Food Hydrocolloids最新文献_第9页

Thermal aggregation and gelation of native mung bean protein in a salt dispersion 天然绿豆蛋白在盐分散中的热聚集和凝胶

IF 11 1区农林科学

Food Hydrocolloids Pub Date : 2026-06-01 Epub Date: 2026-01-23 DOI: 10.1016/j.foodhyd.2026.112465

Quinten Masijn, Arne Riobello-Olalla, Sam De Brabander, Yadong Li, Ilse Fraeye

{"title":"Thermal aggregation and gelation of native mung bean protein in a salt dispersion","authors":"Quinten Masijn, Arne Riobello-Olalla, Sam De Brabander, Yadong Li, Ilse Fraeye","doi":"10.1016/j.foodhyd.2026.112465","DOIUrl":"10.1016/j.foodhyd.2026.112465","url":null,"abstract":"<div><div>Mung bean protein (MBP) is a promising protein source, yet its thermal gelation at conditions found in food systems is still ill understood. Therefore, this work examined the impact of isothermal heating temperature (50 °C, 70 °C, 90 °C and 100 °C) on aggregation and gelation of lab-extracted mung bean protein extract in a phosphate buffered saline dispersion with pH 6.8 and 250 mM NaCl (PBS).</div><div>MBP, non-selectively isolated from mung bean flour by ethanol-isoelectric precipitation, showed high protein nativity (12.7 J/g) and nitrogen solubility (86 %). Aggregation of 0.50 wt% MBP in PBS increased with higher temperatures of isothermal heat treatment, irrespective of protein unfolding. This was confirmed by increasing particle size, increasing turbidity and decreasing nitrogen solubility index, with the last 2 observations also at temperatures below peak denaturation temperature, possibly due to aggregation of the 91 kDa fraction as revealed by SDS-PAGE analysis. Gelation of 17.5 wt% MBP in PBS appeared to rely primarily on hydrophobic interactions, as only 8 M urea increased solubilization of protein molecular weight fractions in gels heat-treated at 90 °C and 100 °C. The resulting MBP gels showed strong gelation properties at high temperatures, as the least gelation concentration decreased from 12 % at 50 °C to 7 % at 90 °C, water holding capacity increased from 65 % at 50 °C to 97 % at 90 °C and fracture stress and strain increased between 90 and 100 °C. These findings underscore MBP's promising potential in heat-treated food gels.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"175 ","pages":"Article 112465"},"PeriodicalIF":11.0,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146074506","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

Modulating the properties of tuna skin collagen-based emulsion gels by moderate hydrolysis: Physical characteristics, stability, and lycopene delivery 通过适度水解调节金枪鱼皮胶原蛋白乳液凝胶的特性：物理特性、稳定性和番茄红素的输送

IF 11 1区农林科学

Food Hydrocolloids Pub Date : 2026-06-01 Epub Date: 2026-01-26 DOI: 10.1016/j.foodhyd.2026.112504

Yugang Liu , Ranran Wang , Yapeng Lu , Haotian Zhang , Yunke Yang , Xin Feng , Kangting Sun , Liang Ma , Yuhao Zhang

{"title":"Modulating the properties of tuna skin collagen-based emulsion gels by moderate hydrolysis: Physical characteristics, stability, and lycopene delivery","authors":"Yugang Liu , Ranran Wang , Yapeng Lu , Haotian Zhang , Yunke Yang , Xin Feng , Kangting Sun , Liang Ma , Yuhao Zhang","doi":"10.1016/j.foodhyd.2026.112504","DOIUrl":"10.1016/j.foodhyd.2026.112504","url":null,"abstract":"<div><div>This study investigated the effects of hydrolysis duration (0–40 min) on the stability of tuna skin collagen (TSC) based emulsion gels (EGs) and the release of encapsulated lycopene (LP). TSC was prepared with a colloid mill, followed by hydrolysis using papain. The EGs were formulated using TSC as the stabilizer and sunflower oil (φ = 75 wt%, with 0.1 wt% LP) as the oil phase. All EGs were O/W type and induced gel formation at 4 °C. Longer hydrolysis duration led to an increase in droplet size and a reduction in ζ-potential of EGs. The EG stabilized by TSC hydrolyzed for 40 min (EG40) exhibited aqueous phase separation after 3 days at 25 °C and the highest oil loss, indicating a relatively poor storage and centrifugal stability. All EGs exhibited solid-like rheological behavior (G′ > G″), but their viscoelasticity decreased with increasing TSC hydrolysis duration. Interfacial dilatational rheology and quartz crystal microbalance with dissipation monitoring (QCM-D) results revealed that EG0 was stabilized by a gel network structure in continuous phase, whereas EG10-EG30 were co-stabilized by viscoelastic interfacial membranes and residual gel networks. Excessive hydrolysis resulted in the formation of weak interfacial layers and a loose gel network, consequently causing the instability of EG40. During the simulated gastrointestinal tract (GIT) digestion, the hydrolyzed TSC-based EGs enhanced oil digestion and LP release. The LP bioaccessibility exceeded 6 % after 60 min in the small intestinal phase for EG20, but it took only 30 min for EG30 and EG40. These findings provide a promising strategy for upcycling marine by-products and offer design principles for encapsulation delivery systems of lipophilic bioactive substances.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"175 ","pages":"Article 112504"},"PeriodicalIF":11.0,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146074560","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

Effect of glycosylated gliadin on the structural and functional properties of highland barley starch gel 糖基化麦胶蛋白对青稞淀粉凝胶结构和功能特性的影响

IF 11 1区农林科学

Food Hydrocolloids Pub Date : 2026-06-01 Epub Date: 2026-01-21 DOI: 10.1016/j.foodhyd.2026.112486

Liping Zhao , Pingcuo Danzeng , Deji Ciren , Wenhao Li

{"title":"Effect of glycosylated gliadin on the structural and functional properties of highland barley starch gel","authors":"Liping Zhao , Pingcuo Danzeng , Deji Ciren , Wenhao Li","doi":"10.1016/j.foodhyd.2026.112486","DOIUrl":"10.1016/j.foodhyd.2026.112486","url":null,"abstract":"<div><div>To improve the processing attributes of highland barley starch in the food, pharmaceutical, and other sectors, this study utilized the Maillard reaction to covalently graft highland barley gliadin (HBG) with galactose and maltose, resulting in the formation of galactose-gliadin complex (BH) and maltose-gliadin complex (MH). Subsequently, highland barley starch was blended with various types of gliadins in different ratios to explore the impact of glycosylated gliadin on the structural and functional properties of highland barley starch hydrogels. The findings revealed that incorporating gliadin decreased the viscosity, elevated the gelatinization temperature, and modified the rheological and thermal characteristics of the gel. Compared to the addition of HBG, glycosylated gliadin reduces the light transmittance, hydrogen bonding, and hydrophobic interactions of the composite gel system, while increasing the chroma value, ionic bond content, and the proportions of A<sub>21</sub> and A<sub>22</sub>. These changes are associated with the degree of glycoprotein browning, the introduction of hydroxyl groups on side chains, and increased steric hindrance. In summary, incorporating BH or MH into the starch system helps inhibit the short-term retrogradation (0–1 day) of starch molecules, with limited efficacy against long-term retrogradation. At a starch-to-glycosylated gliadin ratio of 100:3, BH or MH effectively suppresses short-term retrogradation; at a ratio of 100:9, the gliadin undergoes crosslinking and aggregation, leading to a more ordered, dense gel network, particularly with MH. This research lays the groundwork for an innovative theoretical approach to using glycosylated proteins to mitigate the aging of starch gels.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"175 ","pages":"Article 112486"},"PeriodicalIF":11.0,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146184834","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

Engineering anisotropic hydrogels via directional freezing and salting-out for plant-based meat analogues 工程各向异性水凝胶通过定向冷冻和盐化为植物性肉类类似物

IF 11 1区农林科学

Food Hydrocolloids Pub Date : 2026-06-01 Epub Date: 2026-02-02 DOI: 10.1016/j.foodhyd.2026.112525

Zhongyu Yang , Keying Song , Zhili Wan, Jian Guo, Xiaoquan Yang

{"title":"Engineering anisotropic hydrogels via directional freezing and salting-out for plant-based meat analogues","authors":"Zhongyu Yang , Keying Song , Zhili Wan, Jian Guo, Xiaoquan Yang","doi":"10.1016/j.foodhyd.2026.112525","DOIUrl":"10.1016/j.foodhyd.2026.112525","url":null,"abstract":"<div><div>Driven by environmental, ethical, and health considerations, consumer demand for plant-based meat analogues is rapidly increasing. However, their large-scale commercialization is limited by the difficulty in replicating meat's fibrous, anisotropic protein structures, which are key to its mechanical properties and inherently challenging to reproduce with plant proteins. This study fabricated soy protein isolate (SPI)/konjac glucomannan (KGM) hydrogels <em>via</em> directional freezing and salting-out, which resulted in an anisotropic microstructure and excellent mechanical properties. The temperature-gradient-driven unidirectional growth of ice crystals induced phase separation within the biopolymers, resulting in the formation of aligned fibrous structures that mimic the texture of muscle tissue. Salting-out treatment significantly enhanced the mechanical strength of the hydrogels by reinforcing intermolecular hydrophobic interactions, with higher salt concentrations resulting in increased stress (up to 1.29 MPa) and hardness (89.39 N). Plant-based meat analogues exhibited friction coefficients and water-holding capacities comparable to those of real meat. This work established a generalizable strategy for understanding ion-specific modulation in natural polymers and guiding the fabrication of plant meat analogues.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"175 ","pages":"Article 112525"},"PeriodicalIF":11.0,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146184840","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

Thermal effects of sonication promote non-covalent amorphous aggregation of in-situ Pinto bean protein 超声热效应促进原位平托豆蛋白的非共价无定形聚集

IF 11 1区农林科学

Food Hydrocolloids Pub Date : 2026-06-01 Epub Date: 2026-01-29 DOI: 10.1016/j.foodhyd.2026.112514

Gaurav Kumar , Kajal Sharma , Lavaraj Devkota , Sushil Dhital

{"title":"Thermal effects of sonication promote non-covalent amorphous aggregation of in-situ Pinto bean protein","authors":"Gaurav Kumar , Kajal Sharma , Lavaraj Devkota , Sushil Dhital","doi":"10.1016/j.foodhyd.2026.112514","DOIUrl":"10.1016/j.foodhyd.2026.112514","url":null,"abstract":"<div><div>Hydration is a critical pre-processing step in bean processing, as it softens the seeds for consumption and reduces anti-nutritional factors. Conventional thermal hydration is energy-intensive and has a high carbon footprint. Ultrasound-assisted hydration has been proposed as a greener alternative, yet its effects on in-situ proteins remain unclear, particularly given the complex interplay of thermal and physical sonication effects. To address this, we compared four different hydration strategies for pinto beans: isothermal hydration at 25 °C, ultrasound-assisted hydration with and without temperature control, and high-temperature thermal hydration. Isolated proteins were characterised by chromatography, electrophoresis, calorimetry, and infrared spectroscopy, and their functional properties were evaluated using rheology and texture analysis. Isothermal hydration produced the highest protein purity and the strongest gels. Temperature-controlled ultrasound resulted in weaker gels despite similar molecular features, likely due to co-extracted matrix components inhibiting protein–protein crosslinking. Ultrasound without temperature control and high-temperature hydration generated proteins with higher solubility and firmer textures but dominated by large non-covalent aggregates that acted as inert fillers. The contrasting outcomes of the two ultrasound treatments underscore the importance of thermal management and the need for mechanistic understanding under realistic processing conditions to support industrial applications.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"175 ","pages":"Article 112514"},"PeriodicalIF":11.0,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146184875","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

Volatility-tuned encapsulation in V-type starch: Phase-dependent efficiency and release kinetics v型淀粉挥发性调节包封：相依赖效率和释放动力学

IF 11 1区农林科学

Food Hydrocolloids Pub Date : 2026-06-01 Epub Date: 2026-02-09 DOI: 10.1016/j.foodhyd.2026.112540

Kunheng Lai , Peiying He , Paul Van der Meeren , Bin Zhang , Xiong Fu , Qing Gao , Qiang Huang

{"title":"Volatility-tuned encapsulation in V-type starch: Phase-dependent efficiency and release kinetics","authors":"Kunheng Lai , Peiying He , Paul Van der Meeren , Bin Zhang , Xiong Fu , Qing Gao , Qiang Huang","doi":"10.1016/j.foodhyd.2026.112540","DOIUrl":"10.1016/j.foodhyd.2026.112540","url":null,"abstract":"<div><div>Whereas aroma volatility critically governs encapsulation efficiency in starch-based delivery systems, yet phase-dependent mechanisms remain unclear. This study systematically investigated the impact of aroma volatility on the encapsulation behavior of V-type starch across aqueous, ethanol, and solid phases. The high-volatility compounds (menthone: vapor pressure = 36 Pa at 25 °C) achieved superior loading in aqueous/solid phases (up to 45.0 mg/g) via high-temperature/pressure-enhanced molecular mobility, whereas low-volatility geraniol (vapor pressure = 4 Pa at 25 °C) excelled in ethanol phase (76.0 mg/g) through prolonged equilibrium. The aroma release rate was in the order of ethanol < solid < aqueous phase across different phases, and was ranked as geraniol < linalool ≈ (−)-carvone < menthone among different volatile aromas. Ethanol/solid phases developed stronger V-type crystallinity (up to 25.53%), delaying the aroma release (Avrami <em>k</em> = 0.06–1.29 vs. 0.18–2.43 in physical mixtures), particularly for low-volatility compounds. These findings provided new insights into solvent selection for efficiently encapsulating volatile compounds in starch-based food and pharmaceutical applications.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"175 ","pages":"Article 112540"},"PeriodicalIF":11.0,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146184629","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

Ultrafiltration-driven refinement of soluble pea protein fractions reduces antinutritional load and increases protein content 超滤驱动的可溶性豌豆蛋白馏分的细化减少了抗营养负荷，增加了蛋白质含量

IF 11 1区农林科学

Food Hydrocolloids Pub Date : 2026-06-01 Epub Date: 2026-02-07 DOI: 10.1016/j.foodhyd.2026.112536

Galo Chuchuca Moran, Camila Delgado Valverde, Sophie MacRae, Lutz Grossmann

{"title":"Ultrafiltration-driven refinement of soluble pea protein fractions reduces antinutritional load and increases protein content","authors":"Galo Chuchuca Moran, Camila Delgado Valverde, Sophie MacRae, Lutz Grossmann","doi":"10.1016/j.foodhyd.2026.112536","DOIUrl":"10.1016/j.foodhyd.2026.112536","url":null,"abstract":"<div><div>The albumin-rich soluble pea protein sidestream, generated during isoelectric precipitation of pea protein ingredients, remains underutilized due to its low protein concentration, high levels of carbohydrates and minerals, and the presence of antinutritional compounds like trypsin inhibitors and phytic acid. This study examined the impact of various molecular weight cut-offs (0.6–0.8 to 30 kDa) in a cross-flow ultrafiltration combined with a diafiltration process to refine the soluble pea fraction into a soluble pea protein concentrate. A refined product containing approximately 70% protein (N <span><math><mrow><mo>×</mo></mrow></math></span> 5.36) (∼80% for N<span><math><mrow><mo>×</mo></mrow></math></span> 6.25) was achieved with membrane cut-offs between 1 and 30 kDa, with over 95% of total minerals, sugars, and raffinose family oligosaccharides effectively removed using these membranes. The 30 kDa cut-off membrane was the most effective in removing antinutritional factors, reducing phytic acid to 2.6 mg/g protein and trypsin inhibitor activity to 5.9 TIU/mg protein, achieving over 80% removal from the initial levels. Overall, a 30 kDa membrane cut-off offered the best balance of protein content, yield, and antinutritional factor removal, allowing the soluble protein sidestream to be refined into a high-protein ingredient with compositional properties comparable to the primary concentrate. This improves process efficiency and supports a more circular and sustainable plant protein production system.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"175 ","pages":"Article 112536"},"PeriodicalIF":11.0,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146184633","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

TGase-induced WPI-GA microgels for stabilized HIPEs and encapsulation probiotics with enhanced thermal stability and gastrointestinal survival tgase诱导的WPI-GA微凝胶用于稳定HIPEs和包封益生菌，增强热稳定性和胃肠道存活率

IF 11 1区农林科学

Food Hydrocolloids Pub Date : 2026-06-01 Epub Date: 2026-01-02 DOI: 10.1016/j.foodhyd.2025.112415

Yaxin Yin , Yingnan Zou , Chin Ping Tan , Deyang Li , Xiaojiao Zheng , Daodong Pan , Maolin Tu

{"title":"TGase-induced WPI-GA microgels for stabilized HIPEs and encapsulation probiotics with enhanced thermal stability and gastrointestinal survival","authors":"Yaxin Yin , Yingnan Zou , Chin Ping Tan , Deyang Li , Xiaojiao Zheng , Daodong Pan , Maolin Tu","doi":"10.1016/j.foodhyd.2025.112415","DOIUrl":"10.1016/j.foodhyd.2025.112415","url":null,"abstract":"<div><div>Probiotics demonstrate significant efficacy in regulating gut microbiota and enhancing immune function. However, their sensitivity severely limited their application. This study employed transglutaminase (TGase) to enzymatically cross-link whey protein isolate (WPI) and Gum Arabic (GA), and prepared microgel particles. These were utilized as stabilizers in high internal phase emulsions (HIPEs) to encapsulate <em>Lactobacillus reuteri</em> DSM 17938 (<em>L. reuteri</em>). SDS-PAGE analyses confirmed that TGase-induced polymerization, showing the corresponding formation of high-molecular-weight polymers. This covalent cross-linking inherently altered the microgel structure, leading to significant functional modifications. Particle size and rheological results indicated that HIPEs exhibited excellent viscoelasticity and stability. By investigating the effects of WPI-GA concentration and oil volume fraction, it was found that <em>L. reuteri</em> encapsulated in HIPEs demonstrated outstanding thermal stability and resistance to simulated gastrointestinal digestion. After simulated gastric digestion, the viability of probiotics decreased from 7.6 to 3.0 Lg CFU/mL. The probiotics in the 4% microgel-stabilized HIPEs maintained a higher count of 5.1 Lg CFU/mL. These results show that protein-polysaccharide microgel-stabilized HIPEs can protect probiotics more effectively. The findings also provide useful guidance for developing stable probiotic delivery systems.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"175 ","pages":"Article 112415"},"PeriodicalIF":11.0,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145975755","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

Food Hydrocolloids Pub Date : 2026-06-01 Epub Date: 2026-01-12 DOI: 10.1016/j.foodhyd.2026.112452

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

引用次数: 0

Effect of protein pH on acid-thermal induced fibrillation of soy protein: structural characteristics and application in high internal phase emulsions 蛋白质pH值对大豆蛋白酸热致纤维性颤动的影响：结构特征及其在高内相乳剂中的应用

IF 11 1区农林科学

Food Hydrocolloids Pub Date : 2026-06-01 Epub Date: 2026-01-05 DOI: 10.1016/j.foodhyd.2026.112424

Xiaohan Hua , Wenjia Yan , Huilin Luan , Xin Jia , Lijun Yin

{"title":"Effect of protein pH on acid-thermal induced fibrillation of soy protein: structural characteristics and application in high internal phase emulsions","authors":"Xiaohan Hua , Wenjia Yan , Huilin Luan , Xin Jia , Lijun Yin","doi":"10.1016/j.foodhyd.2026.112424","DOIUrl":"10.1016/j.foodhyd.2026.112424","url":null,"abstract":"<div><div>Soy protein isolate (SPI) can self-assemble into amyloid-like fibrils with highly ordered β-sheet structures that enhance interfacial and emulsifying properties. However, the influence of protein processing-induced structural variations on fibrillation and interfacial behavior remains unclear. In this study, three SPI samples (SPI2, SPI6, and SPI10) were obtained by neutralizing protein dispersions to different pH values (2, 6, and 10), resulting in distinct molecular conformations. The corresponding soy protein amyloid fibrils (SAF2, SAF6, and SAF10) were prepared by controlled hydrolysis at pH 2 and 85 °C. Structural characterization revealed that SPI2 contained smaller peptides that facilitated β-sheet formation, while SPI10 exhibited extensive unfolding and a slower fibrillation rate. Atomic force microscopy (AFM) observations confirmed morphological differences among SAFs, with SAF2 comprising a mixture of rigid and flexible fibrils, whereas SAF10 primarily formed flexible fibrils prone to aggregation. Interfacial measurements demonstrated that SAF10 adsorbed more rapidly at the oil-water interface, yielding high internal phase emulsions (HIPEs) with the highest interfacial protein content (29.6 %) and a thicker, more elastic interfacial layer. Compared with SPI, SAF-stabilized HIPEs showed smaller droplet sizes and superior storage stability (pH 3–8), while maintaining a gel-like structure even after heating at 90 °C. Remarkably, SAF10-stabilized HIPEs exhibited good freeze-thaw reversibility. These results clarify how protein processing-induced structural variations govern amyloid fibril morphology and interfacial functionality, providing new insights for designing fibrous protein stabilizers to construct stable and functional HIPEs for food applications.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"175 ","pages":"Article 112424"},"PeriodicalIF":11.0,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145975761","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