Food Hydrocolloids最新文献

{"title":"Modulating physicochemical properties via high-pressure homogenization and steam explosion to regulate the prebiotic efficacy of Naematelia aurantialba polysaccharides","authors":"Liping Liu ,&nbsp;Xiaoyu Liu ,&nbsp;Jie Feng ,&nbsp;Haowen Sun ,&nbsp;Linlei Yang ,&nbsp;Qingqing Lu ,&nbsp;Rongchun Li ,&nbsp;Yanfang Liu ,&nbsp;Jingsong Zhang","doi":"10.1016/j.foodhyd.2026.112542","DOIUrl":"10.1016/j.foodhyd.2026.112542","url":null,"abstract":"<div><div><em>Naematelia aurantialb</em>a fruiting bodies are valued for their high content of bioactive polysaccharides. This study employed high-pressure homogenization (HPH) and steam explosion (SE) as pretreatments to improve the efficiency of polysaccharide extraction and modify their functional properties. Compared to the polysaccharide obtained by conventional extraction (NAPE, yield 36.90%), HPH and SE achieved significantly higher yields of 44.45% (NAPHE) and 47.00% (NAPSE), likely due to more efficient cell disruption. NAPE showed a molecular weight (<em>M</em>_<em>w</em>) of 1.163 × 10⁶ g/mol, while NAPHE and NAPSE exhibited a reduced <em>M</em>_<em>w</em> of 5.461 × 10⁵ and 8.569 × 10⁵ g/mol. Furthermore, the SE pretreatment released a distinct low-<em>M</em>_<em>w</em> fraction of 8.487 × 10⁴ g/mol in NAPSE. These structural modifications resulted in lower apparent viscosities, which influenced gut microbial fermentation and thereby generated divergent prebiotic activities <em>in vitro</em>. Specifically, NAPHE and NAPSE produced a higher total short-chain fatty acid (SCFA) concentration than NAPE, primarily by enriching microbiota responsible for producing acetic and propionic acids. Conversely, NAPE more selectively enriched microbiota associated with butyrate production. Consequently, the method-imparted structural properties dictate the microbial accessibility and subsequent fermentation of the polysaccharides, which critically determined the resulting prebiotic function. This provides a rationale for selecting extraction techniques to design and obtain targeted prebiotic ingredients.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"176 ","pages":"Article 112542"},"PeriodicalIF":11.0,"publicationDate":"2026-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146162024","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":"Ultrasound-driven structural and functional modifications of grape seed protein revealed by power- and duration-dependent experiments","authors":"Ying-Yang Liu ,&nbsp;Da-Rui Tang ,&nbsp;Shi-Ling Wang ,&nbsp;Wei-Wei Li ,&nbsp;Jun-Wei Xu ,&nbsp;Lian-Bing Lin ,&nbsp;Yu-Hang Jiang ,&nbsp;Qi-Lin Zhang","doi":"10.1016/j.foodhyd.2026.112554","DOIUrl":"10.1016/j.foodhyd.2026.112554","url":null,"abstract":"<div><div>The study aimed to investigate the effects of ultrasound treatment, varying in power and duration, on the solution behavior, multi-level structure, and functional properties of grape seed protein (GSP). Ultrasound significantly enhanced the functional properties of GSP, with optimal improvements at 400 W for 10 min. However, excessive treatment reduced these benefits. SDS-PAGE analysis confirmed the integrity of the primary protein structure after treatment. Circular dichroism spectroscopy revealed a reduction in ordered/stable protein secondary structures (<em>α</em>-helix and <em>β</em>-sheet content, significantly decreased by 24.86% and 21.03% under the optimal ultrasound conditions, respectively, compared to untreated GSP), which was further corroborated by Fourier transform infrared spectroscopy. Intrinsic fluorescence spectroscopy demonstrated significant alterations in the tertiary structure of GSP. Ultrasound treatment improved free sulfhydryl content and surface hydrophobicity (significantly increased by 41.05% and 45.27%, respectively), thereby decreasing protein aggregation. Ultrasound treatment also reduced particle size and increased zeta potential (significantly changed by 54.97% and 24.58%, respectively), promoting protein unfolding and exposure of hydrophobic groups. These structural changes improved its solubility, gel strength, emulsifying and foaming properties, digestibility, and antioxidant activity. Notably, ultrasonication did not induce noticeable oxidative damage to the protein, as the carbonyl groups content increased by only approximately 20%. Collectively, these results demonstrate that properly controlled ultrasound treatment can significantly optimize the structure of GSP, thereby enhancing its functional performance and expanding its potential applications in the food industry.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"176 ","pages":"Article 112554"},"PeriodicalIF":11.0,"publicationDate":"2026-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146187774","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":"Protein-driven interfacial engineering shapes fat networks and mechanical resilience in frozen colloids","authors":"Qian Zhou ,&nbsp;Zhaoyi Fan ,&nbsp;Boxiao Sun ,&nbsp;Xiaoxia Liu ,&nbsp;Huiting Zhang ,&nbsp;Jinhua Hu ,&nbsp;Peng Zhou","doi":"10.1016/j.foodhyd.2026.112557","DOIUrl":"10.1016/j.foodhyd.2026.112557","url":null,"abstract":"<div><div>Proteins play a pivotal role in directing the interfacial assembly and hierarchical structuring of frozen colloidal systems, yet the mechanistic link between protein molecular architecture and macroscopic stability remains poorly understood. Here, we investigate how distinct dairy proteins—whey protein isolate (WPI), micellar casein concentrate (MCC), milk protein concentrate (MPC), and skim milk powder (SMP)—govern the formation of multiscale networks in lactose-free frozen aerated emulsions under low-shear freezing. The structure and flexibility of proteins regulated the relationship between interfacial packing and the mechanical strength of the surrounding network. Samples with limited interfacial coverage (WPI, SMP) stabilized the emulsions through the formation of pervasive, fat-coalesced networks, whereas casein-rich samples (MCC, MPC) relied on cohesive, protein-dense matrices, with macroscopic melting resistance dictated by the large-deformation resilience of the fat network rather than bulk viscosity. Microstructural analysis confirmed that the protein-governed fat architecture templates air-bubble organization and constrains ice crystallization, establishing a multiscale hierarchy that underpins structural integrity. These findings reveal protein-driven interfacial engineering as a dominant mechanism controlling network formation and stability, providing a mechanistic framework for designing next-generation, clean-label, high-protein frozen desserts.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"176 ","pages":"Article 112557"},"PeriodicalIF":11.0,"publicationDate":"2026-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146187772","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":"Sunflower pollen microgel-reinforced Ca-alginate hydrogel beads for protein glutaminase immobilization: Gelation and colloidal behavior and insights into flaxseed protein deamidation modification","authors":"Shangwen Chen ,&nbsp;Xiaoqian Tang ,&nbsp;Yawen Huang ,&nbsp;Ze Zhao ,&nbsp;Song Miao ,&nbsp;Dengfeng Peng ,&nbsp;Yashu Chen ,&nbsp;Bin Zhou ,&nbsp;Qianchun Deng ,&nbsp;Ziyu Deng","doi":"10.1016/j.foodhyd.2026.112552","DOIUrl":"10.1016/j.foodhyd.2026.112552","url":null,"abstract":"<div><div>Protease immobilization is often confronted with issues such as activity loss and mass transfer resistance. This study developed a novel composite gel carrier based on sunflower pollen microgel (SPMG) and Ca-alginate hydrogel beads for immobilizing protein glutaminase (PG). SPMG addition significantly enhanced the activity of PG immobilized on the composite gel carrier, and the optimal SPMG-to-alginate (Alg) volume ratio was 2:1. The immobilized PG demonstrated markedly improved pH and temperature tolerance, as well as enhanced storage stability compared with free PG. These effects may result from the action of SPMG on the carrier microstructure and water distribution through hydrogen bonding interaction with Alg, as well as their interactions with Ca²⁺, thereby regulating the performance of immobilized PG. Subsequently, the carrier-immobilized PG was employed for the deamidation modification of flaxseed protein isolate (FPI) to enhance its functional properties and flavor. At appropriate deamidation levels, the immobilized PG improved the solubility, foaming, and emulsifying properties of FPI by nearly 100%, 50%, and 70%, respectively, while significantly reduced its bitterness. Furthermore, SDS-PAGE, particle size, zeta potential, microstructure, and spectral characteristics were analyzed to characterize the molecular structural changes in the modified FPI, and the underlying mechanisms were analyzed by combining with interfacial rheology. This study elucidates the impact of SPMG incorporation on the properties of gel carrier, which may help regulate the performance of immobilized PG and offer a novel perspective for enzyme immobilization.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"176 ","pages":"Article 112552"},"PeriodicalIF":11.0,"publicationDate":"2026-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146161982","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":"Effects of Hofmeister cation series induced by different alkalizers on the production, structural and functional characteristics of low-sodium soy protein fractions","authors":"Yu Peng ,&nbsp;Rui Wang ,&nbsp;Mo Li ,&nbsp;Xin Wen ,&nbsp;Yuanying Ni ,&nbsp;Sirinan Lasrichan","doi":"10.1016/j.foodhyd.2026.112556","DOIUrl":"10.1016/j.foodhyd.2026.112556","url":null,"abstract":"<div><div>The conventional production of soy protein isolate (SPI) relies on the use of sodium hydroxide (NaOH), resulting in a final product with excessively high sodium content. This study investigated a strategic approach to produce low-sodium soy protein fractions (SPFs) by replacing NaOH with alternative alkalizers during the protein neutralization step, while elucidating how Hofmeister cation series governs their structural and functional properties. The impact of these cations (Na⁺, K⁺, Ca²⁺, Mg²⁺) and their combinations on protein composition, structure, and functionalities was systematically evaluated. The cation introduced during neutralization dominated the final ionic profile, enabling a &gt;90% reduction in sodium content. Chaotropic monovalent cations (K⁺, Na⁺) yielded SPFs with high solubility, fine particle size, and strong electrostatic repulsion, consistent with their role as charge shields. In contrast, kosmotropic divalent cations (Ca²⁺, Mg²⁺) induced significant structural alterations, promoting ionic bridging and hydrophobic interactions that led to extensive protein aggregation, a porous microstructure, and markedly reduced solubility. However, these aggregated SPFs exhibited relative higher water-holding capacity (WHC) and enhanced thermal stability. The more pronounced effects of Mg²⁺ highlighted the role of charge density within the series. Composite formulations enabled tailored properties of SPFs between these extremes, demonstrating the potential for ingredient design. This work established alkalizer substitution engineered by Hofmeister cation series as a practical, single-step strategy not only for sodium reduction but for rationally tailoring the techno-functional properties of soy protein. The findings provided a mechanistic foundation for developing plant-based ingredients that deliver on both health promises and technical requirements.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"176 ","pages":"Article 112556"},"PeriodicalIF":11.0,"publicationDate":"2026-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146162020","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":"Effect of hydrophobic modification on network structure and oil-water separation performance of soybean globulin composite aerogel","authors":"Shiqi Tang ,&nbsp;Zhibin Ma ,&nbsp;Qiuhan Du ,&nbsp;Lianzhou Jiang ,&nbsp;Baokun Qi ,&nbsp;Xingwei Xiang ,&nbsp;Bin Zheng","doi":"10.1016/j.foodhyd.2026.112491","DOIUrl":"10.1016/j.foodhyd.2026.112491","url":null,"abstract":"<div><div>Protein-based aerogels are environmentally friendly and have tunable structures. To enhance the performance of soy protein aerogels and expand their application in food processing, this study investigates the effects of two silane coupling agents on the structure and performance of soy protein aerogels, elucidates the mechanism of hydrophobic modification of silane coupling agents, and examines how non-covalent and covalent interactions between soy globulin (11S) and D-galactose (DG) during the sol stage influence hydrophobic modification. The results showed that both interaction systems, the non-covalent (S-11S/DG) aerogel and the covalent (S/DG-11S) aerogel, exhibited identical functional groups and crystal structures. However, the S-11S/DG system formed a more compact structure at the sol stage, with fewer exposed branches, resulting in thicker aerogel pore walls and enhanced structural stability. Between the two silane coupling agents, methyltrimethoxysilane (MTMS) provided a relatively mild modification, with exposed -OH and alkyl groups appropriately cross-linked, effectively introducing hydrophobic groups while preserving the high specific surface area and mesoporous structure of aerogels, thereby enhancing their hydrophobicity, oil absorption, and compressive strength. In contrast, octadecyltrimethoxysilane (OTMS) induced excessive cross-linking due to its long-chain alkyl group, leading to network skeleton fracture and reduced mechanical properties. Therefore, the chemical structure and thermal degradability of the MTMS hydrophobic modified S-11S/DG aerogel were stability. More hydrophobic groups are fixed on the surface of the aerogel, reducing the likelihood of adsorbed oil droplets detaching, making it more suitable for oil-water separation applications involving emulsions with particle diameters exceeding 600 nm. These findings provide a theoretical basis for the fabrication and performance regulation of soy protein composite aerogels and broaden their application in food processing.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"175 ","pages":"Article 112491"},"PeriodicalIF":11.0,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146184835","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":"Unraveling the shell-core heterogeneity in cooked rice: Impact of milling degree on molecular structure and texture formation","authors":"Luoluo Hu ,&nbsp;Dandan Li ,&nbsp;Tabinda Tariq ,&nbsp;Yanfeng Ding ,&nbsp;Zhenghui Liu","doi":"10.1016/j.foodhyd.2026.112511","DOIUrl":"10.1016/j.foodhyd.2026.112511","url":null,"abstract":"<div><div>During rice cooking, leached starch and other soluble components form a surface film, resulting in the development of a characteristic shell–core structure. However, the compositional, structural, and physicochemical differences between shell and core flours, as well as their distinct contributions to rice texture, remain unclear. Therefore, in this study, the shell and core flours from cooked rice grains subjected to varying degrees of milling (DOMs, 0–60 %) were isolated and characterized. Results suggested that shell starches exhibited shorter chain lengths and smaller granule sizes, favoring the formation of lamellar structures with lower retrogradation tendency. In contrast, core starches contained longer chains and larger granules, which promoted compact aggregate formation and higher retrogradation propensity. As DOM increased, the shell flour showed elevated levels of amylose and short-chain amylopectin, enhancing rice stickiness. Meanwhile, the core flour exhibited a lower retrogradation tendency, accompanied by greater porosity and reduced structural integrity of core region, ultimately reducing rice hardness. These findings provide new insights into the spatial heterogeneity of starch structure and functionality in cooked rice, offering a theoretical basis for the quality improvement of rice-based products.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"175 ","pages":"Article 112511"},"PeriodicalIF":11.0,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146184810","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":"Role of cross-linking in improving the spinnability of biopolymers for production of electrospun fibers/nanofibers","authors":"Mohammad Mahdi Rostamabadi ,&nbsp;Fuat Topuz ,&nbsp;Elham Assadpour ,&nbsp;Hadis Rostamabadi ,&nbsp;Seid Mahdi Jafari","doi":"10.1016/j.foodhyd.2026.112426","DOIUrl":"10.1016/j.foodhyd.2026.112426","url":null,"abstract":"<div><div>Continuous electrospinning (ES) of high-quality natural polymers is essentially dictated by their natural chain entanglement and viscoelastic behavior. By adjusting polymer chain interactions and promoting solution stability, cross-linking (C_link) offers an adaptable route of widening the ES window and attaining fiber morphologies with more uniformity, quality, and consistency. Here, in this review, a structured summary of the principles/techniques of physico-chemical and dynamic C_link methodologies for biopolymers (e.g., alginate, chitosan, gelatin, etc.), is highlighted. Mechanistic influences on how C_link fine-tunes spinnability, jet stability, and fiber morphology are discussed, alongside practical guidance for solution preparation, ES protocols, and polymer selection. Recent progress connecting C_link circumstances to fiber quality/performance are illustrated, with architecture-feature relationships crucial for application-oriented design. The review further outlines novel applications across biomedical scaffolds, functional packaging, and environmental approaches, addressing current challenges and future opportunities. By pairing translational strategies with mechanistic insights, this work offers a robust framework for advancing the electro-spinnability of biopolymers <em>via</em> C_link control.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"175 ","pages":"Article 112426"},"PeriodicalIF":11.0,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146035997","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":"Phosphatidylcholine-protein interactions in soybean lipophilic protein: Structural basis for the foaming potential of β-conglycinin / glycinin /oil body protein binary complexes","authors":"Hanyu Song ,&nbsp;Bingru Li ,&nbsp;Siyu Wu ,&nbsp;Yuxuan Li ,&nbsp;Jingwen Xu ,&nbsp;Baokun Qi ,&nbsp;Shizhang Yan ,&nbsp;Lianzhou Jiang","doi":"10.1016/j.foodhyd.2026.112480","DOIUrl":"10.1016/j.foodhyd.2026.112480","url":null,"abstract":"<div><div>Soybean lipophilic protein (LP) is a protein-phospholipid complex with significant development potential; however, the molecular mechanism underlying its foaming properties remains poorly understood. This study systematically elucidated the interactions between phosphatidylcholine (PC) and the three major protein components (β-conglycinin (7S), glycinin (11S), and oil body-associated proteins (OBPs)) in LP, along with their effects on air-water interface characteristics, by reconstructing binary complexes based on the actual compositional ratios found in LP. Results showed that 7S, 11S, and OBPs accounted for 26.75 %, 19.89 %, and 16.65 % of the major protein mass in LP, respectively, which also contained 28.78 mg/g phospholipids. PC spontaneously binds to all three proteins via hydrophobic interactions (ΔG &lt; 0), with OBPs exhibiting the highest binding affinity (Ka). Upon complex formation, an increase in β-sheet content and static fluorescence quenching were observed, indicating conformational changes in the proteins. Meanwhile, surface hydrophobicity decreased for all protein-PC complexes; the ζ-potential increased for 7S/11S-PC complexes, whereas the particle size of the OBP-PC complex decreased while maintaining stable electrostatic potential; Furthermore, all complexes effectively reduced surface tension, enhanced diffusion and adsorption kinetics at the air-water interface. OBPs exhibited minimal foaming capacity due to severe self-aggregation; 7S and its complexes demonstrated superior foam capacity; whereas the 11S system formed more stable interfacial films, resulting in the most outstanding foam stability. This work provides mechanistic insights into protein-PC interactions, offering a theoretical foundation for understanding multicomponent synergy in LP and guiding the design of high-performance plant-based protein foaming agents.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"175 ","pages":"Article 112480"},"PeriodicalIF":11.0,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146036021","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":"Enhanced stability of bicontinuous bigels based on rapid in situ rapid conjugation of deacetylated chitosan and citral","authors":"Xue Li ,&nbsp;Kai Liu ,&nbsp;Bolin Xu ,&nbsp;Yang Li ,&nbsp;Qiyi Li ,&nbsp;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":"2026-06-01","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}