Food Hydrocolloids最新文献_第7页

Effect of carboxymethyl cellulose on structural, physicochemical, and textural properties of faba bean protein/carboxymethyl cellulose emulsion gel as a plant-based ricotta cheese analog 羧甲基纤维素对植物基乳清干酪类似物蚕豆蛋白/羧甲基纤维素乳凝胶结构、理化和质地特性的影响

IF 11 1区农林科学

Food Hydrocolloids Pub Date : 2025-09-17 DOI: 10.1016/j.foodhyd.2025.111998

Goeun Han, Areum Han, Yoon Hyuk Chang

{"title":"Effect of carboxymethyl cellulose on structural, physicochemical, and textural properties of faba bean protein/carboxymethyl cellulose emulsion gel as a plant-based ricotta cheese analog","authors":"Goeun Han, Areum Han, Yoon Hyuk Chang","doi":"10.1016/j.foodhyd.2025.111998","DOIUrl":"10.1016/j.foodhyd.2025.111998","url":null,"abstract":"<div><div>The aims of this study were to develop a vitamin A-encapsulated emulsion gel and investigate the structural and physicochemical properties of the emulsion gel as a plant-based ricotta cheese analog. Emulsion gel was prepared by ionic gelation with Al<sup>3+</sup> and enzymatic cross-linking using transglutaminase in FBP/CMC emulsion with different CMC concentrations (0.5 %, 1.0 %, 1.5 %, and 2.0 %). CLSM images showed that the oil droplets became smaller and more uniform as the CMC concentrations increased. FT-IR analysis suggested that hydrogen bonding (between CMC and FBP or between FBP molecules) was formed during the preparation of the emulsion gel. The encapsulation efficiency of vitamin A was highest in the emulsion gel with the highest CMC concentration. The solvent holding capacity tended to increase with increasing CMC concentration. In texture profile analysis, the hardness of emulsion gel increased with increasing CMC concentrations, and the emulsion gel with the highest CMC concentration showed similar hardness, cohesiveness, and gumminess as ricotta cheese. In conclusion, this study indicated that CMC could influence the structural stability of emulsion gel by allowing oil droplets to act as active fillers, and emulsion gel can be suitable as a plant-based ricotta cheese analog.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"172 ","pages":"Article 111998"},"PeriodicalIF":11.0,"publicationDate":"2025-09-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145118040","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}

引用次数: 0

Unraveling microstructure and water behavior in diverse food matrices using low-frequency NMR (LF-NMR) on proton: a specific look at 1H-LF-NMR results interpretation 利用质子低频核磁共振（LF-NMR）揭示不同食物基质中的微观结构和水行为：具体看1H-LF-NMR结果解释

IF 11 1区农林科学

Food Hydrocolloids Pub Date : 2025-09-17 DOI: 10.1016/j.foodhyd.2025.111974

Audrey Gilbert, Sylvie L. Turgeon

{"title":"Unraveling microstructure and water behavior in diverse food matrices using low-frequency NMR (LF-NMR) on proton: a specific look at 1H-LF-NMR results interpretation","authors":"Audrey Gilbert, Sylvie L. Turgeon","doi":"10.1016/j.foodhyd.2025.111974","DOIUrl":"10.1016/j.foodhyd.2025.111974","url":null,"abstract":"<div><div>Low-frequency NMR on proton (<sup>1</sup>H-LF-NMR) has become a method of choice to study water mobility in food matrices. It has been applied on matrices varying in complexity such as sucrose solutions and complex hydrocolloid mixed systems. Measurements of spin-spin relaxation time (T<sub>2</sub>) using Carr-Purcell-Meiboom-Gill scan sequences are often used to study hydrated matrices with long relaxation times (>1ms). Studies reported 1 to 4 water populations among which “bound water”, bulk water from serum, and separated water (sedimentation, syneresis).</div><div>Experiments from our team on different food systems and results from the literature will be used to demonstrate how <sup>1</sup>H-LF-NMR can probe food microstructure and the care needed to avoid artifacts. Examples were taken among fermented milk, mixed polysaccharides, mixed protein-polysaccharide systems and legume purée. Water mobility shows similar patterns between these different matrices even though their type (suspension, gel, …), composition and microstructure are different in nature. For instance, in yogurt formulations the serum water mobility correlated with network heterogeneity. The serum water often gets most of the attention in studies as it can be affected by serum solutes, serum viscosity, and gel microstructure (porosity, macromolecular density). However, water mobility was also able to detect and quantify spontaneous serum separation or to detect microstructural heterogeneity due to segregative interactions.</div><div><sup>1</sup>H-LF-NMR when combined with other methods used for microstructure characterization allows to probe water interactions in both model and complex food systems. By revealing water interactions in food matrices, this method is a powerful, simple, and non-destructive tool to inform on macromolecular interactions and their organization.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"172 ","pages":"Article 111974"},"PeriodicalIF":11.0,"publicationDate":"2025-09-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145216298","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}

引用次数: 0

Pea proteins prepared by self-coacervation: Physicochemical characterization and emulsifying properties 自凝聚法制备豌豆蛋白：理化性质及乳化性质

IF 11 1区农林科学

Food Hydrocolloids Pub Date : 2025-09-17 DOI: 10.1016/j.foodhyd.2025.111995

Zhuojia Lin , Jialing Chen , Zixi Liu , Xiang Li , Zhili Wan , Xiaoquan Yang

{"title":"Pea proteins prepared by self-coacervation: Physicochemical characterization and emulsifying properties","authors":"Zhuojia Lin , Jialing Chen , Zixi Liu , Xiang Li , Zhili Wan , Xiaoquan Yang","doi":"10.1016/j.foodhyd.2025.111995","DOIUrl":"10.1016/j.foodhyd.2025.111995","url":null,"abstract":"<div><div>Self-coacervation is a promising method of mild protein extraction to obtain high-purity plant proteins that retain the native protein structure and have satisfactory functionality. This study prepared the novel pea protein isolates by the self-coacervation process in dispersions of pea flour (F-PPI) and pea protein-concentrated flour via air classification (C-PPI), and then investigated their discrepancies with the conventional pea protein isolate (PPI) extracted by the alkali solubilization and acid precipitation at different pH conditions. The results showed that at neutral conditions (pH 7.0), the solubility, structural stability, interfacial activity, and emulsifying properties of F-PPI and C-PPI solutions possessed comparable performances with PPI. However, at pH 3.5, the former displayed significantly improved structural and functional properties. This is attributed to the fact that the F-PPI and C-PPI had a higher isoelectric point of around pH 5.3 than PPI (pH 4.8), thus endowing these proteins with lower protein aggregation and better functional activity under acidic conditions. Oral tribological measurements revealed that compared to the PPI-based emulsions, the emulsions stabilized by F-PPI and C-PPI had superior oral lubrication capacity at both pH 7.0 and 3.5. However, after the addition of saliva, the friction coefficient of F-PPI and C-PPI stabilized emulsions increased, leading to a reduced lubricating effect. This can be explained by their interactions with salivary mucin, leading to the flocculation of oil droplets (pH 7.0) and an increase in emulsion viscosity (pH 3.5). These findings demonstrate that the self-coacervation can be used as an efficient, mild protein extraction method for preparing the naturally low-denatured pea proteins, especially under acidic conditions.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"172 ","pages":"Article 111995"},"PeriodicalIF":11.0,"publicationDate":"2025-09-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145105352","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}

引用次数: 0

Comparative analysis of thermal, structural and rheological properties of protein isolates and kernel flour from Australian sweet lupin varieties using soy as a reference 以大豆为对照，比较分析澳洲甜豆品种分离蛋白和籽粒粉的热、结构和流变特性

IF 11 1区农林科学

Food Hydrocolloids Pub Date : 2025-09-17 DOI: 10.1016/j.foodhyd.2025.112000

Piyumi Chathurangi Wanniarachchi , Mauro Mocerino , Mark J. Hackett , Michael Nesbit , Greg Shea , Ranil Coorey

{"title":"Comparative analysis of thermal, structural and rheological properties of protein isolates and kernel flour from Australian sweet lupin varieties using soy as a reference","authors":"Piyumi Chathurangi Wanniarachchi , Mauro Mocerino , Mark J. Hackett , Michael Nesbit , Greg Shea , Ranil Coorey","doi":"10.1016/j.foodhyd.2025.112000","DOIUrl":"10.1016/j.foodhyd.2025.112000","url":null,"abstract":"<div><div>This study demonstrates the thermal, structural, and rheological properties of flours and protein isolates of five <em>Lupinus angustifolius</em> L. varieties using soy flour and protein isolate as references. Fourier transform infrared (FTIR) analysis of lupin protein isolates in the amide I region revealed significantly higher β-sheet content than α-helices, together comprising ∼50 % of the secondary protein structures. In differential scanning calorimetry (DSC), lupin flour exhibited two distinct peak denaturation temperatures (Td), first between 90 and 91 °C, second between 103 and 105 °C. Similarly, for lupin protein isolates, the two Tds were at 84–86 °C and 96–98 °C, which represent β-conglutin and α-conglutin, respectively. The microstructure of lupin proteins was less interconnected than soy, which had a more compact and continuous protein network. Lupin protein isolates form a weaker and easily deformed gel network compared to soy protein isolates due to their lower complex viscosity (ŋ∗), storage (G′) and loss (G\") moduli, and higher loss factor (tan δ) compared to soy protein isolates. Flours were characterised as more frequency-dependent than protein isolates, indicating weaker gel networks. Rapid viscosity analyser (RVA) profiles revealed that lupin flours exhibited higher peak (237.00–265.00 cP) and final viscosities (3.38–4.89 cP) than soy flour (166.33 cP and 1.11 cP, respectively), indicating the influence of non-starch components on enhanced pasting properties in lupin flours. Since lupin proteins form weaker gels than soy, process modulations are essential to improve their functionality in food products. Moreover, higher Td associated with lupin flour over soy flour demonstrate greater thermal stability, which is potentially beneficial in heat-processed, high-protein products.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"172 ","pages":"Article 112000"},"PeriodicalIF":11.0,"publicationDate":"2025-09-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145155242","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}

引用次数: 0

Electron beam irradiation unlocks the prebiotic potential of wheat bran arabinoxylan: Structural modification and gut microbiota modulation 电子束辐照解锁麦麸阿拉伯木聚糖的益生元潜力：结构修饰和肠道微生物群调节

IF 11 1区农林科学

Food Hydrocolloids Pub Date : 2025-09-17 DOI: 10.1016/j.foodhyd.2025.111992

Chunping Chen , Yonghui Dong , Min Luo , Yushan Liu , Cong Zheng , Xiaotong Zhai , Yaxian Yang , Jiale Zhao , Caian He , Min Wang

{"title":"Electron beam irradiation unlocks the prebiotic potential of wheat bran arabinoxylan: Structural modification and gut microbiota modulation","authors":"Chunping Chen , Yonghui Dong , Min Luo , Yushan Liu , Cong Zheng , Xiaotong Zhai , Yaxian Yang , Jiale Zhao , Caian He , Min Wang","doi":"10.1016/j.foodhyd.2025.111992","DOIUrl":"10.1016/j.foodhyd.2025.111992","url":null,"abstract":"<div><div>Wheat bran arabinoxylan (WBAX), a major dietary fiber in wheat bran, exhibits limited physiological functionality due to its poor solubility and rigid structure. This study investigated the impact of electron beam irradiation (EBI) at 0, 5, 10, and 15 kGy on the structural, physicochemical, and fermentative properties of insoluble WBAX (WIAX). EBI induced dose-dependent depolymerization, glycosidic bond cleavage, and surface alterations, as evidenced by molecular weight analysis, XRD, FTIR, SEM, BET and thermogravimetric characterization. Moderate doses (5 and 10 kGy) significantly improved solubility, hydration properties, lipid-binding capacity, and adsorption of nitrites, bile salts, cholesterol, and glucose. The most pronounced enhancements were observed at 10 kGy, while 15 kGy caused excessive structural degradation and diminished functional performance. <em>In vitro</em> fecal fermentation further demonstrated that WIAX irradiated at 10 kGy promoted bacterial growth, accelerated carbohydrate utilization, and significantly increased antioxidant activity and short-chain fatty acid (SCFAs) production. Microbial community analysis revealed that EBI- treated WIAX, particularly at 10 kGy, enriched beneficial genera such as <em>Limosilactobacillus</em> and <em>Lactobacillus</em> and reduced the abundance of <em>Proteobacteria</em>, indicating improved prebiotic potential. Overall, these findings establish EBI as an effective, non-thermal approach to modulate the structural and functional properties of WIAX. By optimizing the irradiation dose-especially at 10 kGy-EBI-treated WIAX shows strong potential as a functional dietary fiber for gut microbiota regulation and metabolic health promotion.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"172 ","pages":"Article 111992"},"PeriodicalIF":11.0,"publicationDate":"2025-09-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145105293","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}

引用次数: 0

Green dissolution of waxy corn starch in water-rich deep eutectic solvents: Urea-mediated hydrogen bond disruption for non-derivatizing processing 蜡质玉米淀粉在富水深共晶溶剂中的绿色溶解：尿素介导的非衍生化处理的氢键破坏

IF 11 1区农林科学

Food Hydrocolloids Pub Date : 2025-09-17 DOI: 10.1016/j.foodhyd.2025.111997

Fuchang You , Yu Wu , Yingying Guo , Yancheng Zheng

{"title":"Green dissolution of waxy corn starch in water-rich deep eutectic solvents: Urea-mediated hydrogen bond disruption for non-derivatizing processing","authors":"Fuchang You , Yu Wu , Yingying Guo , Yancheng Zheng","doi":"10.1016/j.foodhyd.2025.111997","DOIUrl":"10.1016/j.foodhyd.2025.111997","url":null,"abstract":"<div><div>Starch faces challenges in achieving green, mild, and efficient dissolution, as breaking its dense hydrogen-bonding network typically requires aggressive treatments that tend to induce degradation. In this study, the dissolution behavior and structural characterization of waxy corn starch (WCS) in water-rich deep eutectic solvents (DESs) composed of urea and choline chloride (ChCl) at high molar ratios were systematically investigated. When the urea/ChCl molar ratio exceeded 6 and the water content was 50 %, the resulting DESs exhibited freezing points as low as −20 °C. Under these conditions, WCS dissolved at 60 °C within 30 min, achieving solubility above 98 %. Molecular dynamics simulations revealed that in the water-rich DES with a urea/ChCl molar ratio of 10:1, urea molecules formed more hydrogen bonds with WCS while weakening intermolecular interactions between WCS chains, thereby promoting dissolution. Moreover, the regenerated WCS transformed from a crystalline to an amorphous structure without chemical changes, showing only a slight decrease in molecular weight and negligible change in thermal decomposition temperature. These findings demonstrate that high-molar-ratio urea/ChCl water-rich DESs serve as non-derivatizing, sustainable solvents for the green dissolution and utilization of WCS, providing valuable insights for the design of DESs and the industrial application of starch-based materials.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"172 ","pages":"Article 111997"},"PeriodicalIF":11.0,"publicationDate":"2025-09-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145105299","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}

引用次数: 0

Mixing commercial plant proteins compromises the mechanical properties of heat-set gels 混合商业植物蛋白会损害热固化凝胶的机械性能

IF 11 1区农林科学

Food Hydrocolloids Pub Date : 2025-09-16 DOI: 10.1016/j.foodhyd.2025.111993

Senna W.P.M. Janssen , Meike Lokker , Laurice Pouvreau , Renko J. de Vries

{"title":"Mixing commercial plant proteins compromises the mechanical properties of heat-set gels","authors":"Senna W.P.M. Janssen , Meike Lokker , Laurice Pouvreau , Renko J. de Vries","doi":"10.1016/j.foodhyd.2025.111993","DOIUrl":"10.1016/j.foodhyd.2025.111993","url":null,"abstract":"<div><div>Mixing plant proteins can be a strategy to improve the nutritional value, availability, costs, flavour and functionality of plant proteins in food products. However, a challenge is that the properties of mixed gels cannot yet be predicted by the characteristics of the protein sources alone. To address this challenge, we here systematically study mixed heat-set gels for two commercial plant protein isolates. Separate stock dispersions of two commercial plant protein isolates (pea (PPI) and fava bean (FBPI)) that differ in gelling properties, were created under various conditions: 10–15 % w/w protein, pH 6 and 7, with or without homogenization (500 bar_2cycles) and mixed at different ratios (4:0, 3:1, 2:2, 1:3 and 0:4). We observed mainly anti-synergistic mixing behaviour: shear moduli and fracture stress were lower for mixed gels than for the pure counterparts. Microstructural analysis did not reveal any phase separation, suggesting the proteins were not incompatible. Lowering the pH from pH 7 to pH 6 led to less anti-synergistic mixing behaviour, but overall, large deformation properties decreased. Our results demonstrate that the possible benefits of mixing must be balanced with the impact of mixing on functionality.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"172 ","pages":"Article 111993"},"PeriodicalIF":11.0,"publicationDate":"2025-09-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145155205","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}

引用次数: 0

Phenolics-rich pectin polysaccharide film from cherry pomace for perishable fruit preservation 樱桃果渣中富含酚类物质的果胶多糖薄膜，用于易腐水果保鲜

IF 11 1区农林科学

Food Hydrocolloids Pub Date : 2025-09-16 DOI: 10.1016/j.foodhyd.2025.111990

Yingdan Zhang , Xinxin Cheng , Fangzhou Xu , Yuyi Du , Wenjing Yang , Peng Wu , Dongxiao Sun-Waterhouse

{"title":"Phenolics-rich pectin polysaccharide film from cherry pomace for perishable fruit preservation","authors":"Yingdan Zhang , Xinxin Cheng , Fangzhou Xu , Yuyi Du , Wenjing Yang , Peng Wu , Dongxiao Sun-Waterhouse","doi":"10.1016/j.foodhyd.2025.111990","DOIUrl":"10.1016/j.foodhyd.2025.111990","url":null,"abstract":"<div><div>Pectin-based films hold promising prospects for food preservation but have limitations e.g. poor mechanical strength, high brittleness, and low antibacterial activity. There are ongoing efforts to resolve the trade-offs among the physical performance variables, antibacterial capacity, and greener manufacturing approach during the development of pectin films. Herein, a phenolic-rich pectin polysaccharide (PRPP) was extracted from cherry pomace via a mild non-thermal acid-assisted ultrasonic-mediated process to produce an edible film for fruit preservation. PRPP is a low-methoxyl pectin rich in phenolics (17.3 mg GAE/g) and arabinose/galactose side chains ((Ara + Gal)/Rha: 5.16 mol%). During film formation, intermolecular/intramolecular cross-links occurred between the pectin backbone and side chains, while the phenolics attached to pectin's side chains provided additional sites for hydrogen bonding, thereby increasing the entanglements and cross-links among pectin molecules. The resulting PRPP films exhibited significantly enhanced mechanical strength (increased by 28.5 %), elongation at break (increased by 322 %), water vapor barrier property (increased by 14.7 %), along with excellent UV-blocking, antioxidant, and antibacterial properties. The PRPP films could significantly prolong the shelf life of strawberries and greatly maintained fruit quality during storage. Interestingly, this PRPP film prepared from cherry pomace's pectin underwent color changes at different pHs, indicating its potential for the development of pH-responsive functional films. This research demonstrates an effective and greener strategy for converting cherry pomace into value-added active fresh-keeping edible films. This innovative approach can be applied to other pectin-rich fruit wastes for value-added utilization.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"172 ","pages":"Article 111990"},"PeriodicalIF":11.0,"publicationDate":"2025-09-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145155257","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}

引用次数: 0

Natural non-nutritive sweetener mogroside interacts with ovalbumin to improve the properties of ovalbumin/citrus pectin bilayer emulsion 天然非营养性甜味剂甜苷与卵清蛋白相互作用，改善卵清蛋白/柑橘果胶双层乳状液的性能

IF 11 1区农林科学

Food Hydrocolloids Pub Date : 2025-09-16 DOI: 10.1016/j.foodhyd.2025.111989

Hua Zhang , Ziheng Jin , Zihan Jin , Keming Zhang , Changhu Xue , Zihao Wei

{"title":"Natural non-nutritive sweetener mogroside interacts with ovalbumin to improve the properties of ovalbumin/citrus pectin bilayer emulsion","authors":"Hua Zhang , Ziheng Jin , Zihan Jin , Keming Zhang , Changhu Xue , Zihao Wei","doi":"10.1016/j.foodhyd.2025.111989","DOIUrl":"10.1016/j.foodhyd.2025.111989","url":null,"abstract":"<div><div>Due to its unique structure, the natural zero-calorie sweetener mogroside (MG) has certain surface activity. This study mixed MG with ovalbumin (OVA) and investigated the interaction between MG and OVA using isothermal titration calorimetry (ITC). It was found that the spontaneous binding between MG and OVA was driven mainly by both hydrophobic interactions and hydrogen bonds. This binding reduced the interfacial tension of OVA from 9.51 mN/m to 7.78 mN/m and the contact angle from 115.1 ± 1.6° to 88.9 ± 0.5°. In addition, a bilayer emulsion was prepared by adsorbing citrus pectin (PC) onto the surface of the OVA-MG complex via electrostatic deposition. Zeta potential and confocal laser scanning microscopy were used to confirm the formation of the bilayer emulsion. A comprehensive investigation of how varying interfacial compositions impacted emulsion properties was conducted. It was found that the presence of MG and PC could improve the resistance of the emulsion to external environmental stress to a certain extent. Confocal Raman spectroscopy showed that MG promoted the interaction between proteins and lipid chains, which might also affect the rheological behavior of the emulsion. In addition, the <em>in vitro</em> digestion characteristics of emulsions with different interface layers loading β-carotene were evaluated. The results showed that MG significantly increased the release of free fatty acids and the delivery efficiency of β-carotene. This experiment offers fresh perspectives on the application of MG in the food industry.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"172 ","pages":"Article 111989"},"PeriodicalIF":11.0,"publicationDate":"2025-09-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145105292","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}

引用次数: 0

Controlling the cold-set gelation of Bovine Serum Albumin protein using alcohol and ionic surfactant 用酒精和离子表面活性剂控制牛血清白蛋白冷凝

IF 11 1区农林科学

Food Hydrocolloids Pub Date : 2025-09-16 DOI: 10.1016/j.foodhyd.2025.111991

Debasish Saha , Sugam Kumar , Purushottam S. Dubey , Jitendra P. Mata , Andrew E. Whitten , Joachim Kohlbrecher , Henrich Frielinghaus , Vinod K. Aswal

{"title":"Controlling the cold-set gelation of Bovine Serum Albumin protein using alcohol and ionic surfactant","authors":"Debasish Saha , Sugam Kumar , Purushottam S. Dubey , Jitendra P. Mata , Andrew E. Whitten , Joachim Kohlbrecher , Henrich Frielinghaus , Vinod K. Aswal","doi":"10.1016/j.foodhyd.2025.111991","DOIUrl":"10.1016/j.foodhyd.2025.111991","url":null,"abstract":"<div><div>Heating of globular protein solutions usually leads to protein denaturation and subsequent gelation at high temperatures. Under “cold gelation”, protein forms a gel at a much lower temperature than its original gelation temperature (<em>T</em><sub>G</sub>), which can be achieved by modifying various physicochemical conditions such as the pH of the solution, the presence of salts, etc. In this study, we investigated the cold gelation of Bovine Serum Albumin (BSA) protein induced by ethanol and controlled by ionic surfactant, using small-angle neutron scattering (SANS), dynamic light scattering (DLS), and rheology The results show that the <em>T</em><sub><em>G</em></sub> of the protein with ethanol is systematically decreased as compared to the that of pure BSA solutions (∼80 °C), reaching ∼60 °C at 10 wt% ethanol, ∼55 °C at 20 wt% and finally as low as ∼38 °C in presence of 30 wt% ethanol in the solution. Rheological measurements demonstrate a significant strengthening of the gel network, with the enhancement in storage modulus (G′) from ∼20 Pa at 0 wt% to ∼250 Pa at 30 wt% ethanol. Structural characterization reveals an increase in fractal dimension with rising ethanol content, indicating denser and more branched gel networks. Interestingly, the addition of the anionic surfactant sodium dodecyl sulfate (SDS) inhibits the alcohol-assisted cold gelation of BSA protein, depending upon the relative amount of ethanol and SDS in solution. The results are explained based on the interplay of interactions in the protein, manipulated by the presence of alcohol, elevated temperatures, and ionic surfactant. Our study highlights the tunability of gelation pathways and offers useful inputs for controlled protein gelation in biomaterial and food industry.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"172 ","pages":"Article 111991"},"PeriodicalIF":11.0,"publicationDate":"2025-09-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145105301","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}

引用次数: 0