INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
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2022
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IF 8.025
Zhi-Wei Liu,Ying-Xue Zhou,Yi-Cheng Tan,Jun-Hu Cheng,Alaa El-Din Bekhit,Amin Mousavi Khaneghah,Rana Muhammad Aadil
The effects of dielectric-barrier discharge (DBD) plasma treatment (20 s to 120 s treatment time with 40 kV, 12 kHz) induced mild oxidation on the gelling properties, and related structural changes of glycinin were investigated. The gelling ability of glycinin was improved by the mild oxidation induced by the plasma treatment. Treated glycinin gels exhibited a continuous and uniform network microstructure. Samples treated for 120 s had a 2.07-, 3.99- and 2.03-fold increase in hardness, chewiness, and resilience compared to the 20 s treated samples. Structural analyses showed that primary and secondary structures of glycinin were unaffected. The tertiary structure was shifted, accompanied by a decrease in free sulfhydryl (-SH) content. At the same time, carbonyl content and average particle diameter were increased by DBD treatment. The DBD treatment facilitated the generation/exchange of intermolecular disulfide bonds and enhanced gelling properties of glycinin. It is concluded that controlled plasma-induced protein oxidation can improve protein functionality.
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
FOOD CHEMISTRY
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2025
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IF 9.8
Peng Bo Huang,Jing Long Qu,Shuo Yang,Tian Jiao Shui,Huan Huan Yang,Li Ping Cheng,Yang Qin,Jun Xi
Glycinin is a common food allergen, which may cause allergic shock in severe cases, thus posing a threat to public health. Therefore, rapid and accurate detection of glycinin is crucial. In this study, we synthesized Au Ag core–shell nanoparticles loaded with the Raman reporter molecule 5,5′-dithiobis(2-nitrobenzoic acid) (DTNB), which provides both colorimetric and Raman signal capabilities. These nanoparticles were applied to colorimetric lateral flow immunoassay (CM-LFIA) and surface-enhanced Raman scattering-based lateral flow immunoassay (SERS-LFIA), respectively. The CM-LFIA achieved a visual limit of detection (LOD) of 1 ng/mL, while the SERS-LFIA exhibited a LOD of 40 pg/mL, with good linearity over the range of 1 ng/mL to 10 4 ng/mL (R 2 = 0.997). Moreover, the quantitative SERS-LFIA demonstrated satisfactory performance in spiked food matrix samples, achieving acceptable recoveries of 82–88 % and RSD ranging from 4.88 % to 6.97 %.
研究领域:
食品科学
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免疫学
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纳米技术
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产品关联
DOI
PubMed
高影响因子
FOOD CHEMISTRY
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2025
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IF 9.8
Guangzheng Wang,Yisheng Du,Xu Cheng,Weiwei Li,Dandan Li,Chong Xie,Runqiang Yang,Pei Wang
Selectively hydrolyzed soy protein can enhance wheat-based product quality by modulating gluten thermal polymerization. This study examined the effects of β-conglycinin (7S) and glycinin hydrolysate (GH) on gluten rheological and thermal properties, particle size, Raman spectra, and microstructure during heating. Both 7S and GH improved gluten viscoelasticity, with their combined addition (7S/GH) showing the strongest effect. 7S/GH increased the denaturation temperature by 4.94 °C and enthalpy by 43.84 %, while the D50 at 95 °C was 97.99 % higher than the control. These enhancements were linked to reinforced glutenin–gliadin crosslinking and a strengthened gluten network. 7S and GH synergistically promoted disulfide bond formation, buried tryptophan and tyrosine residues, and induced a more compact gluten conformation. Confocal laser scanning microscopy and micro-computed tomography confirmed a denser gluten network after heating. Overall, 7S and GH act synergistically to improve gluten stability, offering theoretical insights for soy protein hydrolysates in wheat-based product quality improvement.
研究领域:
食品科学
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高分子科学
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蛋白质化学
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生物物理学
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谷物化学
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产品关联
DOI
PubMed
高影响因子
FOOD HYDROCOLLOIDS
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2024
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IF 11
Kang Ni,Shuxing Yin,Jing Hu,Anhong Liu,Weihong Zeng,Tengchuan Jin,Xiaodong Ye
In food systems, complexes formed between soybean protein and polyelectrolytes are extensively utilized. However, the mechanisms governing their interactions remain elusive, especially when they possess similar net charges. This study investigates the complexation between like-charged glycinin (11S) and diblock copolymers of polyethylene glycol- block -poly(sodium styrene sulfonate) (PEG- b -PSS) using analytical ultracentrifugation (AUC), a first-principle technique that examines macromolecular characteristics such as molecular weight , stoichiometry , and binding properties. The results reveal that 11S can interact with polyelectrolytes of the same net charges. At ionic strengths above 0.1 M, under a specific concentration of PEG- b -PSS with a PSS degree of polymerization of 33, reducing ionic strength augments the binding strength between PEG- b- PSS and 11S while enhancing the electrostatic repulsion between complexes. Consequently, association occurs as ionic strength decreases from 0.5 to 0.3 M due to the predominance of binding strength, and the association disappears at 0.1 M because electrostatic repulsion becomes predominant. Moreover, PEG- b- PSS with a higher degree of polymerization in the PSS blocks facilitates the formation of insoluble complexes of 11S via soluble intermediates. At an ionic strength of 0.025 M, PEG- b- PSS induces the dissociation of 11S into subunits and peptides. This study demonstrates that by controlling the ionic strength and the degree of polymerization of the polyelectrolyte, it is possible to regulate the binding strength between 11S and polyelectrolyte, as well as the structural changes during binding. Furthermore, this study contributes to understanding the complex formation mechanism between soybean protein and polyelectrolytes , and further expands the application of AUC in studying their binding.
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
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
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2026
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IF 8.7
Yujiao Zhang,Chengxin Fei,Ruojie Zhao,Oujun Dai,Zhixiong Deng,Bei Fan,Fengzhong Wang,Yatao Huang
11S globulin forms a more stable network with PA due to higher surface charge density than 7S. • Binding of phytic acid triggered protein unfolding and decreased β-sheet content. • PA-protein complexes inhibited proteolysis, reducing hydrolysis degree by about 30%. • Electrostatic interactions serve as the primary driving force, stabilized by hydrogen bonds and hydrophobic interactions. This study investigated the complexation of phytic acid (PA) with soybean β-conglycinin (7S) and glycinin (11S) and its effects on protein structure and digestibility. Complex formation was most pronounced near pH 3.0, accompanied by decreased solubility and enhanced aggregation. PA binding reduced β-sheet content from 36.0% to 31.4% in 7S and from 37.3% to 35.1% in 11S, indicating conformational rearrangement. During simulated gastric digestion, hydrolysis decreased from 10.59% to 7.42% for 7S and from 9.93% to 6.92% for 11S, whereas hydrolysis increased during subsequent intestinal digestion. Molecular docking and molecular dynamics simulations provided theoretical support for interpreting the experimental observations, suggesting contributions from electrostatic interactions and hydrogen bonding, with more extensive contacts predicted for PA-11S. Isothermal titration calorimetry confirmed a higher affinity of PA for 11S, with dissociation constants of 12.3 μM for 11S and 32.5 μM for 7S. At pH 3.0 and 37 °C, binding was enthalpically and entropically favorable for 7S but enthalpy-driven for 11S. These findings provide molecular insights into PA-soy protein interactions and their implications for protein hydrolysis during simulated gastrointestinal digestion. Download: Download high-res image (154KB) Download: Download full-size image
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DOI
高影响因子
ULTRASONICS SONOCHEMISTRY
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2026
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IF 10.2
Xinran Niu,Di An,Liang Li
This study systematically investigated the effects of ultrasonic pretreatment on the fibrillation behavior of soy protein isolate (SPI), β-conglycinin (7S) and glycinin (11S). A multi-analytical approach combining Thioflavin T fluorescence spectroscopy, SDS-PAGE, dynamic light scattering, zeta potential measurement, and spectroscopic analyses was employed to monitor fibrillation kinetics and structural modifications. Ultrasonication significantly accelerated the fibrillation process by enhancing nucleation, increasing the apparent rate constant of 7S by 44% and that of SPI by 67%. SDS-PAGE analysis indicated that ultrasound treatment promoted protein degradation, generating a greater number of low-molecular-weight peptides, which may have facilitated fibril nucleation. Ultrasound treatment reduced protein particle size, increased surface charge, and promoted conformational transitions toward β-sheet-rich structures, with U-7SN showing a 20.8% rise in β-sheet content. These structural changes were correlated with enhanced functional properties, including improved solubility, emulsifying activity, and viscosity. The findings demonstrated that ultrasound promoted fibrillation by enhancing hydrophobic interactions and the formation of β-sheet structures, offering a theoretical basis for tailoring plant protein nanofibrils with targeted functionalities for food and material applications.
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产品关联
DOI
PubMed
高影响因子
FOOD RESEARCH INTERNATIONAL
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2025
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IF 8
Zhijie Huang,Weixiang Xu,Xudong Yang,Mingxi Liu,Lijun Yin,Weibin Bai,Xin Jia
Non-covalent interactions between soybean storage proteins β-conglycinin (7S) and glycinin (11S) and two tea polyphenols, catechin and epigallocatechin-3-gallate (EGCG), were examined to elucidate their effects on protein conformation, stability, digestibility, allergenicity, and antioxidant capacity. Due to its smaller molecular size, catechin more easily penetrated the hydrophobic cores of proteins, yielding higher binding stoichiometry and concentration-dependent aggregation. At 4 mM, extensive aggregation masked proteolytic cleavage sites, reducing gastrointestinal digestibility by 7.3 % for 7S and 15.1 % for 11S. In contrast, EGCG, with an additional galloyl moiety and a denser hydroxyl network, interacted with proteins through synergistic hydrogen bonding, π–π stacking, and hydrophobic forces. It produced more stable supramolecular complexes with much larger diameters (462.2 ± 6.8 nm for 11S-EGCG, versus 30.3 ± 1.5 nm for native 11S), and lowered IgE-binding capacity by approximately 19.5–38.7 %, probably through epitope masking and surface-charge changes. For both polyphenols, binding significantly decreased solvent accessibility of hydrophobic regions, reorganized secondary structure (α-helix loss and β-sheet gain), and markedly enhanced intrinsic antioxidant capacity. These findings demonstrate that selecting an appropriate polyphenol type and dose can simultaneously confer hypoallergenic potential, controlled digestibility, and elevated antioxidant function. These findings highlight the potential of non-covalent protein-polyphenol assemblies to develop plant-based foods and nutraceuticals with improved health benefits.
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产品关联
DOI
PubMed
高影响因子
FOOD CHEMISTRY
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2025
·
IF 9.8
Ziteng Lian,Sai Yang,Yaqi Tang,Qianqian Zhang,Xiaolei Guo,Qianqi Chi,Xiaohong Tong,Lianzhou Jiang,Huan Wang
This research aimed to improve the conformational flexibility, oil/water interface and emulsifying properties of soy glycinin (11S) by enzymatic hydrolysis and glycosylation with carboxymethyl cellulose (CMC, 0–0.75 %, w/v). Enzymatic hydrolysis increased degree of grafting of 11S to CMC, with a maximum observed at 0.5 % CMC concentration. SR-FTIR tracing showed that 11S-CMC reacted mainly by inducing C O, C O and O H changes, while hydrolysis enhanced the C N effect. Pepsin hydrolysis disrupted disulfide bonds in 11S and increased protein flexibility; CMC enhanced steric hindrance through covalent grafting. The synergistic modification promoted interfacial diffusion, penetration and rearrangement of 11S to form more stable interfacial film. The modified protein-stabilized emulsions showed reduced droplet size and more uniform distribution, increased emulsifying activity and stability to 54.52 m 2 /g and 105.52 min. Rheological data displayed elevated apparent viscosity, G′, G″ and LAOS response properties of emulsions. These findings offer a dual-modification approach to enhance emulsifying potential of 11S.
研究领域:
食品科学
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生物技术
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生物化学
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胶体与界面科学
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高分子科学
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产品关联
DOI
PubMed
高影响因子
FOOD HYDROCOLLOIDS
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2026
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IF 13.8
Hanyu Song,Bingru Li,Siyu Wu,Jingwen Xu,Baokun Qi,Shizhang Yan,Lianzhou Jiang
Soybean lipophilic protein (LP) is composed of β-conglycinin (7S), glycinin (11S), and oil body protein-phosphatidylcholine (OBPs-PC), but the interactions among its components and their effects on foaming properties remain unclear. In this study, we reconstituted these components at the native LP ratio and systematically investigated the regulatory mechanism of protein-protein interactions on foaming properties. The results showed that the nature of component interactions determined foaming properties. 7S and 11S exhibited a synergistic effect: compared with the individual components, their combination underwent conformational rearrangement, characterized by decreased particle size, transition from β-sheet to random coil, increased free sulfhydryl content, reduced surface hydrophobicity, and fluorescence quenching. These changes enhanced interfacial adsorption and foam stability, making 7S + 11S exhibit the optimal foaming ability (136.44%) and stability (58.42%). In contrast, OBPs-PC, due to its strong hydrophobicity and large-sized aggregates, inhibited interfacial adsorption, causing a significant decrease in the foaming ability of OBPs-PC-containing complexes. Molecular interaction analysis indicated that hydrogen bonds and hydrophobic interactions were the main non-covalent forces driving complex formation. Rheological results confirmed that 7S + 11S foam had the highest storage modulus and the widest linear viscoelastic region. In conclusion, 7S and 11S achieved optimal foaming properties through conformational rearrangement and synergistic interfacial behavior, while the strong hydrophobicity and large-sized aggregates of OBPs-PC disrupted interfacial equilibrium and inhibited foaming. This study provides a theoretical basis for expanding the application of LP as efficient gas-water interface stabilizers and foaming agents.
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DOI
高影响因子
FOOD HYDROCOLLOIDS
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2016
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IF 3.858
Fu Liu,Chuan-He Tang
Formulation of food-grade Pickering emulsions has attracted growing attention in the food and drug fields, due to their promising potential as novel delivery systems for lipophilic bioactive ingredients. The present work reported that a kind of gel-like Pickering emulsions stabilized by heat (at 100 °C)-treated soy glycinin (SG; a major globulin in soy proteins), fabricated by modulating protein concentration ( c ) and/or oil fraction ( ϕ ), can perform as sustained release delivery systems for β -carotene. Rheological measurements and microstructural observations indicated that increasing c and/or ϕ resulted in a progressive strengthening of gel-like network in the emulsions stabilized by heated SG, which was closely related to a high percentage of proteins adsorbed at the interface, or entrapped within the network. In contrast, no distinct gel formation was observed for the emulsions stabilized by unheated SG. In vitro intestinal digestion experiments showed that for the emulsions (stabilized by unheated or heated SG) without distinct gel formation, the release behavior of β -carotene was mainly determined by droplet size , while in the case of gel-like emulsions by heated SG, the gel-like network formation greatly slowed down the β -carotene release (irrespective of the applied c and/or ϕ ). All the test emulsions did not suffer a distinct degradation of β -carotene over the whole digestion process. The findings are of great interest for the development of novel sustained delivery systems for lipophilic components, based on Pickering emulsions stabilized by a kind of protein-based particle stabilizers.
研究领域:
食品科学
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生物医学工程
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DOI
高影响因子
危险品化学品经营许可证（带存储）