globulins exhibit distinct binding modes with chitosan oligosaccharide. • The 7S/11S ratio determines the gelation pathway and network architecture. • 11S-rich systems form rigid, covalently cross-linked hydrogels. • Globulin composition modulates water mobility and mechanical properties. Soy protein isolate (SPI) is widely used in food applications, but the natural variation in its 7S/11S globulin ratio leads to inconsistent gel properties. In this study, we investigated how the 7S/11S ratio influences the structural and rheological properties of composite hydrogels formed with chitosan oligosaccharide (COS). Spectroscopic analyses revealed that 7S-rich systems maintain a more flexible conformation with higher α-helix content (12.7%), whereas 11S-rich systems adopt a rigid, β-sheet-rich structure with β-sheet content increasing to 49.6% (compared to 34.7% in 7S-rich systems). Rheological measurements showed that increasing the 11S fraction progressively enhances the storage modulus, which reaches approximately five times that of 7S-rich gels, transforming the gel network from physically entangled to covalently cross-linked. Microstructural and water mobility analyses confirmed that 11S-rich gels form dense, compact structures that restrict water mobility, with transverse relaxation time decreasing from 238 ms to 180 ms, whereas 7S-rich gels exhibit looser structures. These findings demonstrate that the 7S/11S ratio is a critical determinant of the macroscopic properties of SPI-COS composite gels, providing a practical strategy for tailoring plant protein gel textures. Download: Download high-res image (200KB) Download: Download full-size image
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高影响因子
BIOMACROMOLECULES
·
2026
·
IF 5.9
Qin Sheng,Xuan Sha,Hanyu Wu,Jing He
This study employed soy 7S globulin and its enzymatic hydrolyzates as model systems to elucidate how protein size, surface hydrophobicity, and secondary structure affect the thermo-induced network formation of methylcellulose (MC). Protein hydrolysis decreased the protein size, reduced hydrophobicity, and triggered partial rearrangement of its secondary structure. Atomic force microscopy (AFM), confocal laser scanning microscopy (CLSM), and rheology showed that, at high temperatures, unhydrolyzed 7S globulin (P0) promoted MC fibril interchain association through hydrophobic interactions, creating a strong yet heterogeneous network. In contrast, higher hydrolysis levels (P1–P3) produced smaller, more uniformly distributed protein aggregates and thinner, more interconnected fibrils but a mechanically weaker network. Overall, enzymatic hydrolysis can finely regulate the morphology and mechanical properties of protein–MC networks at high temperatures, providing insights for designing protein–polysaccharide composite systems and optimizing their performance in food and material applications.
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PubMed
高影响因子
Journal of Future Foods
·
2025
·
IF 7.2
Kexin Du,Yapu Zhang,Xinya Liu,Yang Tian,Mengfan Wang,Xin Peng
In this paper, soybean 7S and 11S protein nanocarriers were constructed through heat treatment (H7S/H11S) to encapsulate and protect quercetin (Que). The incubation temperature and the mass ratio of protein to Que were optimized for the nanocomplexes fabrication, and it was found that the encapsulation efficiency of H7S/H11S-Que nanocomplexes reached 94.59% and 85.77%, respectively, when the temperature was 60 °C and the mass ratio of protein to Que was 40:1. Compared with free Que, the nanocomplexes can significantly improve the stability and antioxidant capacity of Que, reduce its degradation by the digestive system and enhance its inhibitory effect on CT26 cell proliferation. Additionally, the H7S/H11S-Que nanocomplexes also exhibited good inhibitory ability against α-glucosidase/α-amylase. Fluorescence spectral results demonstrated that the spontaneous interaction between Que and H7S/H11S could decrease the intrinsic fluorescence of 7S/11S through static quenching mechanism, and a non-covalent protein-Que complex with a 1:1 binding stoichiometry was formed, primarily involving hydrophobic interactions and hydrogen bonds. Simultaneously, the binding of Que induced significant secondary structural modifications (increasing α-helix and random coil content, while decreasing β-sheet and β-turn content) and reduced the surface hydrophobicity of H7S/H11S. These findings offered a promising new approach for developing soybean protein-based nanocarriers with exceptional encapsulation capability, and also broaden the application of Que in the fields of food and medicine.
研究领域:
食品科学与技术
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纳米技术
·
药学
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生物化学
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营养生物化学
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分子生物学
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高影响因子
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
·
2025
·
IF 6.2
Yu Zhang,Songyuan Luo,Kai Huang,Jie Liu,Sen Li,Hongdong Song,Hongwei Cao,Xiao Guan
This study systematically evaluated the gastrointestinal fate of pea 7S, 11S globulin, and pea protein isolate (PPI) and their impact on gut using INFOGEST digestion, fecal fermentation, and multiomics approaches. During the gastrointestinal stage, pea proteins were largely digested, while pea 7S globulins and PPI exhibited partial resistance to gastric digestion. Intestinal digestion significantly enhanced Lys bioavailability, although Met remained as the first limiting amino acid across all pea proteins. During in vitro fermentation inoculated with microbiota from hyperuricemic individuals, pea proteins significantly reduced the production of trimethylamine N-oxide (TMAO) and guanosine relative to beef protein. Concurrently, pea protein supplementation promoted the generation of short-chain fatty acids and selectively enriched beneficial populations of gut microbiota such as Phascolarctobacterium and Akkermansia. Spearman correlation revealed that amino acid composition of pea proteins significantly affected microbial composition and gut-produced metabolites. Our results elucidate the structural-digestive-microbial interactions of pea proteins.
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高影响因子
危险品化学品经营许可证（带存储）