Food Hydrocolloids最新文献

{"title":"Understanding the effect of pH on structure formation in high moisture extrudates produced from soy protein-dietary fiber blends","authors":"Jiashu Li ,&nbsp;Frederik Janssen ,&nbsp;Annelise Vallaey ,&nbsp;Diete Verfaillie ,&nbsp;Kristof Brijs ,&nbsp;Jan A. Delcour ,&nbsp;Atze Jan van der Goot ,&nbsp;Geert Van Royen ,&nbsp;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}

{"title":"Modulating the gel strength of filled whey protein hydrogels by altering oil droplets characteristics: Theory and experiments","authors":"Xiaoyan Hu ,&nbsp;Yajuan Li ,&nbsp;Jaekun Ryu ,&nbsp;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}

{"title":"Hydration-driven structural engineering via enzymatic glycation: Sustained quercetin release in pullulan-zein coatings for extended walnut preservation","authors":"Zi-han Wang ,&nbsp;Xue-li Liu ,&nbsp;Rui-qi Sun ,&nbsp;Bin Qi ,&nbsp;Jun-xia Xia ,&nbsp;Da-yong Zhou ,&nbsp;Liang Song","doi":"10.1016/j.foodhyd.2025.111705","DOIUrl":"10.1016/j.foodhyd.2025.111705","url":null,"abstract":"<div><div>This study developed pullulan-based edible coatings incorporating quercetin-loaded glycated zein nanoparticles (<em>g</em>Zein I–III-Que) to mitigate oxidative rancidity in walnuts. Enzymatic glycation-driven hydration engineering modulated interfacial interactions between zein and pullulan, forming structurally homogeneous nanocomposites. The optimized intermediate glycation coating (<em>g</em>Zein II-Que@Pul) resolved incompatibility between hydrophobic antioxidants and hydrophilic matrices through uniform nanoparticle dispersion (PDI 0.19 ± 0.02) and enhanced mechanical strength (28.48 ± 0.52 MPa). Hydration-mediated structural reorganization balanced molecular mobility and diffusion resistance, sustaining antioxidant release <em>via</em> non-Fickian kinetics (Korsmeyer-Peppas n = 0.55). The coatings reduced oxygen permeability to 0.10 ± 0.02 kg m⁻²·s⁻¹ and demonstrated high antioxidant efficiency (I₅₀ = 1.4 mg/mL) alongside cytocompatibility exceeding 80 % cell viability. Applied to walnuts, <em>g</em>Zein II-Que@Pul extended shelf life by 528 ± 25 % at 25 °C, retaining 91.76 ± 1.17 % omega-3 and 95.22 ± 0.76 % omega-6 fatty acids. MRI spatial analysis visualized lipid oxidation suppression spatially correlated with hydration-driven quercetin release, validated by peroxide value reductions (57.53 ± 2.73 %). By tailoring glycation degree, this work establishes enzymatic hydration engineering as a scalable strategy for sustainable food preservation. The optimized coating harmonizes bioactive delivery and structural integrity through hydration-modulated diffusion kinetics and interfacial stability, leveraging renewable biopolymers to advance plant protein-polysaccharide hybrids as functional barriers for minimizing postharvest losses in lipid-rich foods.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"170 ","pages":"Article 111705"},"PeriodicalIF":11.0,"publicationDate":"2025-07-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144564017","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":"Plant-based hydrogel beads for vitamin D bioaccessibility: The role of protein denaturation and dimension","authors":"Tugba Dursun Capar ,&nbsp;Xiaoyan Hu ,&nbsp;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 D₃-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 D₃ 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 D₃ 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}

{"title":"Effects of different exogenous proteins on rice starch retrogradation behavior and their potential mechanisms","authors":"Tianjiao Fan ,&nbsp;Yang Yang ,&nbsp;Chunmin Ma,&nbsp;Yue Xu,&nbsp;Yan Wang,&nbsp;Bing Wang,&nbsp;Guang Zhang,&nbsp;Xiaofei Liu,&nbsp;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 &gt; PPI &gt; SPI:66 % &gt; 64 %&gt;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 &gt; SPI &gt; 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}

{"title":"Regulation of disulfide bond cleavage on the physicochemical and digestive properties of EGCG-gluten covalent complexes","authors":"Qiu-Yue Ma ,&nbsp;Qian-Da Xu ,&nbsp;Nan Chen ,&nbsp;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}

{"title":"Tailoring the properties of bigels by beeswax content for 3D food printing, astaxanthin delivery, and freshness sensing","authors":"Haitao Wang ,&nbsp;Yuanda Sun ,&nbsp;Pengjing Zhang ,&nbsp;Zongcai Tu ,&nbsp;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}

{"title":"Electrokinetic interaction and dynamic wetting behavior of soy protein/gum arabic coacervates as soft particles","authors":"Zhongyu Yang,&nbsp;Lang Qin,&nbsp;Keying Song,&nbsp;Jingyang Guo,&nbsp;Jian Guo,&nbsp;Zhili Wan,&nbsp;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}

{"title":"Unravelling the multi-scale structure of cell walls from edible seaweed species and the impact of processing treatments","authors":"Laura María Vega-Gómez ,&nbsp;Elena Torrego-Moreno ,&nbsp;Vera Cebrián-Lloret ,&nbsp;María Castanedo ,&nbsp;Juan Carlos Martínez ,&nbsp;Isidra Recio ,&nbsp;Marta Martínez-Sanz","doi":"10.1016/j.foodhyd.2025.111720","DOIUrl":"10.1016/j.foodhyd.2025.111720","url":null,"abstract":"<div><div>A sequential protocol combining solvent and mechanical treatments, originally designed for land plants, was adapted to concentrate the cell walls of two edible seaweed species, <em>Ulva lacinulata</em> and <em>Porphyra dioica</em> (Nori). However, complete isolation of the cell walls without altering their natural structure was challenging due to strong interactions between polysaccharides and other components, such as proteins. Instead, the process concentrated the cell walls, resulting in polysaccharide contents of 61–63 %. In Ulva, cellulose was identified as the main structural component, while in Nori, porphyrans constituted the semi-crystalline, microfibrillar backbone, closely resembling cellulose in arrangement. These structural variations affected how the cell walls responded to mechanical (ultrasounds, US) and thermal (steam cooking) treatments, as evidenced by the advanced structural characterisation of the samples, combining Small Angle X-ray Scattering (SAXS) and X-ray diffraction (XRD) with microscopy and monosaccharide analyses. In Ulva, steam cooking preserved cell wall integrity while releasing intracellular components, whereas US disrupted the crystalline cellulose structure, causing significant cell wall breakdown and the release of proteins and polysaccharides. For Nori, steam cooking promoted protein release and the migration of some polysaccharides into the extracellular matrix, while US altered the crystalline structure of porphyrans but preserved cellular integrity due to the dense, gel-like extracellular matrix. These results highlight the importance of the composition and structure of the cell wall in seaweeds in determining their mechanical integrity and transformation responses.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"170 ","pages":"Article 111720"},"PeriodicalIF":11.0,"publicationDate":"2025-07-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144548618","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":"Microencapsulation in alginate-pectin based capsules of probiotic Lactobacillus plantarum WCFS1: pectin source and degree of blockwise distribution of methyl esters are critical parameters for the efficacy of protection under gastrointestinal conditions","authors":"Xin Tang ,&nbsp;Lei Liu ,&nbsp;Xiaochen Chen ,&nbsp;Naschla Gasaly ,&nbsp;Astrid Benie ,&nbsp;André Brodkorb ,&nbsp;Denis Poncelet ,&nbsp;Paul de Vos","doi":"10.1016/j.foodhyd.2025.111722","DOIUrl":"10.1016/j.foodhyd.2025.111722","url":null,"abstract":"<div><div>Microencapsulation, widely used across industries, enhances the delivery of bioactive compounds and probiotics in the gastrointestinal tract. The growing demand for functional foods has highlighted pectin as a promising encapsulation material, due to its favorable physicochemical properties and fermentability by gut microbiota, which supports intestinal health. In this study, we focused on encapsulating the pH sensitive probiotic <em>Lactobacillus plantarum</em> WCFS1 using various alginate-pectin compositions to evaluate their variability and functionality under simulated gastrointestinal conditions. Pectins with different degrees of methyl-esterification (DM) and blockiness distribution (DB) were enzymatically modified, characterized and tested. Results indicated that capsules with a 3:1 alginate to pectin ratio provided optimal stability. According to a three-way ANOVA analysis, the source, the DB, the pH, and the interaction between the resource and DB impact the viability of encapsulated <em>L. plantarum</em> WCFS1. Pectin with a lower DB enhanced the protection of <em>L. plantarum</em> WCFS1 under pH 3, 5, and 7. Under simulated digestive fluid conditions, the source, the DB, and the simulated fluids independently affect the viability of encapsulated <em>L. plantarum</em> WCFS1. Notably, orange pectin with a high DB (98 %) demonstrated the greatest efficacy in maintaining bacterial viability under simulated gastrointestinal conditions. The findings suggest that the pectin source and structural properties significantly influence the viability and survival of encapsulated probiotics under gastrointestinal conditions, which may lead to the tailored design of pectin-based capsules for controlled delivery of bacteria to specific parts of the gastrointestinal tract.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"170 ","pages":"Article 111722"},"PeriodicalIF":11.0,"publicationDate":"2025-07-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144564056","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}