Food Hydrocolloids最新文献

{"title":"Construction of enzymatic crosslinking beta-lactoglobulin-camellia oil emulsion gels: Microstructural characterization, stability, and curcumin delivery behavior","authors":"Liwei Zhao ,&nbsp;Taijiao Xiang ,&nbsp;Jiaoyu Wang ,&nbsp;Ziming Xu ,&nbsp;Danli Wang ,&nbsp;Tinglan Yuan ,&nbsp;Ling Li ,&nbsp;Haina Yuan ,&nbsp;Gongshuai Song ,&nbsp;Mengna Zhang ,&nbsp;Jinyan Gong","doi":"10.1016/j.foodhyd.2025.111257","DOIUrl":"10.1016/j.foodhyd.2025.111257","url":null,"abstract":"<div><div>Protein-based emulsion gels with transglutaminase (TG)-catalyzed crosslinking exhibit great potential for delivering hydrophobic bioactive substances. However, effects of TG-catalyzed crosslinking modifications under different reaction times on the structural and textural characterization, stability, and delivery behavior have rarely been reported. This study investigated the effect of TG-catalyzed crosslinking on the physicochemical, structural, and functional properties of β-lactoglobulin (β-LG) - camellia oil (CAO) emulsion gels by cold-gelation under different reaction times. Results revealed that prolonged reaction times could improve the formation of intramolecular and intermolecular covalent bonds between lysine and glutamine residues. Rheological analysis showed an increase in both the storage modulus (G′) and loss modulus (G″), indicating enhanced the gel elasticity and stability. Furthermore, the oxidative stability, the water-holding capacity, and functional stability (freeze-thaw, UV-light, thermal, and salt stability) of the emulsion gels were enhanced by the TG-catalyzed crosslinking. In the <em>in vitro</em> digestion process, the encapsulation efficiency and bioaccessibility of curcumin (Cur) were enhanced in the TG-catalyzed crosslinking β-LG-CAO emulsion gel system when the reaction time exceeded 3 h. The dense gel structure, improved stability, and great Cur delivery behavior of the emulsion gel could be formed by TG-catalyzed crosslinking at 4 h. This study benefited the encapsulation and release behavior of Cur in oil-in-water emulsions and the application in food and nutraceutical products.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"165 ","pages":"Article 111257"},"PeriodicalIF":11.0,"publicationDate":"2025-02-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143509892","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":"Beyond tradition: Improvement of structural and physicochemical properties of genus Gracilaria agar by steam explosion technology","authors":"Changrong Wang ,&nbsp;Mengfan Lin ,&nbsp;Qingyu Yang ,&nbsp;Yue Tang ,&nbsp;Zebin Guo","doi":"10.1016/j.foodhyd.2025.111261","DOIUrl":"10.1016/j.foodhyd.2025.111261","url":null,"abstract":"<div><div>Agar obtained by traditional extraction and processing methods has limitations in its gel properties. This study used steam explosion (SE) technology to modify genus <em>Gracilaria</em> agar for the preparation of high-quality agar. The SE modification conditions were optimized by response surface methodology, and the gel strength of <em>Gracilaria tenuistipitata</em> (<em>G.t</em>) agar and <em>Gracilaria lemaneiformis</em> (<em>G.l</em>) agar were enhanced by 26.52% and 31.56%, respectively. The gel network structure of the agar became more compact and porous due to SE. Although SE did not change the crystal type of the agar, it decreased the crystallinity, which is crucial for its thermal decomposition properties. SE induced structural changes led to an improved physicochemical property. SE increased the 3,6-AG content and decreased the sulfate content of the agar, which significantly improved the gel strength. The whiteness and transparency of the agar were improved, which facilitated in its observation of colonies when used as a culture medium. These results revealed the potential applicability of SE modification to enhance the quality of agar.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"165 ","pages":"Article 111261"},"PeriodicalIF":11.0,"publicationDate":"2025-02-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143509893","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":"Regulatory mechanism of cellulose nanocrystal from tea residue in coordination with calcium ions on the thermal gelation of pea protein amyloid fibrils","authors":"Sixu Lv ,&nbsp;Ye Huang ,&nbsp;Jianxia Xu ,&nbsp;Wenzhe Yin ,&nbsp;Kang Zhong ,&nbsp;Xiaonan Sui ,&nbsp;Yingnan Liu ,&nbsp;Zhenyu Yu ,&nbsp;Yaqing Xiao","doi":"10.1016/j.foodhyd.2025.111258","DOIUrl":"10.1016/j.foodhyd.2025.111258","url":null,"abstract":"<div><div>This study was conducted to investigate the effect of tea residue cellulose nanocrystal (CNC) in coordination with Ca²⁺ on the thermal gelation of pea protein amyloid fibrils (PAFs) and its potential mechanism. The results showed that CNC (0.12%) inhibited the aggregation of PAFs molecules, reduced the surface hydrophobicity and increased the solubility of the solution, and further formed PAFs-based gels with high water holding capacity and high gel strength. However, Ca²⁺ (400 mM) promoted the aggregation of PAFs molecules, which made the solution have high surface hydrophobicity and low solubility, and finally formed a PAFs-based gel with low water holding capacity and high gel strength. The intermolecular force of PAFs-CNC/Ca²⁺ gel was enhanced, and the content of β-sheet conformation was increased. CNC fragments bound to specific amino acid sites of PAFs through non-covalent forces (hydrogen bonding and van der Waals forces), and Ca²⁺ might enhance the cross-linking and interaction between CNC and protein, thus making the two synergies enhance the gel strength and viscoelasticity of PAFs. The research results will provide a new perspective for the diversified regulation of PAFs gel properties and the design and development of PAFs gel-based products.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"166 ","pages":"Article 111258"},"PeriodicalIF":11.0,"publicationDate":"2025-02-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143529032","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":"Characterization of the fibrillation of pumpkin seed protein: Kinetics, structure, and fibril-forming regions","authors":"Hekai Zhao ,&nbsp;Xu Zhang ,&nbsp;Yao Lu ,&nbsp;Yuyang Huang ,&nbsp;Shizhang Yan ,&nbsp;Yang Li","doi":"10.1016/j.foodhyd.2025.111254","DOIUrl":"10.1016/j.foodhyd.2025.111254","url":null,"abstract":"<div><div>Protein fibril formed via the self-assembly of ordered cross-β sheets have attracted considerable attention owing to their functional properties. In this study, we evaluate the fibrillation of pumpkin seed protein (PSP) under acidic heating conditions (pH 2.0, 85 °C, 0–72 h). The growth kinetics, conformational and morphological transitions, and rheological properties of the fibril are analyzed using thioflavin T (Th T) fluorescence, Fourier-transform infrared spectroscopy, circular dichroism, atomic force microscopy, and rotational rheometry. Fibril-forming regions were identified by trapped ion mobility spectrometry time-of-flight mass spectrometry. PSP fibrillation is accompanied by protein hydrolysis, yielding peptide fragments (∼10 kDa) within 24 h. A significant lag phase (0–9 h) is followed by an elongation phase (9–48 h) and subsequent plateau phase (48–60 h), with a conversion rate of 52%. Mature fibrils measuring approximately 1 μm have a height of 7 nm and a compact periodic pitch of 33.4 nm. The variation in height along the direction perpendicular to the fibril axis suggests that fibrillation occurs via a secondary nucleation mechanism. Additionally, the ratio of antiparallel to parallel β-sheets decreased with fibril growth. The solution retained its liquid-like behavior despite an increase in the storage modulus with the degree of fibrillation. The PSP contained abundant hydrophobic fibril-forming regions, with 32 unique peptides (32 unique peptides, 61.04% coverage) from 11S, and 12 unique peptides (12 unique peptides, 60.99% coverage) from 2S. This study provides valuable insights into the fibrillation dynamics of PSP and provides a foundation for its future use as a functional biocompatible material.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"165 ","pages":"Article 111254"},"PeriodicalIF":11.0,"publicationDate":"2025-02-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143480445","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":"Exploring sustainable sources and modification techniques of plant-based alternative proteins for high internal phase emulsion systems: From Camellia oleifera seed meal, copra meal, and soybean meal","authors":"Reng Zou ,&nbsp;Jing Xu ,&nbsp;Zengwang Guo ,&nbsp;Zhongjiang Wang ,&nbsp;Zhaoxian Huang ,&nbsp;Lechuan Wang ,&nbsp;Lianzhou Jiang","doi":"10.1016/j.foodhyd.2025.111256","DOIUrl":"10.1016/j.foodhyd.2025.111256","url":null,"abstract":"<div><div>Meal was a by-product of extracting oil from oilseed crops and a promising source of plant-based alternative proteins, still has limited knowledge of the functional properties of its plant-based alternative proteins. In this study, three plant-based alternative proteins extracted from meal were selected: <em>Camellia oleifera</em> seed protein (CSP), coconut protein isolate (CPI), and soy protein isolate (SPI), which were further modified in their structural and functional properties through ultrasound-assisted glycosylation co-treatment (U-G), and high internal phase emulsions (HIPEs) were prepared. The results indicated that after modification with U-G, the spatial conformation of plant proteins underwent changes, leading to an increase in solubility (14.8%–50.4%), an increase in the absolute value of zeta potential (2mV–11mV), an increase in H₀ (305.9–327.6), and significant improvement in interfacial properties. In particular, compared to other plant proteins, CSP-U-G stabilized-HIPEs exhibited smaller particle sizes, higher apparent viscosity, superior stability, and a finer 3D printing framework. Our findings suggested that U-G was a promising approach to improving the functional properties of plant-based alternative proteins and provided valuable information for expanding the sources of plant-based alternative proteins.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"166 ","pages":"Article 111256"},"PeriodicalIF":11.0,"publicationDate":"2025-02-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143520942","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":"Universal compression behaviour of semi-hard cheeses: A basis for designing plant-based cheese alternatives?","authors":"Jolien de Boer ,&nbsp;Benoît Goldschmidt ,&nbsp;Remko Boom ,&nbsp;Erik van der Linden ,&nbsp;Jasper Landman ,&nbsp;Claudine F. Diedericks","doi":"10.1016/j.foodhyd.2025.111246","DOIUrl":"10.1016/j.foodhyd.2025.111246","url":null,"abstract":"<div><div>In this study, we explored the fracture and rheological behaviour semi-hard cheeses varying in age (0–15 weeks), composition (dry matter 43–58%, protein 22–25% and fat 10–30%) and processing history, through microstructural observation after stepwise uniaxial compression and assessment of the shear deformation within and beyond the linear viscoelastic regime. The semi-hard cheeses exhibited similar behaviour at high deformation regimes despite the compositional variation. Both visual observations and compressive deformation showed significant fracture of the various semi-hard cheeses at 70% strain, leading to subsequent propagation throughout the cheese matrices. Microscopic failure, however, already commenced at ∼30% compression and 10 kPa stress for all cheeses, as determined through image analysis of micrographs from confocal laser scanning microscopy after 0–90% compression. A (semi-)dynamic imaging approach allowed the demonstration and quantification of the structural changes in cheese matrices at different length scales. Insights into the universality of the fracture behaviour of the semi-hard cheese investigated in our study serve as a valuable reference for designing protein-continuous plant-based cheeses.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"165 ","pages":"Article 111246"},"PeriodicalIF":11.0,"publicationDate":"2025-02-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143509889","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":"Corrigendum to “Influence of gluten and starch granules interactions on dough mixing properties in wheat (Triticum aestivum L.)” [Food Hydrocolloids 106 (2020) 105885]","authors":"Xin Gao ,&nbsp;Jingyang Tong ,&nbsp;Lei Guo ,&nbsp;Liwei Yu ,&nbsp;Shaopeng Li ,&nbsp;Bingpeng Yang ,&nbsp;Libin Wang ,&nbsp;Yang Liu ,&nbsp;Faji Li ,&nbsp;Jun Guo ,&nbsp;Shengnan Zhai ,&nbsp;Cheng Liu ,&nbsp;Ata-ur Rehman ,&nbsp;Asgar Farahnaky ,&nbsp;Pei Wang ,&nbsp;Zhonghua Wang ,&nbsp;Xinyou Cao","doi":"10.1016/j.foodhyd.2025.111242","DOIUrl":"10.1016/j.foodhyd.2025.111242","url":null,"abstract":"","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"165 ","pages":"Article 111242"},"PeriodicalIF":11.0,"publicationDate":"2025-02-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143445191","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":"Bean powders improved the quality characteristics of high-moisture extrudate prepared from pea protein isolate: Texture, structure and sensory","authors":"Jiao Ge ,&nbsp;Rong Yang ,&nbsp;Guanchen Liu ,&nbsp;Cuixia Sun ,&nbsp;Yapeng Fang","doi":"10.1016/j.foodhyd.2025.111232","DOIUrl":"10.1016/j.foodhyd.2025.111232","url":null,"abstract":"<div><div>The textured vegetable proteins (TVP) prepared by high-moisture extrusion (HME) are considered ideal substitutes for animal meat due to their similar texture and taste of muscle fibers. However, HME-TVP has the problems of hard texture and low fibrous degree, which cannot meet the consumers’ demand. In this study, the effects of three bean powders (including black kidney bean, chickpea and broad bean powders) on the texture, structure and sensory of high-moisture extruded pea protein isolate (PPI) were investigated to improve the quality of PPI extrudate. The hardness of PPI extrudate significantly decreased with increasing bean powder ratio, which was closely related to the carbohydrates (such as starch and dietary fiber) in bean powder. Synchronously, the incorporation of bean powder enhanced the fibrous degree of PPI extrudate by 16%, possibly because the protein in bean powder promoted the aggregation of PPI. The PPI extrudates containing 15% (w/w) bean powder had obvious fibrous structure and the highest sensory score. During the HME process, bean powder promoted the transformation of random coil structure in textured PPI into α-helix and β-sheet structures, meanwhile promoted the conversion of immobilized water in textured PPI into bound water and free water. Furthermore, the vegetarian beef cube product prepared by PPI extrudate containing 15% (w/w) bean powder was close to the real beef cube in appearance, color and taste, and received high overall acceptability. This study provided valuable insights for improving the quality of plant-based meat analogues.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"165 ","pages":"Article 111232"},"PeriodicalIF":11.0,"publicationDate":"2025-02-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143488680","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":"Underlying the interactions in myofibrillar proteins and κ-carrageenan mixed sols as mediated by microbial transglutaminase based on conformational alterations, rheological behavior and molecular docking","authors":"Yangyang Feng ,&nbsp;Xin Li ,&nbsp;Zihan Zhao ,&nbsp;Baohua Kong ,&nbsp;Chuanai Cao ,&nbsp;Fangda Sun ,&nbsp;Qian Liu ,&nbsp;Xinning Huang","doi":"10.1016/j.foodhyd.2025.111253","DOIUrl":"10.1016/j.foodhyd.2025.111253","url":null,"abstract":"<div><div>The influence of transglutaminase (TG) on the interactional behaviour between myofibrillar protein (MP) and <em>κ</em>-carrageenan (KC) was investigated based on conformational alterations, rheological behavior and molecular docking. The results indicated that the addition of TG or KC obviously decreased the solubility of MP, resulting in a decrease in the fluidity and uniformity of MP sol, but increased the turbidity and surface hydrophobicity of mixed sols (<em>P</em> &lt; 0.05). Meanwhile, an appropriate TG concentration promoted the interaction between MP and KC via hydrophobic interaction and hydrogen bonds and induced protein conformational transformation from α-helix to β-sheet (<em>P</em> &lt; 0.05). Moreover, ultraviolet and fluorescence spectra demonstrated that TG incorporation changed the microenvironment of the aromatic amino acids in MP and increasingly protected them from the fluorescence-quenching effect of KC. Furthermore, microscopic observations revealed that TG-induced protein aggregation gradually intensified with increasing TG concentration and was attenuated in the presence of KC. At a TG concentration of 0.3%, the protein distribution within the MP–KC mixed sol was more uniform and exhibited a weak network structure, possibly explaining the synergistic effect of TG and KC on improving the apparent viscosity, dynamic viscoelasticity and mechanical properties (e.g., firmness, consistency, cohesiveness, and viscosity) of the mixed sols. Additionally, the molecular docking and molecular dynamics (MD) simulation results suggested that van der Waals, electrostatic, and nonpolar solvation energy all help maintain the stability of the interactions of myosin with KC and TG. However, the positive polar solvation energy was not conducive to the stability of the mixed systems. These findings potentially provide a more comprehensive understanding of the TG-mediated interactional behaviour in MP–KC sols.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"165 ","pages":"Article 111253"},"PeriodicalIF":11.0,"publicationDate":"2025-02-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143471269","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":"Pickering food emulsions stabilized by bio-nanoparticle complexes: Super high internal phase and 3D printability","authors":"Yanpeng Cheng ,&nbsp;Qi Dai ,&nbsp;Jiayi Lv,&nbsp;Yingying Wang,&nbsp;Tiexin Sun,&nbsp;Zhiguo Li,&nbsp;Yang Liu,&nbsp;Siqi Huan,&nbsp;Shouxin Liu,&nbsp;Long Bai","doi":"10.1016/j.foodhyd.2025.111251","DOIUrl":"10.1016/j.foodhyd.2025.111251","url":null,"abstract":"<div><div>The use of high internal phase emulsion in renewable engineer functional food materials is challenging. Here, an edible sunflower oil-in-water high internal phase Pickering emulsion (HIPPE) was fabricated through complexation of oppositely charged cellulose nanofibrils (CNF) and nanochitin (NCh) as stabilizing agents. The CNF/NCh complexes can adsorb onto the surfaces of liquid droplets as well as their interfaces, which form a fortified protective stratum and an intricate three-dimensional network structure to prevent the fracturing and fusion of droplets. As a result, HIPPE can be kept at room temperature for at least 60 days, with a super high oil volume fraction of 88% (sunflower oil) and 89% (cyclohexane). In addition, due to the inherent microscale adjustability and viscoelasticity of HIPPEs, they can be used as edible emulgel inks and hierarchical porous structures for 3D printing via direct ink writing. This research will provide crucial insights and a platform for the future development and utilization of multifunctional emulsions in areas such as 3D foods and food-based super-light aerogels.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"165 ","pages":"Article 111251"},"PeriodicalIF":11.0,"publicationDate":"2025-02-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143474121","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}