Food Hydrocolloids最新文献

{"title":"Amyloid-like fibrils accelerate pre-cooked gluten depolymerization during freeze-thaw cycles","authors":"Ying Liang ,&nbsp;Penghui Zhang ,&nbsp;Liu Yang ,&nbsp;Hao Liu ,&nbsp;Mei Liu ,&nbsp;Baoshan He ,&nbsp;Jinshui Wang","doi":"10.1016/j.foodhyd.2025.112020","DOIUrl":"10.1016/j.foodhyd.2025.112020","url":null,"abstract":"<div><div>This study investigated the impact of amyloid-like fibrils (AFs), derived from thermally processed wheat gluten, on pre-cooked wheat gluten (PCWG) during freeze–thaw (FT) cycles. A systematic analysis was conducted encompassing rheological properties, molecular weight distribution, conformational structure, molecular chain size, and conformation. Key findings demonstrated that the incorporation of AFs exacerbated the reduction in elasticity and viscosity of PCWG under FT treatment. Notably, the tan δ of PCWG containing 1.0 % AFs increased to 1.552 at 1 Hz, indicating an AFs-induced phase transition from a solid-like to a fluid-like state. In addition, AFs competitively establish irreversible covalent cross-links with both glutenin and gliadin subunits, thereby intensifying FT-induced depolymerization of PCWG. Structural analyses revealed that the introduction of 1.0 % AFs reduced the proportions of α-helix and gauche–gauche–gauche disulfide bonds in PCWG after FT treatment to 12.75 % and 22.41 %, respectively. These results indicate that AFs disrupt the hydrogen bonding network and destabilize the stability of disulfide bonds in PCWG. Moreover, the presence of AFs further exacerbated the FT-induced contraction of molecular-chain dimensions; after 10 FT cycles, the radius of gyration of PCWG with 1.0 % AFs decreased to 0.184 nm. Collectively, these findings clarify the mechanism by which AFs exacerbate PCWG depolymerization during FT cycles and offer a theoretical foundation for optimizing the quality of frozen cooked flour-based food systems.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"172 ","pages":"Article 112020"},"PeriodicalIF":11.0,"publicationDate":"2025-09-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145154745","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}

{"title":"The effects of additives on the frozen storage quality of rice noodles: Guar gum, hydroxypropyl corn starch, composite phosphate, and their composite mixture","authors":"Wenhao Xiao ,&nbsp;Ji Ma ,&nbsp;Danyu Lv ,&nbsp;Yuhuan Geng ,&nbsp;Wenhong Gao ,&nbsp;Xin-An Zeng ,&nbsp;Zhong Han","doi":"10.1016/j.foodhyd.2025.112024","DOIUrl":"10.1016/j.foodhyd.2025.112024","url":null,"abstract":"<div><div>This study aimed to investigate the effects of guar gum (GG), hydroxypropyl corn starch (HCS), composite phosphate (CP), and their composite additive (GHC) on the overall quality of rice noodles (RN) during frozen storage. After 28 days, the control RN showed marked quality deterioration, with the breakage rate increasing from 24.1 % to 38.5 % and hardness decreasing from 5307.4 g to 3684.8 g. In contrast, samples with single additives exhibited moderate improvements: the breakage rate were 25.0 % for RN-GG, 32.6 % for RN-HCS, and 28.7 % for RN-CP, while hardness values reached 4530.8 g, 4229.9 g, and 4481.5 g, respectively. Notably, the GHC demonstrated superior performance, maintaining the breakage rate at 21.1 % and hardness at 4912.8 g. Low-field NMR analysis revealed a significantly higher A₂₁ value in RN-GHC compared to the single-additive RN, indicating enhanced water-holding capacity of the gel structure. SEM observations showed a more continuous and compact gel network of RN-GHC, which helped inhibit ice crystal growth and physical damage. XRD and Raman spectroscopy confirmed that the additives effectively suppressed starch retrogradation. After the storage period, the resistant starch content in RN-GHC was 22.12 % higher than that in control RN. This is attributed to GHC maintaining a more continuous and dense gel network, whose intact structure physically restricts enzyme permeation and binding, thereby increasing the resistant starch fraction. These findings highlight the potential of composite additives for enhancing the quality and extending the shelf life of frozen starch-based foods.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"172 ","pages":"Article 112024"},"PeriodicalIF":11.0,"publicationDate":"2025-09-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145155208","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}

{"title":"Synergistic modification of sunflower seed protein by pH-cycling and ultrasound to improve its structural and functional properties","authors":"Zhenyuan Li ,&nbsp;Xuegang Huang ,&nbsp;Jiaxin Guo ,&nbsp;Yumeng Hu ,&nbsp;Karim Gafurov ,&nbsp;Jinchuang Zhang ,&nbsp;Qiang Wang ,&nbsp;Qin Guo","doi":"10.1016/j.foodhyd.2025.112017","DOIUrl":"10.1016/j.foodhyd.2025.112017","url":null,"abstract":"<div><div>Sunflower seed protein (SPI) is a high-quality plant-based protein with balanced nutrition, low allergenicity, and excellent sustainability. However, its limited solubility hinders the full expression of its functional properties, thereby restricting its broader application in food processing. To address this issue, SPI was modified via a synergistic treatment combining pH-cycling and ultrasound in this study, and its modification mechanism and functional properties were comprehensively evaluated. The results indicate that the combined treatment induced protein structural aggregation-disaggregation-rearrangement, significantly enhancing SPI solubility to 81.27 %, representing a 58.14 % increase compared to unmodified protein. During modification, pH-cycling treatment converted SPI molecules into a molten globule state, while ultrasonic cavitation and shear forces effectively disrupted protein aggregates. This led to increased exposure of chromophores on side chains, enhanced fluorescence intensity, reduced particle size to 81.08 nm, and increased ζ-potential (−38.77 mV), thereby improving system stability. The modified SPI exhibited a higher enthalpy change (ΔH = 3.58 J/g), along with markedly improved functional characteristics: foaming capacity and foam stability increased by 2.29 times and 2.69 times, respectively; emulsifying activity and stability reached 6.23 m²/g and 88.72 %; and oil-holding capacity was enhanced to 5.52 g/g, representing 2.73 times increase. Overall, the synergistic pH-cycling and ultrasound modification proved highly effective in improving the solubility and functional performance of sunflower seed protein, offering promising potential for its application in advanced food systems.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"172 ","pages":"Article 112017"},"PeriodicalIF":11.0,"publicationDate":"2025-09-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145216299","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}

{"title":"Probing multiscale structure of plant protein-based food system: Application of small-angle X-ray and neutron scattering (SAXS/SANS)","authors":"Zhi Yang ,&nbsp;Lirong Cheng","doi":"10.1016/j.foodhyd.2025.112016","DOIUrl":"10.1016/j.foodhyd.2025.112016","url":null,"abstract":"<div><div>Plant-based foods are gaining momentum as sustainable and health-conscious alternatives to animal-derived products. Understanding the structural organization of plant protein systems from molecular to mesoscopic scales is essential for designing products with desirable texture, stability, and nutritional performance. Small-angle X-ray scattering (SAXS) and small-angle neutron scattering (SANS) are powerful, non-destructive techniques that provide detailed insights into the hierarchical structures of these systems under realistic, hydrated conditions. This review summarizes recent advances in the use of SAXS and SANS to study plant-based gels, foams, emulsions, meat analogues, dairy alternatives, and <em>in vitro</em> digestion. These techniques reveal critical information on protein aggregation, network formation, interfacial structuring, and digestion dynamics, often inaccessible by conventional methods. We also outline future research directions, including expanding to non-thermal gelation pathways, integrating <em>in situ</em> processing environments, coupling with complementary techniques, and leveraging AI for structural interpretation. SAXS and SANS are poised to play a central role in the rational design of next-generation plant-based foods with optimized functional and sensory attributes.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"172 ","pages":"Article 112016"},"PeriodicalIF":11.0,"publicationDate":"2025-09-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145155255","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}

{"title":"Changes of physicochemical and structural properties of wheat gluten induced by apple pectin with different molecular weights","authors":"Cuixia Li ,&nbsp;Jinfeng Chen ,&nbsp;Yunxiang Ma","doi":"10.1016/j.foodhyd.2025.112004","DOIUrl":"10.1016/j.foodhyd.2025.112004","url":null,"abstract":"<div><div>In this study, apple pectin (AP) was first subjected to ultrasonic degradation to obtain four kinds of pectins (AP₅₁₈, AP₃₈₄, AP₃₃₅ and AP₂₉₇) with different molecular weights (Mw). Subsequently, the structure-activity relationship between the Mw of AP and the impact of AP on gluten characteristics and network structure was investigated. The result indicated that AP and gluten protein mainly interacted through hydrogen bonds, thus changing the gluten characteristics and network structure. Notely, the changes of gluten properties and network were closely related to the Mw of AP. Specifically, low-Mw AP enhanced the water holding capacity and rheological properties of gluten protein. Compared with the control group, AP₂₉₇ significantly increased the surface hydrophobicity of gluten protein from 86.19 to 105.33, while decreasing the fluorescence intensity of gluten protein from 224.17 to 200.23. The result indicated that AP₂₉₇ was more likely to interact with gluten protein and form protein aggregates. Meanwhile, compared with AP₅₁₈, AP₂₉₇ significantly increased the enthalpy (from 120.83 J/g to 164.82 J/g), β-sheet content (from 32.52 % to 44.28 %), and disulfide bonds content (from 15.67 μmol/g to 19.38 μmol/g) of gluten protein. These above results suggested that the network structure of gluten protein was improved and became more stable. In addition, SEM also further confirmed that AP₂₉₇ could better maintain the gluten network structure. These findings can be said to offer theoretical support for the rational application of AP with varying Mw in wheat flour products.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"172 ","pages":"Article 112004"},"PeriodicalIF":11.0,"publicationDate":"2025-09-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145118042","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}

{"title":"Extraction of proteins from brewer's spent grain using ultrasound and alkaline hydrogen peroxide: Impact on extraction yield, structural and techno-functional properties","authors":"Marcio Augusto Ribeiro-Sanches ,&nbsp;Sérgio Luís Ferreira Júnior ,&nbsp;Caroline Santezi ,&nbsp;Ícaro Putinhon Caruso ,&nbsp;Pedro Esteves Duarte Augusto ,&nbsp;Javier Telis-Romero ,&nbsp;Tiago Carregari Polachini","doi":"10.1016/j.foodhyd.2025.112012","DOIUrl":"10.1016/j.foodhyd.2025.112012","url":null,"abstract":"<div><div>BSG (brewer's spent grain) is an abundant agro-industrial by-product and a potential low-cost sustainable source of proteins. In this study, we evaluated the use of high-intensity ultrasound (US) and/or alkaline hydrogen peroxide (AHP) to improve the protein extraction process, as well as the structural and technical-functional properties of the obtained proteins. Four extraction processes were evaluated: EC - extraction using the conventional method; EAHP - extraction using alkaline hydrogen peroxide (3 %); EUS - ultrasound extraction (1200 W); EAHPUS -extraction using AHP (3 %) and US (1200 W). EAHP, EUS, and EAHPUS caused structural changes in the BSG, resulting in higher protein extraction yield compared to EC (69.6–139.6 %). Structural analyses (SEM, FTIR, CD, and X-ray diffraction) showed that the EAHP, EUS, and EAHPUS concentrates exhibited particle fragmentation, changes in the secondary structures of proteins, an increase in disordered structures (random coil), and a reduction in the size of crystals. Each extraction method influenced differently the techno-functional properties. EUS improved the water-holding capacity (∼24 %) and did not affect the color of the extracted proteins, whereas EAHP and EAHPUS reduced the water-holding capacity (11.50–22.05 %), increased solubility (3.22–46.66 % depending on pH), and caused a noticeable change in color. Compared with EC, all treatments improved the foaming capacity (28.05–31.06 %) and stability (11.48–22.19 %), emulsifying capacity (13.66–27.60 %) and stability (16.07–26.12 %), while no effect was observed on the oil-holding capacity. Therefore, the results highlight the potential of using ultrasound and/or alkaline hydrogen peroxide to improve the extraction of BSG proteins, although the effects on techno-functional properties must be considered for different applications.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"172 ","pages":"Article 112012"},"PeriodicalIF":11.0,"publicationDate":"2025-09-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145154743","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}

{"title":"Controlled release system inducing change in stability of volatile essential oil emulsion incorporated in a hydrogel using a responsive polymer for practical active food packaging","authors":"Sungmo Ahn ,&nbsp;Umin Park ,&nbsp;Hyungsup Kim ,&nbsp;Choongjin Ban ,&nbsp;Seokwon Lim","doi":"10.1016/j.foodhyd.2025.112015","DOIUrl":"10.1016/j.foodhyd.2025.112015","url":null,"abstract":"<div><div>Controlled-release systems have garnered significant interest across various industries, particularly in applications involving active compounds. The release of these compounds from packaging improves their functionality and efficiency. Active packaging systems utilizing essential oils have been extensively researched due to their antimicrobial properties and high volatility. However, their rapid depletion during the initial stages restricts their effectiveness and practical applications. This study proposes a humidity-responsive controlled-release active packaging system to overcome this challenge. To enhance emulsion stability, two nonionic emulsifiers, Tween 20 (polyoxyethylene (20) sorbitan monolaurate, water soluble) and Span 60 (sorbitan monostearate, oil soluble), were combined with polyvinyl alcohol (PVA). The resulting formulation was used as a film in the experiment. Using this system, an antimicrobial hydrogel film incorporating lemongrass essential oil (LO), a volatile antimicrobial substance, was fabricated and evaluated for its release behavior, antimicrobial activity, and mechanical properties to assess the film quality. LO-PVA hydrogel films were prepared via casting, and their humidity-responsive release was analyzed at various relative humidity (RH) levels (30, 50, 70, and 90 %) over 72 h. LO retention within the films was 61.29 ± 5.56 % at 26 % RH, decreasing to 9.98 ± 1.42 % at 90 % RH, demonstrating that the release rate of LO increased with higher humidity levels. To assess their practical applications, the antimicrobial properties of the fabricated films were evaluated using microbiological assays and real-food packaging tests with ready-to-eat food. Our findings demonstrate the effectiveness of the developed controlled-release system for fabricating and evaluating antimicrobial hydrogel films, as well as its applicability to active antimicrobial food packaging.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"172 ","pages":"Article 112015"},"PeriodicalIF":11.0,"publicationDate":"2025-09-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145105353","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}

{"title":"Key structural domains of resistant starch and their role in modulating gut microbiota and short-chain fatty acids production","authors":"Bo Zheng ,&nbsp;Hui Wen ,&nbsp;Yiping Zhong ,&nbsp;Bin Zheng ,&nbsp;Xingwei Xiang ,&nbsp;Ling Chen","doi":"10.1016/j.foodhyd.2025.112014","DOIUrl":"10.1016/j.foodhyd.2025.112014","url":null,"abstract":"<div><div>Resistant starch (RS), an indigestible dietary carbohydrate, plays a pivotal role in modulating gut health through microbial fermentation to short-chain fatty acids (SCFAs) including acetate, propionate, and butyrate which mediate multiple health benefits. Accumulating evidence highlights that the digestive resistance and fermentative behavior of RS are fundamentally determined by its structural characteristics, such as amylose-to-amylopectin ratio, granule morphology, crystalline type, chain-length distribution, and interactions with other food components. This review provides a comprehensive synthesis of current knowledge on the classification and structural domains of RS, their influence on fermentation kinetics and SCFA profiles, and their interactions with gut microbiota. Additionally, we discuss how these structure-function relationships translate into health outcomes and inform the development of functional starch ingredients. Emerging strategies, including genetic breeding for high amylose content, controlled physical processing, chemical modification, and esterification with SCFAs, offer opportunities to tailor RS properties for specific nutritional goals. Future research directions should further clarify how these structural attributes can be leveraged within precision nutrition frameworks to develop functional foods and dietary interventions aligned with individual microbiome variability and health needs.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"172 ","pages":"Article 112014"},"PeriodicalIF":11.0,"publicationDate":"2025-09-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145154744","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}

{"title":"Modulation mechanism of starch gelatinization and gluten network restructuring in wheat flour during atmospheric steam treatment","authors":"Xiangqi Fan ,&nbsp;Jikai Jiang ,&nbsp;Mohsin Rasheed ,&nbsp;Ming Li ,&nbsp;Yingquan Zhang ,&nbsp;Yutong Cui ,&nbsp;Bo Zhang ,&nbsp;Boli Guo","doi":"10.1016/j.foodhyd.2025.112006","DOIUrl":"10.1016/j.foodhyd.2025.112006","url":null,"abstract":"<div><div>This study elucidates the competitive molecular interplay between starch gelatinization and protein aggregation in wheat flours of varying gluten strengths (strong, medium, weak) during atmospheric steam treatment (AST). Through integrated microstructural, crystallographic, spectroscopic, thermal, chromatographic, and electrophoretic analysis, we demonstrate a phase-dependent shift in dominance between starch gelatinization and protein aggregation. During initial AST (0–2 min), rapid starch hydration drives partial gelatinization, disrupting crystalline domains, reducing short-range molecular order, and promoting amylose-lipid complex formation. With extended treatment (4–10 min), dominance shifted to protein aggregation, where heat-induced conformational unfolding triggered α-helix to β-sheet transitions, exposing buried sulfhydryl groups and hydrophobic residues. These changes facilitated irreversible protein network formation via disulfide cross-linking and hydrophobic associations. Concurrently, protein aggregates adhered to starch granule surfaces, forming physical barriers that restricted water penetration and suppressed further gelatinization. Gluten strength critically modulated these competitive interactions. During initial AST (2 min), gelatinization degrees reached 30.03 %, 35.02 %, and 37.86 % for strong gluten flour (SGF), medium gluten flour (MGF), and weak gluten flour (WGF), reaching 50.83 %, 55.16 %, and 58.14 % after 10 min treatment. Following AST, SGF formed dense, cross-linked protein matrices that tightly encapsulated partially gelatinized starch fragments. In contrast, WGF formed extensive starch gel phases with relatively sparse protein aggregates, resulting in a more open network. MGF displayed a balanced structure with interpenetrating starch and protein networks reflecting intermediate structural characteristics. These findings elucidate the molecular mechanisms governing starch-protein interplay during AST, providing mechanistic foundation for process optimization and targeted wheat-based products development with desirable functional properties.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"172 ","pages":"Article 112006"},"PeriodicalIF":11.0,"publicationDate":"2025-09-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145105296","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}

{"title":"Heterologous amyloid fibril complexes formed by rice glutelin and soy protein: Assembly behavior and physicochemical properties","authors":"Chuping Zhang ,&nbsp;Dong Wang ,&nbsp;Ting Li ,&nbsp;Xinxia Zhang ,&nbsp;Juan Li ,&nbsp;Mingqin Li ,&nbsp;Li Wang","doi":"10.1016/j.foodhyd.2025.111969","DOIUrl":"10.1016/j.foodhyd.2025.111969","url":null,"abstract":"<div><div>The low fibrillation efficiency of rice glutelin (RG) and the strong aggregation tendency of soy protein isolate (SPI) limit their practical applications. This study investigated RG/SPI co-fibrillation behavior to elucidate the structural features and physicochemical properties of the resulting heterologous amyloid fibrils. Results demonstrated that the 5:5 RG/SPI mixture achieved a 37.31 % higher fibril conversion rate than RG alone. Furthermore, increasing RG proportion mitigated the aggregation of SPI fibrils, enhancing dispersion uniformity. Structural analysis revealed that all samples developed more ordered β-sheet structures after fibrillation. Notably, the cross-β-sheet structure in heterologous amyloid fibrils was more compactly arranged than in single-amyloid fibrils. The viscosity, storage modulus (G′) and loss modulus (G″) of heterologous fibrils were lower than those of single-amyloid fibrils, improving the fluidity of samples. In conclusion, the high conversion rate and low aggregation tendency of heterologous amyloid fibrils are expected to play a more significant role in enhancing the efficiency of bioactive delivery and improving the performance of functional materials.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"172 ","pages":"Article 111969"},"PeriodicalIF":11.0,"publicationDate":"2025-09-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145105350","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}