Food Hydrocolloids最新文献

{"title":"Characterisation of enzymatically-induced arabinoxylan-protein interactions in gluten-free model batter","authors":"Ulrich Sukop ,&nbsp;Katharina Hoefler ,&nbsp;Victoria Wiesmann ,&nbsp;Philipp L. Fuhrmann ,&nbsp;Mario Jekle ,&nbsp;Regine Schoenlechner ,&nbsp;Konrad J. Domig ,&nbsp;Denisse Bender ,&nbsp;Stefano D'Amico","doi":"10.1016/j.foodhyd.2026.112458","DOIUrl":"10.1016/j.foodhyd.2026.112458","url":null,"abstract":"<div><div>The absence of a viscoelastic gluten network remains a major factor limiting the quality of gluten-free (GF) bakery products. This study examined whether arabinoxylans (AX) from maize (alkaline-extracted, M-CEAX; xylanase-extracted, M-XEAX) and wheat (wheat-extracted AX, WEAX), in combination with maize gluten meal (MGM), can form a cohesive joint polymeric network resembling gluten. Cross-linking was enzymatically induced using laccase or glucose oxidase (GOX) with horseradish peroxidase (HRP). Model batters were assessed through rheological tests (amplitude, frequency, time sweep) and physicochemical methods (particle and molecular size, polymer solubility and bound phenolic/ferulic acid) to evaluate AX-protein interactions. Rheological analyses revealed that laccase increased elasticity in M-CEAX systems but failed to promote strong AX-protein interactions. In contrast, GOX-HRP significantly enhanced the storage modulus (G′) in M-CEAX-MGM added model batters, suggesting stronger cross-linking. Particle size results supported this, showing larger d-values and higher span, especially in enzymatically treated M-CEAX formulations. AX solubility increased with M-CEAX alone but remained unchanged with protein addition. Bound phenolic content was higher in laccase-treated than in GOX-HRP-treated systems, indicating weaker cross-linking. Size exclusion chromatography (SEC) showed increased molecular weight in M-CEAX and MGM model batters treated with GOX-HRP, whereas M-CEAX-MGM combinations showed no clear size shift, which can be attributed to large insoluble aggregates not detected by the method. Overall, these findings highlighted the importance of polymer structure and enzyme specificity in modulating network formation. The results suggested that AX-protein interactions can enhance GF batter viscoelasticity and stability, offering a promising strategy to improve the structure of GF bakery products.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"175 ","pages":"Article 112458"},"PeriodicalIF":11.0,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146036018","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":"Molecular insights into whey protein fibril-sodium alginate-piperine complexes for stabilizing astaxanthin emulsions with improved bioaccessibility","authors":"Junquan Zheng ,&nbsp;Daobang Tang ,&nbsp;Xueming Liu ,&nbsp;Xuping Wang ,&nbsp;Yaosheng Lin ,&nbsp;Mingjun Zhu ,&nbsp;Jingrong Cheng","doi":"10.1016/j.foodhyd.2026.112437","DOIUrl":"10.1016/j.foodhyd.2026.112437","url":null,"abstract":"<div><div>Astaxanthin (AST) suffers from poor water solubility, low stability, and limited oral bioavailability, which restrict its practical application. To address these issues, this study developed a whey protein fibril-sodium alginate (WPF/SA) stabilized Pickering emulsion for the co-delivery of AST and piperine (Pip), the latter being a natural bioenhancer known to improve intestinal absorption by inhibiting drug-metabolizing enzymes and efflux transporters. The interaction mechanisms among WPF, SA, and Pip, the emulsion's environmental stability, and the bioavailability-enhancing effect were systematically investigated using molecular docking, spectroscopic analysis, emulsion characterization, and a Caco-2 cell model. Results indicated that Pip binds to WPF via hydrophobic interactions, while SA associates through electrostatic forces at pH 5.0. These interactions led to a reduction in β-sheet content from 28.73 % to 23.58 % and an increase in random coil from 23.18 % to 28.88 %. The SA incorporation significantly improved emulsion stability, raising the absolute zeta potential from +9 mV to −38.5 mV and enhancing rheological properties. Compared to the SA-free system, the W(P)/SA (1:2)-E increased AST retention by 0.85-fold after 90 °C heating and by 1.26-fold after UV irradiation. In Caco-2 cells, Pip was shown to significantly enhance the cellular uptake of AST. The highest uptake level (65.79 ng/μg protein) was observed at a W(P) to SA ratio of 1:2, representing a 1.28-fold increase over the WPF-stabilized emulsion, and indicating a clear synergistic effect between Pip and SA. This study offers an effective strategy for enhancing both the stability and bioavailability of AST, supporting its potential application in functional foods and nutraceuticals.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"175 ","pages":"Article 112437"},"PeriodicalIF":11.0,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146035990","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":"A CMCS/TA-Fe hydrogel film based on metal-phenolic network coordination for intelligent preservation of cooked meat","authors":"Shiqi Yang ,&nbsp;Donglei Luan ,&nbsp;Yahui Wen ,&nbsp;Bin Zhao ,&nbsp;Tianxi Yang ,&nbsp;Juan Yan","doi":"10.1016/j.foodhyd.2026.112539","DOIUrl":"10.1016/j.foodhyd.2026.112539","url":null,"abstract":"<div><div>Ready-to-eat cooked meat products contain high levels of moisture and nutrients, making them highly vulnerable to microbial contamination and subsequent quality degradation during storage. Therefore, the development of green packaging materials that integrate active preservation functions with freshness indication is of great significance. In this work, a carboxymethyl chitosan (CMCS)/tannic acid (TA)-Fe³⁺ coordination hydrogel (CMCS/TA-Fe) film with favorable biocompatibility and degradability was fabricated through a facile coordination-driven self-assembly strategy, leveraging the multiple interactions among CMCS, TA, and ferric ions (Fe³⁺). The introduction of the TA-Fe³⁺ metal-polyphenol markedly enhanced the mechanical performance of the film, increasing its storage modulus (G′) to approximately 2.4 × 10⁴ Pa, and endowed it with efficient photothermal conversion capability. Under near-infrared irradiation at 808 nm, the film surface temperature rapidly increased to 103 °C within 15 min, enabling complete inactivation of <em>Escherichia coli</em> and <em>Staphylococcus aureus</em>. In addition, the dynamic coordination structure of TA-Fe³⁺ exhibited pH-responsive chromatic behavior in a model system, resulting in distinct and reversible color changes under different pH conditions. These color variations suggest the potential of the CMCS/TA-Fe film as a visual indicator for freshness-related pH changes. When applied to the refrigerated preservation of cooked chicken breast, the CMCS/TA-Fe film combined with near-infrared irradiation effectively inhibited microbial proliferation, delayed pH increase, reduced moisture loss, and preserved textural and sensory quality. Overall, this study demonstrates a multifunctional and environmentally friendly hydrogel film that integrates photothermal antibacterial activity with a pH-responsive color indication function, offering a promising strategy for intelligent food packaging applications.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"175 ","pages":"Article 112539"},"PeriodicalIF":11.0,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146184765","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":"Physicochemical characteristics changes in post-ripening of wheat flour mill streams: Effects on dough properties and steamed bread quality","authors":"Meng-Li Zhang ,&nbsp;Xiao-Na Guo ,&nbsp;Xiao-Hong Sun ,&nbsp;Ke-Xue Zhu","doi":"10.1016/j.foodhyd.2026.112523","DOIUrl":"10.1016/j.foodhyd.2026.112523","url":null,"abstract":"<div><div>This study investigated the effects of three mill streams (representing distinct parts of wheat grain) and straight run flour (a blend of mill streams) on dough characteristics and steamed bread quality during post-ripening. Throughout the post-ripening period, the mill streams (2M) from the wheat endosperm exhibited a more stable dough stabilization time, while the bran-rich mill streams (2S and 2B) displayed a downward trend. In addition, when mill streams were post-ripened for 20 days, the viscoelasticity and gas retention of dough were enhanced, and internal crumb structure in steamed bread was improved. After mill streams post-ripening, the increase in glutenin macropolymer content promoted formation of a dense and elastic gluten network structure in dough. The results demonstrated that post-ripening promoted protein aggregation of wheat flour mill streams. Among them, 2M streams (the second reduction) showed the slightest changes in protein properties, 2S streams (the second sizing) and 2B streams (the second break) exhibited a significant decline in free sulfhydryl content and gliadin content, and an increase in glutenin content. More pronounced changes in gelatinization properties and peroxidase activity were observed in the 2S and 2B streams. Principal component analysis indicated that the gluten network formation promoted by mill streams post-ripening contributed more obvious to improved quality of steamed bread dough. These results proved the differences in mill streams post-ripening and provided a valuable theoretical basis for improving steamed bread dough with specific mill streams during post-ripening.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"175 ","pages":"Article 112523"},"PeriodicalIF":11.0,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146184809","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":"Sulfatase-induced in situ gelation of κ-carrageenan provides an enzyme-based texturizing solution for plant-based milk systems","authors":"Alexander Fuchs ,&nbsp;Enrico Hupfeld ,&nbsp;Volker Sieber","doi":"10.1016/j.foodhyd.2026.112519","DOIUrl":"10.1016/j.foodhyd.2026.112519","url":null,"abstract":"<div><div>Carrageenans are essential texturizers in various dairy products, where they form elastic gel networks through specific interactions with casein micelles, enabling effective structure formation even at low concentrations. Plant-based milk alternatives on the other side, such as almond- or oat-based products, recently experience a rising consumer demand, but are devoid of these protein–polysaccharide interactions, which poses major challenges for their efficient texturization. Consequently, new mild, adaptable, and label-friendly gelation strategies are required to achieve desirable texture and stability in such systems. Here, we present an enzymatic approach to trigger gel formation in non-dairy matrices using the carrageenan sulfatase CaCgS1 from <em>Cellulophaga algicola</em> DSM 14237. The enzyme catalyzes the desulfation of κ-carrageenan to a κ/β-hybrid carrageenan under mild conditions, which triggers the gelation of the reaction product in-situ and yields a homogenous hydrogel with enhanced gel strength and thermal stability by an increased helical aggregation activity of the modified polymer chains. The increased gel strength relies exclusively on the cleavage of sulfate groups without the need to alter the ionic composition or increase the polymer concentration. Applied to plant-based milk formulations, this process enables the generation of homogeneous, stable textures at low polymer concentrations. The concept provides a novel method for structuring plant-based foods and expands the application scope of enzyme-induced gelation in modern food design, and beyond.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"175 ","pages":"Article 112519"},"PeriodicalIF":11.0,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146184876","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":"Formation of soy protein amyloid fibrils-tannic acid complexes: structure remodeling of fibrils and enhanced antioxidant properties","authors":"Shunan Jia ,&nbsp;Xiaoshuai Wang ,&nbsp;Hongyan Jin ,&nbsp;Yingxue Chang ,&nbsp;Yan Zhang ,&nbsp;Zejian Xu ,&nbsp;Xiaonan Sui","doi":"10.1016/j.foodhyd.2026.112420","DOIUrl":"10.1016/j.foodhyd.2026.112420","url":null,"abstract":"<div><div>Functional polyphenol, such as tannic acid (TA), possesses numerous desirable characteristics for food applications. However, their instability and resulting low bioavailability currently limit their use within the food industry. Amyloid fibrils represent a desired food matrix for improving the bioavailability and bioaccessibility of polyphenols, owing to their highly ordered structure and abundant functional groups on their surface. In the present work, soy protein amyloid fibrils (SAFs), <em>β</em>-conglycinin (7S globulin) amyloid fibrils (7SAFs) and glycinin (11S globulin) amyloid fibrils (11SAFs) loaded with high content of TA were successfully prepared and the evolution of fibrils polymorphic structure was investigated. Structural analysis revealed that the incorporation of TA induced the cracking of long rigid fibrils and the formation of thicker and more clustered of short-curved fibrils. Concurrently, TA induced an increase in <em>β</em>-sheet contents, from 55.12 % to 65.84 % in SAFs and from 52.64 % to 60.33 % in 7SAFs. 11SAFs showed the highest TA loading rate of 94.76 % compared to that of SAFs and 7SAFs. However, SAFs and 7SAFs showed high TA retention rate of about 79.02 % and 78.89 % in ultraviolet experiment, respectively. In addition, the formed complexes demonstrated high antioxidant activity (ABTS: 76.98 %), offering a promising approach for designing amyloid fibril-based antioxidant materials. This research shed lights into the structural rational modulation of SAFs, 7SAFs and 11SAFs with TA, and paved the way for the preparation of value-added food ingredient composed of food protein amyloid fibrils and TA.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"175 ","pages":"Article 112420"},"PeriodicalIF":11.0,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146074507","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":"Digestible properties and formation mechanism of rice starch-gelatin-tea polyphenols ternary composite gel: Effect of tea polyphenol concentration, type of gelatin and gelatin/starch ratios","authors":"Chen-Chen Wang ,&nbsp;Jing-jing Xu ,&nbsp;Yan Liu ,&nbsp;Fan Wang ,&nbsp;Ran Feng ,&nbsp;Bao Zhang","doi":"10.1016/j.foodhyd.2026.112502","DOIUrl":"10.1016/j.foodhyd.2026.112502","url":null,"abstract":"<div><div>In order to develop starch-based food with low digestibility and high nutritional quality, this study constructed and systematically discussed the ternary composite gel system of rice starch, gelatin and tea polyphenols. The effects of rice starch-to-gelatin ratio (ranging from 0:8 to 6:2) and tea polyphenol (TP) concentration (0.1 %, 0.3 %, and 0.5 %) on the formation mechanism and functional properties of ternary composite gels. Compared to type A gelatin (GA), type B gelatin (GB)-based gels exhibited significantly enhanced water-holding capacity (WHC), although WHC decreased from 97.75 % to 75.57 % with increasing starch proportion. The incorporation of TP at 0.3 % concentration was identified as optimal for enhancing the gel network through polyphenol-mediated cross-linking, while higher TP content (0.5 %) induced phase separation and structural heterogeneity. An optimal starch-to-gelatin ratio of 4:4 with 0.3 % TP produced the most uniform gel network. At this and higher ratios, V-type crystalline complexes formed between starch and TP, which correlated with a substantial reduction in rapidly digestible starch content to 54.27 %. The strong electrostatic attraction of GA-TP effectively immobilized TP. In contrast, the non-electrostatic and weak interactions between GB and TP facilitated the formation of a V-type structure. These revealed that GA and GB regulate starch digestion through physical barriers and promote the formation of V-type complexes, respectively. These findings provide crucial insights for designing functional starch-based foods with tailored textures and improved nutritional profiles.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"175 ","pages":"Article 112502"},"PeriodicalIF":11.0,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146074504","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":"Elucidating the fibril formation and degradation process of soy protein: identification of fibril-forming regions and insights into the self-assembly mechanism","authors":"Hekai Zhao ,&nbsp;Yuyang Huang ,&nbsp;Baokun Qi ,&nbsp;Yang Li","doi":"10.1016/j.foodhyd.2026.112478","DOIUrl":"10.1016/j.foodhyd.2026.112478","url":null,"abstract":"<div><div>Plant protein fibrils have demonstrated increasing potential in food processing and the development of novel materials. Understanding of their fibrillation mechanisms at the molecular level, particularly through the identification of fibril-forming regions, is crucial for the controllable structural design. In this study, the fibrillation of soy protein was categorized into a formation phase (0–24 h) and a degradation phase (&gt;24 h), with a focus on the assembly and identification of fibril-forming regions. SDS-PAGE analysis revealed small peptides were rapidly released from the subunits within the first 12 h, while Th T fluorescence indicated a very short lag phase (0.15 h) and a rapid fibril growth rate of 0.36 FU h⁻¹. AFM imaging showed the contour length of the fibrils increased to approximately 250 nm at 24 h during formation period, with gradually enhancement in flexibility, accompanied by increased β-sheet content. Prolonged incubation disrupted intermolecular hydrogen bonds, causing detachment of non-core regions and aggregation of fibril cores. TIMS-TOF-MS identified 190 fibril-forming peptides, including 104 core peptides with low net charge and high hydrophobicity. Compared with 11 S, the fibril-core regions exhibited a higher coverage rate in 7 S and constituted a larger proportion of fibril-forming peptides. Molecular dynamics simulations revealed that the β-residues, β-sheet content, and inter-peptide hydrogen bonds of the representative fibril core peptide system increased over time, indicating a pronounced fibrillation propensity. This study systematically elucidates the self-assembly process of soy protein nanofibrils, providing a theoretical basis for their structural regulation and functional design.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"175 ","pages":"Article 112478"},"PeriodicalIF":11.0,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146074552","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":"Alginate polysaccharides stabilized yolk W/O/W emulsions for DHA-based multinutrient delivery: Interfacial design, stability and spray-dried powder characteristics","authors":"Lin Deng ,&nbsp;Mingzhu Li ,&nbsp;Xi Liu ,&nbsp;Mohamed Salama ,&nbsp;Haoyang Sun ,&nbsp;Xiaomeng Li ,&nbsp;Zhaoxia Cai","doi":"10.1016/j.foodhyd.2026.112489","DOIUrl":"10.1016/j.foodhyd.2026.112489","url":null,"abstract":"<div><div>The effective co-delivery of structurally diverse nutrients in functional foods remains challenging. This study aimed to develop a stable yolk-based water-in-oil-in-water (W/O/W) emulsion system to co-encapsulate lipophilic DHA with hydrophilic vitamin B12, folic acid, and Zn/Fe. Hydrophilic micronutrients were dissolved in the internal aqueous phase, while DHA-enriched algae oil formed the oil phase. Enzymatically hydrolyzed egg yolk served as a functional external aqueous phase. W/O/W emulsions were fabricated by high-speed shearing followed by high-pressure homogenization, and 6 % (w/v) polyglycerol polyricinoleate was optimized as the oil-phase emulsifier. Structurally intact double emulsions achieved a DHA encapsulation efficiency of 94.8 %. Introducing 0.10 % (w/v) anionic polysaccharides, sodium alginate (SA) or propylene glycol alginate (PGA), further reduced droplet size and narrowed the size distribution. Zeta potential and confocal microscopy indicated enhanced negative surface charge and formation of a continuous protein–polysaccharide interfacial film, suppressing droplet aggregation. The optimized emulsions were spray dried into multi-nutrient yolk powders with low moisture content (2.56 % for PGA) and high solubility (74.51 % for SA). FTIR and secondary structure analysis suggested strengthened hydrogen bonding and a shift toward more ordered protein conformations after polysaccharide addition. Overall, this yolk-based W/O/W system provides a practical strategy for co-encapsulating DHA, vitamins, and minerals in next-generation maternal–infant functional foods.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"175 ","pages":"Article 112489"},"PeriodicalIF":11.0,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146074561","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":"Rheological assessment of printed overhang designs for starch, protein, and combined food inks","authors":"Md Ibrahim Khalil ,&nbsp;Yashwanth Kumar Kondabathula ,&nbsp;Ranadip Pal ,&nbsp;Gordon F. Christopher ,&nbsp;Farnaz Maleky ,&nbsp;Paul F. Egan","doi":"10.1016/j.foodhyd.2026.112463","DOIUrl":"10.1016/j.foodhyd.2026.112463","url":null,"abstract":"<div><div>Achieving high shape fidelity for customized 3D food printing applications requires creation of food inks with optimized rheological properties, especially when printing complex structures, such as overhang geometries. Printing overhangs requires an ink with smooth extrusion that is structurally stable, which is dependent on rheological properties that often oppose one another. This study experimentally investigates the printability of mashed potato (MP) and pea protein (PP) inks by assessing overhang printability informed by moisture content and rheological properties. MP inks achieved optimal printability from 76 to 81 % moisture content, while PP inks performed best from 72 to 76 % moisture content. Rheological analyses identified optimal ink properties including yield stress (<em>τ</em>_<em>y</em>) (∼100–300 Pa for MP, ∼500-1000 Pa for PP) and average storage modulus (G′) in the linear viscoelastic region (LVR) (∼12,300–25,900 Pa for MP, ∼7200–14,700 Pa for PP) that are necessary to achieve high fidelity structurally stable prints. Inks with combined MP and PP formulations at varied ratios were then printed to demonstrate the potential for ingredient customization while retaining overhang printability. These results quantify a printability window of rheological properties that enable high fidelity food prints of varied ingredient mixtures and complex geometrical features for customized food delivery.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"175 ","pages":"Article 112463"},"PeriodicalIF":11.0,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146074563","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}