Food Hydrocolloids最新文献

{"title":"The xanthan gum oriented for dysphagia management: the relationship between its structure and shear and extensional rheological properties","authors":"Jiao Wang ,&nbsp;Fei Liu ,&nbsp;Maoshen Chen ,&nbsp;Ling Chen ,&nbsp;Yixun Xia ,&nbsp;Fang Zhong","doi":"10.1016/j.foodhyd.2025.111731","DOIUrl":"10.1016/j.foodhyd.2025.111731","url":null,"abstract":"<div><div>Xanthan gum (XG) is an excellent thickener for dysphagia management due to its superior palatability and thickening ability. For dysphagia management, it is not only important to understand shear rheology but also the extensional rheology of it, which is not widely studied. The objective of this study was to evaluate the shear and extensional rheology characters of various XG samples and relate the performance with molecular structure. The shear rheology results showed that XG with the higher Mw showed higher [η] and better shear thinning behaviors, indicating easier swallowing. Additionally, the filament break-up time and Trouton ratio of high Mw XG solution was significantly larger than the others, exhibiting excellent extensional viscosities and cohesiveness either at the same XG concentration or with varied XG concentration but the same shear viscosity at 50 s⁻¹, which suggested safer swallowing. Fine structure analysis revealed that, at similar Mw, XG with more pyruvate groups or branched chains exhibited higher viscosity. Compared with the XG with low pyruvate acid (1.64 %) and branching degree (70.99 %), the η₅₀ (0.5 %, w/v) of the sample with high pyruvate (5.05 %) and branching degree (75.53 %) increased by 27.55 %. These were attributed to the combined effect of hydrodynamic volume and intermolecular interactions at concentrations above c∗. The effects of Mw, [η], pyruvate content and branching degree on extensional rheology are consistent with shear rheology. The results of this study contributed to the structural design of XG to fulfill the rheological properties required for safe and efficient food intake in elderly individual.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"170 ","pages":"Article 111731"},"PeriodicalIF":11.0,"publicationDate":"2025-07-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144581105","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":"Improved freeze-thaw resistance of emulsified myofibrillar protein gels: Effects of starch crystalline polymorphs and hydrophobic modification on dual structural regulation","authors":"Yuxin Ding ,&nbsp;Zhiwen Shen ,&nbsp;Yujie Ding ,&nbsp;Yanshun Xu ,&nbsp;Dawei Yu ,&nbsp;Zhifei Zhu","doi":"10.1016/j.foodhyd.2025.111727","DOIUrl":"10.1016/j.foodhyd.2025.111727","url":null,"abstract":"<div><div>Freeze-thaw (FT) deterioration severely limits the functional stability of emulsified myofibrillar protein (MP) gels, primarily due to interfacial protein film (IPF) disruption and bulk network collapse caused by ice/lipid crystallization. This study elucidated the synergistic mechanism by which starch crystalline polymorphs (A-, B-, and C-types) combined with octenyl succinic anhydride (OSA) esterification enhanced the FT stability of emulsified MP gels. Among the natural starches, A-type starch outperformed B- and C-types by maintaining tight interfacial co-adsorption and double-network entanglement with MP, providing a structural basis for cryoprotection. Building on this, OSA-induced amphiphilic modification further reinforced gel stability. OSA-starch anchored the interfacial film through hydrophobic interactions and strengthened cross-linking with the hydrophilic bulk network, thereby preserving desirable gel properties under FT stress. This dual structural stabilization, resulting from the appropriate OSA distribution and hydrophilic-lipophilic balance in A-OS starch, effectively inhibited ice/lipid crystallization and maintained matrix continuity in the emulsified MP gel. Macroscopic assessments, texture analysis, and microscopic observations confirmed that A-OS imparted superior liquid retention (thawing loss: 0.61 %; cooking loss: 3.03 %) and mechanical properties (hardness: 1307.88 g; springiness: 93.65 %) to the frozen gels, significantly outperforming other starch formulations. This work provides novel insights into stabilization strategies for protein-lipid colloidal systems and promotes the industrial application of high-quality frozen foods.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"170 ","pages":"Article 111727"},"PeriodicalIF":11.0,"publicationDate":"2025-07-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144581015","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":"Covalent modification of whey protein isolate by rosmarinic Acid: Impacts on physicochemical and functional properties","authors":"Qing Yang ,&nbsp;Shiyun Chen ,&nbsp;Xuanpei Wang ,&nbsp;Yijie Chen ,&nbsp;Lin Xu ,&nbsp;Xiao Guo ,&nbsp;Zhiyong Gong ,&nbsp;Hao-Long Zeng ,&nbsp;Xin Liu","doi":"10.1016/j.foodhyd.2025.111726","DOIUrl":"10.1016/j.foodhyd.2025.111726","url":null,"abstract":"<div><div>Molecular modification has emerged as a promising strategy to enhance the functional properties of food proteins. In this study, rosmarinic acid (RA) was successfully conjugated to whey protein isolate (WPI) through a radical-mediated grafting approach, achieving a conjugation efficiency of 60.23 mg/g protein (WPI-RA 0.1). Electrophoretic analysis confirmed the formation of high-molecular-weight conjugates, while comprehensive spectroscopic characterization (FTIR, fluorescence spectroscopy, and UV absorption) revealed significant structural reorganization of WPI following RA conjugation. Notably, the <em>α-</em>Helix content decreased from 22.73 % (WPI-RA 0) to 17.55 % (WPI-RA 0.05), accompanied by an increase in <em>β</em>-turn content from 25.46 % (WPI-RA 0) to 41.82 % (WPI-RA 0.05). RA conjugation conferred multiple functional improvements to WPI. The allergenicity of WPI was significantly reduced, as evidenced by decreased IgG binding affinity (83.85 % for WPI-RA 0.1). Antioxidant capacity was markedly (<em>P</em> &lt; 0.05) enhanced, with WPI-RA 0.1 demonstrating 74.37 % DPPH and 88.48 % ABTS⁺ radical scavenging activities. Additionally, the foaming and emulsifying properties of WPI-RA 0.1 were substantially improved, with foaming capacity (FC) increased to 104.39 %, foaming stability (FS) to 63.15 %, foaming half-life to 165.33 min, emulsifying activity index (EAI) to 1.11 m²/g, and emulsion stability index (ESI) to 92.37 min. Importantly, emulsions stabilized by WPI-RA exhibited superior oxidative stability during 14-day storage, with significantly reduced peroxide formation compared to native WPI. These findings demonstrate that RA conjugation effectively mitigates WPI allergenicity while enhancing its functional and antioxidant properties. This highlights its promising potential for nutritional food development, particularly in formulating hypoallergenic and high-performance protein ingredients.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"170 ","pages":"Article 111726"},"PeriodicalIF":11.0,"publicationDate":"2025-07-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144581104","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":"Emulsifier synergism in aerated emulsions: coordinated regulation of fat crystallization and protein interfacial adsorption","authors":"Xiuhang Chai,&nbsp;Yi Su,&nbsp;Yuanfa Liu","doi":"10.1016/j.foodhyd.2025.111725","DOIUrl":"10.1016/j.foodhyd.2025.111725","url":null,"abstract":"<div><div>Plant-animal hybrid fat-based creams often suffer from compromised stability, texture, and sensory attributes due to mismatched fat crystallization behaviors and suboptimal interfacial film integrity. While emulsifiers are pivotal in modulating these properties, their synergistic mechanisms in hierarchically regulating fat-protein-colloid interactions remain poorly understood. This study systematically decoupled the roles of hydrophilic (Span20, Tween20/40/60, Polyglyceryl-10 Laurate (PGE-L); HLB 8.6–15.6) and lipophilic (Glyceryl monostearate (GMS); Hydrophile-lipophile balance (HLB) 3.8) emulsifiers in a palm kernel stearin-palm oil stearin-anhydrous milk fat (PP-AMF) matrix, focusing on crystallization kinetics, interfacial remodeling, and aerated structural evolution. Crystallization analysis demonstrated that GMS elevated onset temperatures to 33.21 °C via epitaxially templated heterogeneous nucleation, forming dense <em>β′</em>-polymorphic microcrystals (2.00 <span><math><mrow><mo>±</mo></mrow></math></span> 0.18 μm) that accelerated partial coalescence. Hydrophilic emulsifiers minimally affected crystallization temperatures but reduced fat crystal size. Interfacial dynamics revealed that hydrophilic emulsifiers (e.g., Tween20, PGE-L) displaced sodium caseinate at oil-water interfaces, reducing tension from 19.90 mN/m (protein alone) to 7.23–8.55 mN/m through rapid molecular packing. Conversely, GMS crystallized at interfaces, enhancing shear-induced aggregation for structural rigidity. A ternary emulsifier system (GMS + Span20+Tween40) synergistically balanced overrun (237.41 %), hardness (59.46 g), and 30-min structural retention by decoupling crystallization control (GMS-driven <em>β′</em> networks) from interfacial stabilization (Tween40-mediated steric hindrance). The modulation of fat crystallization by emulsifiers, combined with the synergistic interplay between casein molecules and hydrophilic surfactants to enhance emulsion stability and coalescence resistance, serves as a critical determinant in the fabrication of aerated emulsions.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"170 ","pages":"Article 111725"},"PeriodicalIF":11.0,"publicationDate":"2025-07-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144563343","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":"Wet ball-milling fabricated deacetylated chitin nanofibers for meat saltiness enhancement","authors":"Jing Liao ,&nbsp;Xingyue Zhao ,&nbsp;Yuhang Zhou ,&nbsp;Jiamin Zhang","doi":"10.1016/j.foodhyd.2025.111729","DOIUrl":"10.1016/j.foodhyd.2025.111729","url":null,"abstract":"<div><div>The reduction of salt usage in meat products is of significant interest to the meat processing industry. In this context, chitin nanofibers (ChNFs) have emerged as a potential candidate for reducing salt usage in meat products. In this study, deacetylated chitin nanofibers (D-ChNFs) with varying degrees of deacetylation (DDs) were prepared by subjecting native chitin to a partial deacetylation process, followed by a wet ball-milling treatment. The fabricated D-ChNFs were characterized and used as saltiness enhancers for pork fillets. The enhanced saltiness mechanism was elucidated by exploring the interaction between ChNFs and Cl⁻. The results have shown that when DD is increased from 5.9 % to 28.6 %, D-ChNFs with a more dispersed nanostructure can be obtained, with a diameter range of 10–30 nm and a length of several microns. Furthermore, the pork fillets cured with D-ChNFs exhibited higher saltiness values compared to the control groups, and the optimal perceived saltiness was obtained when the ChNF-12 (DD = 28.6 %) was added. Quantum chemical calculation results demonstrated that the interaction intensity between Cl⁻ and the functional groups on the D-ChNFs is in the order of -NH₃⁺/−OH &gt; -NH₃⁺&gt;-NHCOCH₃. D-ChNFs can bind Cl⁻ to their surface through electrostatic attraction as the dominant force, and scale up the proportion of Na⁺ on the meat surface that can bind to taste receptor cells, thus enhancing the meat saltiness. The findings of this study provide a theoretical basis for the development of novel salt reduction methods in meat industry.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"170 ","pages":"Article 111729"},"PeriodicalIF":11.0,"publicationDate":"2025-07-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144564014","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":"Partially removing galactose unit on tamarind gum improves the gel-related features of tamarind gum/xanthan gels by strengthening their synergistic assembly","authors":"Zhiyong Niu ,&nbsp;Xizhong Liu ,&nbsp;Yunying Li ,&nbsp;Mengzhou Zhou ,&nbsp;Yi Liu ,&nbsp;Binjia Zhang ,&nbsp;Guohua Zhao ,&nbsp;Jia Chen ,&nbsp;Dongling Qiao ,&nbsp;Fengwei Xie","doi":"10.1016/j.foodhyd.2025.111728","DOIUrl":"10.1016/j.foodhyd.2025.111728","url":null,"abstract":"<div><div>The amalgamation of tamarind gum (TMG) and xanthan generates synergistic interaction gels (SIGs), which have been used to design novel textural systems and to develop cell-cultured meat as well as health foods tailored for elderly individuals with dysphagia. However, the strong aggregated tendency of TMG chains limited the expose of active sites, thereby hindering full binding with xanthan and resulting in suboptimal gel properties. This study demonstrated that the removal of galactose units from TMG enhances specific interactions between TMG and xanthan by modulating the aggregation behavior of TMG chains. After removing galactose to 71.30 %, the reduced steric hindrance facilitated the transformation of disordered TMG chains into a helical structure, thereby exposing more binding sites (<em>i.e.</em>, hydrophilic groups) to interact with pyruvate groups on xanthan. This enhanced the specific interactions, as evidenced by an increase in enthalpy change from 2.80 × 10⁻² J/g to 3.90 × 10⁻² J/g, and thus the gel structure (suggested by the increased <em>n</em> and reduced <span><math><mrow><msub><mi>ξ</mi><mrow><mi>c</mi><mi>h</mi><mi>a</mi><mi>i</mi><mi>n</mi></mrow></msub></mrow></math></span> values in Table 1) and gel strength both in <em>G</em>′ and gel hardness. However, further removal of galactose reduced the dissociation ability of TMG chains from clusters and resulted in the formation of elongated clusters, thereby decreasing the contact surface between TMG and xanthan, which weakened their specific interactions and gel strength. These results provide insights for the design and development of SIG-based systems in food industry.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"170 ","pages":"Article 111728"},"PeriodicalIF":11.0,"publicationDate":"2025-07-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144572030","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":"Understanding the effect of pH on structure formation in high moisture extrudates produced from soy protein-dietary fiber blends","authors":"Jiashu Li ,&nbsp;Frederik Janssen ,&nbsp;Annelise Vallaey ,&nbsp;Diete Verfaillie ,&nbsp;Kristof Brijs ,&nbsp;Jan A. Delcour ,&nbsp;Atze Jan van der Goot ,&nbsp;Geert Van Royen ,&nbsp;Arno G.B. Wouters","doi":"10.1016/j.foodhyd.2025.111710","DOIUrl":"10.1016/j.foodhyd.2025.111710","url":null,"abstract":"<div><div>The effect of pH on the structure and texture of high moisture extrudates prepared from blends of soy protein isolate (SPI) and a soy dietary fiber-enriched fraction (SDF), achieving different protein-DF ratios, was studied. Samples hydrated to 50 % moisture at pH 3.0, 5.0, and 7.0 underwent rheological analysis following a temperature profile (40–140–60 °C) relevant for high moisture extrusion (HME). At pH 7.0, lower complex viscosity (|η∗|) at 140 °C and steeper |η∗| increase during cooling indicated greater protein-protein interaction disruption at high temperature followed by enhanced intermolecular interaction and/or cross-linking during cooling than at pH 3.0 and 5.0. The use of a lower protein-DF ratio resulted in elevated |η∗| during heating and lower |η∗| after cooling at all pH values, the latter due to DFs interfering with protein network formation. Extrudates produced at pH 7.0 using a Thermo Fisher Process 11 extruder exhibited distinct anisotropic structure and pronounced water syneresis, whereas extrudates produced at low pH had mostly isotropic structure. This was attributed to the lower viscosity and thus greater deformability at the end of the barrel and to more pronounced disulfide bond formation upon cooling in samples at neutral pH, compared to at low pH. The use of a lower protein-DF ratio at pH 7.0 transformed extrudate structures from layered to fibrous and reduced disulfide bond formation. This study demonstrated that pH and protein-DF ratios significantly affect bulk viscosity and disulfide bond formation during extrusion, thereby determining the structure and texture of the resulting extrudates.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"170 ","pages":"Article 111710"},"PeriodicalIF":11.0,"publicationDate":"2025-07-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144623739","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":"Modulating the gel strength of filled whey protein hydrogels by altering oil droplets characteristics: Theory and experiments","authors":"Xiaoyan Hu ,&nbsp;Yajuan Li ,&nbsp;Jaekun Ryu ,&nbsp;David Julian McClements","doi":"10.1016/j.foodhyd.2025.111721","DOIUrl":"10.1016/j.foodhyd.2025.111721","url":null,"abstract":"<div><div>Protein-based hydrogels are used in a wide range of food products, including desserts, confectionary, dressings, spreads, and meat analogs. For many applications, it is important to modulate the textural attributes of the hydrogels so that they meet consumer expectations. In this study, the impact of oil droplet characteristics, especially size and concentration, on the rheological properties of filled whey protein hydrogels was examined. The experimental measurements were compared to the predictions made by a theoretical model for the elastic properties of filled composite materials consisting of non-dilute spherical fluid particles dispersed within a solid matrix. This theory predicted that the mechanical strength of filled hydrogels can either increase or decrease with increasing oil droplet concentration depending on the size of the droplets. Small droplets have a high Laplace pressure, which makes them more resistant to deformation. Consequently, they may increase the gel strength when their effective rigidity is higher than that of the surrounding protein network. In contrast, large droplets have a low Laplace pressure, which makes them highly susceptible to deformation. As a result, they tend to reduce the gel strength. In this study, we prepared oil-in-water emulsions with different mean droplet diameters and then used them to form heat-set whey protein gels with a range of droplet and protein concentrations. The theory and experiments showed good qualitative agreement but there was a poor quantitative agreement, which was attributed to the fact that the real emulsion gels did not conform to the assumptions used to derive the theoretical model. Even so, this mathematical model is useful for understanding and predicting the behavior of filled food gels.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"170 ","pages":"Article 111721"},"PeriodicalIF":11.0,"publicationDate":"2025-07-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144572029","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":"Hydration-driven structural engineering via enzymatic glycation: Sustained quercetin release in pullulan-zein coatings for extended walnut preservation","authors":"Zi-han Wang ,&nbsp;Xue-li Liu ,&nbsp;Rui-qi Sun ,&nbsp;Bin Qi ,&nbsp;Jun-xia Xia ,&nbsp;Da-yong Zhou ,&nbsp;Liang Song","doi":"10.1016/j.foodhyd.2025.111705","DOIUrl":"10.1016/j.foodhyd.2025.111705","url":null,"abstract":"<div><div>This study developed pullulan-based edible coatings incorporating quercetin-loaded glycated zein nanoparticles (<em>g</em>Zein I–III-Que) to mitigate oxidative rancidity in walnuts. Enzymatic glycation-driven hydration engineering modulated interfacial interactions between zein and pullulan, forming structurally homogeneous nanocomposites. The optimized intermediate glycation coating (<em>g</em>Zein II-Que@Pul) resolved incompatibility between hydrophobic antioxidants and hydrophilic matrices through uniform nanoparticle dispersion (PDI 0.19 ± 0.02) and enhanced mechanical strength (28.48 ± 0.52 MPa). Hydration-mediated structural reorganization balanced molecular mobility and diffusion resistance, sustaining antioxidant release <em>via</em> non-Fickian kinetics (Korsmeyer-Peppas n = 0.55). The coatings reduced oxygen permeability to 0.10 ± 0.02 kg m⁻²·s⁻¹ and demonstrated high antioxidant efficiency (I₅₀ = 1.4 mg/mL) alongside cytocompatibility exceeding 80 % cell viability. Applied to walnuts, <em>g</em>Zein II-Que@Pul extended shelf life by 528 ± 25 % at 25 °C, retaining 91.76 ± 1.17 % omega-3 and 95.22 ± 0.76 % omega-6 fatty acids. MRI spatial analysis visualized lipid oxidation suppression spatially correlated with hydration-driven quercetin release, validated by peroxide value reductions (57.53 ± 2.73 %). By tailoring glycation degree, this work establishes enzymatic hydration engineering as a scalable strategy for sustainable food preservation. The optimized coating harmonizes bioactive delivery and structural integrity through hydration-modulated diffusion kinetics and interfacial stability, leveraging renewable biopolymers to advance plant protein-polysaccharide hybrids as functional barriers for minimizing postharvest losses in lipid-rich foods.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"170 ","pages":"Article 111705"},"PeriodicalIF":11.0,"publicationDate":"2025-07-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144564017","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":"Plant-based hydrogel beads for vitamin D bioaccessibility: The role of protein denaturation and dimension","authors":"Tugba Dursun Capar ,&nbsp;Xiaoyan Hu ,&nbsp;David Julian McClements","doi":"10.1016/j.foodhyd.2025.111723","DOIUrl":"10.1016/j.foodhyd.2025.111723","url":null,"abstract":"<div><div>Encapsulating bioactive components within hydrogel beads provides an effective method of improving their stability and efficacy, thereby enhancing their potential health benefits. In this study, vitamin D₃-loaded nanoemulsions were encapsulated within plant-based hydrogel beads comprised of pea protein (heated or unheated) and calcium alginate. The impact of bead composition and dimensions on lipid digestibility and vitamin D bioaccessibility was then investigated. The hydrogel beads containing heated pea protein were more stable to simulated oral and stomach phases than those containing unheated pea protein. This effect was attributed to the formation of heat-induced pea protein aggregates that were better retained within the calcium alginate network inside the beads. The bioaccessibility of vitamin D₃ was improved when it was encapsulated within the beads, which may have been due to their ability to protect the vitamin from chemical degradation, especially under acidic gastric conditions. The beads containing the heated protein provided the best protection during stomach digestion, leading to around 86 % of the original vitamin D₃ still being bioaccessible after the small intestine phase. The results of this study may lead to the development of novel hydrogel delivery systems that can improve the efficacy of oil-soluble vitamins in plant-based foods.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"170 ","pages":"Article 111723"},"PeriodicalIF":11.0,"publicationDate":"2025-07-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144581101","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}