Food Hydrocolloids最新文献_第5页

Impact of ageing and heat treatment on the colloidal state of oat protein dispersions 老化和热处理对燕麦蛋白分散体胶体状态的影响

IF 11 1区农林科学 Q1 CHEMISTRY, APPLIED

Food Hydrocolloids

Pub Date : 2026-01-13 DOI: 10.1016/j.foodhyd.2026.112455

Ines Pynket , Frederik Janssen , Christophe M. Courtin , Christophe Chassenieux , Taco Nicolai , Arno G.B. Wouters

Oats are increasingly being used for the production of liquid and semi-solid foods, such as dairy alternatives. Studying the colloidal state of oat proteins in aqueous systems is crucial for understanding their stability and functionality in these types of foods. Here, a stock solution containing mostly unaggregated oat proteins was prepared starting from an in-house produced oat protein isolate (OPI) derived from non-heat-treated oat groats. Then, the impact of ageing (0–72 h) and heat treatment (30–90 °C) on the colloidal state of OPI dispersions as a function of pH (7.0–9.0) was investigated. It was observed that OPI dispersions (2.0% w_protein/v) were unstable at 20 °C, gradually aggregating over time. Such aggregation at 20 °C occurred more rapidly at lower than at higher pH. Heating these OPI dispersions at 90 °C (10 min) induced dissociation of aggregates and formation of stable protein structures. This effect was reversible upon cooling as larger protein structures were re-formed. Interestingly, after extended ageing of OPI dispersions (20 °C, 72 h), heating at 90 °C (10 min) resulted in the formation of gel-like structures, an effect that could not be reversed upon cooling. It is thus clear that the colloidal state of oat proteins depends strongly on the interplay of ageing time and heat treatment. Our findings contribute to understanding the stability and functionality of oat proteins in liquid and semi-solid foods.

燕麦越来越多地被用于生产液体和半固体食品，如乳制品替代品。研究燕麦蛋白在水系统中的胶体状态对于理解它们在这类食品中的稳定性和功能至关重要。在这里，从内部生产的燕麦分离蛋白（OPI）开始制备含有大部分未聚集的燕麦蛋白的原液，该蛋白来源于未经热处理的燕麦粥。然后，研究了时效（0 ~ 72 h）和热处理（30 ~ 90℃）对OPI分散体胶体状态随pH（7.0 ~ 9.0）的变化规律。观察到OPI分散体（2.0% wprotein/v）在20℃时不稳定，随着时间的推移逐渐聚集。这种聚集在20°C下比在较高ph下发生得更快。在90°C（10分钟）加热这些OPI分散体，诱导聚集体解离并形成稳定的蛋白质结构。这种影响在冷却时是可逆的，因为更大的蛋白质结构被重新形成。有趣的是，OPI分散体延长时效（20°C, 72 h）后，在90°C（10分钟）下加热导致凝胶状结构的形成，这一效应在冷却时无法逆转。因此很清楚，燕麦蛋白的胶体状态在很大程度上取决于老化时间和热处理的相互作用。我们的发现有助于理解燕麦蛋白在液体和半固体食物中的稳定性和功能。

{"title":"Impact of ageing and heat treatment on the colloidal state of oat protein dispersions","authors":"Ines Pynket , Frederik Janssen , Christophe M. Courtin , Christophe Chassenieux , Taco Nicolai , Arno G.B. Wouters","doi":"10.1016/j.foodhyd.2026.112455","DOIUrl":"10.1016/j.foodhyd.2026.112455","url":null,"abstract":"<div><div>Oats are increasingly being used for the production of liquid and semi-solid foods, such as dairy alternatives. Studying the colloidal state of oat proteins in aqueous systems is crucial for understanding their stability and functionality in these types of foods. Here, a stock solution containing mostly unaggregated oat proteins was prepared starting from an in-house produced oat protein isolate (OPI) derived from non-heat-treated oat groats. Then, the impact of ageing (0–72 h) and heat treatment (30–90 °C) on the colloidal state of OPI dispersions as a function of pH (7.0–9.0) was investigated. It was observed that OPI dispersions (2.0% w<sub>protein</sub>/v) were unstable at 20 °C, gradually aggregating over time. Such aggregation at 20 °C occurred more rapidly at lower than at higher pH. Heating these OPI dispersions at 90 °C (10 min) induced dissociation of aggregates and formation of stable protein structures. This effect was reversible upon cooling as larger protein structures were re-formed. Interestingly, after extended ageing of OPI dispersions (20 °C, 72 h), heating at 90 °C (10 min) resulted in the formation of gel-like structures, an effect that could not be reversed upon cooling. It is thus clear that the colloidal state of oat proteins depends strongly on the interplay of ageing time and heat treatment. Our findings contribute to understanding the stability and functionality of oat proteins in liquid and semi-solid foods.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"175 ","pages":"Article 112455"},"PeriodicalIF":11.0,"publicationDate":"2026-01-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146035998","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Proanthocyanidin/laccase-mediated cross-linking enhances the structural stability and rheological properties of collagen solutions 原花青素/漆酶介导的交联增强了胶原溶液的结构稳定性和流变性能

IF 11 1区农林科学 Q1 CHEMISTRY, APPLIED

Food Hydrocolloids

Pub Date : 2026-01-12 DOI: 10.1016/j.foodhyd.2025.112360

Junhong Xie , Li Feng , Fanghui Deng , Wei Yue , Wei Liang , Qiannan Zhao , Wentao Ma , Jianhua Rong , Shanbai Xiong , Yang Hu

Increasing the added value of freshwater fish by-product processing and reducing the economic losses are currently research hotspots in the field of aquatic products. However, the collagen-based products derived from freshwater fish cannot be widely applied due to their disadvantages such as low mechanical properties. Enzymatic cross-linking modification to improve the physicochemical properties of collagen-based materials is a better solution. This study focused on the self-assembly behavior of collagen molecules, investigated the cross-linking of collagen solutions mediated by laccase and proanthocyanidins, and improved their rheological properties and structural characteristics. The results showed that the volume ratio of collagen-proanthocyanidins/laccase (COL-PL) within the range of 1:0.01 to 1:0.4 is more conducive to the stability of collagen molecules. All cross-linked groups exhibited shear thinning properties. Collagen-proanthocyanidins (COL-PA) enhanced the mechanical properties of collagen molecules to a certain extent. However, when the volume ratio of COL-PL is 1:0.02, it not only accelerates the aggregation of collagen molecules, but also generates a complex with the best gel performance. This is mainly because low-concentration laccase can catalyze the generation of proanthocyanidin active groups. The interaction between the C=O bond and the -NH₂ bond in the collagen molecule peptide chain provides more sites for the aggregation of collagen molecules, and at the same time, the chemical bond interaction also makes the collagen aggregate more closely. Finally, through atomic force microscopy observation, after 24 h, COL-PL 1:0.02 group collagen molecules formed a dense reticular cross-linked structure. The research provides a new approach to expanding freshwater fish collagen potential application prospects.

提高淡水鱼副产品加工的附加值，减少经济损失是目前水产品领域的研究热点。然而，从淡水鱼中提取的胶原蛋白制品由于其机械性能低等缺点而不能得到广泛应用。酶法交联改性是改善胶原基材料理化性能的较好解决方案。本研究着眼于胶原分子的自组装行为，研究漆酶和原花青素介导的胶原溶液的交联，并改善其流变学性质和结构特征。结果表明，胶原-原花青素/漆酶（COL-PL）体积比在1:0.01 ~ 1:0.4范围内更有利于胶原分子的稳定性。所有交联基团均表现出剪切减薄特性。胶原原花青素（COL-PA）在一定程度上增强了胶原分子的力学性能。而当COL-PL的体积比为1:0.02时，它不仅加速胶原蛋白分子的聚集，而且生成了凝胶性能最好的复合物。这主要是因为低浓度漆酶能催化原花青素活性基团的生成。胶原分子肽链中C=O键与-NH2键的相互作用为胶原分子聚集提供了更多的位点，同时化学键的相互作用也使胶原聚集更加紧密。最后通过原子力显微镜观察，24 h后，COL-PL 1:0.02基团胶原分子形成致密的网状交联结构。该研究为拓展淡水鱼胶原蛋白的潜在应用前景提供了新的途径。

{"title":"Proanthocyanidin/laccase-mediated cross-linking enhances the structural stability and rheological properties of collagen solutions","authors":"Junhong Xie , Li Feng , Fanghui Deng , Wei Yue , Wei Liang , Qiannan Zhao , Wentao Ma , Jianhua Rong , Shanbai Xiong , Yang Hu","doi":"10.1016/j.foodhyd.2025.112360","DOIUrl":"10.1016/j.foodhyd.2025.112360","url":null,"abstract":"<div><div>Increasing the added value of freshwater fish by-product processing and reducing the economic losses are currently research hotspots in the field of aquatic products. However, the collagen-based products derived from freshwater fish cannot be widely applied due to their disadvantages such as low mechanical properties. Enzymatic cross-linking modification to improve the physicochemical properties of collagen-based materials is a better solution. This study focused on the self-assembly behavior of collagen molecules, investigated the cross-linking of collagen solutions mediated by laccase and proanthocyanidins, and improved their rheological properties and structural characteristics. The results showed that the volume ratio of collagen-proanthocyanidins/laccase (COL-PL) within the range of 1:0.01 to 1:0.4 is more conducive to the stability of collagen molecules. All cross-linked groups exhibited shear thinning properties. Collagen-proanthocyanidins (COL-PA) enhanced the mechanical properties of collagen molecules to a certain extent. However, when the volume ratio of COL-PL is 1:0.02, it not only accelerates the aggregation of collagen molecules, but also generates a complex with the best gel performance. This is mainly because low-concentration laccase can catalyze the generation of proanthocyanidin active groups. The interaction between the C=O bond and the -NH<sub>2</sub> bond in the collagen molecule peptide chain provides more sites for the aggregation of collagen molecules, and at the same time, the chemical bond interaction also makes the collagen aggregate more closely. Finally, through atomic force microscopy observation, after 24 h, COL-PL 1:0.02 group collagen molecules formed a dense reticular cross-linked structure. The research provides a new approach to expanding freshwater fish collagen potential application prospects.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"175 ","pages":"Article 112360"},"PeriodicalIF":11.0,"publicationDate":"2026-01-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146036017","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Enhancement of composite film properties by sweeping-frequency ultrasound modified xanthan gum and nano ZnO: structural and functional characterization 扫描频率超声改性黄原胶和纳米ZnO增强复合膜性能：结构和功能表征

IF 11 1区农林科学 Q1 CHEMISTRY, APPLIED

Food Hydrocolloids

Pub Date : 2026-01-12 DOI: 10.1016/j.foodhyd.2026.112449

Lei Zhang , Haiyang Zhang , Shanshan Zhou , Binglin Fu , Jilong Deng , Yan Shen , Hafida Wahia , Xiaojie Yu , Haile Ma , Cunshan Zhou

Xanthan gum (XG) with different structures was prepared by being subjected to sweeping-frequency ultrasound (SFU) modification, and then incorporated with nano ZnO to fabricate composite films for active food packaging applications. Effects of SFU power density (0、6.25、25, 100 W⋅L⁻¹) on the molecular weight, monosaccharide composition, and structure of XG were systematically investigated. XG/ZnO composite films were prepared using the solution casting method. Physical properties of composite films were characterized by mechanical properties, color, UV absorption, thermal stability, and gas transmission rate. The interaction between XG and nano ZnO was elucidated through rheological properties and microscopic morphology. Furthermore, the antioxidant and antibacterial activities of composite films were evaluated. Results indicated that SFU effectively reduced the molecular weight of XG, with the weight-average molecular weight (Mw) decreasing to 7.92 × 10⁴ Da after 25 W⋅L⁻¹ SFU treatment. Side-chain glycosidic bonds were disrupted, leading to a 31.58 % reduction in glucuronic acid (GluA) content. By loading 10 % nano ZnO (relative to XG dry weight), the composite film exhibited enhanced tensile strength (TS) of 32.43 MPa, excellent UV shielding properties, reduced gas transmission rate, and improved thermal stability. Rheological and microstructure analysis revealed strong interfacial bonding between SFU modified XG and ZnO nanoparticles. Consequently, composite films exhibited significant antioxidant and antibacterial activities, inhibiting E. coli by 85.90 % and S. aureus by 88.16 %. It was demonstrated that SFU modified XG/ZnO composite films can be promising for functional food packaging.

采用扫频超声（SFU）对黄原胶（XG）进行改性，制备出不同结构的黄原胶（XG），并与纳米ZnO复合制备活性食品包装膜。系统研究了SFU功率密度（0、6.25、25、100 W·L−1）对XG分子量、单糖组成和结构的影响。采用溶液铸造法制备了XG/ZnO复合薄膜。对复合膜的物理性能进行了表征，包括力学性能、颜色、紫外吸收、热稳定性和气体透过率。通过流变性能和微观形貌表征了XG与纳米ZnO的相互作用。此外，还对复合膜的抗氧化和抗菌活性进行了评价。结果表明，SFU能有效降低XG的分子量，经25 W·L−1 SFU处理后，XG的分子量（Mw）降至7.92 × 104 Da。侧链糖苷键被破坏，导致葡萄糖醛酸（GluA）含量降低31.58%。通过添加10%的纳米ZnO（相对于XG干重），复合膜的抗拉强度（TS）提高了32.43 MPa，具有优异的紫外线屏蔽性能，降低了气体透过率，提高了热稳定性。流变学和微观结构分析表明，SFU修饰的XG和ZnO纳米颗粒之间存在很强的界面键合。结果表明，复合膜对大肠杆菌的抑制率为85.90%，对金黄色葡萄球菌的抑制率为88.16%。结果表明，SFU改性XG/ZnO复合薄膜在功能性食品包装方面具有广阔的应用前景。

{"title":"Enhancement of composite film properties by sweeping-frequency ultrasound modified xanthan gum and nano ZnO: structural and functional characterization","authors":"Lei Zhang , Haiyang Zhang , Shanshan Zhou , Binglin Fu , Jilong Deng , Yan Shen , Hafida Wahia , Xiaojie Yu , Haile Ma , Cunshan Zhou","doi":"10.1016/j.foodhyd.2026.112449","DOIUrl":"10.1016/j.foodhyd.2026.112449","url":null,"abstract":"<div><div>Xanthan gum (XG) with different structures was prepared by being subjected to sweeping-frequency ultrasound (SFU) modification, and then incorporated with nano ZnO to fabricate composite films for active food packaging applications. Effects of SFU power density (0、6.25、25, 100 W⋅L<sup>−1</sup>) on the molecular weight, monosaccharide composition, and structure of XG were systematically investigated. XG/ZnO composite films were prepared using the solution casting method. Physical properties of composite films were characterized by mechanical properties, color, UV absorption, thermal stability, and gas transmission rate. The interaction between XG and nano ZnO was elucidated through rheological properties and microscopic morphology. Furthermore, the antioxidant and antibacterial activities of composite films were evaluated. Results indicated that SFU effectively reduced the molecular weight of XG, with the weight-average molecular weight (Mw) decreasing to 7.92 × 10<sup>4</sup> Da after 25 W⋅L<sup>−1</sup> SFU treatment. Side-chain glycosidic bonds were disrupted, leading to a 31.58 % reduction in glucuronic acid (GluA) content. By loading 10 % nano ZnO (relative to XG dry weight), the composite film exhibited enhanced tensile strength (TS) of 32.43 MPa, excellent UV shielding properties, reduced gas transmission rate, and improved thermal stability. Rheological and microstructure analysis revealed strong interfacial bonding between SFU modified XG and ZnO nanoparticles. Consequently, composite films exhibited significant antioxidant and antibacterial activities, inhibiting <em>E. coli</em> by 85.90 % and <em>S. aureus</em> by 88.16 %. It was demonstrated that SFU modified XG/ZnO composite films can be promising for functional food packaging.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"175 ","pages":"Article 112449"},"PeriodicalIF":11.0,"publicationDate":"2026-01-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146035994","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Mechanistic insights into the interactions between wheat gluten and egg white foams: interfacial behavior, molecular interactions, and conformational remodeling 小麦面筋和蛋清泡沫之间相互作用的机理：界面行为、分子相互作用和构象重塑

IF 11 1区农林科学 Q1 CHEMISTRY, APPLIED

Food Hydrocolloids

Pub Date : 2026-01-12 DOI: 10.1016/j.foodhyd.2026.112451

Xiaoli Liu , Ruixuan Zhang , Haobo Jin , Xuan Yao , Jiaxuan Ma , Yumeng Shan , E. Zhao , Keshan Wang , Yuanyuan Liu , Yongguo Jin

Wheat gluten (WG) and egg white foams frequently coexist in baked products, yet their interaction mechanisms remain unclear. This study investigated the effects of WG addition on the physicochemical properties, interfacial behavior and structural characteristics of egg white foam systems. Low levels of WG (0.25 %–0.5 %) remarkedly enhanced foaming capacity (FC), reaching 136.67 %. At these levels, WG formed soluble complexes with egg white proteins (EWPs) via hydrophobic interactions, reducing interfacial tension and promoting bubble formation. The shielding of gluten hydrophobic cores by hydrophilic regions of EWPs led to decreased surface hydrophobicity, increased solubility (82.3 %) and high absolute zeta potential (32.5 mV), indicating strong electrostatic repulsion and suppressed aggregation. When WG exceeded 0.5 %, intensified hydrophobic interactions induced large aggregates (347.75 nm), reduced protein adsorption at the air–water interface and thus diminished FC. However, increased viscosity and the formation of a more viscoelastic interfacial film improved foam stability (FS) (91.6 %). Circular dichroism (CD) analysis showed decreased α-helix (18.8 %) and increased β-sheet (22.1 %) and β-turn (12.3 %) contents, suggesting partial unfolding and exposure of hydrophobic groups that favored interfacial adsorption. Overall, glutenin and gliadin interacted with EWPs through hydrogen bonding and hydrophobic interactions, with low gluten levels enhancing foam formation and high levels improving FS. These findings provided a theoretical basis for optimizing formulations of wheat flour–egg white foam products.

小麦面筋和蛋清泡沫在烘焙食品中经常共存，但它们的相互作用机制尚不清楚。研究了WG的加入对蛋清泡沫体系理化性质、界面行为和结构特性的影响。低水平的WG（0.25% - 0.5%）再次显著提高了发泡能力（FC），达到136.67%。在这些水平下，WG通过疏水相互作用与蛋清蛋白（EWPs）形成可溶性复合物，降低界面张力并促进气泡形成。EWPs亲水性区域对面胶疏水性核的屏蔽导致面胶表面疏水性降低，溶解度提高（82.3%），zeta电位高（32.5 mV），显示出强烈的静电斥力和抑制聚集。当WG超过0.5%时，疏水相互作用加剧，形成大聚集体（347.75 nm），减少了空气-水界面的蛋白质吸附，从而降低了FC。然而，增加粘度和形成更粘弹性的界面膜提高了泡沫稳定性（FS）（91.6%）。圆二色性（CD）分析表明，α-螺旋（18.8%）含量降低，β-sheet（22.1%）和β-turn（12.3%）含量增加，表明疏水性基团的部分展开和暴露有利于界面吸附。总体而言，谷蛋白和麦胶蛋白通过氢键和疏水相互作用与EWPs相互作用，低谷蛋白水平促进泡沫形成，高谷蛋白水平改善FS。研究结果为优化小麦粉-蛋清泡沫产品的配方提供了理论依据。

{"title":"Mechanistic insights into the interactions between wheat gluten and egg white foams: interfacial behavior, molecular interactions, and conformational remodeling","authors":"Xiaoli Liu , Ruixuan Zhang , Haobo Jin , Xuan Yao , Jiaxuan Ma , Yumeng Shan , E. Zhao , Keshan Wang , Yuanyuan Liu , Yongguo Jin","doi":"10.1016/j.foodhyd.2026.112451","DOIUrl":"10.1016/j.foodhyd.2026.112451","url":null,"abstract":"<div><div>Wheat gluten (WG) and egg white foams frequently coexist in baked products, yet their interaction mechanisms remain unclear. This study investigated the effects of WG addition on the physicochemical properties, interfacial behavior and structural characteristics of egg white foam systems. Low levels of WG (0.25 %–0.5 %) remarkedly enhanced foaming capacity (FC), reaching 136.67 %. At these levels, WG formed soluble complexes with egg white proteins (EWPs) via hydrophobic interactions, reducing interfacial tension and promoting bubble formation. The shielding of gluten hydrophobic cores by hydrophilic regions of EWPs led to decreased surface hydrophobicity, increased solubility (82.3 %) and high absolute zeta potential (32.5 mV), indicating strong electrostatic repulsion and suppressed aggregation. When WG exceeded 0.5 %, intensified hydrophobic interactions induced large aggregates (347.75 nm), reduced protein adsorption at the air–water interface and thus diminished FC. However, increased viscosity and the formation of a more viscoelastic interfacial film improved foam stability (FS) (91.6 %). Circular dichroism (CD) analysis showed decreased α-helix (18.8 %) and increased β-sheet (22.1 %) and β-turn (12.3 %) contents, suggesting partial unfolding and exposure of hydrophobic groups that favored interfacial adsorption. Overall, glutenin and gliadin interacted with EWPs through hydrogen bonding and hydrophobic interactions, with low gluten levels enhancing foam formation and high levels improving FS. These findings provided a theoretical basis for optimizing formulations of wheat flour–egg white foam products.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"175 ","pages":"Article 112451"},"PeriodicalIF":11.0,"publicationDate":"2026-01-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146036013","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Structural modification and functional improvement of pea protein isolate by covalent grafting with EGCG induced by electron beam irradiation 电子束辐照诱导EGCG共价接枝豌豆分离蛋白的结构修饰和功能改良

IF 11 1区农林科学 Q1 CHEMISTRY, APPLIED

Food Hydrocolloids

Pub Date : 2026-01-12 DOI: 10.1016/j.foodhyd.2026.112445

Nana Yang , Huiling Li , Kui Li , Ruyu Shangguan , Wei Niu , Tian Jiang , Hongjie Lei

The objective of our study was to explore the feasibility of EGCG covalent grafting onto pea protein isolate (PPI) induced by electron beam irradiation (EBI). Subsequently, the structural and functional characteristics of the covalent conjugate (PPI-EGCG) were evaluated. The decrease in free amino group, free -SH and free tryptophan contents, as well as an increase in EGCG binding equivalent, all confirmed the successful grafting of EGCG. Multispectral analysis revealed that EGCG grafting induced PPI structural unfolding, transforming from ordered to more flexible structures with internal hydrophobic groups exposed to a more polar environment. The covalent grafting of EGCG to hydrophobic groups reduced the surface hydrophobicity of PPI. These structural changes led to improved solubility, antioxidant activity, thermal stability, and emulsifying properties, as verified by Pearson correlation analysis. Furthermore, the strong steric stabilizing effect provided by EGCG acting as cross-linking agents might account for the higher stability of emulsions prepared by PPI-EGCG during 15 d of storage. These results demonstrated that EBI was a green and efficient technique for promoting polyphenol covalent grafting onto proteins, providing an innovative procedure for enhancing the functional characteristics of PPI.

本研究旨在探讨电子束辐照（EBI）诱导EGCG共价嫁接到豌豆分离蛋白（PPI）上的可行性。随后，对共价共轭物（PPI-EGCG）的结构和功能特性进行了评价。游离氨基、游离sh和游离色氨酸含量降低，EGCG结合当量增加，证实EGCG接枝成功。多光谱分析表明，EGCG接枝诱导PPI结构展开，从有序结构转变为更灵活的结构，内部疏水性基团暴露在更极性的环境中。EGCG与疏水性基团的共价接枝降低了PPI的表面疏水性。这些结构变化导致溶解性、抗氧化活性、热稳定性和乳化性能的改善，Pearson相关分析证实了这一点。此外，EGCG作为交联剂所提供的强立体稳定作用可能是PPI-EGCG制备的乳剂在储存15 d时具有较高稳定性的原因。这些结果表明，EBI是一种绿色高效的促进多酚共价接枝到蛋白质上的技术，为提高PPI的功能特性提供了一种创新的方法。

{"title":"Structural modification and functional improvement of pea protein isolate by covalent grafting with EGCG induced by electron beam irradiation","authors":"Nana Yang , Huiling Li , Kui Li , Ruyu Shangguan , Wei Niu , Tian Jiang , Hongjie Lei","doi":"10.1016/j.foodhyd.2026.112445","DOIUrl":"10.1016/j.foodhyd.2026.112445","url":null,"abstract":"<div><div>The objective of our study was to explore the feasibility of EGCG covalent grafting onto pea protein isolate (PPI) induced by electron beam irradiation (EBI). Subsequently, the structural and functional characteristics of the covalent conjugate (PPI-EGCG) were evaluated. The decrease in free amino group, free -SH and free tryptophan contents, as well as an increase in EGCG binding equivalent, all confirmed the successful grafting of EGCG. Multispectral analysis revealed that EGCG grafting induced PPI structural unfolding, transforming from ordered to more flexible structures with internal hydrophobic groups exposed to a more polar environment. The covalent grafting of EGCG to hydrophobic groups reduced the surface hydrophobicity of PPI. These structural changes led to improved solubility, antioxidant activity, thermal stability, and emulsifying properties, as verified by Pearson correlation analysis. Furthermore, the strong steric stabilizing effect provided by EGCG acting as cross-linking agents might account for the higher stability of emulsions prepared by PPI-EGCG during 15 d of storage. These results demonstrated that EBI was a green and efficient technique for promoting polyphenol covalent grafting onto proteins, providing an innovative procedure for enhancing the functional characteristics of PPI.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"175 ","pages":"Article 112445"},"PeriodicalIF":11.0,"publicationDate":"2026-01-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145947905","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Hydrophilic anchoring by C-phycocyanin enhances pea protein nanofibril gelation c -藻蓝蛋白的亲水性锚定增强了豌豆蛋白纳米纤维的凝胶化

IF 11 1区农林科学 Q1 CHEMISTRY, APPLIED

Food Hydrocolloids

Pub Date : 2026-01-12 DOI: 10.1016/j.foodhyd.2026.112452

Chengxin He , Xuanyi Zhang , Siyi Liu , David Julian McClements , Weibiao Zhou

Pea protein amyloid fibrils are promising building blocks for creating plant-based hydrogels, but their gelation capacity is limited by high flexibility and low solubility. This study demonstrates that simple mixing of C-phycocyanin with pea protein nanofibrils drives gelation through hydrophilic anchoring. C-phycocyanin increases nanofibril hydrophilicity and restricts fibril flexibility, while hydrogen bonding and hydrophobic interactions at the nanofibril–phycocyanin interface stabilize the resulting complexes. These effects promote thermally induced network formation. Unlike nanofibrils alone, the hybrid systems form hydrogels with markedly improved water resistance and mechanical strength. This study provides a versatile approach for constructing functional nanofibril-based hydrogels with potential applications in food structuring, bioactive delivery, and biomaterials.

豌豆蛋白淀粉样原纤维是制造植物基水凝胶的有前途的基石，但它们的凝胶能力受到高柔韧性和低溶解度的限制。该研究表明，c -藻蓝蛋白与豌豆蛋白纳米原纤维的简单混合通过亲水性锚定驱动凝胶化。c -藻蓝蛋白增加了纳米纤维的亲水性，限制了纤维的柔韧性，而纳米纤维-藻蓝蛋白界面上的氢键和疏水相互作用稳定了所得到的配合物。这些效应促进了热诱导网络的形成。与单独的纳米原纤维不同，混合体系形成的水凝胶具有明显改善的耐水性和机械强度。该研究为构建功能性纳米纤维水凝胶提供了一种通用的方法，在食品结构、生物活性递送和生物材料方面具有潜在的应用前景。

引用次数: 0

Insights into citrus peel cellulose nanofiber enhanced pea protein isolate emulsion gels: Mechanical properties, microstructure, and gelation mechanism 柑橘皮纤维素纳米纤维增强豌豆分离蛋白乳液凝胶的研究：机械性能、微观结构和凝胶机制

IF 11 1区农林科学 Q1 CHEMISTRY, APPLIED

Food Hydrocolloids

Pub Date : 2026-01-12 DOI: 10.1016/j.foodhyd.2026.112450

Jieqiong Lin , Weixiang Mao , Jun Yang , Lanlan Chen , Jia Kong , Fengjuan Chen , Jianhua Xie

Pea protein isolate (PPI), known for its high nutritional quality and low allergenicity, exhibits limited applicability in emulsion gel systems due to its weak gel-forming ability. In this work, the influence of citrus peel-derived cellulose nanofibers (CNFs) on the gelling behavior and structural characteristics of PPI emulsion gels was investigated. Rheological and textural analyses indicated that the incorporation of CNFs significantly enhanced the viscoelastic properties and gel strength of PPI-CNFs emulsion gels. Lissajous curve analysis further showed that under low strain (1.0 %), all samples exhibited predominantly elastic behavior, while gels containing CNFs displayed excellent deformation resistance and shear recovery. Thermogravimetric analysis confirmed that CNFs addition enhanced the thermal stability of PPI emulsion gels. Fourier transform infrared spectroscopy revealed the formation of stronger hydrogen bonds between CNFs and PPI molecules. This interaction favored the development of a dense gel network, facilitating the conversion of free water to bound water within the system. Overall, this work offers a sustainable and green strategy to improve the functional and structural properties of legume protein emulsion gels, while promoting the high-value utilization of citrus peel.

豌豆分离蛋白（Pea protein isolate， PPI）以其高营养品质和低致敏性而闻名，但由于其弱凝胶形成能力，在乳液凝胶体系中的适用性有限。本文研究了柑橘皮衍生纤维素纳米纤维（CNFs）对PPI乳液凝胶的凝胶行为和结构特性的影响。流变学和结构分析表明，CNFs的加入显著提高了PPI-CNFs乳液凝胶的粘弹性和凝胶强度。Lissajous曲线分析进一步表明，在低应变（1.0%）下，所有样品都表现出主要的弹性行为，而含有CNFs的凝胶具有优异的抗变形和剪切恢复能力。热重分析证实，CNFs的加入增强了PPI乳液凝胶的热稳定性。傅里叶变换红外光谱显示CNFs和PPI分子之间形成了更强的氢键。这种相互作用有利于致密凝胶网络的发展，促进了系统内自由水向结合水的转化。综上所述，本研究为改善豆科蛋白乳液凝胶的功能和结构特性，促进柑橘皮的高价值利用提供了可持续和绿色的策略。

{"title":"Insights into citrus peel cellulose nanofiber enhanced pea protein isolate emulsion gels: Mechanical properties, microstructure, and gelation mechanism","authors":"Jieqiong Lin , Weixiang Mao , Jun Yang , Lanlan Chen , Jia Kong , Fengjuan Chen , Jianhua Xie","doi":"10.1016/j.foodhyd.2026.112450","DOIUrl":"10.1016/j.foodhyd.2026.112450","url":null,"abstract":"<div><div>Pea protein isolate (PPI), known for its high nutritional quality and low allergenicity, exhibits limited applicability in emulsion gel systems due to its weak gel-forming ability. In this work, the influence of citrus peel-derived cellulose nanofibers (CNFs) on the gelling behavior and structural characteristics of PPI emulsion gels was investigated. Rheological and textural analyses indicated that the incorporation of CNFs significantly enhanced the viscoelastic properties and gel strength of PPI-CNFs emulsion gels. Lissajous curve analysis further showed that under low strain (1.0 %), all samples exhibited predominantly elastic behavior, while gels containing CNFs displayed excellent deformation resistance and shear recovery. Thermogravimetric analysis confirmed that CNFs addition enhanced the thermal stability of PPI emulsion gels. Fourier transform infrared spectroscopy revealed the formation of stronger hydrogen bonds between CNFs and PPI molecules. This interaction favored the development of a dense gel network, facilitating the conversion of free water to bound water within the system. Overall, this work offers a sustainable and green strategy to improve the functional and structural properties of legume protein emulsion gels, while promoting the high-value utilization of citrus peel.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"175 ","pages":"Article 112450"},"PeriodicalIF":11.0,"publicationDate":"2026-01-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146035993","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Enhanced stability of bicontinuous bigels based on rapid in situ rapid conjugation of deacetylated chitosan and citral 脱乙酰壳聚糖与柠檬醛原位快速偶联增强双连续凝胶的稳定性

IF 11 1区农林科学 Q1 CHEMISTRY, APPLIED

Food Hydrocolloids

Pub Date : 2026-01-11 DOI: 10.1016/j.foodhyd.2026.112447

Xue Li , Kai Liu , Bolin Xu , Yang Li , Qiyi Li , Jun Zhao

In this study, we developed a bigel system by introducing covalent cross-linking between citral (CT) and chitosan, with CT serving as a natural cross-linker. hydrogel-in-oleogel (W/O), oleogel-in-hydrogel (O/W), and bicontinuous were first prepared using chitosan and beeswax (BW). CT was then added to the oil phase, initiating a rapid in-situ chemical reaction at the oil–water interface between the aldehyde group of CT and the amine group of chitosan via Schiff base covalent interactions, yielding a cross-linked bigel. This cross-linking significantly reduced droplet size and promoted a thick, dense interfacial film. Consequently, the oil-holding capacity, water-holding capacity, and gel strength of the bigels were enhanced. CT addition also enhanced the thermodynamic stability and viscoelasticity, thereby limiting lipase access and reducing triglyceride digestibility from 25.9 ± 0.98 % to 12.32 ± 0.92 %. Notably, the higher CT concentration in W/O-type bigels enhanced the extent of the Schiff base reaction, further enhancing stability. Overall, this study presents a novel approach to constructing highly stable bigel systems through Schiff base covalent interactions.

本研究以壳聚糖为天然交联剂，引入柠檬醛（CT）与壳聚糖共价交联，构建了一种新型的交联体系。首次以壳聚糖和蜂蜡为原料制备了水凝胶-油凝胶（W/O）、油凝胶-水凝胶（O/W）和双连续（BW）。然后将CT加入到油相中，通过希夫碱共价相互作用，在CT的醛基和壳聚糖的胺基之间的油水界面上引发快速的原位化学反应，生成交联bigel。这种交联显著减小了液滴尺寸，促进了厚而致密的界面膜的形成。从而提高了凝胶的持油能力、持水能力和凝胶强度。CT的加入也增强了热力学稳定性和粘弹性，从而限制了脂肪酶的进入，将甘油三酯的消化率从25.9±0.98%降低到12.32±0.92%。值得注意的是，W/ o型bigels中较高的CT浓度增强了Schiff碱反应的程度，进一步增强了稳定性。总的来说，本研究提出了一种通过希夫碱共价相互作用构建高稳定bigel体系的新方法。

{"title":"Enhanced stability of bicontinuous bigels based on rapid in situ rapid conjugation of deacetylated chitosan and citral","authors":"Xue Li , Kai Liu , Bolin Xu , Yang Li , Qiyi Li , Jun Zhao","doi":"10.1016/j.foodhyd.2026.112447","DOIUrl":"10.1016/j.foodhyd.2026.112447","url":null,"abstract":"<div><div>In this study, we developed a bigel system by introducing covalent cross-linking between citral (CT) and chitosan, with CT serving as a natural cross-linker. hydrogel-in-oleogel (W/O), oleogel-in-hydrogel (O/W), and bicontinuous were first prepared using chitosan and beeswax (BW). CT was then added to the oil phase, initiating a rapid in-situ chemical reaction at the oil–water interface between the aldehyde group of CT and the amine group of chitosan via Schiff base covalent interactions, yielding a cross-linked bigel. This cross-linking significantly reduced droplet size and promoted a thick, dense interfacial film. Consequently, the oil-holding capacity, water-holding capacity, and gel strength of the bigels were enhanced. CT addition also enhanced the thermodynamic stability and viscoelasticity, thereby limiting lipase access and reducing triglyceride digestibility from 25.9 ± 0.98 % to 12.32 ± 0.92 %. Notably, the higher CT concentration in W/O-type bigels enhanced the extent of the Schiff base reaction, further enhancing stability. Overall, this study presents a novel approach to constructing highly stable bigel systems through Schiff base covalent interactions.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"175 ","pages":"Article 112447"},"PeriodicalIF":11.0,"publicationDate":"2026-01-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145975762","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Electrosprayed hempseed protein/oilbody emulsions for encapsulation and oxidative stabilization of PUFA-rich oils 电喷大麻籽蛋白/油体乳剂用于富含pufa的油的包封和氧化稳定

IF 11 1区农林科学 Q1 CHEMISTRY, APPLIED

Food Hydrocolloids

Pub Date : 2026-01-10 DOI: 10.1016/j.foodhyd.2026.112436

Aikaterini Natsia , Aikaterini Papadaki , Anastasios C. Manikas , Maria Giovanna Pastore Carbone , Vassileios Dracopoulos , Nikolaos Kopsahelis

This study investigated the hypothesis that electrosprayed PUFA-rich oils with low peroxide value can be obtained by applying oilbodies instead of oil. Electrospraying was performed using emulsions prepared with hempseed protein isolate (HPI) and hempseed oilbodies (HOB) or hempseed oil (HO) at varying protein:lipid ratios (2:1, 3:1, 4:1, and 5:1). Emulsion characterization showed that both lipid type and protein content significantly affected their properties. HPI-HOB emulsions showed no creaming at any tested temperature (4, 25 and 37 °C) and remained stable throughout the 20-day storage period. In contrast, HPI-HO emulsions exhibited phase separation, reaching the highest creaming index of 11.0 % at 2:1 protein:lipid ratio and 37 °C. Encapsulation efficiency (EE) was influenced by lipid type and protein:lipid ratio, reaching a maximum of 84.2 % for HPI-HOB and 68.8 % for HPI-HO particles at a 5:1 protein:lipid ratio. Scanning electron microscopy (SEM) indicated similar morphologies for HPI-HO and HPI-HOB electrosprayed particles. Atomic Force Microscopy (AFM) and RAMAN mapping confirmed that both HO and HOB were homogeneously distributed within the electrosprayed structures, supporting process reproducibility and stability. HPI-HOB particles exhibited almost 70 % lower peroxide value than HPI-HO, at a 5:1 protein:lipid ratio, highlighting that the use of HOB contributed to superior oxidative stability during electrospraying. Pearson's correlation analysis revealed strong negative correlations between peroxide value of HPI-HOB and the EE and protein ratio. Overall, combining HOB with high protein levels enhanced both EE and oxidative stability, providing a novel approach for the effective encapsulation and stabilization of PUFA-rich oils through emulsion electrospraying.

本研究探讨了用油体代替油可以得到低过氧化值富pufa电喷涂油的假设。用不同蛋白脂比（2:1,3:1,4:1和5:1）的大麻籽分离蛋白（HPI）和大麻籽油体（HOB）或大麻籽油（HO）制备的乳剂进行电喷涂。乳液表征表明，脂质类型和蛋白质含量对其性能有显著影响。HPI-HOB乳剂在任何测试温度（4、25和37°C）下均未发生乳化，并在20天的储存期内保持稳定。相比之下，HPI-HO乳剂表现出相分离，在2:1的蛋白脂比和37°C条件下，成乳指数最高，为11.0%。脂质类型和蛋白脂比均影响包封效率，在蛋白脂比为5:1时，HPI-HOB和HPI-HO颗粒的包封效率分别达到84.2%和68.8%。扫描电镜（SEM）显示HPI-HO和HPI-HOB电喷涂颗粒形貌相似。原子力显微镜（AFM）和拉曼图谱证实，HO和HOB在电喷涂结构中均匀分布，支持工艺的再现性和稳定性。在5:1的蛋白脂比下，HPI-HOB颗粒的过氧化值比HPI-HO低近70%，这表明在电喷涂过程中，使用HOB有助于提高氧化稳定性。Pearson相关分析显示HPI-HOB过氧化值与EE和蛋白比呈显著负相关。综上所述，将HOB与高蛋白水平相结合，提高了EE和氧化稳定性，为乳液电喷涂富含pufa的油的有效封装和稳定提供了一种新的方法。

{"title":"Electrosprayed hempseed protein/oilbody emulsions for encapsulation and oxidative stabilization of PUFA-rich oils","authors":"Aikaterini Natsia , Aikaterini Papadaki , Anastasios C. Manikas , Maria Giovanna Pastore Carbone , Vassileios Dracopoulos , Nikolaos Kopsahelis","doi":"10.1016/j.foodhyd.2026.112436","DOIUrl":"10.1016/j.foodhyd.2026.112436","url":null,"abstract":"<div><div>This study investigated the hypothesis that electrosprayed PUFA-rich oils with low peroxide value can be obtained by applying oilbodies instead of oil. Electrospraying was performed using emulsions prepared with hempseed protein isolate (HPI) and hempseed oilbodies (HOB) or hempseed oil (HO) at varying protein:lipid ratios (2:1, 3:1, 4:1, and 5:1). Emulsion characterization showed that both lipid type and protein content significantly affected their properties. HPI-HOB emulsions showed no creaming at any tested temperature (4, 25 and 37 °C) and remained stable throughout the 20-day storage period. In contrast, HPI-HO emulsions exhibited phase separation, reaching the highest creaming index of 11.0 % at 2:1 protein:lipid ratio and 37 °C. Encapsulation efficiency (EE) was influenced by lipid type and protein:lipid ratio, reaching a maximum of 84.2 % for HPI-HOB and 68.8 % for HPI-HO particles at a 5:1 protein:lipid ratio. Scanning electron microscopy (SEM) indicated similar morphologies for HPI-HO and HPI-HOB electrosprayed particles. Atomic Force Microscopy (AFM) and RAMAN mapping confirmed that both HO and HOB were homogeneously distributed within the electrosprayed structures, supporting process reproducibility and stability. HPI-HOB particles exhibited almost 70 % lower peroxide value than HPI-HO, at a 5:1 protein:lipid ratio, highlighting that the use of HOB contributed to superior oxidative stability during electrospraying. Pearson's correlation analysis revealed strong negative correlations between peroxide value of HPI-HOB and the EE and protein ratio. Overall, combining HOB with high protein levels enhanced both EE and oxidative stability, providing a novel approach for the effective encapsulation and stabilization of PUFA-rich oils through emulsion electrospraying.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"175 ","pages":"Article 112436"},"PeriodicalIF":11.0,"publicationDate":"2026-01-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145975756","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Molecular dynamics elucidation of the synergistic regulation of thermal kinetics and sodium caseinate on the crystalline and interfacial architecture of solid lipid particles 热动力学和酪蛋白酸钠对固体脂质颗粒晶体和界面结构协同调节的分子动力学研究

IF 11 1区农林科学 Q1 CHEMISTRY, APPLIED

Food Hydrocolloids

Pub Date : 2026-01-10 DOI: 10.1016/j.foodhyd.2026.112442

Yongbo Gou , Mengli Li , Jiayan Xu , Yuan Cheng , Xingyu Guan , Yongchun Huang , Xiangyi Tang

Solid lipid particles (SLPs) are widely used in food emulsification and drug delivery owing to their biocompatibility and controllable release properties. However, the crystallization and interfacial behaviors of emulsifier-modified high-melting lipids remain poorly understood. This study combined experiments and molecular dynamics simulations to examine sodium caseinate (Na-Cas) effects on sugarcane wax SLPs. At 2.0–2.5 wt%, Na-Cas formed a dense surface layer that reduced interfacial tension and improved dispersion through electrostatic and steric stabilization. Differential scanning calorimetry and X-ray diffraction showed that Na-Cas disrupted crystal packing, inhibited grain growth, and lowered crystallization enthalpy, producing uniform microcrystals. Simulations revealed a three-step crystallization process—chain extension, nucleation, and growth—with cooling rate governing defect density and crystal size. Hydrophobic interactions and hydrogen bonding stabilized crystal surfaces. These results clarify the crystallization mechanism of high-melting lipids and support the design of functional SLPs.

固体脂质颗粒具有良好的生物相容性和可控性，在食品乳化和药物输送中得到了广泛的应用。然而，乳化剂改性高熔点脂的结晶和界面行为仍然知之甚少。本研究结合实验和分子动力学模拟研究了酪蛋白酸钠（Na-Cas）对甘蔗蜡SLPs的影响。在2.0-2.5 wt%时，Na-Cas形成了致密的表面层，通过静电和空间稳定降低了界面张力，改善了分散。差示扫描量热法和x射线衍射结果表明，Na-Cas破坏了晶体堆积，抑制了晶粒生长，降低了晶化焓，形成了均匀的微晶。模拟结果显示了一个三步结晶过程：链延伸、成核和生长，而冷却速度决定了缺陷密度和晶体尺寸。疏水相互作用和氢键稳定晶体表面。这些结果阐明了高熔点脂类的结晶机理，为功能性slp的设计提供了依据。

{"title":"Molecular dynamics elucidation of the synergistic regulation of thermal kinetics and sodium caseinate on the crystalline and interfacial architecture of solid lipid particles","authors":"Yongbo Gou , Mengli Li , Jiayan Xu , Yuan Cheng , Xingyu Guan , Yongchun Huang , Xiangyi Tang","doi":"10.1016/j.foodhyd.2026.112442","DOIUrl":"10.1016/j.foodhyd.2026.112442","url":null,"abstract":"<div><div>Solid lipid particles (SLPs) are widely used in food emulsification and drug delivery owing to their biocompatibility and controllable release properties. However, the crystallization and interfacial behaviors of emulsifier-modified high-melting lipids remain poorly understood. This study combined experiments and molecular dynamics simulations to examine sodium caseinate (Na-Cas) effects on sugarcane wax SLPs. At 2.0–2.5 wt<em>%</em>, Na-Cas formed a dense surface layer that reduced interfacial tension and improved dispersion through electrostatic and steric stabilization. Differential scanning calorimetry and X-ray diffraction showed that Na-Cas disrupted crystal packing, inhibited grain growth, and lowered crystallization enthalpy, producing uniform microcrystals. Simulations revealed a three-step crystallization process—chain extension, nucleation, and growth—with cooling rate governing defect density and crystal size. Hydrophobic interactions and hydrogen bonding stabilized crystal surfaces. These results clarify the crystallization mechanism of high-melting lipids and support the design of functional SLPs.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"175 ","pages":"Article 112442"},"PeriodicalIF":11.0,"publicationDate":"2026-01-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145975757","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0