LWT-FOOD SCIENCE AND TECHNOLOGY
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2025
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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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产品关联
DOI
高影响因子
JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE
·
2022
·Vol. 103
·期 3
·1194-1204
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IF 4.125
Pengyu Zhu,Chunmin Ma,Jing Fan,Yang Yang,Xiaofei Liu,Xin Bian,Likun Ren,Yue Xu,Dehui Yu,Linlin Liu,Yu Fu,Jian Gao,Na Zhang
BACKGROUND Soybean 11S globulin has good functional properties, which are widely used in the field of food. However, natural soybean 11S globulin (N-11S) has low flexibility and is easy to aggregate, impacting its foaming process. Studies have shown that soybean 11S globulin in molten globule state (MG-11S) has better molecular flexibility than N-11S, and trehalose has been shown to improve the properties of proteins. Therefore, this study investigated the interaction mechanism between trehalose and MG-11S, and its impact on rheological and foaming properties of MG-11S. RESULTS The molecular docking and intrinsic fluorescence results showed that hydrogen bonding was the main interaction force at lower than 0.5 mol L −1 trehalose added. Meanwhile, rheology and foaming showed that the MG-11S–trehalose complexes had better viscoelasticity, foaming ability (66.67–86.67%) and foaming stability (75.00–89.29%) than N-11S (16.67% foaming ability and 40.00% foaming stability); however, when the trehalose was higher than 0.5 mol L −1 , molecular crowding occurred and H-bonds were weakened, resulting in reduction of foaming capacities. Microstructure determination showed that trehalose attached to the surface of foam membrane; meanwhile, the foaming structure of the complex with 0.5 mol L −1 trehalose had a thicker liquid film with decreased drainage rate, less agglomeration and disproportionation of foam, illustrating the best foaming ability and foaming stability. CONCLUSION The results suggested that trehalose at different concentrations can interact with MG-11S through different mechanisms, and improve the foaming capacity of MS-11S. This provided a reference for the application of MS-11S in foaming food. © 2022 Society of Chemical Industry.
研究领域:
食品科学
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生物化学
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产品关联
DOI
PubMed
高影响因子
LWT-FOOD SCIENCE AND TECHNOLOGY
·
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
CHINESE JOURNAL OF CHEMICAL PHYSICS
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2024
·Vol. 37
·期 4
·563-570
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IF 1.2
Shi Hehang,Ye Xiaodong
Two soy protein 11S fractions with different surface sulfhydryl contents were prepared. Utilizing analytical ultracentrifugation, the effects of storage time and hydrogen peroxide at different concentrations (0.5—100 mmol/L) on the two 11S fractions were investigated. Results show that after removing 2-mercaptoethanol (2-ME) by size exclusion chromatography, the 11S fraction with high surface sulfhydryl content (2.0 mol sulfhydryl/mol 11S) progressively formed 15S and 21S in dilute solutions during storage at 4 °C for 82 days. While, the 11S fraction with low surface sulfhydryl content (0.2 mol sulfhydryl/mol 11S) was stable under the same condition. Moreover, after treating the 11S with high surface sulfhydryl content with 1 mmol/L H 2 O 2 , the weight percentage of 15S reached the maximum value of 20%. The 15S induced by air and H 2 O 2 could be totally converted to 11S with the addition of 10 mmol/L 2-ME, which could be attributed to that the disulfide bond linking two 11S molecules is on the surface of the 15S and easily accessible to the reducing agent 2-ME. This study helps us to deeply understand the formation mechanism of 15S and the stability of 11S.
研究领域:
食品科学
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蛋白质化学
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分析化学
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DOI
高影响因子
Foods
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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
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蛋白质化学
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产品关联
DOI
PubMed
高影响因子
MOLECULES
·
2022
·Vol. 27
·期 20
·7099
·
IF 4.927
Kuo Yong,Sidra Kaleem,Mingzhu Ma,Xiaoyuan Lian,Zhizhen Zhang
Marine-derivedPenicilliumfungi are one of the most important sources for the discovery of new bioactive natural products. This study characterized the isolation, structures, and antiglioma activities of twelve compounds, including three novel ones—penipyridinone B (1), 11S-(−)-penilloid A (2), and 11R,14E-(+)-penilloid A (3)—from the marine fungusPenicilliumsp. ZZ1750. The structures of the novel compounds were determined via extensive nuclear magnetic resonance (NMR) spectroscopic analyses, high-resolution electrospray ionization mass spectroscopy (HRESIMS) data, Mosher’s method, optical rotation (OR) calculations, and electronic circular dichroism (ECD) calculations. Penipyridinone B represents the first example of its structural type and showed potent antiglioma activity, with IC50values of 2.45 μM for U87MG cells and 11.40 μM for U251 cells. The known compounds of questiomycin A (9) and xanthocillin X (10) also showed antiproliferative activity against both U87MG and U251 cells, with IC50values of 13.65 μM to 22.56 μM. The antiglioma activity of questiomycin A and xanthocillin X may be related to the promotion of reactive oxygen species (ROS) production, the reduction of mitochondrial membrane potential (MMP), and the enhancement of caspase-3 enzyme activity.Keywords:marinePenicilliumsp. ZZ1750;penipyridinone B;11S-(−)-penilloid A;11R,14E-(+)-penilloid A;structure elucidation;antiglioma activity
研究领域:
天然产物化学
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药理学
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海洋生物学
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癌症研究
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产品关联
DOI
PubMed
高影响因子
Food Chemistry-X
·
2026
·
IF 9.2
Yaxin Zhou,Jianyu Yang,Chaojiang Dong,Miaomiao Liu,Yanan Guo,Linyi Zhou,Xue Geng,Zengwang Guo,Zhongjiang Wang
As 11S limits SPI emulsifying properties, this study investigated how dextran molecular weight regulates 11S interfacial adsorption. Maillard conjugation with 5000 Da dextran enhanced 11S flexibility and emulsifying properties, yielding a 35.0% increase in EAI (65 m 2 /g) and improved ESI (92%). The resulting emulsions exhibited markedly smaller and more uniform droplets (approximately 10–20 μm) compared to aggregated native 11S. Adsorption kinetics revealed a critical molecular weight dependency: 5000 Da dextran induced optimal structural transformation and interfacial reorganization, strengthening stability. In contrast, larger dextrans likely induced steric hindrance and provided limited flexibility enhancement, which may have contributed to suppressing interfacial rearrangement and limiting emulsification improvement. Based on these findings, we propose a chain-length balance model, and the results strongly suggest that Maillard glycation is an effective strategy to enhance non-glycosylated 11S functionality, elucidating a molecular weight-dependent modulation mechanism and providing new insights for improving protein emulsifying properties.
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DOI
高影响因子
FOOD RESEARCH INTERNATIONAL
·
2026
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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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DOI
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
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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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产品关联
DOI
高影响因子
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
·
2025
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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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产品关联
DOI
PubMed
高影响因子
LWT-FOOD SCIENCE AND TECHNOLOGY
·
2023
·
IF 6
Lijie Zhu,Yingyan Li,Jiakun Yu,He Liu,He Li,Xinqi Liu,Lei Chen,Guozhen Wang,Xiuying Liu,Wenping Ding
Thermosonication (TS) is an unconventional processing technique that modifies the structure and aggregation of proteins to improve their functional properties. In this study, we investigated the effect of TS at 40 °C, 60 °C, and 80 °C on the emulsification properties of glycinin (11S). The findings revealed that TS reduced the size of the protein particles while increasing their surface hydrophobicity index to 8177.83. TS treatment improved the stability of the emulsion, increasing the interfacial protein content, apparent viscosity, and emulsion stability, while reducing the adsorption pressure of 11S at the oil–water interface. After TS treatment at 80 °C followed by storage at 4 °C for 21 d, the emulsion turbiscan stability index (TSI) value (2.5) remained stable. By altering the adsorption characteristics of 11S at the oil–water interface, TS can increase the stability of the produced emulsion.
研究领域:
食品科学
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蛋白质化学
·
胶体与表面化学
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产品关联
DOI
高影响因子
危险品化学品经营许可证（带存储）