{"title":"Wet ball-milling fabricated deacetylated chitin nanofibers for meat saltiness enhancement","authors":"Jing Liao , Xingyue Zhao , Yuhang Zhou , Jiamin Zhang","doi":"10.1016/j.foodhyd.2025.111729","DOIUrl":"10.1016/j.foodhyd.2025.111729","url":null,"abstract":"<div><div>The reduction of salt usage in meat products is of significant interest to the meat processing industry. In this context, chitin nanofibers (ChNFs) have emerged as a potential candidate for reducing salt usage in meat products. In this study, deacetylated chitin nanofibers (D-ChNFs) with varying degrees of deacetylation (DDs) were prepared by subjecting native chitin to a partial deacetylation process, followed by a wet ball-milling treatment. The fabricated D-ChNFs were characterized and used as saltiness enhancers for pork fillets. The enhanced saltiness mechanism was elucidated by exploring the interaction between ChNFs and Cl<sup>−</sup>. The results have shown that when DD is increased from 5.9 % to 28.6 %, D-ChNFs with a more dispersed nanostructure can be obtained, with a diameter range of 10–30 nm and a length of several microns. Furthermore, the pork fillets cured with D-ChNFs exhibited higher saltiness values compared to the control groups, and the optimal perceived saltiness was obtained when the ChNF-12 (DD = 28.6 %) was added. Quantum chemical calculation results demonstrated that the interaction intensity between Cl<sup>−</sup> and the functional groups on the D-ChNFs is in the order of -NH<sub>3</sub><sup>+</sup>/−OH > -NH<sub>3</sub><sup>+</sup>>-NHCOCH<sub>3</sub>. D-ChNFs can bind Cl<sup>−</sup> to their surface through electrostatic attraction as the dominant force, and scale up the proportion of Na<sup>+</sup> on the meat surface that can bind to taste receptor cells, thus enhancing the meat saltiness. The findings of this study provide a theoretical basis for the development of novel salt reduction methods in meat industry.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"170 ","pages":"Article 111729"},"PeriodicalIF":11.0,"publicationDate":"2025-07-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144564014","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Food HydrocolloidsPub Date : 2025-07-04DOI: 10.1016/j.foodhyd.2025.111728
Zhiyong Niu , Xizhong Liu , Yunying Li , Mengzhou Zhou , Yi Liu , Binjia Zhang , Guohua Zhao , Jia Chen , Dongling Qiao , Fengwei Xie
{"title":"Partially removing galactose unit on tamarind gum improves the gel-related features of tamarind gum/xanthan gels by strengthening their synergistic assembly","authors":"Zhiyong Niu , Xizhong Liu , Yunying Li , Mengzhou Zhou , Yi Liu , Binjia Zhang , Guohua Zhao , Jia Chen , Dongling Qiao , Fengwei Xie","doi":"10.1016/j.foodhyd.2025.111728","DOIUrl":"10.1016/j.foodhyd.2025.111728","url":null,"abstract":"<div><div>The amalgamation of tamarind gum (TMG) and xanthan generates synergistic interaction gels (SIGs), which have been used to design novel textural systems and to develop cell-cultured meat as well as health foods tailored for elderly individuals with dysphagia. However, the strong aggregated tendency of TMG chains limited the expose of active sites, thereby hindering full binding with xanthan and resulting in suboptimal gel properties. This study demonstrated that the removal of galactose units from TMG enhances specific interactions between TMG and xanthan by modulating the aggregation behavior of TMG chains. After removing galactose to 71.30 %, the reduced steric hindrance facilitated the transformation of disordered TMG chains into a helical structure, thereby exposing more binding sites (<em>i.e.</em>, hydrophilic groups) to interact with pyruvate groups on xanthan. This enhanced the specific interactions, as evidenced by an increase in enthalpy change from 2.80 × 10<sup>−2</sup> J/g to 3.90 × 10<sup>−2</sup> J/g, and thus the gel structure (suggested by the increased <em>n</em> and reduced <span><math><mrow><msub><mi>ξ</mi><mrow><mi>c</mi><mi>h</mi><mi>a</mi><mi>i</mi><mi>n</mi></mrow></msub></mrow></math></span> values in Table 1) and gel strength both in <em>G</em>′ and gel hardness. However, further removal of galactose reduced the dissociation ability of TMG chains from clusters and resulted in the formation of elongated clusters, thereby decreasing the contact surface between TMG and xanthan, which weakened their specific interactions and gel strength. These results provide insights for the design and development of SIG-based systems in food industry.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"170 ","pages":"Article 111728"},"PeriodicalIF":11.0,"publicationDate":"2025-07-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144572030","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Food HydrocolloidsPub Date : 2025-07-04DOI: 10.1016/j.foodhyd.2025.111710
Jiashu Li , Frederik Janssen , Annelise Vallaey , Diete Verfaillie , Kristof Brijs , Jan A. Delcour , Atze Jan van der Goot , Geert Van Royen , Arno G.B. Wouters
{"title":"Understanding the effect of pH on structure formation in high moisture extrudates produced from soy protein-dietary fiber blends","authors":"Jiashu Li , Frederik Janssen , Annelise Vallaey , Diete Verfaillie , Kristof Brijs , Jan A. Delcour , Atze Jan van der Goot , Geert Van Royen , Arno G.B. Wouters","doi":"10.1016/j.foodhyd.2025.111710","DOIUrl":"10.1016/j.foodhyd.2025.111710","url":null,"abstract":"<div><div>The effect of pH on the structure and texture of high moisture extrudates prepared from blends of soy protein isolate (SPI) and a soy dietary fiber-enriched fraction (SDF), achieving different protein-DF ratios, was studied. Samples hydrated to 50 % moisture at pH 3.0, 5.0, and 7.0 underwent rheological analysis following a temperature profile (40–140–60 °C) relevant for high moisture extrusion (HME). At pH 7.0, lower complex viscosity (|η∗|) at 140 °C and steeper |η∗| increase during cooling indicated greater protein-protein interaction disruption at high temperature followed by enhanced intermolecular interaction and/or cross-linking during cooling than at pH 3.0 and 5.0. The use of a lower protein-DF ratio resulted in elevated |η∗| during heating and lower |η∗| after cooling at all pH values, the latter due to DFs interfering with protein network formation. Extrudates produced at pH 7.0 using a Thermo Fisher Process 11 extruder exhibited distinct anisotropic structure and pronounced water syneresis, whereas extrudates produced at low pH had mostly isotropic structure. This was attributed to the lower viscosity and thus greater deformability at the end of the barrel and to more pronounced disulfide bond formation upon cooling in samples at neutral pH, compared to at low pH. The use of a lower protein-DF ratio at pH 7.0 transformed extrudate structures from layered to fibrous and reduced disulfide bond formation. This study demonstrated that pH and protein-DF ratios significantly affect bulk viscosity and disulfide bond formation during extrusion, thereby determining the structure and texture of the resulting extrudates.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"170 ","pages":"Article 111710"},"PeriodicalIF":11.0,"publicationDate":"2025-07-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144623739","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Food HydrocolloidsPub Date : 2025-07-03DOI: 10.1016/j.foodhyd.2025.111721
Xiaoyan Hu , Yajuan Li , Jaekun Ryu , David Julian McClements
{"title":"Modulating the gel strength of filled whey protein hydrogels by altering oil droplets characteristics: Theory and experiments","authors":"Xiaoyan Hu , Yajuan Li , Jaekun Ryu , David Julian McClements","doi":"10.1016/j.foodhyd.2025.111721","DOIUrl":"10.1016/j.foodhyd.2025.111721","url":null,"abstract":"<div><div>Protein-based hydrogels are used in a wide range of food products, including desserts, confectionary, dressings, spreads, and meat analogs. For many applications, it is important to modulate the textural attributes of the hydrogels so that they meet consumer expectations. In this study, the impact of oil droplet characteristics, especially size and concentration, on the rheological properties of filled whey protein hydrogels was examined. The experimental measurements were compared to the predictions made by a theoretical model for the elastic properties of filled composite materials consisting of non-dilute spherical fluid particles dispersed within a solid matrix. This theory predicted that the mechanical strength of filled hydrogels can either increase or decrease with increasing oil droplet concentration depending on the size of the droplets. Small droplets have a high Laplace pressure, which makes them more resistant to deformation. Consequently, they may increase the gel strength when their effective rigidity is higher than that of the surrounding protein network. In contrast, large droplets have a low Laplace pressure, which makes them highly susceptible to deformation. As a result, they tend to reduce the gel strength. In this study, we prepared oil-in-water emulsions with different mean droplet diameters and then used them to form heat-set whey protein gels with a range of droplet and protein concentrations. The theory and experiments showed good qualitative agreement but there was a poor quantitative agreement, which was attributed to the fact that the real emulsion gels did not conform to the assumptions used to derive the theoretical model. Even so, this mathematical model is useful for understanding and predicting the behavior of filled food gels.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"170 ","pages":"Article 111721"},"PeriodicalIF":11.0,"publicationDate":"2025-07-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144572029","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Food HydrocolloidsPub Date : 2025-07-03DOI: 10.1016/j.foodhyd.2025.111723
Tugba Dursun Capar , Xiaoyan Hu , David Julian McClements
{"title":"Plant-based hydrogel beads for vitamin D bioaccessibility: The role of protein denaturation and dimension","authors":"Tugba Dursun Capar , Xiaoyan Hu , David Julian McClements","doi":"10.1016/j.foodhyd.2025.111723","DOIUrl":"10.1016/j.foodhyd.2025.111723","url":null,"abstract":"<div><div>Encapsulating bioactive components within hydrogel beads provides an effective method of improving their stability and efficacy, thereby enhancing their potential health benefits. In this study, vitamin D<sub>3</sub>-loaded nanoemulsions were encapsulated within plant-based hydrogel beads comprised of pea protein (heated or unheated) and calcium alginate. The impact of bead composition and dimensions on lipid digestibility and vitamin D bioaccessibility was then investigated. The hydrogel beads containing heated pea protein were more stable to simulated oral and stomach phases than those containing unheated pea protein. This effect was attributed to the formation of heat-induced pea protein aggregates that were better retained within the calcium alginate network inside the beads. The bioaccessibility of vitamin D<sub>3</sub> was improved when it was encapsulated within the beads, which may have been due to their ability to protect the vitamin from chemical degradation, especially under acidic gastric conditions. The beads containing the heated protein provided the best protection during stomach digestion, leading to around 86 % of the original vitamin D<sub>3</sub> still being bioaccessible after the small intestine phase. The results of this study may lead to the development of novel hydrogel delivery systems that can improve the efficacy of oil-soluble vitamins in plant-based foods.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"170 ","pages":"Article 111723"},"PeriodicalIF":11.0,"publicationDate":"2025-07-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144581101","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Food HydrocolloidsPub Date : 2025-07-03DOI: 10.1016/j.foodhyd.2025.111708
Tianjiao Fan , Yang Yang , Chunmin Ma, Yue Xu, Yan Wang, Bing Wang, Guang Zhang, Xiaofei Liu, Na Zhang
{"title":"Effects of different exogenous proteins on rice starch retrogradation behavior and their potential mechanisms","authors":"Tianjiao Fan , Yang Yang , Chunmin Ma, Yue Xu, Yan Wang, Bing Wang, Guang Zhang, Xiaofei Liu, Na Zhang","doi":"10.1016/j.foodhyd.2025.111708","DOIUrl":"10.1016/j.foodhyd.2025.111708","url":null,"abstract":"<div><div>Retarding starch retrogradation is essential for developing food products with desirable qualities. The inhibitory effects of three proteins on rice starch (RS) retrogradation, as well as the effects of soybean isolate protein (SPI), pea isolate protein (PPI) and whey isolate protein (WPI) through competitive hydration related to the content of polar amino acids (WPI > PPI > SPI:66 % > 64 %>61 %), have been systematically revealed by using multiscale characterization techniques; a molecular weight-dependent physical barrier effect (The molecular weight of WPI is small and distributed between 10 and 70 kDa); the formation of rice amyloid protein V complexes and competitive hydration advantages and high solubility properties of WPI through hydrogen bonding and hydrophobic interactions were the most effective in inhibiting the short-range ordered structures (6.00 %, 7.04 %) and the long-range crystalline network (16.79 % after 1 day and 7 days, respectively and 24.62 %) were most effective. In contrast, SPI, with the largest molecular weight but higher content of hydrophobic groups, had a better complex-binding ability than PPI, which resulted in a hierarchical relationship of inhibition effect of WPI > SPI > PPI. The concentration effect study showed that the inhibition of rice starch retrogradation by the proteins was positively correlated with the amount of protein added, but the synergistic effect tended to saturate once the protein concentration exceeded 15 %. This study explored the mechanisms by which three common exogenous proteins prevent rice starch retrogradation, offering a theoretical foundation for using plant or animal proteins to control the texture and shelf-life of starch-based foods.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"170 ","pages":"Article 111708"},"PeriodicalIF":11.0,"publicationDate":"2025-07-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144581110","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}
Food HydrocolloidsPub Date : 2025-07-03DOI: 10.1016/j.foodhyd.2025.111724
Qiu-Yue Ma , Qian-Da Xu , Nan Chen , Wei-Cai Zeng
{"title":"Regulation of disulfide bond cleavage on the physicochemical and digestive properties of EGCG-gluten covalent complexes","authors":"Qiu-Yue Ma , Qian-Da Xu , Nan Chen , Wei-Cai Zeng","doi":"10.1016/j.foodhyd.2025.111724","DOIUrl":"10.1016/j.foodhyd.2025.111724","url":null,"abstract":"<div><div>Disulfide bond critically govern gluten structure and its covalent interactions with polyphenols, ultimately determining gluten-polyphenol complex properties. This study investigated how disulfide bond cleavage modulates gluten structure, enhances epigallocatechin gallate (EGCG)-gluten covalent binding, and regulates the physicochemical/digestive properties of their complexes. Sodium metabisulfite treatment (0–25 mM treatment) induced disulfide bonds cleavage, which promoted the structural unfolding and exposed reactive groups for covalent binding with EGCG. With analysis of particle size, fluorescence spectroscopy, fourier-transform infrared spectroscopy, and thermogravimetric analysis, disulfide bond cleavage significantly reduced the particle size (from 124.5 to 62.26 μm) of gluten, altered the secondary (α-helix decreased from 23.4 % to 15.1 %, β-sheet from 32.8 % to 23.7 %) and tertiary structures of gluten, increased its surface hydrophobicity and enhanced its binding efficiency (from 51.98 % to 62.02 %) with EGCG. With increase of disulfide bond cleavage, EGCG-gluten covalent complexes exhibited enhanced thermal, pH, and oxidation stability, along with strong antioxidant activity. In addition, the disulfide bond cleavage of gluten inhibited the premature releasing and degradation of EGCG from covalent complexes during the digestion process, which was beneficial for improving the bioaccessibility of EGCG. All results suggest that the disulfide bond cleavage of gluten improve the physicochemical and digestive properties of EGCG-gluten covalent complexes, which provides a potential approach to regulate the properties of proteins-polyphenols covalent complexes as delivery systems of active compounds for functional foods and nutraceuticals.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"170 ","pages":"Article 111724"},"PeriodicalIF":11.0,"publicationDate":"2025-07-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144564013","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}
Food HydrocolloidsPub Date : 2025-07-02DOI: 10.1016/j.foodhyd.2025.111703
Haitao Wang , Yuanda Sun , Pengjing Zhang , Zongcai Tu , Mingqian Tan
{"title":"Tailoring the properties of bigels by beeswax content for 3D food printing, astaxanthin delivery, and freshness sensing","authors":"Haitao Wang , Yuanda Sun , Pengjing Zhang , Zongcai Tu , Mingqian Tan","doi":"10.1016/j.foodhyd.2025.111703","DOIUrl":"10.1016/j.foodhyd.2025.111703","url":null,"abstract":"<div><div>Bigels, an emerging biphasic system comprising both hydrogels and oleogels, have garnered significant attention. In this study, a novel bigel was developed, consisting of beeswax-based oleogels as the oil phase and gelatin-pectin hydrogels as the water phase. The findings indicated that an increase in beeswax concentration led to enhanced bigel stability, with the maximum storage duration reaching 60 days without phase separation. Additionally, bigels containing beeswax exhibited remarkable freeze-thaw stability, withstanding 12 consecutive cycles of freezing and thawing. The 6 % beeswax bigels demonstrated optimal thermal, ionic, and pH stability. These findings underscore the potential of bigels as multifaceted materials, not only serving as extrudable inks for 3D printing but also functioning as smart sensors for food freshness. Additionally, bigels demonstrated significant advantages in the delivery of bioactive compounds The encapsulation efficiency of astaxanthin exhibited a positive correlation with increasing beeswax content, increasing from 78.71 ± 0.25 % to 90.73 ± 0.77 %. These findings underscore the potential of bigels as a versatile platform for 3D food printing, astaxanthin delivery, and food freshness sensing.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"170 ","pages":"Article 111703"},"PeriodicalIF":11.0,"publicationDate":"2025-07-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144548627","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}
Food HydrocolloidsPub Date : 2025-07-02DOI: 10.1016/j.foodhyd.2025.111712
Zhongyu Yang, Lang Qin, Keying Song, Jingyang Guo, Jian Guo, Zhili Wan, Xiaoquan Yang
{"title":"Electrokinetic interaction and dynamic wetting behavior of soy protein/gum arabic coacervates as soft particles","authors":"Zhongyu Yang, Lang Qin, Keying Song, Jingyang Guo, Jian Guo, Zhili Wan, Xiaoquan Yang","doi":"10.1016/j.foodhyd.2025.111712","DOIUrl":"10.1016/j.foodhyd.2025.111712","url":null,"abstract":"<div><div>In recent years, the growing demand for sustainable and clean-label health foods has made mild processing a key approach to obtaining less denatured and high-quality plant-based protein ingredients. This study compared soy protein isolate (SPI) obtained <em>via</em> salt extraction (S-SPI) with SPI obtained <em>via</em> the conventional alkali-solubilization and acid-precipitation method (A-SPI), to investigate the impact of protein aggregation structure on the formation of SPI/gum arabic (GA) complex coacervation. Native-PAGE and SDS-PAGE results revealed that mild extraction processes lead to the enrichment of glycinin in SPI. The electrokinetic interactions of S-SPI/GA coacervates were analyzed using soft particle theory, linking the charged properties of biopolymers to their complex structures. Dynamic wetting behavior results showed that the low interfacial tension of S-SPI/GA coacervates facilitated wetting at the oil–water interface and the formation of a continuous layer. This study proposed a novel approach to developing low-denaturation, natural plant proteins and provided new insights into the formation mechanisms of plant protein-based complex coacervates.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"170 ","pages":"Article 111712"},"PeriodicalIF":11.0,"publicationDate":"2025-07-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144572083","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}