Food Hydrocolloids最新文献

{"title":"Rheological evidence for asymmetric phase separation mechanisms in soy glycinin's reentrant coacervation","authors":"Lang Qin ,&nbsp;Jian Guo ,&nbsp;Zhili Wan ,&nbsp;Weixiang Sun ,&nbsp;Xiaoquan Yang","doi":"10.1016/j.foodhyd.2025.111976","DOIUrl":"10.1016/j.foodhyd.2025.111976","url":null,"abstract":"<div><div>We mapped the isothermal (25 °C), isohydric (pH 7.0) phase diagram of soy-glycinin/NaCl/water and combined it with small-strain and large-amplitude oscillatory shear (LAOS) rheometry to relate salt-driven structural transitions to viscoelastic behavior. The diagram shows classic re-entrance—two single-phase regions separated by a protein-rich coacervate corridor—yet its boundaries are asymmetric: coacervates harvested at low salt (50 mM–100 mM) contain percolating 7S-trimer networks, whereas those formed at high salt (150 mM–200 mM) are populated by dispersed 11S-hexamers. Consequently, low-salt samples are solid-like (<em>G</em>′ &gt; <em>G</em>″ for <em>ω</em> ≳ 10 rad/s) and exhibit pronounced non-linearities (<em>I</em>_3/1 ≥ 0.1), while high-salt samples behave as weak power-law fluids (<em>G</em>′ ∝ <em>G</em>″ ∝ <em>ω</em>^0.8) with frequency-dependent shear thinning. Pipkin diagrams confirm a shift from frequency-independent plasticity at 50 mM to viscous flow at 200 mM. These results establish a direct link between glycinin's salt-controlled quaternary structure and the mechanics of its self-coacervates, providing design guidelines for plant-protein adhesives, encapsulants and other soft, sustainable materials.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"172 ","pages":"Article 111976"},"PeriodicalIF":11.0,"publicationDate":"2025-09-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145105220","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":"W1/O/W2 double emulsions stabilized by natural diosgenin and ultrasound-treated pea protein nanoparticles: A plant-based system for iron fortification","authors":"Chao Zhang ,&nbsp;Xuan Hu ,&nbsp;Yu Zhang ,&nbsp;Lingfei Li ,&nbsp;Shufang Zhao ,&nbsp;Quanfang Zhang ,&nbsp;Yanli Yu ,&nbsp;Wei Liu","doi":"10.1016/j.foodhyd.2025.111975","DOIUrl":"10.1016/j.foodhyd.2025.111975","url":null,"abstract":"<div><div>This study developed and optimized a fully natural W1/O/W2 double emulsion system for oral iron delivery, using diosgenin, a natural triterpenoid saponin, to stabilize the inner water–oil (W1/O) interface and pea protein nanoparticles (PPNs) to stabilize the outer oil–water (O/W2) interface. The optimal primary emulsion, containing 9 % diosgenin in the oil phase and a W1:O ratio of 2:8, exhibited excellent centrifugal and storage stability. External aqueous phases (W2) were prepared from 2 %, 4 %, and 6 % pea protein dispersions, which underwent ultrasound treatment followed by centrifugation to produce corresponding PPNs suspensions designated as PPN-2 %, PPN-4 %, and PPN-6 %, respectively. The primary iron-containing W1/O emulsion was dispersed into these W2 phases at a W1/O: W2 ratio of 2:8, yielding stable W1/O/W2 emulsions with iron encapsulation efficiencies exceeding 99 %. <em>In vitro</em> simulated digestion revealed that the emulsions with PPN-6 % effectively minimized iron release in the gastric phase (&lt;1 %) while promoting controlled release in the intestinal phase, thereby improving bioavailability and potentially reducing gastric irritation. Compared to synthetic PGPR-stabilized emulsions, the diosgenin-PPNs system demonstrated superior structural stability and digestive performance. This multilayered, food-grade emulsion system offers a promising, health-oriented alternative for iron fortification in functional foods.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"172 ","pages":"Article 111975"},"PeriodicalIF":11.0,"publicationDate":"2025-09-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145045393","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":"Gellan gum as a clean-label additive to improve whole wheat bread characteristics: A multimodal characterization approach","authors":"Debmalya Banerjee ,&nbsp;Bala Chakravarthy Neelapu ,&nbsp;Sivaraman Jayaraman ,&nbsp;Mihaela Skrt ,&nbsp;Maciej Jarzębski ,&nbsp;Nataša Poklar Ulrih ,&nbsp;Arfat Anis ,&nbsp;Kunal Pal","doi":"10.1016/j.foodhyd.2025.111952","DOIUrl":"10.1016/j.foodhyd.2025.111952","url":null,"abstract":"<div><div>This study delineated the concentration-dependent effects of gellan gum (GeG; 0–2.000 % w/w) on the physicochemical attributes of whole wheat bread (WWB) formulations. Nine formulations were systematically examined using a multimodal analytical framework comprising surface microscopy, colorimetric analysis, hyperspectral imaging, texture profile analysis, stress relaxation studies, and FTIR spectroscopy. Among the tested concentrations, the 0.125 % GeG (GG0.125) formulation demonstrated the most balanced alignment with the control (GG0.000, without GeG). Texture profile analysis revealed that GG0.125 exhibited comparable hardness, springiness, cohesiveness, and resilience to the control. Stress relaxation analysis further confirmed that GG0.125 preserved viscoelastic behaviour, as evident from the comparable F₆₀ (1.344 N) and %SR (47.217 %) values to those of the control. Microscopic examination revealed a smoother crumb surface and more homogeneously distributed pores in the GG0.125 sample, indicating an enhanced internal structure. FTIR spectra showed strong correlation with the control (ρ = 0.99639) and minimal shifts in amide and carbohydrate bands, reflecting preserved molecular organization. Hyperspectral imaging at 477, 513, 523, and 619 nm further revealed uniform chromophore distribution in GG0.125, comparable to that of the control. Collectively, these findings establish 0.125 % GeG as the optimal concentration capable of maintaining the structural, mechanical, and molecular features of the control formulation, thereby supporting its application in clean-label bread reformulation.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"172 ","pages":"Article 111952"},"PeriodicalIF":11.0,"publicationDate":"2025-09-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145216469","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":"Structural and functional characterisation of hydrogels prepared from Porphyridium purpureum under acidic conditions","authors":"Lora Tubić ,&nbsp;Milorad Dragić ,&nbsp;Marija S. Nikolić ,&nbsp;Marija Stojadinović ,&nbsp;Zorana Jovanović ,&nbsp;Steva M. Lević ,&nbsp;Vladimir Pavlović ,&nbsp;Milan Nikolić ,&nbsp;Nikola Gligorijević ,&nbsp;Simeon Minić","doi":"10.1016/j.foodhyd.2025.111963","DOIUrl":"10.1016/j.foodhyd.2025.111963","url":null,"abstract":"<div><div>The red microalgae <em>Porphyridium purpureum</em> exhibits exceptional nutritional properties due to rich protein content, extracellular polysaccharides, polyunsaturated fatty acids, vitamins, and minerals. The coloured and bioactive phycobiliproteins make this microalga a valuable source for developing innovative food products. Herein, we developed a simple procedure to induce the formation of coloured hydrogels (POR) from <em>P. purpureum</em> under acidic conditions (pH 2) by inhibiting the repulsion of charged groups and facilitating polysaccharide chain association. We further investigated the effects of adding alginate at a 0.5 % concentration on the gel structure (POR ALG) and techno-functional properties. The resulting vividly coloured hydrogels were characterised in terms of microstructure (<em>via</em> SEM and confocal microscopy), functional groups (FTIR), rheological behaviour, water uptake and water-holding capacity, digestibility, and antioxidant activity. Alginate addition significantly improved the gel consistency (POR ALG), decreased porosity, and increased the storage modulus by one order of magnitude compared to POR gel. Confocal microscopy revealed that alginate inhibited phycobiliprotein agglomeration, reduced fluorescence, and provided more uniform protein distribution. The water uptake capacity was notably higher in POR ALG hydrogel at pH 2, whereas POR hydrogel had the highest capacity at neutral pH. <em>In vitro</em> digestion studies demonstrated that the hydrogels resisted gastric digestion, while bioactive (chromo)peptides are released in the intestinal phase, thereby preserving their antioxidant activity. Lyophilisation emerged as the preferred drying method, maintaining rehydration potential and structural integrity. The developed <em>P. purpureum</em>-based hydrogels demonstrate significant potential as functional food ingredients, offering bioactive benefits, vibrant colour stability, and protection for sensitive molecules during digestion.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"172 ","pages":"Article 111963"},"PeriodicalIF":11.0,"publicationDate":"2025-09-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145045395","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":"Printability and interfacial performance of emulsion gels and bigels in multi-material dual and coaxial food 3D printing","authors":"Linnea Johansson ,&nbsp;Isabel Badager ,&nbsp;Annika Krona ,&nbsp;Mehdi Abdollahi","doi":"10.1016/j.foodhyd.2025.111964","DOIUrl":"10.1016/j.foodhyd.2025.111964","url":null,"abstract":"<div><div>Structured fats like emulsion gels and bigels have emerged as promising animal fat substitutes for plant-based meat analogs. This study investigated the printability, rheological behavior, and interfacial compatibility of emulsion gels and bigels in combination with pea protein isolate (PPI) for extrusion-based single- and multi-material dual and coaxial 3D food printing (3DFP). Rheological analysis confirmed that despite having both systems exhibiting shear-thinning and thixotropic behavior, bigels demonstrate higher mechanical strength (G’ = 1000 Kpa vs 10 Kpa) and structural integrity (yield stress = 500 Pa vs 200 Pa). These properties translated into better print fidelity, with bigels maintaining defined structures across a range of temperatures (30–60 °C) in single-material 3DFP while emulsion gels were prone to phase separation, deformation and collapsing. In multi-material 3DP with PPI, bigels consistently demonstrated clear material separation, forming distinct core-shell structures in coaxial setups as well as maintaining well-defined, evenly distributed phases in dual extrusion. In contrast, emulsion gels exhibited smearing, irregular distribution, and poor interfacial definition in both setups, indicating weaker phase stability and compatibility with the protein matrix. Confocal laser scanning microscopy confirmed better interfacial phase boundaries between bigels and PPI, aligning with rheological and printing outcomes. In conclusion, bigels show high promise as multi-functional structuring agents and fat substitutes in multi-material 3DFP, while emulsion gels require further optimization to enhance their print performance and material compatibility.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"172 ","pages":"Article 111964"},"PeriodicalIF":11.0,"publicationDate":"2025-09-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145045387","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 protein gelation and nutritional properties in pea protein gels through enzymatic deamidation","authors":"Lijuan Luo ,&nbsp;Ping Li ,&nbsp;Yuanyuan Deng ,&nbsp;Guang Liu ,&nbsp;Yan Zhang ,&nbsp;Xiaojun Tang ,&nbsp;Pengfei Zhou ,&nbsp;Zhihao Zhao ,&nbsp;Jiarui Zeng ,&nbsp;Mingwei Zhang","doi":"10.1016/j.foodhyd.2025.111968","DOIUrl":"10.1016/j.foodhyd.2025.111968","url":null,"abstract":"<div><div>Pea protein exhibits poor gelation properties due to low cysteine content, limiting its application as a structural ingredient in food systems. This study investigated the effects of enzymatic deamidation on calcium-induced thermal gelation of pea protein and elucidated the mechanism of improved digestibility through microstructural modification. Results show that enzymatic deamidation significantly improves calcium-induced thermal gelation of pea protein isolate, reducing minimum gelation concentration from 9 % to 3 % and increasing calcium tolerance from 20 mM to 40 mM compared to native pea protein isolate (NPPI). Microstructural analysis revealed deamidated PPI (DPPI) formed homogeneous fine-stranded networks, while NPPI developed rough porous networks composed of large-sized protein aggregates. This structural transformation, attributed to increased carboxyl groups facilitating calcium bridging, enhanced gel strength, water-holding capacity, and digestive nutritional properties. The fine-stranded network structure of DPPI gels significantly improved protein digestibility (68–86 % vs. 57 %) and calcium bioavailability (85–90 % vs. 77 %) by promoting contact between digestive enzymes and protein substrates, increasing the accessibility of cleavage sites and facilitating the release of calcium-peptide complexes. Deamidation offers a promising strategy for creating pea protein gels with superior functionality and nutritional value.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"172 ","pages":"Article 111968"},"PeriodicalIF":11.0,"publicationDate":"2025-09-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145105221","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":"Non-thermal extraction and modification of chia seed mucilage using Pulsed electric field","authors":"Divyang Solanki ,&nbsp;Jervee M. Punzalan ,&nbsp;Indrawati Oey ,&nbsp;Adeline Meriaux ,&nbsp;Keith C. Gordon ,&nbsp;Bhesh Bhandari ,&nbsp;Jatindra K. Sahu ,&nbsp;Sangeeta Prakash","doi":"10.1016/j.foodhyd.2025.111954","DOIUrl":"10.1016/j.foodhyd.2025.111954","url":null,"abstract":"<div><div>This research investigates a non-thermal, chemical-free method for extracting and modifying chia seed mucilage (CSM) using Pulsed Electric Field (PEF) technology. The impact of different specific energy inputs - low (PEF1), medium (PEF2), and high (PEF3) on the yield, physical, functional, structural (FTIR), thermal (DSC), and microstructural (SEM) properties of CSM was investigated. PEF treatment significantly (<em>p &lt; 0.05</em>) increased mucilage yields: PEF2 (8.27 ± 0.83 %), PEF3 (8.02 ± 0.26 %), and PEF1 (7.20 ± 0.17 %) compared to the untreated control CSM (5.75 ± 1.46 %). Higher energy input (PEF3) altered proximate composition, colour, true density, and functional properties such as water holding capacity (WHC) and oil holding capacity (OHC). Low and medium PEF enhanced the colour profile of CSM. However, PEF1 exhibited significantly (<em>p &lt; 0.05</em>) higher storage (<em>G′</em>) and loss (<em>G′′</em>) moduli than PEF3. Solubility and zeta potential were found to be dependent on the pH of the medium. Modification of CSM through PEF was also revealed from the changes observed in the structural, thermal, and microstructural properties. PEF can be a sustainable, chemical-free approach for the mucilage extraction and modification, supporting the development of plant-based food nutrient-dense ingredients.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"172 ","pages":"Article 111954"},"PeriodicalIF":11.0,"publicationDate":"2025-09-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145105216","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":"Sub-denaturing thermal pretreatment modulates lactoferrin-quercetin interactions: Structural dynamics, binding mechanisms, and functional synergy","authors":"Si-Jie Wu ,&nbsp;Qi-Bin Kuang ,&nbsp;Ran Feng ,&nbsp;Ran Meng ,&nbsp;Qiu-Ya Ji ,&nbsp;Han Tao ,&nbsp;Bao-Cai Xu ,&nbsp;Bao Zhang","doi":"10.1016/j.foodhyd.2025.111939","DOIUrl":"10.1016/j.foodhyd.2025.111939","url":null,"abstract":"<div><div>Heat treatment, as one of the most common processing methods in protein modification, has unclear mechanisms affecting protein-polyphenol interactions. This study investigated the effects of sub-denaturing temperature pretreatment on protein structure-function relationships and their interactions with polyphenols using the quercetin-lactoferrin (Que-LF, QLF) system as a model. Results demonstrated that among 25–55 °C gradient heat treatments, LF pretreated at 40 °C (LF40) formed metastable aggregates through moderate structural unfolding, with significantly exposed hydrophobic cavities that enhanced binding affinity to Que (<em>K</em>_<em>a</em> = 7.11 × 10⁵ L/mol). Preheating optimized the conformational flexibility and spatial compatibility of LF binding pockets, enabling Que to embed into hydrophobic cavities via hydrophobic interactions (<em>ΔH</em> = 23.82 kJ mol⁻¹, <em>ΔS</em> = 188.27 J mol⁻¹·K⁻¹) and multiple hydrogen bonding networks. The QLF40 complex exhibited optimal binding free energy (−85.1 kJ/mol) and conformational stability. Furthermore, Que binding synergistically improved thermal stability (2 °C increase in denaturation temperature) and antioxidant activity (64.7 % DPPH and 98.4 % ABTS scavenging rates) of the complex through masking hydrophobic sites, strengthening hydrogen bond networks, and inducing local structural rigidity. This study provides theoretical foundation for designing efficient active ingredient delivery systems based on controlled protein structural modification.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"172 ","pages":"Article 111939"},"PeriodicalIF":11.0,"publicationDate":"2025-09-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145045878","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":"Comparative study of cross-linking strategies for β-lactoglobulin-hyaluronic acid-neochlorogenic acid ternary complexes: Structural characteristics and functional implications for curcumin delivery","authors":"Tinglan Yuan ,&nbsp;Tian Tian ,&nbsp;Tingyu Wang ,&nbsp;Xue Gao ,&nbsp;Yaoruixi Yang ,&nbsp;Gongshuai Song ,&nbsp;Danli Wang ,&nbsp;Ling Li ,&nbsp;Ziyuan Wang ,&nbsp;Jinyan Gong","doi":"10.1016/j.foodhyd.2025.111957","DOIUrl":"10.1016/j.foodhyd.2025.111957","url":null,"abstract":"<div><div>To elucidate the effects of different cross-linking methods on the structural and functional properties of ternary complexes, this study systematically engineered β-lactoglobulin-hyaluronic acid-neochlorogenic acid (β-Lg-HA-3CQA) complexes using six distinct strategies: non-covalent cross-linking, ultrasonic-assisted treatment, enzymatic grafting, free radical cross-linking, genipin conjugation, and the Maillard reaction. Structural and functional analyses demonstrated that covalent strategies, significantly outperformed non-covalent and ultrasonic treatment in terms of structural integrity and functional efficacy. Notably, the Maillard-enzymatic approach exhibited the optimal performance, with a solubility of 93.71 %, 3CQA binding content of 73.05 μg/mL, and curcumin entrapment efficiency of 86.55 %. It also significantly enhanced the system stability, as well as its thermal and environmental tolerance. In contrast, ultrasonic treatment offered only transient improvements in dispersion and failed to overcome the intrinsic structural instability of non-covalent complexes. This systematic comparison of multiple cross-linking methods provides both a theoretical framework and practical foundation for optimizing the protein-polysaccharide-polyphenol complexes, thereby enhancing their functional properties and broadening their applicability in food and pharmaceutical fields.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"172 ","pages":"Article 111957"},"PeriodicalIF":11.0,"publicationDate":"2025-09-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145026962","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":"Juiciness of plant-based meat analogues is driven by serum release rather than serum composition and viscosity","authors":"Yifan Zhang ,&nbsp;Luka Mtiulishvili ,&nbsp;Guido Sala ,&nbsp;Elke Scholten ,&nbsp;Markus Stieger","doi":"10.1016/j.foodhyd.2025.111950","DOIUrl":"10.1016/j.foodhyd.2025.111950","url":null,"abstract":"<div><div>Juiciness and fattiness are key drivers of consumer acceptance for plant-based meat analogue (PBMA) patties. Previous studies showed that these attributes correlated strongly with the amount of released serum (expressible fluid) during mastication, while the role of serum properties remains unclear. This study aimed to reveal the effects of serum quantity, composition and viscosity on juiciness and fattiness of PBMA patties, identifying the main drivers for these sensory attributes. A factorial design (2 × 3 × 2) was used to systematically vary serum properties by varying raw patty formulations in hydration level of textured vegetable proteins (TVPs), fat and maltodextrin content. This resulted in patties which varied in quantity of serum release from 8 to 20 %w/w, and varied in serum water content from 29 to 85 %w/w, fat content from 12 to 65 %w/w, and serum viscosity from 6 to 360 mPa⋅s. As expected, juiciness and fattiness increased with increasing serum release. Systematic variation in serum viscosity and fat content allowed separation of their effects. Increasing serum viscosity alone did not affect juiciness and fattiness. Fattiness rose with increasing serum fat content, while juiciness remained unaffected. Fat thus contributed to those mouthfeel attributes not only through its effect on viscosity, but potentially also through other effects, such as lubrication. These results showed that juiciness and fattiness arise from different mechanisms. Juiciness of PBMA patties was primarily driven by the quantity of serum released upon compression rather than serum composition and viscosity, while fattiness was influenced by both serum quantity and fat content.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"172 ","pages":"Article 111950"},"PeriodicalIF":11.0,"publicationDate":"2025-09-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145045391","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}