Food Hydrocolloids最新文献

{"title":"Solubility and bioavailability enhancement of baicalin by modified citrus pectin: preparation, in silico, in vitro and in vivo evaluation","authors":"Wenxin Ma ,&nbsp;Fangling Du ,&nbsp;Tongcheng Xu,&nbsp;Xiuxiu Wang,&nbsp;Baorui Li,&nbsp;Hao Yue,&nbsp;Min Jia,&nbsp;Aizhen Zong","doi":"10.1016/j.foodhyd.2025.112023","DOIUrl":"10.1016/j.foodhyd.2025.112023","url":null,"abstract":"<div><div>Baicalin, a flavonoid compound with various health benefits, faces significant limitations in its application due to poor solubility. Identifying a nontoxic, biodegradable, and readily available solubilizer is therefore critical for improving the solubility of baicalin and related analogues. This study aimed to evaluate the potential of citrus pectin and its acid-hydrolyzed derivatives to improve baicalin solubility, elucidating the underlying mechanisms of solubilization. Three fractions, MCP-1, MCP-2, and MCP-3, were obtained via partial acid hydrolysis followed by anion exchange chromatography. The results demonstrated that MCP-3, composed of 91.2 % galacturonic acid and 8.8 % rhamnose, exhibited the highest efficacy in enhancing baicalin solubility. Fourier transform infrared (FTIR) spectroscopy, X-ray diffraction (XRD), thermodynamic, molecular dynamics (MD) simulation confirmed that MCP-3 adopted a helical structure in solution, encapsulating baicalin within its helical cavity through hydrogen bonding between carboxyl and hydroxyl groups, as well as hydrophobic interactions and van der Waals forces. The MCP-3/baicalin complex exhibited good pH and temperature stability. Pharmacokinetic studies demonstrated that MCP-3 significantly enhanced the <em>in vivo</em> bioavailability of baicalin by 1.95-fold, and the complex exhibited low cytotoxicity. This study offers a promising strategy for the development of more effective flavonoid-based products.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"172 ","pages":"Article 112023"},"PeriodicalIF":11.0,"publicationDate":"2025-09-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145155243","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":"Mechanism of gum Arabic and mannoprotein complexes in suppressing bitter aftertaste and application in nutritious dysphagia gel beads","authors":"Binghong Gao ,&nbsp;Xiaomin Zang ,&nbsp;Xingmeng Lei ,&nbsp;Xiaochuan Huang ,&nbsp;Chuanyan Rao ,&nbsp;Yi Qin ,&nbsp;Dongqing Ye ,&nbsp;Yanlin Liu ,&nbsp;Yuyang Song","doi":"10.1016/j.foodhyd.2025.112031","DOIUrl":"10.1016/j.foodhyd.2025.112031","url":null,"abstract":"<div><div>This study investigated the bitter aftertaste-masking mechanism of grape seed extract (MOPC) and developed a dysphagia-friendly delivery system using gum Arabic (GA)-mannoproteins (2082) complexes. Multi-scale characterization revealed the mechanism by which GA-2082 suppresses the bitter aftertaste of MOPC. The results demonstrated that at an optimal concentration (0.6 mg/mL GA), the formation of stable ternary complexes with artificial saliva (AS) was driven by free hydroxyl groups, OH⋯<em>π</em> interactions, and hydrophobic forces. This promoted chromogenic amino acid folding and <em>α</em>-helix exposure within AS, ultimately leading to the formation of a dense AS-GA-2082 molecular network. This network effectively hindered the penetration of MOPC through the salivary pellicle. Texture analysis further indicated that GA-2082 exhibited strong tongue-adhesion properties, significantly reducing the retention of MOPC on the tongue surface and subsequent activation of bitter taste receptors. When incorporated into sodium alginate (SA) gel beads, GA-2082 improved the encapsulation efficiency of MOPC, achieving a maximum of 97.68 % at 0.75 % SA concentration, while maintaining safe swallowing characteristics. These findings demonstrated GA-2082 possessed dual functionality as both an effective bitter aftertaste-masking agent and a delivery vehicle for bioactive compounds, providing a promising nutrient-dense formulations for dysphagia management.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"172 ","pages":"Article 112031"},"PeriodicalIF":11.0,"publicationDate":"2025-09-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145155244","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":"Enhancement of rheological properties and oxidative stability of OSA starch oleogels by chitosan-EGCG conjugates: Influence of chitosan viscosity","authors":"Wenbo Miao ,&nbsp;David Julian McClements ,&nbsp;Junqing Han ,&nbsp;Hangyan Ji ,&nbsp;Zhengyu Jin ,&nbsp;Chao Qiu","doi":"10.1016/j.foodhyd.2025.112027","DOIUrl":"10.1016/j.foodhyd.2025.112027","url":null,"abstract":"<div><div>The rheology and oxidative stability of oleogels are critical factors impacting their application as solid fat substitutes in the food industry. For this reason, the influence of chitosan-EGCG conjugates on the rheology and oxidative stability of OSA-starch (OS) oleogels was examined. Conjugates were prepared from chitosan ingredients with different viscosities (low viscosity: &lt;200 mPa s and high viscosity: &gt;400 mPa s). Chitosan-EGCG conjugates (HCE) prepared from the high viscosity chitosan provided the highest antioxidant activity. Moreover, oleogel containing a high concentration of HCE (OS-HCE₁) had the highest viscoelasticity, thixotropic recovery (91.79 %), and oil-holding capacity (90.95 %), mainly attributed to the formation of more stable protective coatings. The oxidative stability analysis showed that HCE was most effective in delaying lipid oxidation of OS oleogels during storage. Finally, the potential of using the optimized oleogels (OS-HCE₁) as fat substitutes in bread products was evaluated by partially or fully substituting fat at levels of 0 %, 25 %, 50 %, 75 %, and 100 %. The results indicated that up to 50 % of commercial margarine could be replaced with oleogel in bread formulations without adversely affecting key quality parameters, including color, shape, texture, and sensory acceptability. In conclusion, this study offers an effective approach for improving both the structural and oxidative stability of OSA starch-based oleogels and provides valuable guidance for the formulation of healthier lipid systems in bakery applications.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"172 ","pages":"Article 112027"},"PeriodicalIF":11.0,"publicationDate":"2025-09-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145155256","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":"Upcycling seaweed residues via comparative pretreatment evaluation to develop functional protein ingredients for soy-based high-moisture meat analogs","authors":"Hyun Woo Choi ,&nbsp;Hyung Joo Kim ,&nbsp;Jungwoo Hahn ,&nbsp;Hyun-Seok Kim ,&nbsp;Young Jin Choi","doi":"10.1016/j.foodhyd.2025.111984","DOIUrl":"10.1016/j.foodhyd.2025.111984","url":null,"abstract":"<div><div>Growing environmental concerns and demand for sustainable diets are driving interest in alternative proteins for plant-based meat analogs. Seaweeds are an attractive option due to their high protein and nutrient content, but their tough cell walls make protein extraction challenging. Upcycled seaweed residues (USR) offer a sustainable solution for developing functional protein ingredients. Therefore, this study systematically evaluates seaweed residues subjected to different pretreatments, mildly acidic extraction, autoclaving, and enzymatic hydrolysis, to develop functional protein ingredients for soy-based high-moisture meat analogs. Among these, enzymatic hydrolysis significantly enhances the protein purity and solubility while reducing the water holding capacity and surface charge stability. When incorporated into Soy Protein Isolate (SPI) blends, USR alters the gelation behavior and enhances the gel strength and hardness owing to thermally induced polysaccharide–protein interactions. However, higher USR concentrations (≥15 %) compromise structural anisotropy, as indicated by lower texturization indices, disrupted fibrous structures, and an increased proportion of random coil structures. Chemical analysis further reveals weakened hydrogen bonds, disulfide bonds, and hydrophobic interactions at elevated USR levels, highlighting the adverse effects of excessive USR incorporation on protein network formation. Consequently, moderate inclusion (≤10 %) of USR proves optimal, achieving a balance between improved mechanical properties and desirable fibrous texture. These findings highlight the potential of enzymatically treated USR as a sustainable and functional protein-rich ingredient in advanced plant-based meat analog formulations.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"172 ","pages":"Article 111984"},"PeriodicalIF":11.0,"publicationDate":"2025-09-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145155327","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":"Exploring the role of phytochemical saponins in preventing the thermal aggregation of α-lactalbumin: A multi-dimensional spectrometric analysis","authors":"Yutong Jiang ,&nbsp;Xin Wen ,&nbsp;Jiahui Guo ,&nbsp;Hongyu Li ,&nbsp;Zhanmei Jiang ,&nbsp;Yun Chen","doi":"10.1016/j.foodhyd.2025.112029","DOIUrl":"10.1016/j.foodhyd.2025.112029","url":null,"abstract":"<div><div>This study investigated how tea saponin (Ts), gypenoside (Gyp), mogroside V (Mog), glycyrrhizic acid (GA) and stevioside (STE) affected the heat-induced aggregates of α-lactalbumin (Ala), focusing on the inhibition mechanisms of disulfide cross-linking and their impact on structural and physicochemical properties. SDS-PAGE and size exclusion chromatography (SEC) confirmed that saponins probably bound Ala monomers via hydrophobic forces and hydrogen bonds, inhibiting the formation of disulfide bonds in heat-induced Ala (H-Ala) and effectively decreasing polymer generation, with the inhibitory effect in the order of Gyp, GA, Ts, STE, Mog. LC-MS/MS analysis revealed that Ala (6), Ala (91), Ala (111) and Ala (120) were the most active sites for the disulfide cross-linking reaction in H-Ala. Specifically, the number of intramolecular disulfide cross-linked peptides of heat-induced Ala-Mog, Ala-STE, Ala-GA, Ala-Ts and Ala-Gyp complexes significantly decreased by 5, 6, 7, 8 and 10, respectively, compared with H-Ala. Notably, the heat-induced Ala-Gyp complex exhibited the highest absolute zeta potential, smallest particle size, and lowest hydrophobicity, which correlated with its superior inhibition of aggregation. The study highlighted the potential of saponins as natural additives for the stabilization of heat-sensitive proteins during thermal processing, offering new insights for food industry applications.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"172 ","pages":"Article 112029"},"PeriodicalIF":11.0,"publicationDate":"2025-09-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145216300","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 of pectin esterification degree in low-sodium myofibrillar hydrogels: Synergistic enhancement of mechanical properties, freeze-thaw resistance, and sustained digestive release","authors":"Lixian Zhang ,&nbsp;Zhenzhen Ge ,&nbsp;Lihua Zhang ,&nbsp;Wei Zong","doi":"10.1016/j.foodhyd.2025.112021","DOIUrl":"10.1016/j.foodhyd.2025.112021","url":null,"abstract":"<div><div>The severe deterioration of low-sodium myofibrillar protein (MP) gels represents a critical challenge for the development of minimally salted meat products. This study systematically explored the impacts of pectin esterification degree on the mechanical properties, digestion characteristics, and freeze-thaw stability of low-sodium MP hydrogel. The underlying mechanism was elucidated <em>via</em> integrating dynamic rheology, microstructure and molecular interaction forces. Results revealed that in low-sodium conditions, high/medium esterification pectin (H/M-pectin) promoted the formation of a continuous and dense cross-linked network through hydrophobic interactions and covalent bonding, thereby enhancing the mechanical strength and structural integrity of the composite gel. In high-sodium environments, pectin induced microstructural coarsening and pore enlargement through charge screening effects and facilitation of excessive protein aggregation. The incorporation of pectin regulated the digestion rates of MP by pore filling and covalent cross-linking, enabling the low-sodium-H/M-pectin composite gel with slow-release properties under simulated gastrointestinal conditions. Moreover, the compact structure of the low-sodium-H/M-pectin gel effectively suppressed ice crystal extrusion, manifesting superior freeze-thaw stability compared to high-sodium systems. This study provides fundamental insights into the design of functional hydrogel systems for innovative low-salt meat product applications.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"172 ","pages":"Article 112021"},"PeriodicalIF":11.0,"publicationDate":"2025-09-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145216315","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":"Viscoelastic characterisation of high protein ice cream: Predicting tactile sensory properties via time–concentration superposition and large amplitude oscillatory shear (LAOS) rheology","authors":"Simone Musollini ,&nbsp;Christos Soukoulis ,&nbsp;Roberta Tolve ,&nbsp;Lingxin You ,&nbsp;Matteo Zanoni ,&nbsp;Eugenio Aprea ,&nbsp;Flavia Gasperi ,&nbsp;Fabio Favati","doi":"10.1016/j.foodhyd.2025.112028","DOIUrl":"10.1016/j.foodhyd.2025.112028","url":null,"abstract":"<div><div>In the present work we report on the exploration of time concentration superposition principle (TCS) and non-linear dynamic rheology (LAOS) as useful instrumental tools for predicting tactile sensory modalities of ice cream at serving temperature (−14 °C). Three common tactile sensory properties of ice cream i.e., resistance to scooping (scoopability), creaminess and gumminess were assessed in high protein formulations differing in their protein to fat ratio (φ_P/F = 0.9 to 4) and protein source (milk protein concentrate (MPC) vs whey protein isolate-sodium caseinate (WPICAS) 1:1 blend). The complex viscosity – angular frequency data obeyed the TCS principle with the calculated shift factors reflecting effectively the compositional profile of ice creams i.e., a_c ∝ φ_P/F^1.16 and φ_P/F^2.23, b_c ∝ φ_P/F^−1.27 and φ_P/F^−1.75 for MPC and WPICAS fortified systems. LAOS assessment revealed a clear impact of protein type and φ_P/F on the shearing deformation of ice creams. MPC fortification and decrease in the φ_P/F enhanced the shear flowing ability of the ice creams. In all cases, the onset of shear stiffening and thickening behaviour was observed at shear stresses below the flow point, which indicates gel-like or colloid glass-like structures. According to partial least squares regression analysis, the TCS parameters (a_c and b_c), damping factor (tanδ) and the shear strain (γ_f) and elastic modulus (log <span><math><mrow><msubsup><mi>G</mi><mi>f</mi><mo>′</mo></msubsup></mrow></math></span>) at flow point were determined as the most important parameters predicting tactile sensory modalities on large deformation (spooning) such as scoopability, creaminess and gumminess.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"172 ","pages":"Article 112028"},"PeriodicalIF":11.0,"publicationDate":"2025-09-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145216297","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":"Fibrillation mechanism of soybean protein isolate and pea protein isolate composites: Focused on structure and rheological properties","authors":"Fei Teng ,&nbsp;Huiyue Chi ,&nbsp;Lijia Li ,&nbsp;Xixi Wu ,&nbsp;Yiting Gao ,&nbsp;Mengjie Geng","doi":"10.1016/j.foodhyd.2025.112019","DOIUrl":"10.1016/j.foodhyd.2025.112019","url":null,"abstract":"<div><div>Plant protein fibrils have significant potential for development in the food industry and have garnered considerable attention in recent years. However, the interactions between heterologous plant proteins during fibril formation remain largely unexplored. In this study, novel composite fibrils (PSF) were fabricated under acidic heating (pH 2.0, 85 °C, 0–24 h) using hybrid proteins prepared through pH-shifting treatment of soy protein isolate and pea protein isolate at varying ratios (1:2, 1:1, 2:1). SPI and PPI exhibited competitive growth mechanism within PSF, with the dominant protein component dictating the fibrillation process. When heated for 12 h, PSF with a SPI to PPI ratio of 1:1 demonstrated the strongest fibrillation capability and optimal rheological properties, achieving a fibril conversion rate exceeding 60 % and a β-sheet content of 45.21 %. Microstructural analysis revealed that increasing the PPI proportion resulted in smoother fibril surfaces (Rq = 1.33 nm), effectively suppressing the surface gelation tendency of soy protein fibrils. FTIR analysis confirmed hydrogen bonding and hydrophobic interactions as the primary driving forces for fibril formation, and the incorporation of PPI enhanced the structural stability of the fibrillar network. Molecular docking validated the binding potential between PPI and SPI, laying the theoretical groundwork for subsequent fibrillation. This study innovatively engineered structurally and functionally tunable plant protein fibrils to broaden their applications in the food industry.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"172 ","pages":"Article 112019"},"PeriodicalIF":11.0,"publicationDate":"2025-09-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145155207","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":"Advances in microwave-induced physical modification of flours: From structural changes to product development","authors":"Ainhoa Vicente ,&nbsp;Pedro A. Caballero ,&nbsp;Marina Villanueva ,&nbsp;Felicidad Ronda","doi":"10.1016/j.foodhyd.2025.112026","DOIUrl":"10.1016/j.foodhyd.2025.112026","url":null,"abstract":"<div><div>Cereal-based products are staple foods in most human diets worldwide. Starch, the main component of cereals, is commonly modified to enhance its functionality and overcome its functional limitations. Physical hydrothermal treatment assisted by microwave (MW) radiation has recently gained considerable attention as an energy-efficient and cost-efficient alternative to traditional thermal methods. While most studies have focused on starch modification, the direct modification of flours and whole grains has emerged as a promising strategy for producing more nutrient-dense ingredients with enhanced functionality. In this context, the role of proteins, the second major biopolymers, and the interplay between endogenous components in determining the behaviour of complex starchy matrices is of great interest. This review explores recent advances in MW treatment of flours and grains, with particular emphasis on the structural and functional changes in starch and proteins, and the implications of these changes for product development. MW treatment has been shown to effectively alter the morphology and structure of both biopolymers. This led to modifications in functionality that varied depending on the botanical source and treatment conditions. These modifications effectively enhance the quality of cereal-based food products, particularly gluten-free bread. Overall, MW technology offers a promising green strategy for developing customised, functional ingredients tailored to specific dietary needs, with growing relevance to broader applications in the food industry.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"172 ","pages":"Article 112026"},"PeriodicalIF":11.0,"publicationDate":"2025-09-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145216463","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":"Gelation dynamics and rheological properties of stirred yogurt alternatives manufactured from pulse protein isolates and their hydrolysates","authors":"Usman Amin,&nbsp;Haotian Zheng","doi":"10.1016/j.foodhyd.2025.112018","DOIUrl":"10.1016/j.foodhyd.2025.112018","url":null,"abstract":"<div><div>This study investigated the impact of enzymatic proteolysis of pulse proteins on the gelation dynamics, rheological, and tribology properties of plant-based yogurt alternatives (PBYA). Pea (PPI) and lentil (LPI) protein isolates were partially hydrolyzed to ∼1 % degree of hydrolysis. Both protein isolates (PPI and LPI) and their respective hydrolysates (PPH and LPH) were used to manufacture PBYA via fermentation. The fermentation-induced gelation took nearly 5 h to reach pH 4.3 as the target pH. The gel hardness of PPH- and LPH-PBYA gels was reduced compared to PPI- and LPI-PBYA. Hydrophobic interactions dominated in stabilizing the PBYA gel structure, irrespective of the hydrolysis treatment. In contrast, partial hydrolysis increased other intermolecular interactions in PPH- and LPH-PBYA, e.g., electrostatic, hydrogen bonding, and disulfide interactions. Despite such an increase, stirred PPH- and LPH-PBYA exhibited reduced gel particle size and increased syneresis rate. These phenomena may be attributed to the production of smaller-sized polypeptides during hydrolysis. Consequently, an increase in the overall population of reactive components for protein-protein interactions may be expected; this resulted in a more compacted structure of protein aggregates or network, but not necessarily strengthening the gel structure, which is mediated by hydrophobic interactions. PBYA made from hydrolysates (PPH or LPH) showed higher frequency dependence regarding rheological properties tested in LAOS regimes. These findings may direct new product development activities for improving PBYA texture with smoother and softer textural attributes. Future research efforts are recommended to explore approaches for improving PBYA gel phase stability.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"172 ","pages":"Article 112018"},"PeriodicalIF":11.0,"publicationDate":"2025-09-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145216884","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}