Food Hydrocolloids最新文献

{"title":"Lupin protein isolates influence the nutrition, rheology, and protein profile of lupin-oat yoghurt analogues through probiotic activity","authors":"Damodar Dhakal ,&nbsp;Jane Muir ,&nbsp;Dongdong Ni ,&nbsp;Sushil Dhital","doi":"10.1016/j.foodhyd.2025.111618","DOIUrl":"10.1016/j.foodhyd.2025.111618","url":null,"abstract":"<div><div>Substituting animal proteins with plant-based alternatives offers a sustainable approach to reducing the ecological footprint of livestock farming. This study explores the effect of protein composition on lupin-oat yoghurt analogues, utilizing oat water extract enriched with protein isolates from <em>Lupinus angustifolius</em> (ANG, rich in legumin) and <em>Lupinus albus</em> (ALB, rich in vicilin), fermented with probiotics <em>Lactobacillus plantarum</em> and <em>Bifidobacterium (BB12).</em> Rheological, textural and microstructural analyses revealed that addition of protein isolates improved water-holding capacity, firmness, cohesiveness and gel strength. However, ALB, rich in vicilin, exhibited superior gel matrix density and stability, while ANG, rich in legumin, contributed to enhanced emulsion stability. Acidification kinetics showed similar pH trends, but lower titratable acidity in ANG, sample suggests distinct protein interactions driven by its legumin-rich profile compared to the vicilin-rich ALB. Fermentation effectively reduced Fermentable Oligosaccharides, Disaccharides, Monosaccharides, and Polyols (FODMAPs) content, particularly galactooligosaccharides, suggesting improved digestibility for individuals with irritable bowel syndrome. Organic acid profiling showed greater phytic acid degradation in ANG, which may be linked to enhanced mineral bioavailability. Fermentation led to greater protein breakdown in <em>Lupinus albus</em> than <em>Lupinus angustifolius</em>, with SDS-PAGE revealing dominant vicilin proteins in <em>Lupinus albus</em> and legumin proteins in <em>Lupinus angustifolius</em>, which influenced their gelation behaviour. Allergen mapping suggested probiotic fermentation as a potential method for reducing allergenic proteins, with notable degradation of <em>Lup an 1</em> in ANG. These findings highlight the potential of lupin protein isolates to optimize plant-based yoghurt analogues by enhancing texture, nutrition, and reducing allergenic properties.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"169 ","pages":"Article 111618"},"PeriodicalIF":11.0,"publicationDate":"2025-06-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144242048","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":"Calcium ion-regulated oil body-filled pea protein isolate-inulin emulsion gels for dysphagia-oriented products","authors":"Wenqian Xu,&nbsp;Xiaoyu Li,&nbsp;Xuekang Wen,&nbsp;Yanbo Wang,&nbsp;Baoguo Sun,&nbsp;Duoxia Xu","doi":"10.1016/j.foodhyd.2025.111605","DOIUrl":"10.1016/j.foodhyd.2025.111605","url":null,"abstract":"<div><div>The demographic shift toward an aging population is becoming increasingly pronounced. One consequence of this trend is an increase in swallowing and chewing difficulties among elderly people. This has driven the demand for specifically formulated foods that address dysphagia. This study investigated how different concentrations of Ca²⁺ affected the structural, water-holding, textural, and rheological properties of oil body-filled pea protein isolate-inulin emulsion gels. The aim was to assess their suitability as dysphagia-friendly foods. The results revealed a critical threshold for gel texture modulation via Ca²⁺, with 15 mM Ca²⁺ producing a dense honeycomb-like network structure, improved self-supporting ability, and enhanced water retention. Interactions between Ca²⁺ and functional groups (-OH and COO-) facilitated the formation of “calcium bridges”, which significantly increased gel hardness and cohesiveness. Rheological analysis and the International Dysphagia Diet Standardization Initiative (IDDSI) tests revealed that gel without Ca²⁺ exhibited the highest strain in the creep recovery test and could be classified as level 3 dysphagia foods. As the Ca²⁺ concentration increased, the gels showed higher viscoelastic modulus and lower yield stress, indicating a tendency toward brittleness. These modified gels corresponded to IDDSI levels 4–6. This study offers a theoretical foundation for the design of novel gel-based foods tailored to the specific swallowing needs of individuals with dysphagia.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"169 ","pages":"Article 111605"},"PeriodicalIF":11.0,"publicationDate":"2025-06-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144242046","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":"Development of a dual-layer collagen film with insulating, antioxidant, antimicrobial, and pH-sensitive properties for the maintenance and visual monitoring of shrimp freshness","authors":"Ruimin Ran ,&nbsp;Xiaoyun Luo ,&nbsp;Dongmei Zhai ,&nbsp;Yeqing He ,&nbsp;Xin Guo ,&nbsp;Linjing He ,&nbsp;Guoying Li","doi":"10.1016/j.foodhyd.2025.111603","DOIUrl":"10.1016/j.foodhyd.2025.111603","url":null,"abstract":"<div><div>Accurate temperature control during food transportation is essential, as temperature fluctuations can accelerate bacterial proliferation and fat rancidity. Optimal packaging strategies should, therefore, minimize temperature variability in stored food whilst proactively inhibiting microbial growth, delaying fat rancidity, and enabling real-time freshness monitoring. In this study, a multifunctional bilayer collagen film (COL-OPCD) was prepared by a layer-by-layer deposition technique, consisting of an inner layer with antimicrobial, antioxidant, and pH-sensitive properties (oxidized bilberry extract/Pickering emulsion/collagen) and an outer thermally insulating layer (citric acid-diatomite, CD/collagen). The COL-OPCD film exhibited excellent thermal insulation (thermal diffusivity, 0.131 mm²/s; reflectivity, 64.71 %), antioxidant activity (DPPH radical scavenging, 91.83 %; ABTS radical scavenging, 99.73 %), and antibacterial activity (<em>Escherichia coli</em> inhibition rate, 90.07 %; <em>Staphylococcus aureus</em> inhibition rate, 87.09 %), and allowed real-time monitoring of freshness through visible color changes. It should be emphasized that due to the favorable protection provided by the insulated outer layer, temperature fluctuations inside the package were minimized, with a maximum temperature of 4.80 °C lower than that of the control group, preserving the antioxidant, antimicrobial, and pH-responsive properties of the inner film under high-temperature conditions. An assessment of shrimp preservation at 37 °C showed that the COL-OPCD film not only retarded temperature fluctuations in the packaging shrimp but also extended the shrimp shelf life (9 h) and monitored shrimp freshness in real-time.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"169 ","pages":"Article 111603"},"PeriodicalIF":11.0,"publicationDate":"2025-06-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144242119","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":"Ultrasound regulates pea protein fibrillation: Impact on aggregation kinetics, physicochemical properties, structure and morphology","authors":"Kai Fu ,&nbsp;Tiange Pan ,&nbsp;Hao Wang ,&nbsp;Congyi Xu ,&nbsp;Tianyi Yan ,&nbsp;Yunqi Ni ,&nbsp;Liang Zhang ,&nbsp;Donghong Liu ,&nbsp;Wenjun Wang","doi":"10.1016/j.foodhyd.2025.111609","DOIUrl":"10.1016/j.foodhyd.2025.111609","url":null,"abstract":"<div><div>Ultrasonication can alter the structure of proteins and modify their physicochemical properties. However, there was little information concerning the ultrasound-induced protein fibrillation during the specific fibrillation process. In this study, ultrasound with different power densities (2.17, 2.39, 2.65, 3.19, and 3.73 W/mL) was applied to regulate the growth kinetics of the fibrillation process of pea protein isolates (PPI) at the beginning of fibrillation process (t0), the end of lag phase (t0.1) and the end of the exponential phase (t0.9). The morphology, physicochemical and structural properties of PPI, and the corresponding fibrils (PPIF) were investigated. The results showed that ultrasound treatments with power densities of 2.65, 3.19, and 3.73 W/mL at t0 accelerated fibrillation. The decreased hydrodynamic diameter and the higher proportions of β-sheet of PPI after ultrasonication indicated a disassociation of PPI agglomerates and a structure transformation, which may help PPI go through the lag phase. Ultrasound treatment increased the growth rate of PPIF with higher power density at t0.1 (3.73 W/mL) but lower power density at t0.9 (2.17 W/mL), which may be because appropriate ultrasound power broke protein oligomers into fragments as the template for fibril elongation, resulting in decreased hydrodynamic diameters and increased surface hydrophobicity. The morphology of ultrasound treated samples exhibited shorter contour lengths and higher flexibility than that of the control group, revealing the important role of ultrasound in regulating the protein fibrillation process.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"169 ","pages":"Article 111609"},"PeriodicalIF":11.0,"publicationDate":"2025-06-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144222900","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":"pH-responsive packaging films based on modified bacterial cellulose Pickering emulsions: Effect of emulsion concentration and droplet size","authors":"Yucong Shi,&nbsp;Jianhua Yuan,&nbsp;Yong Qin,&nbsp;Lei Zhou,&nbsp;Junzhen Zhong,&nbsp;Taotao Dai,&nbsp;Jun Chen,&nbsp;Chengmei Liu","doi":"10.1016/j.foodhyd.2025.111607","DOIUrl":"10.1016/j.foodhyd.2025.111607","url":null,"abstract":"<div><div>Active films have gained significant attention as an emerging technology, yet research on Pickering emulsion films with environment-responsive release performance remains limited. Bacterial cellulose (BC) was modified to obtain two solid particles (BC-COOH and BC-PEI), which were subsequently used to prepare corresponding emulsions (PE-COOH and PE-PEI). Characterization revealed differences between the emulsions: PE-COOH showed larger droplets (6.46 μm) with zeta potential of −45.16 mV, whereas PE-PEI exhibited smaller droplets (320.56 nm) with zeta potential of +54.96 mV. Two emulsion types with distinct droplet sizes were incorporated into sodium alginate (SA), prepared composite films (EC and EP). The influence of emulsion concentration (5–15 % v/v) and droplet size on film morphology and properties was investigated. SEM images showed that EP3 showed non-porous morphology, and the surface had good compatibility with SA. The EP3 films exhibited excellent UV–vis blocking efficiency (92.4 % at 280 nm), thermal stability and significant antioxidant properties. However, there were limitations in mechanical properties, with tensile strength and elongation at break decreasing by 15.72 % and 57.90 %, respectively. Based on the comprehensive performance evaluation, EP3 was selected for pH responsiveness testing. The cumulative release of EP3 film was 0.175 μL/mg at pH 7.2. When the pH increased to 8.5 and 10.0, the cumulative release increased by 53.14 % and 76.0 %, respectively. Under alkaline environment (pH 10), the particle size of PE-PEI increased to 6663.33 nm and the zeta potential changed to 37.43 mV, which further confirmed the pH-responsive property of the films loaded with emulsion.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"169 ","pages":"Article 111607"},"PeriodicalIF":11.0,"publicationDate":"2025-06-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144230496","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":"Towards tailoring the viscoelasticity of liquid-liquid interfaces in emulsions: understanding phospholipid-protein interactions at the oil-water interface","authors":"Kerstin Risse ,&nbsp;Jean-Luc Bridot ,&nbsp;Sabrina Bäther ,&nbsp;Leonard Sagis ,&nbsp;Stephan Drusch","doi":"10.1016/j.foodhyd.2025.111594","DOIUrl":"10.1016/j.foodhyd.2025.111594","url":null,"abstract":"<div><div>In the food industry, oil-water emulsions often contain a mixture of phospholipids (PL) and proteins such as β-lactoglobulin (β-LG), resulting in either the displacement of β-LG by PL on the interface or co-existence driven by β-LG + PL interactions. The PL's molecular structure (headgroup, fatty acyl chain), as well as the system's pH and temperature, impact the extent of intermolecular PL-PL interactions. Differences in β-LG + PL interactions as a function of these parameters are also expected.</div><div>This study aimed to analyse the effects of the molecular structure of PL on the interaction with β-LG at the oil-water interface, taking temperature cycles and the system's pH into account. PL with varying headgroups (choline PC, ethanolamine PE) and fatty acyl chain (FA; C18:0, C18:1) were used. The interfacial rheological properties at pH 3.5 and 6.5 were investigated within and outside the linear viscoelastic regime via dilatational and interfacial shear rheological measurements. Possible β-LG + PL interactions were tested in bulk via FTIR measurements.</div><div>In the case of β-LG + <em>saturated</em> PL, an increase in the storage modulus was measured, while the interface behaved predominated viscous in the case of β-LG + <em>unsaturated</em> PL. It is, thus, assumed that the unsaturated PL fully displaced the protein from the interface while the saturated PL co-exist with β-LG, allowing β-LG + PL interactions to occur. In both dilatation and shear rheology, the PE 18:0 + β-LG (<em>small headgroup, saturated FA</em>) initially showed the strongest interface, possibly due to the formation of a crystalline PE:18:0 sublayer on the interface during the cooling step. The storage modulus increased further with decreasing pH due to attractive interactions between β-LG and PL's charged headgroup.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"169 ","pages":"Article 111594"},"PeriodicalIF":11.0,"publicationDate":"2025-06-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144261258","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":"Conversion of D-galactose and guar gum hydrolysate to D-tagatose using L-arabinose isomerase immobilized in sodium alginate-silica hydrogel","authors":"Yan Wen,&nbsp;Yan Zhang,&nbsp;Na Lü,&nbsp;Zehui Xuan,&nbsp;Lili Lu","doi":"10.1016/j.foodhyd.2025.111617","DOIUrl":"10.1016/j.foodhyd.2025.111617","url":null,"abstract":"<div><div>D-tagatose is an attractive functional sweetener, and its production via enzymatic synthesis is simple and environmentally friendly; however, it faces challenges related to enzyme and substrate costs. In this study, a novel and cost-effective method for synthesizing D-tagatose was established using L-arabinose isomerase (L-AI) immobilized within a sodium alginate (SA) composite hydrogel, with the low-cost guar gum as the starting material. Eight inorganic or organic materials were individually combined with SA to encapsulate L-AI. The immobilized enzyme prepared with SA and 50-nm SiO₂ particles demonstrated superior properties, including enhanced mechanical strength and improved reusability, compared to enzymes immobilized with other carriers. The structure of the immobilized enzyme was characterized by scanning electron microscopy, Fourier-transform infrared spectroscopy, and X-ray diffraction. The D-tagatose synthesis reaction using the immobilized enzyme was optimized through both single-factor and statistical methods. The maximum yield of D-tagatose reached 30.12 % from 1 M D-galactose at 68°C, with a productivity of 6.78 g/L/h. The immobilized enzyme was reusable for 20 cycles of reaction at 60 °C, retaining over 55% of its initial activity and accumulating a high amount of 863.74 g/L D-tagatose. Furthermore, it efficiently converted guar gum hydrolysate into D-tagatose, retaining over 50% enzyme activity and yielding 114.32 g/L of D-tagatose after 10 cycles. The excellent enzyme reusability and the exploration of an economic substrate would significantly reduce production costs in large-scale D-tagatose synthesis in the future.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"169 ","pages":"Article 111617"},"PeriodicalIF":11.0,"publicationDate":"2025-06-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144261278","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":"Mechanistic insights into the impact of thermally induced endogenous β-glucan structural modifications on the digestibility of highland barley flour","authors":"Weiwei Hu ,&nbsp;Junchao Gu ,&nbsp;Kai Yang ,&nbsp;Zhiguo Zhang ,&nbsp;Daqun Liu ,&nbsp;Weicheng Wu","doi":"10.1016/j.foodhyd.2025.111589","DOIUrl":"10.1016/j.foodhyd.2025.111589","url":null,"abstract":"<div><div>Thermal processing is inevitable during highland barley (HB) production, but few studies pay attention to the component changes and their impact on HB properties. This study explored the different thermal effects of HB on the molecular, structural and physicochemical properties of β-glucan, as well as the related ultrastructural properties of kernels and the nutritional properties of HB flour (HBF). Microstructure images illustrated that thermal treatment dramatically disrupted endosperm cell walls, roughening their surfaces and almost gelatinised the starch granules of the HB kernel. The molecular weight and polydispersity index of β-glucan decreased from 253.10 ± 0.05 × 10⁴ g/mol to 9.68 ± 0.03 × 10⁴ g/mol and 13.64 ± 0.08 to 1.66 ± 0.04, respectively. X-ray diffraction and infrared spectroscopy demonstrated that thermal processing resulted in the breaking of polymer chains in β-glucan, but its main functional groups remained unchanged. Structural modifications in β-glucan led to reduced thermal stability and lower G′ and G″ values, indicating weaker gel structures. Heat treatment increased the peak viscosity of 100-5-HBF and 150-5-HBF, while reducing it in 150-50-HBF and 200-5-HBF due to the effects of starch gelatinisation and depolymerisation. Meanwhile, higher pasting viscosity and much slower starch digestion were apparent in the HBF than in the HBF-non β-glucan system. The results indicated the structural disruption of endosperm cell walls enhanced component interactions, which was also evidenced by varying β-glucan release rates during initial digestion (20 min). Thus, controlled thermal processing that minimally disrupts cellular structures or forms starch-encapsulating complexes may produce β-glucan-rich products with reduced starch digestibility.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"169 ","pages":"Article 111589"},"PeriodicalIF":11.0,"publicationDate":"2025-06-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144204002","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 and structure-activity relationship of phenolic compounds with different structures on the physicochemical properties of casein and its action mechanism","authors":"Zi-Jian Feng ,&nbsp;Qian-Da Xu ,&nbsp;Nan Chen ,&nbsp;Wei-Cai Zeng","doi":"10.1016/j.foodhyd.2025.111606","DOIUrl":"10.1016/j.foodhyd.2025.111606","url":null,"abstract":"<div><div>Effects of phenolic compounds with different structures on the physicochemical properties of casein were investigated, and their structure–activity relationships and action mechanisms were further explored. Nine phenolic compounds, including ortho-hydroxybenzoic acid (SA), meta-hydroxybenzoic acid (M-HA), para-hydroxybenzoic acid (P-HA), kaempferol (KF), quercetin (QC), myricetin (MC), gallic acid (GA), ellagic acid (EA), and tannic acid (TA), affected the solubility, foaming properties, emulsifying properties, and surface hydrophobicity of casein in diverse action rules. Multispectral analysis revealed that these phenolic compounds exhibited different capabilities to alter casein's structure due to their different structures. At 297 K, the order of their binding constants with α-casein was: SA &gt; M-HA &gt; P-HA, KF &gt; MC &gt; QC, TA &gt; EA &gt; GA; for β-casein was: SA &gt; M-HA &gt; P-HA, MC &gt; KF &gt; QC, TA &gt; EA &gt; GA. The order in which structural characteristics affected their binding capability was: ortho-substitution &gt; meta-substitution &gt; para-substitution; larger molecular weight &gt; smaller molecular weight; and more phenolic hydroxyl groups &gt; fewer hydroxyl groups. Molecular docking analysis indicated that their interactions with casein involved hydrogen bonding, hydrophobic interactions, and van der Waals forces. Molecular electrostatic potential calculations showed that the order of their dipole moments was: SA (4.82) &gt; M-HA (3.78) &gt; P-HA (1.93), MC (5.85) &gt; KF (4.42) &gt; QC (2.91), GA (3.20) &gt; EA (0.0025), which contributed to their different binding capability with casein. All results suggested that the molecular weight, substitution position of hydroxyl groups, number of hydroxyl groups, and molecular polarity of phenolic compounds affected their interactions with casein and played a crucial role for their modifying effects on the structures and properties of casein.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"169 ","pages":"Article 111606"},"PeriodicalIF":11.0,"publicationDate":"2025-06-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144213039","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":"Induction of beta-lactoglobulin amyloid fibril formation by acid heating to reduce allergenicity and improve functional properties: Insights from structural changes and protein hydrolysis","authors":"Lidong Pang ,&nbsp;Ming Liu ,&nbsp;Yue Gao ,&nbsp;Chen Chen ,&nbsp;Qianyu Zhao ,&nbsp;Xinyan Yang ,&nbsp;Wei Zhang ,&nbsp;Yujun Jiang","doi":"10.1016/j.foodhyd.2025.111592","DOIUrl":"10.1016/j.foodhyd.2025.111592","url":null,"abstract":"<div><div>This study investigated the effect of acid heating induction (pH 2.0, heating at 85 °C for 0–12 h) on the allergenicity and functional properties of beta-lactoglobulin (<em>β</em>-Lg) amyloid fibrils (F<em>β</em>-Lg). Sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed the gradual hydrolysis of <em>β</em>-Lg with increasing acid heating time. Thioflavin T fluorescence intensity and transmission electron microscopy further illustrated the formation of amyloid fibrils. The findings from multispectroscopy and peptidomics revealed that the amyloid fibrils induced a more ordered secondary structure in <em>β</em>-Lg (Random coil decreased from 30.4 % to 28 % and β-sheets increased from 23.4 % to 29.5 %), a de-folding of the spatial conformation, and a modification in peptide composition over time. Notably, the allergenicity gradually decreased and the antioxidant activity gradually increased with the prolongation of treatment time. Among them, the IgE binding capacity of <em>β</em>-Lg heated by acid for 12 h was as low as 60.47 % and IgG binding capacity was as low as 80.27 %. This enhancement is attributed to the disruption of allergenic epitopes and the exposure of antioxidant peptides and functional groups, which are a consequence of amyloid fibrils treatment. Moreover, the IgE and IgG binding capacity of F<em>β</em>-Lg induced by acid heating for 10 h was not significantly different from that of 12 h, while the foaming characteristic was the best at 66.33 %. Overall, F<em>β</em>-Lg prepared by acid heat induction for 10 h demonstrated both hypoallergenicity and excellent functional properties. This finding offers novel insights into the preparation of hypoallergenic protein feedstocks.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"169 ","pages":"Article 111592"},"PeriodicalIF":11.0,"publicationDate":"2025-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144203990","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}