Food Hydrocolloids最新文献

{"title":"Revealing the interaction mechanism between pectin and sugar: A case study of peach pectin and trehalose","authors":"Fengzhao Wang ,&nbsp;Jinfeng Bi ,&nbsp;Yuting Huang ,&nbsp;Jian Lyu","doi":"10.1016/j.foodhyd.2025.111388","DOIUrl":"10.1016/j.foodhyd.2025.111388","url":null,"abstract":"<div><div>In order to explore the interaction mechanism between pectin and sugar molecules, a simulation system containing peach pectin and trehalose was constructed. The compared studies were carried out based on the changes in structural characteristics of pectin (P), pectin with heat treatment (HP) and pectin compounding with trehalose with heat treatment (TP). Firstly, pectin from peaches was characterized by the molecular weight, monosaccharide, chemical group and nanostructure. Furthermore, the isothermal titration calorimetry (ITC) and molecular docking were applied to explain the bonding force between pectin and trehalose. Results showed that the highest molecular weight (4.17 × 10⁵ g/mol) depicted in TP illustrated the retarded effect of trehalose on the depolymerization or decomposition of pectin during thermal processing, which might ascribed to the branched chain structure of pectin and the intact three-dimensional network structure. Fourier transform infrared (FT-IR) spectroscopy and nuclear magnetic resonance (NMR) spectra revealed the imbedding of trehalose molecules within the pectin chains. ITC analysis suggested the exothermic binding between trehalose and pectin (Δ<em>H</em> = −27.89 kJ/mol) was primarily driven by enthalpy, and the binding stoichiometry (trehalose/pectin) was above 3:1. Molecular docking confirmed that hydrogen bond with a binding energy of −6.061 kcal/mol was the bonding force between trehalose and pectin. The results will provide a theoretical foundation for elucidating the effect of osmotic dehydration on the structural changes in pectin, which will significantly affect the textural formation of dehydrated fruits and vegetables.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"167 ","pages":"Article 111388"},"PeriodicalIF":11.0,"publicationDate":"2025-03-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143746837","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":"Enhancing protein interactions in Zein-β-lactoglobulin complexes by (-)-Epigallocatechin-3-gallate: Expanding the potential of molecular glues in food application","authors":"Qingbo Jiao ,&nbsp;Gerui Ren ,&nbsp;Nan Lv ,&nbsp;Hao Li ,&nbsp;Tianrong Wang ,&nbsp;Min Huang ,&nbsp;Ruibo Wu ,&nbsp;Zexing Cao ,&nbsp;Hujun Xie","doi":"10.1016/j.foodhyd.2025.111398","DOIUrl":"10.1016/j.foodhyd.2025.111398","url":null,"abstract":"<div><div>Enhancing protein-protein interactions (PPIs) has been intensively studied, and the use of molecular glues is a cutting-edge technology. Although the number of molecular glues approved by the Food and Drug Administration is limited, (−)-Epigallocatechin-3-gallate (EGCG) has shown potential as a molecular glue. This study aimed to investigate how EGCG regulated the mechanism of PPIs using zein and β-lactoglobulin (β-LG) as model proteins. The molecular dynamics simulations revealed that EGCG enhanced hydrogen bonding and hydrophobic interactions in Zein-β-LG complexes, thereby improving their stability and compactness. The Δ<em>G</em> values for the formation of the complexes were all higher than −20 kcal/mol, suggesting strong protein interactions and spontaneous binding process. To validate the theoretical calculations, experimental verification was also conducted. The turbidity, particle size, and ζ-potential results demonstrated that EGCG enhanced the aggregation and stability of Zein-β-LG complexes. Fluorescence experiments indicated that the Δ<em>G</em> values at 298K were −27.57 kJ‧mol⁻¹ at pH 5.5, −26.26 kJ‧mol⁻¹ at pH 7.0, and −25.58 kJ‧mol⁻¹ at pH 2.5, and the corresponding binding sites were 1.036, 1.018, and 1.118, respectively. Thermodynamic parameters suggested that hydrogen bonding and hydrophobic interactions were the main driving forces involved in the complexation of EGCG and Zein-β-LG. EGCG binding significantly altered the secondary structures and surface properties of the complexes. These insights emphasized the potential of EGCG in modulating protein interactions, with significant implications for protein-based material and delivery system in the food and pharmaceutical industries.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"167 ","pages":"Article 111398"},"PeriodicalIF":11.0,"publicationDate":"2025-03-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143746838","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":"Effect of pH and ionic strength on heat-induced pea protein isolate aggregation and gel formation","authors":"Yi Zhang ,&nbsp;Anja Herneke ,&nbsp;Maud Langton ,&nbsp;Mathias Johansson ,&nbsp;Milena Corredig","doi":"10.1016/j.foodhyd.2025.111393","DOIUrl":"10.1016/j.foodhyd.2025.111393","url":null,"abstract":"<div><div>Heat-induced aggregation and gelation of salt extracted pea protein isolates (PPI) was studied as a function of NaCl concentration (0.0–0.4 M) and pH (3.5–8.5). It was hypothesized that an isolate extracted with NaCl, and subsequently dialyzed would show different composition and techno-functional properties depending on its ionic environment. Protein solubility of PPI was affected by NaCl concentrations and pH, with the lowest solubility measured at pH 4.5, regardless of NaCl concentrations. At pH 3.5, solubility was high at low ionic strengths and decreased with increasing salt. At pH between 4.5 and 7, protein solubility increased in solutions at higher NaCl concentrations. At alkaline pH, where proteins are highly charged, salt concentrations did not affect solubility. Heating induced extensive protein aggregation in the presence of NaCl. However, in the case of heated samples in deionized water at pH 3.5 and 8.5, limited aggregation was noticed. These results were confirmed using atomic force microscopy on water redispersed samples. Analysis of viscoelastic properties at the least gelation concentration showed that pH and ionic strength affected not only the stiffness but also the linear viscoelastic regime. This work clearly demonstrated that solubility and thermal stability of PPI are affected by charge properties and how the structure and properties of pea protein aggregates may be modulated through careful control of pH and ionic environment, ultimately affecting the bulk properties of pea protein heat-induced gels.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"167 ","pages":"Article 111393"},"PeriodicalIF":11.0,"publicationDate":"2025-03-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143761211","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The molecular mechanism of enhanced heat-induced polymerization behavior of gluten by mixed β-conglycinin and hydrolysates of glycinin","authors":"Guangzheng Wang ,&nbsp;Xu Cheng ,&nbsp;Tao Yang ,&nbsp;Yisheng Du ,&nbsp;Weiwei Li ,&nbsp;Dandan Li ,&nbsp;Chong Xie ,&nbsp;Runqiang Yang ,&nbsp;Pei Wang","doi":"10.1016/j.foodhyd.2025.111396","DOIUrl":"10.1016/j.foodhyd.2025.111396","url":null,"abstract":"<div><div>The selectively hydrolyzed soy protein composed of β-conglycinin (7S) and glycinin hydrolysates (GH) can improve the quality of cereal products by enhancing the polymerization behavior of gluten. To clarify the potential mechanism, 7S and GH were isolated and combined in varied ratios to examine the effects on the thermal polymerization of gluten. The results demonstrated that both 7S and mixed 7S and GH promoted thermal polymerization of glutenin and gliadin by facilitating the formation of disulfide (SS) bonds, with the optimal effect observed at equal level of 7S and GH. 7S primarily promoted the formation of SS bonds by unfolding the gluten molecular structure upon heating, while the synergistic effect of 7S and GH enabled the polymerized gluten to adopt a more folded conformation with stronger stability than that of 7S. The mixed 7S and GH significantly enhanced the polymerization capacity of α-/γ-gliadins into glutenins, especially for γ-gliadin. The polymerization of gliadin and high molecular weight glutenin subunits (HMS) was promoted by mixed 7S and GH, while the involvement of low molecular weight glutenin subunits (LMS) was inhibited. By promoting gliadin unfolding, 7S and GH enhanced the polymerization tendency of γ-gliadin D2, while the folding behavior suppressed LMS PTDUCD1 participation in cross-linking. This study could provide theoretical support for optimizing the gluten network in wheat-based products supplemented with soy protein and for developing efficient improvers to enhance the techno-functionality of cereal products.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"167 ","pages":"Article 111396"},"PeriodicalIF":11.0,"publicationDate":"2025-03-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143746836","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":"Dose-effect relationship and molecular mechanism of cellulose nanocrystals from green tea residue on the gel behavior of pea protein-derived amyloid fibrils","authors":"Jianxia Xu ,&nbsp;Lu Lin ,&nbsp;Xiyao Liang ,&nbsp;Wenbin Zha ,&nbsp;Wenzhe Yin ,&nbsp;Yingnan Liu ,&nbsp;Zhenyu Yu ,&nbsp;Xiaonan Sui ,&nbsp;Yaqing Xiao","doi":"10.1016/j.foodhyd.2025.111385","DOIUrl":"10.1016/j.foodhyd.2025.111385","url":null,"abstract":"<div><div>In this paper, the dose-effect relationship and molecular mechanism of tea residue derived cellulose nanocrystals (CNC) to improve the gel behavior of pea protein-derived amyloid fibrils (PAFs) were studied. The results showed that the gel strength and water holding capacity of PAFs+1.5 % CNC gel increased respectively by 21.40 % and 37.50 % compared with PAFs gel (<em>p</em> &lt; 0.05). At the same time, CNC promoted the aggregation of PAFs to form protein aggregates with large size and uniform distribution. In addition, compared with PAFs gel, the relative content of α-helix in PAFs+1.5 % CNC gel decreased by 14.90 % (<em>p</em> &lt; 0.05), while the relative content of β-sheet increased by 6.50 % (<em>p</em> &lt; 0.05). With the increase of CNC addition, the ionic bonds, hydrogen bonds and disulfide bonds were strengthened in the PAFs-based composite gel, while the hydrophobic interactions were weakened. Gradient CNC could change the aggregation behavior and multi-scale structure of PAFs molecules to different degrees, promote the exposure of functional groups and strengthen the interaction between molecules, and realize the targeted regulation of PAFs-based gel strength and water holding capacity. This study provided a theoretical reference for the wide application of PAFs-CNC composite gel system in functional protein substrates and food ingredients.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"167 ","pages":"Article 111385"},"PeriodicalIF":11.0,"publicationDate":"2025-03-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143761209","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":"Fabrication and characterization of novel sericin bigels for the co-encapsulation of bioactive ingredients and in vitro gastrointestinal release profile","authors":"Thinzar Aung ,&nbsp;Choon Young Kim ,&nbsp;Mi Jeong Kim","doi":"10.1016/j.foodhyd.2025.111386","DOIUrl":"10.1016/j.foodhyd.2025.111386","url":null,"abstract":"<div><div>While sericin, a protein from silkworms, has been explored on biomaterials and pharmaceuticals, its integration into functional food systems remains underdeveloped. This study addresses the gap in utilizing the sericin in food processing by innovating the novel sericin bigel beads with a co-encapsulation function. Bigel beads were formulated using different ratios (1:1, 1:4, and 1:8) of oleogels and sericin hydrogels encapsulating β-carotene and L-ascorbic acid simultaneously. Their physical characteristics, stability, and release profile through <em>in vitro</em> gastrointestinal (GI) digestion were determined. Bigel beads with lower oleogel content had low hardness values. Bigel beads with equal contents of oleogel and hydrogel exhibited the highest water-holding capacity. On Fourier transform-infrared spectroscopy, no new peak formation or peak shifts were found, signifying the lack of interaction between oleogels and hydrogels. On differential scanning calorimetry analysis, bigel beads with higher sericin hydrogel contents exhibited a stronger and more stable gel network structure. The encapsulation efficiency (EE) of β-carotene in bigel beads with higher oleogel contents showed higher stability, whereas beads with higher hydrogel contents had a higher EE of L-ascorbic acid. Bigel beads stored at 4 °C and 25 °C exhibited similar stability, retaining approximately 40 % of bioactive compounds after 15 days of storage. In the simulated GI digestion of bigel beads, the release rate of encapsulated bioactive compounds was higher during the intestinal phase. This study offers a new perspective on the co-encapsulation of lipophilic and hydrophilic bioactive components in sericin bigel bead, showing promise for the creation of functional food with controlled nutrient delivery.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"166 ","pages":"Article 111386"},"PeriodicalIF":11.0,"publicationDate":"2025-03-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143734515","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":"Interfacial and oil-in-water emulsifying properties of ovalbumin enriched in amyloid-like fibrils and peptides","authors":"Arne M.R. Huyst ,&nbsp;Trui Luyckx ,&nbsp;Margarita Monge-Morera ,&nbsp;John Van Camp ,&nbsp;Jan A. Delcour ,&nbsp;Paul Van der Meeren","doi":"10.1016/j.foodhyd.2025.111367","DOIUrl":"10.1016/j.foodhyd.2025.111367","url":null,"abstract":"<div><div>The combination of heat and enzymatic treatment on ovalbumin (OVA) has been shown to lead to a mixture of amyloid-like fibrils (ALFs) and peptides. Due to their gelling behavior, these mixtures are able to stabilize oil-in-water (O/W) emulsions. As peptides present alongside the OVA ALFs can impact interfacial behavior, it is necessary to remove them. Here, the ability to separate peptides from OVA ALFs by ultracentrifugation and dialysis was investigated. Size exclusion-high performance liquid chromatography results showed that dialysis produced pure OVA ALFs, while ultracentrifugation resulted in both a fibril- and a peptide-enriched fraction. Drop shape tensiometry confirmed that dialysis removed peptides, as a delayed decrease in interfacial tension indicated slower adsorption kinetics of larger structures. This was further supported by an increase in dilatational elasticity compared to samples containing peptides. Emulsions [10.0 % (O/W)] with only fibrils (obtained by dialysis) contained oil droplets that were noticeably larger than those in emulsions containing peptides. However, these emulsions exhibited high creaming and coalescence stability. In contrast, emulsions with peptide-enriched OVA dispersions contained smaller oil droplets but were prone to coalescence due to the lack of a thick viscoelastic layer or a highly viscous continuous phase. The obtained results suggest that peptides, when present, preferentially adsorb at the interface, favoring small emulsion droplets, while the long OVA ALFs form a gel-like network in the continuous phase. This distinct interfacial behavior of peptides and ALFs, in the presence or absence of each other, may be useful when considering their use in food products.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"166 ","pages":"Article 111367"},"PeriodicalIF":11.0,"publicationDate":"2025-03-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143747647","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":"Structural differences in novel pectic polysaccharides from Rosa roxburghii tratt drive distinct gut microbiota profiles: Evidence from in vitro fecal fermentation","authors":"Han Qiu,&nbsp;Angxin Song,&nbsp;You Luo","doi":"10.1016/j.foodhyd.2025.111381","DOIUrl":"10.1016/j.foodhyd.2025.111381","url":null,"abstract":"<div><div><em>Rosa roxburghii</em> Tratt fruits are rich in polysaccharides. Two novel polysaccharides, RRTP-1 and RRTP-2, were purified and characterized as pectin using HPLC, FTIR, GC-MS, and NMR analysis. RRTP-1 was primarily composed of homogalacturonan (HG), featuring a linear main chain with various branching structures including galactose, glucose, arabinose, and mannose residues. RRTP-2 was also a highly branched HG with significant contributions from galactose, rhamnose and arabinose. Compared to RRTP-2 (262.35 kDa, DE 22.03 %), RRTP-1 exhibited a lower molecular weight (179.05 kDa) and a higher degree of esterification (DE, 41.10 %). Both of them were efficiently utilized by gut microbes to produce butyric acid and lower pH. Their structural differences led to distinct gut microbiota composition. RRTP-1 selectively enriched <em>Phocaeicola</em>, <em>Faecalibacterium</em>, and <em>Bifidobacterium</em>, whereas RRTP-2 selectively enriched <em>Limosilactobacillus</em>, <em>Lachnospira</em>, and <em>Coprococcus</em>. Despite structure differences in RRTP-1 and RRTP-2, the keystone microbes and enzymes involved in their degradation exhibited similarities. <em>Bacteroides</em> and <em>Megamonas</em> emerged as dominant contributors. Glycoside hydrolases and carbohydrate esterases were identified as the primary enzymes facilitating their breakdown. These findings suggest that the fine structure of pectin exerts a selective effect on fermenting consortia. Furthermore, both RRTP-1 and RRTP-2 show promise as effective prebiotics.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"166 ","pages":"Article 111381"},"PeriodicalIF":11.0,"publicationDate":"2025-03-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143724265","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":"Unveiling the impact of superheated steam treatment on nutritional, functional and rheological behavior of guar germ protein isolates","authors":"Ankan Kheto ,&nbsp;Rachna Sehrawat ,&nbsp;Khalid Gul ,&nbsp;Sakamon Devahastin","doi":"10.1016/j.foodhyd.2025.111383","DOIUrl":"10.1016/j.foodhyd.2025.111383","url":null,"abstract":"<div><div>Superheated steam (SHS) treatment offers a rapid and efficient approach for modifying biopolymers, minimizing oxidation and degradation compared to conventional heating methods. Guar germ protein isolates (GGPI), rich in essential amino acids, remain underexplored despite their nutritional potential. However, GGPI faces limitations in solubility, digestibility, and gelling ability. This study investigates the impact of SHS treatment on the nutritional, structural, functional, and rheological properties of GGPI at temperatures of 120, 130, and 140 °C for 5 and 10 min. SHS treatment significantly increased <em>in-vitro</em> protein digestibility up to 130 °C-10 min (89.08 %). However, prolonged exposure to higher temperatures led to a significant reduction in essential amino acids, accompanied by changes in carbonyl and disulfide content. At lower SHS temperatures, no apparent changes in band intensity of SDS-PAGE patterns were found. Also, non-significant differences in surface hydrophobicity and particle size variation suggested that larger aggregates of GGPI were not formed. Partial unfolding of GGPI was observed at lower SHS temperatures, as indicated by higher random coil structure. On the other hand, at higher SHS temperatures, reorganization of unfolded structure into compact structure occurred, as noted by a significant impact on β-sheet structure (37.34–45.12 %). Furthermore, increasing SHS temperature and time significantly improved the solubility (5.99 %) and emulsifying capacity (4.14 %) of GGPI up to 130 °C-10 min. Broader particle size distribution profiles of GGPI after SHS treatment might have accounted for the non-significant variation in water absorption capacity (1.9–2.11 g/g) and foaming capacity. Simultaneously, GGPI treated at 120 °C for 10 min formed a weaker gel with frequency-dependent behavior. Conclusively, SHS treatment could be more effective for preprocessing GGPI or other plant proteins at temperatures ranging from 120 to 130 °C to enhance solubility, digestibility, and gelling ability. Limited oxidation at higher SHS temperature (140 °C) reduced essential amino acids but did not form larger aggregates, making it suitable for producing low viscous food items.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"166 ","pages":"Article 111383"},"PeriodicalIF":11.0,"publicationDate":"2025-03-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143760156","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":"Stability and tribological properties of oil-in-water emulsions stabilized with native corn starch and olive leaves phenolic extracts","authors":"Umer Farooq ,&nbsp;Elke Scholten ,&nbsp;Carla Di Mattia ,&nbsp;Marco Faieta ,&nbsp;Paola Pittia","doi":"10.1016/j.foodhyd.2025.111382","DOIUrl":"10.1016/j.foodhyd.2025.111382","url":null,"abstract":"<div><div>In this work, the tribological behaviour of o/w model emulsions stabilized by native corn starch particles in association with a surface-active olive leaf phenolic extract (OLE) was studied. Preliminarily, starch particles were submitted to a high-pressure homogenization pre-treatment and were then separated, by sedimentation, into small (&lt;5 μm, centered on 2.5 μm) and large (&lt;50 μm, centered on 17 μm) particles. Oil-in-water emulsions (10 % dispersed phase, w/v) were prepared using native corn starch particles in the presence of OLE as an emulsifier and characterized for particle size, microstructure and tribological behaviour. OLE and starch particles were both needed for system structuration, providing stability with different mechanisms. OLE triggered oil droplet formation acting as a low molecular weight emulsifier, while starch particles played a different role in the stabilization of the emulsions based on their size: the small starch particles provide stability by adsorbing onto the o/w interface, while the large particles provide stability by forming an interconnected network in the continuous phase, which embedded OLE-stabilized oil droplets. The tribological study showed that emulsions stabilized by small particles showed higher friction coefficients. In these emulsions, the stable emulsion droplets provided particle lubrication. In emulsions stabilized by large particles, lower friction coefficients were observed, which was due to the low stability of the oil droplets. The oil droplets could easily coalesce under flow, causing the formation of an oil film, which was more efficient in lowering the friction coefficient than the oil droplets stabilized with smaller particles. Such findings demonstrated that the size of starch particles played an important role in the stabilization mechanism of the emulsions as well as of their lubrication properties, and can be used to control different properties of emulsions.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"166 ","pages":"Article 111382"},"PeriodicalIF":11.0,"publicationDate":"2025-03-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143734514","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}