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":"Gelatin-chitosan edible film with kesum essential oil nanoemulsion: Film structure and release kinetics of nanoemulsified kesum essential oil influenced by the presence of different salts in ethanolic food simulants","authors":"Ianne Kong ,&nbsp;Benbettaieb Nasreddine ,&nbsp;Debeaufort Frédéric ,&nbsp;Degraeve Pascal ,&nbsp;Liew Phing Pui ,&nbsp;Kar Lin Nyam","doi":"10.1016/j.foodhyd.2026.112503","DOIUrl":"10.1016/j.foodhyd.2026.112503","url":null,"abstract":"<div><div>Natural bioactive compound enriched edible films are increasingly acceptable as environmentally friendly substitutes for traditional plastic packaging. These films can provide antibacterial and antioxidant properties to improve food safety and extend shelf-life in addition to reducing their negative effects on the environment. The impact of incorporating nanoemulsified kesum (<em>Persicaria minor</em> Huds.) essential oil (KEO-NE) into gelatin-chitosan edible films was investigated focusing on structural, thermal, and release properties. Fourier transform infrared spectroscopy (FTIR) revealed no significant changes indicating physical interactions with the biopolymer matrix in FTIR spectra following KEO-NE incorporation. Scanning electron microscopy (SEM) showed KEO-NE induced surface irregularities and internal heterogeneities, with pores and bubbles indicating droplet migration during drying, contrasting control films. Differential scanning calorimetry indicated a decline in the thermal stability after the introduction of KEO-NE that evidenced by diminished endothermic peak and enthalpy values. Release kinetics studies in various food simulants showed that addition of salts in ethanol significantly enhanced KEO-NE release rates, affecting diffusion coefficients and total release amounts. The total KEO release varied from 3426.5 ± 396.7 mg/L to 64129.1 ± 1379.3 mg/L with the maximum release observed in a solution of 50 % ethanol and 1 % of NaCl. Consequently, the diffusion coefficients exhibited considerable variation which was 0.9 ± 0.1 to 15.0 ± 4.2 x 10⁻¹² m²/s implying increased diffusion in salt-infused ethanol attributed to salting-out activities. The proportion of the KEO release varied from 1.1 ± 0.2 % to 18.7 ± 1.8 % with MgCl₂ facilitating the most significant release fraction. Higher release rates in ethanol with salts suggest salt-induced changes in film solubility and matrix interactions play a pivotal role in controlling KEO-NE diffusion due to salting-out effects. This study contributes to SDG (Sustainable Development Goal) 12 (Responsible Consumption and Production) by developing biodegradable edible films with controlled release of bioactive compounds, offering a sustainable alternative to conventional food packaging materials.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"175 ","pages":"Article 112503"},"PeriodicalIF":11.0,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146184761","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":"Proanthocyanidin/laccase-mediated cross-linking enhances the structural stability and rheological properties of collagen solutions","authors":"Junhong Xie ,&nbsp;Li Feng ,&nbsp;Fanghui Deng ,&nbsp;Wei Yue ,&nbsp;Wei Liang ,&nbsp;Qiannan Zhao ,&nbsp;Wentao Ma ,&nbsp;Jianhua Rong ,&nbsp;Shanbai Xiong ,&nbsp;Yang Hu","doi":"10.1016/j.foodhyd.2025.112360","DOIUrl":"10.1016/j.foodhyd.2025.112360","url":null,"abstract":"<div><div>Increasing the added value of freshwater fish by-product processing and reducing the economic losses are currently research hotspots in the field of aquatic products. However, the collagen-based products derived from freshwater fish cannot be widely applied due to their disadvantages such as low mechanical properties. Enzymatic cross-linking modification to improve the physicochemical properties of collagen-based materials is a better solution. This study focused on the self-assembly behavior of collagen molecules, investigated the cross-linking of collagen solutions mediated by laccase and proanthocyanidins, and improved their rheological properties and structural characteristics. The results showed that the volume ratio of collagen-proanthocyanidins/laccase (COL-PL) within the range of 1:0.01 to 1:0.4 is more conducive to the stability of collagen molecules. All cross-linked groups exhibited shear thinning properties. Collagen-proanthocyanidins (COL-PA) enhanced the mechanical properties of collagen molecules to a certain extent. However, when the volume ratio of COL-PL is 1:0.02, it not only accelerates the aggregation of collagen molecules, but also generates a complex with the best gel performance. This is mainly because low-concentration laccase can catalyze the generation of proanthocyanidin active groups. The interaction between the C=O bond and the -NH₂ bond in the collagen molecule peptide chain provides more sites for the aggregation of collagen molecules, and at the same time, the chemical bond interaction also makes the collagen aggregate more closely. Finally, through atomic force microscopy observation, after 24 h, COL-PL 1:0.02 group collagen molecules formed a dense reticular cross-linked structure. The research provides a new approach to expanding freshwater fish collagen potential application prospects.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"175 ","pages":"Article 112360"},"PeriodicalIF":11.0,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146036017","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":"Phosphorylation-modified fava bean 11S protein fibril-based oleogels: A novel strategy to enhance network flexibility and alter rheological and textural properties","authors":"Zhihao Xu ,&nbsp;Xuemei Lin ,&nbsp;Wenzhong Zhao ,&nbsp;Xiaoqi Ding ,&nbsp;Xianglin Sun ,&nbsp;Yuting Ding ,&nbsp;Hui Chen ,&nbsp;Pengbo Cui","doi":"10.1016/j.foodhyd.2026.112477","DOIUrl":"10.1016/j.foodhyd.2026.112477","url":null,"abstract":"<div><div>This study developed novel protein-based fish oil oleogels employing protein nanofibrils derived from sodium tripolyphosphate-phosphorylated (STPP) <em>fava bean</em> 11S globulin. X-ray photoelectron spectroscopy confirmed successful phosphorylation through a P_2p peak at 133.3 eV, supported by FTIR bands at 972 cm⁻¹ (P–O stretching) and 894 cm⁻¹ (P=O vibration). Phosphorylation disrupted the crystalline structure of 11S globulin, increasing β-turns and reducing random coils as revealed by XRD. Under acid-heat treatment (pH 2.0, 85 °C), phosphorylated 11S (P11S) formed finer and more uniform nanofibrils compared to the heterogeneous network of native 11S. Thioflavin T fluorescence showed faster nucleation and higher intensity for P11S fibrils, indicating enhanced fibrillation kinetics. P11S fibrils also exhibited superior emulsifying activity and emulsion stability. Mass spectrometry identified self-assembling peptide segments and phosphorylation sites, clarifying the molecular mechanism. When incorporated into oleogels, phosphorylated fibril oleogel (P11SG) displayed a softer, cream-like texture than the harder 11S oleogel (11SG). Rheological and texture analyses confirmed that P11SG had a lower storage modulus, hardness, and chewiness, but higher resilience and similar oil-binding capacity. Overall, phosphorylation effectively modulates the self-assembly and functional characteristics of 11S globulin. This providing a promising strategy to design protein-based oleogels with tunable textures and enhanced interfacial performance for food applications.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"175 ","pages":"Article 112477"},"PeriodicalIF":11.0,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146036019","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 novel scaffold platform for in situ lipid integration in cultivated meat","authors":"Mursalin Sajib ,&nbsp;Inyoung Choi ,&nbsp;Fariba Mohebichamkhorami ,&nbsp;Ahmed El-Moghazy ,&nbsp;Andrew J. Gravelle ,&nbsp;Nitin Nitin","doi":"10.1016/j.foodhyd.2026.112431","DOIUrl":"10.1016/j.foodhyd.2026.112431","url":null,"abstract":"<div><div>Cultivated meat often lacks integrated fat, primarily because co-culturing muscle and fat cells is technologically challenging and because most scaffolds are designed without integrated fat. This limits texture, flavor, and mouthfeel, all key factors for palatability and consumer acceptance. In this study, we developed a novel scaffold incorporating structured oil into a gelatin hydrogel matrix at a 1:4 ratio, forming an oleogel-in-hydrogel (bigel) system. The oleogel phase was structured using 15 % monoacylglycerol and 8 % stearic acid in canola oil and formed an elongated crystalline fibers. The bigel scaffolds were stabilized with either 0.1 % w/w Tween-20 or 0.2 % w/w lecithin as emulsifiers, and produced hardness values ranging from 4.8 N to 7.9 N after overnight of soaking in DPBS buffer. Both scaffold types supported cell proliferation and differentiation; however, the 0.1 % Tween-20 scaffold produced significantly higher cell proliferation and differentiation into mature myotubes, indicating superior biocompatibility. Overall, this study highlights the potential of a bigel scaffold approach as a building block for whole-cut cultivated meats by combining <em>in situ</em> integration of lipids with tunable functional, textural, flavor, and nutritional properties for improved consumer acceptance.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"175 ","pages":"Article 112431"},"PeriodicalIF":11.0,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146036020","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":"Quality control of gum arabic – Molecular basis and a new screening method","authors":"Frederike Kersten ,&nbsp;Désirée Martin ,&nbsp;Ulrike S. van der Schaaf ,&nbsp;Daniel Wefers","doi":"10.1016/j.foodhyd.2026.112454","DOIUrl":"10.1016/j.foodhyd.2026.112454","url":null,"abstract":"<div><div>Gum arabic (GA) is commonly used as a stabilizer in aroma oil and beverage emulsions due to its amphiphilic character. However, different GA batches exhibit varying levels of functionality, which so far cannot be related to a molecular parameter. Therefore, the aim of our study was to investigate the relationship between the industrial quality of eight selected GA samples and the (macro)molecular structure and functionality of their glycoprotein fractions in detail, to establish a new quality parameter, and to develop a simplified analytical method for a direct quality assessment. Each GA sample was separated into the three major glycoprotein fractions, which were analyzed for their structural and functional properties. GA quality strongly correlated with the amount of arabinogalactan protein (AGP) and its molecular expansion, expressed via the gyration radius. Based on these results, a new quality parameter was defined as the product of AGP content and the volume of AGP molecules. Furthermore, the spatial expansion of AGP showed a strong positive correlation with the rhamnose and glucuronic acid content, identifying both as a marker for the degree of branching and molecular expansion. For the development of a simplified analytical method, the HIC separation was successfully scaled down, enabling a rapid quantitative isolation of AGP and the subsequent determination of the quality parameter with HPSEC-RI/UV/MALLS. By applying the method to 40 GA samples, it was demonstrated that it allows for a fast and reproducible analysis of GA quality. Thus, the developed analytical approach can complement or replace time-consuming emulsion stability tests.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"175 ","pages":"Article 112454"},"PeriodicalIF":11.0,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146035988","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}