Pub Date : 2025-11-26DOI: 10.1016/j.foodhyd.2025.112307
Yu Deng , Lirong Dai , Yazhu Yang , Jiajun Yu , Die Dong , Meng Zhao , Chao Yuan , Bo Cui
Oleogels represent a promising strategy for saturated fats substitution, offering unique structural and functional advantages. In this study, high-oil-absorption cryogels were fabricated via a foam-templated approach using freeze-dried aqueous foams. These foams were co-stabilized by octenyl succinic anhydride modified starch (OSAS), hydroxypropyl methylcellulose (HPMC) and tannic acid (TA). Results showed hydrogen bonding was the primary driver of the interactions between OSAS, HPMC, and TA, forming the polysaccharide/polyphenol-based networks in the cryogels. At concentrations of 2 % HPMC and 0.15 % TA, the cryogels exhibited an oil absorption capacity of 75.45 g/g with an oil containment capacity of 75.18 %. Rheological measurement showed that suitable HPMC and TA concentration (HPMC:1.5 %–2 %; TA: 0.1 %–0.15 %) could enhance the network density and hardness of cryogels. This resulted in the formation of oleogels with improved viscoelasticity. Simulated mastication suggested that the addition of HPMC and TA dominated the lubrication properties of the oleogels through structural modulation of cryogels. These findings indicated that starch-based cryogels are ideal for constructing highly oil-absorbent oleogels. This approach not only pioneers a novel strategy to replace saturated fats in foods through tunable physicochemical properties but also unlocks broader potential for developing bio-functional oleogel-based materials in nutritional and pharmaceutical applications.
{"title":"Preparation and characterization of edible oleogels from starch-based aqueous foams via foam-templated approach","authors":"Yu Deng , Lirong Dai , Yazhu Yang , Jiajun Yu , Die Dong , Meng Zhao , Chao Yuan , Bo Cui","doi":"10.1016/j.foodhyd.2025.112307","DOIUrl":"10.1016/j.foodhyd.2025.112307","url":null,"abstract":"<div><div>Oleogels represent a promising strategy for saturated fats substitution, offering unique structural and functional advantages. In this study, high-oil-absorption cryogels were fabricated via a foam-templated approach using freeze-dried aqueous foams. These foams were co-stabilized by octenyl succinic anhydride modified starch (OSAS), hydroxypropyl methylcellulose (HPMC) and tannic acid (TA). Results showed hydrogen bonding was the primary driver of the interactions between OSAS, HPMC, and TA, forming the polysaccharide/polyphenol-based networks in the cryogels. At concentrations of 2 % HPMC and 0.15 % TA, the cryogels exhibited an oil absorption capacity of 75.45 g/g with an oil containment capacity of 75.18 %. Rheological measurement showed that suitable HPMC and TA concentration (HPMC:1.5 %–2 %; TA: 0.1 %–0.15 %) could enhance the network density and hardness of cryogels. This resulted in the formation of oleogels with improved viscoelasticity. Simulated mastication suggested that the addition of HPMC and TA dominated the lubrication properties of the oleogels through structural modulation of cryogels. These findings indicated that starch-based cryogels are ideal for constructing highly oil-absorbent oleogels. This approach not only pioneers a novel strategy to replace saturated fats in foods through tunable physicochemical properties but also unlocks broader potential for developing bio-functional oleogel-based materials in nutritional and pharmaceutical applications.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"173 ","pages":"Article 112307"},"PeriodicalIF":11.0,"publicationDate":"2025-11-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145621070","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}
Pub Date : 2025-11-26DOI: 10.1016/j.foodhyd.2025.112298
Linhai Jiang , Lu Yang , Manman Yu , Liang Yuan , Zengyong Li
Developing intelligent indicators for real-time and accurate food freshness detection in complex environments remains a critical challenge. Herein, a dual-responsive colorimetric and fluorescent label was developed for real-time visual monitoring of food freshness. Curcumin was encapsulated into casein via a pH-driven method, achieving a binding affinity with Vina score of −7.4 kcal/mol. The thermal and photochemical stability of curcumin was significantly enhanced by 62.95 % and 57.50 %, respectively, after being encapsulated into casein. The casein-encapsulated curcumin exhibited intense fluorescence with a lifetime of 0.729 ns. Structural rearrangement induced by molecular interactions endowed the composite with pH-dependent dual-responsive behaviors, characterized by a visible color transition from pale to deep yellow and a reduction in fluorescence intensity as pH increased. The label demonstrated excellent mechanical strength with stress at break of 73.57 MPa, balanced hydrophilicity-hydrophobicity with water contact angle of 90.30°, and high biodegradability with degradation of 77.87 %. The label demonstrated reversible dual-responsive changes to ammonia vapor. Practical application confirmed its capability to dynamically monitor shrimp and fish freshness through real-time visual changes, alongside remarkable reusability. This work provides an eco-friendly, intelligent indicator with significant potential to ensure food quality and safety.
{"title":"A colorimetric and fluorescent label based on water-soluble curcumin encapsulated by casein for real-time visual monitoring of food freshness","authors":"Linhai Jiang , Lu Yang , Manman Yu , Liang Yuan , Zengyong Li","doi":"10.1016/j.foodhyd.2025.112298","DOIUrl":"10.1016/j.foodhyd.2025.112298","url":null,"abstract":"<div><div>Developing intelligent indicators for real-time and accurate food freshness detection in complex environments remains a critical challenge. Herein, a dual-responsive colorimetric and fluorescent label was developed for real-time visual monitoring of food freshness. Curcumin was encapsulated into casein <em>via</em> a pH-driven method, achieving a binding affinity with Vina score of −7.4 kcal/mol. The thermal and photochemical stability of curcumin was significantly enhanced by 62.95 % and 57.50 %, respectively, after being encapsulated into casein. The casein-encapsulated curcumin exhibited intense fluorescence with a lifetime of 0.729 ns. Structural rearrangement induced by molecular interactions endowed the composite with pH-dependent dual-responsive behaviors, characterized by a visible color transition from pale to deep yellow and a reduction in fluorescence intensity as pH increased. The label demonstrated excellent mechanical strength with stress at break of 73.57 MPa, balanced hydrophilicity-hydrophobicity with water contact angle of 90.30°, and high biodegradability with degradation of 77.87 %. The label demonstrated reversible dual-responsive changes to ammonia vapor. Practical application confirmed its capability to dynamically monitor shrimp and fish freshness through real-time visual changes, alongside remarkable reusability. This work provides an eco-friendly, intelligent indicator with significant potential to ensure food quality and safety.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"173 ","pages":"Article 112298"},"PeriodicalIF":11.0,"publicationDate":"2025-11-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145621122","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}
Pub Date : 2025-11-26DOI: 10.1016/j.foodhyd.2025.112305
Yung-Jia Chan , Ping-Hsiu Huang , Xiao-Song Huang , Wen-Chien Lu , Zeng-Chin Liang , Po-Hsien Li
High-pressure processing (HPP) is a non-thermal technology that allows for targeted modifications of flour, the main carbohydrate polymer in wheat flour, thus enhancing the functional and textural properties of flour-based systems. This study evaluated the effects of HPP at 200, 400, and 600 MPa for 5 min on the structural, thermal, and rheological characteristics of wheat starch within flour and dough. The findings revealed pressure-dependent modifications, with moderate pressure (200 MPa) enhancing starch–protein interactions, preserving starch granule integrity, and improving dough elasticity and cohesion. These effects may be attributed to partial unfolding of gluten proteins and rearrangement of hydrogen bonds, which promote non-covalent interactions between starch and protein molecules. In contrast, higher pressures (400–600 MPa) caused extensive starch gelatinisation and protein aggregation, disrupting granular structure and weakening gluten networks, likely through irreversible denaturation and formation of aggregated protein structures. Differential scanning calorimetry (DSC) showed a rise in gelatinisation temperature at 200 MPa, while elevated pressures decreased enthalpy, indicating loss of crystalline order in starch. Rheological analysis further confirmed improved viscoelasticity at moderate pressure, while higher pressure weakened dough structure. Microscopic observations supported these results by showing progressive disruption of starch granules and gluten matrices. Overall, this study demonstrated that HPP can selectively tailor the structure and behaviour of wheat starch in flour and dough systems, offering an effective strategy for modulating textural quality in starch-based food products.
{"title":"Mechanistic insights into high-pressure-induced structural and thermal changes of wheat starch in flour and dough systems","authors":"Yung-Jia Chan , Ping-Hsiu Huang , Xiao-Song Huang , Wen-Chien Lu , Zeng-Chin Liang , Po-Hsien Li","doi":"10.1016/j.foodhyd.2025.112305","DOIUrl":"10.1016/j.foodhyd.2025.112305","url":null,"abstract":"<div><div>High-pressure processing (HPP) is a non-thermal technology that allows for targeted modifications of flour, the main carbohydrate polymer in wheat flour, thus enhancing the functional and textural properties of flour-based systems. This study evaluated the effects of HPP at 200, 400, and 600 MPa for 5 min on the structural, thermal, and rheological characteristics of wheat starch within flour and dough. The findings revealed pressure-dependent modifications, with moderate pressure (200 MPa) enhancing starch–protein interactions, preserving starch granule integrity, and improving dough elasticity and cohesion. These effects may be attributed to partial unfolding of gluten proteins and rearrangement of hydrogen bonds, which promote non-covalent interactions between starch and protein molecules. In contrast, higher pressures (400–600 MPa) caused extensive starch gelatinisation and protein aggregation, disrupting granular structure and weakening gluten networks, likely through irreversible denaturation and formation of aggregated protein structures. Differential scanning calorimetry (DSC) showed a rise in gelatinisation temperature at 200 MPa, while elevated pressures decreased enthalpy, indicating loss of crystalline order in starch. Rheological analysis further confirmed improved viscoelasticity at moderate pressure, while higher pressure weakened dough structure. Microscopic observations supported these results by showing progressive disruption of starch granules and gluten matrices. Overall, this study demonstrated that HPP can selectively tailor the structure and behaviour of wheat starch in flour and dough systems, offering an effective strategy for modulating textural quality in starch-based food products.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"173 ","pages":"Article 112305"},"PeriodicalIF":11.0,"publicationDate":"2025-11-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145681229","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}
Pub Date : 2025-11-26DOI: 10.1016/j.foodhyd.2025.112301
Hossein Mohammad-Beigi , Thomas O. Mason , Tijs Albert Maria Rovers , Tanja Christine Jæger , Marie Sofie Møller , Richard Ipsen , Anni Bygvrå Hougaard , Birte Svensson , Alexander K. Buell
Casein micelles are essential protein structures in milk and are crucial for its stability and nutritional properties. Understanding their self-assembly and dissociation dynamics is vital for applications in food science, biotechnology, and pharmaceuticals. In this study, we introduce Taylor Dispersion Analysis of Micellization (TDAM), a microcapillary-based technique combining intrinsic and extrinsic fluorescence detection to investigate the Ca2+-dependent colloidal stability, viscosity, and association/dissociation kinetics of α-, β-, and κ-casein (αCN, βCN, κCN) micelles. Our results reveal distinctly different behaviors between the types of caseins: αCN micelles exhibit the lowest stability, rapidly dissociating in the absence of Ca2+ and pronounced sensitivity to Ca2+-induced size changes. βCN forms concentration-dependent micellar species, with complex dissociation patterns, while κCN micelles remain highly stable under all investigated conditions. TDAM, complemented by dynamic light scattering (DLS) and finite element modeling, uncovers the critical influence of Ca2+ on micelle association, viscosity, and dissociation kinetics. Although excessive Ca2+ can induce aggregation and thereby reduce the colloidal stability of casein micelles, Ca2+ also promotes the formation of micellar aggregates that are more resistant to dissociation upon dilution under flow conditions and exhibit reduced monomer exchange rates, particularly for κCN. This study provides fundamental insights into casein micellization mechanisms, advancing the understanding of their structural and functional properties. The TDAM methodology offers a powerful tool for characterizing protein self-assembly in complex matrices, with broad implications for dairy science, biomaterials, and protein engineering.
{"title":"Taylor dispersion analysis of micellization (TDAM) reveals distinct assembly and dissociation pathways of α-, β-, and κ-casein micelles","authors":"Hossein Mohammad-Beigi , Thomas O. Mason , Tijs Albert Maria Rovers , Tanja Christine Jæger , Marie Sofie Møller , Richard Ipsen , Anni Bygvrå Hougaard , Birte Svensson , Alexander K. Buell","doi":"10.1016/j.foodhyd.2025.112301","DOIUrl":"10.1016/j.foodhyd.2025.112301","url":null,"abstract":"<div><div>Casein micelles are essential protein structures in milk and are crucial for its stability and nutritional properties. Understanding their self-assembly and dissociation dynamics is vital for applications in food science, biotechnology, and pharmaceuticals. In this study, we introduce Taylor Dispersion Analysis of Micellization (TDAM), a microcapillary-based technique combining intrinsic and extrinsic fluorescence detection to investigate the Ca<sup>2+</sup>-dependent colloidal stability, viscosity, and association/dissociation kinetics of α-, β-, and κ-casein (αCN, βCN, κCN) micelles. Our results reveal distinctly different behaviors between the types of caseins: αCN micelles exhibit the lowest stability, rapidly dissociating in the absence of Ca<sup>2+</sup> and pronounced sensitivity to Ca<sup>2+</sup>-induced size changes. βCN forms concentration-dependent micellar species, with complex dissociation patterns, while κCN micelles remain highly stable under all investigated conditions. TDAM, complemented by dynamic light scattering (DLS) and finite element modeling, uncovers the critical influence of Ca<sup>2+</sup> on micelle association, viscosity, and dissociation kinetics. Although excessive Ca<sup>2+</sup> can induce aggregation and thereby reduce the colloidal stability of casein micelles, Ca<sup>2+</sup> also promotes the formation of micellar aggregates that are more resistant to dissociation upon dilution under flow conditions and exhibit reduced monomer exchange rates, particularly for κCN. This study provides fundamental insights into casein micellization mechanisms, advancing the understanding of their structural and functional properties. The TDAM methodology offers a powerful tool for characterizing protein self-assembly in complex matrices, with broad implications for dairy science, biomaterials, and protein engineering.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"173 ","pages":"Article 112301"},"PeriodicalIF":11.0,"publicationDate":"2025-11-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145681339","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}
Pub Date : 2025-11-25DOI: 10.1016/j.foodhyd.2025.112254
Chi-Han Li , Chih-Ying Chi , Feng-Huei Lin , Chia-Ting Chang , I-Hsuan Yang
While cultured meat has gained attention as a meat analog to improve animal welfare and global sustainability, the conventional fabrication methods pose challenges in achieving cost-effectiveness, optimizing composition, enhancing scalability, and recreating meat-like texture. In this study, alginate-gelatin-carboxymethyl cellulose (AGC) microgrooved and meshed scaffolds, fabricated using a custom-built 3D food printing system, were designed to support the formation of muscle-like and adipose-like tissues. These scaffolds could be assembled in an alternating stacked structure to form layered cultured meat. The defined microgrooved widths of 154.7 ± 6.3 μm and mesh sizes of 0.019 ± 0.005 mm2 supported cell proliferation, differentiation, and the protein expression of myosin and PPAR-γ, without inducing cytotoxicity after 14 days of culture. The porous structure and secreted extracellular matrix facilitated cell infiltration and growth throughout the 3D construct, enabling the seamless integration of the stacked cultured meat. Furthermore, the developed AGC cultured meat exhibited a Young's modulus, shear modulus, and hardness comparable to values reported for raw beef steak. Thus, the AGC sandwich-like stacked cultured meat presents a promising approach to producing steak-like meat analogs, potentially offering a solution to future food security solutions.
{"title":"Biomimetic fabrication of cultured meat using 3D-printed microgrooved and meshed scaffolds with alternating muscle and adipose layers","authors":"Chi-Han Li , Chih-Ying Chi , Feng-Huei Lin , Chia-Ting Chang , I-Hsuan Yang","doi":"10.1016/j.foodhyd.2025.112254","DOIUrl":"10.1016/j.foodhyd.2025.112254","url":null,"abstract":"<div><div>While cultured meat has gained attention as a meat analog to improve animal welfare and global sustainability, the conventional fabrication methods pose challenges in achieving cost-effectiveness, optimizing composition, enhancing scalability, and recreating meat-like texture. In this study, alginate-gelatin-carboxymethyl cellulose (AGC) microgrooved and meshed scaffolds, fabricated using a custom-built 3D food printing system, were designed to support the formation of muscle-like and adipose-like tissues. These scaffolds could be assembled in an alternating stacked structure to form layered cultured meat. The defined microgrooved widths of 154.7 ± 6.3 μm and mesh sizes of 0.019 ± 0.005 mm<sup>2</sup> supported cell proliferation, differentiation, and the protein expression of myosin and PPAR-γ, without inducing cytotoxicity after 14 days of culture. The porous structure and secreted extracellular matrix facilitated cell infiltration and growth throughout the 3D construct, enabling the seamless integration of the stacked cultured meat. Furthermore, the developed AGC cultured meat exhibited a Young's modulus, shear modulus, and hardness comparable to values reported for raw beef steak. Thus, the AGC sandwich-like stacked cultured meat presents a promising approach to producing steak-like meat analogs, potentially offering a solution to future food security solutions.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"173 ","pages":"Article 112254"},"PeriodicalIF":11.0,"publicationDate":"2025-11-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145621062","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}
Pub Date : 2025-11-25DOI: 10.1016/j.foodhyd.2025.112297
Navya Mary Jose, Taco Nicolai, Frédéric Renou, Lazhar Benyahia
This study investigates gelation of κ-carrageenan (κ-car) in water-in-water (W/W) emulsions formed by mixing two incompatible polymers. Gelation was induced by cooling in the presence of KCl. Polyethylene oxide (PEO), dextran (Dex), pullulan (Pul), and gelatin (Gel) were used to prepare the W/W emulsions and to form emulsion gels (emulgels) by adding κ-car. In first instance, κ-car was added to solutions of each of these polymers in order to establish the effect of the presence of these polymers on the gelation of κ-car. It was found that the microstructure of the κ-car network was more homogeneous with increasing viscosity of the polymer solution, but their impact on the storage modulus (G′) and gelation temperature (Tg) was very small. Subsequently, κ-car was added to W/W emulsions where it partitioned between the two phases in a manner that depended on the types of polymers. Strong partitioning to the dispersed phase led to a large decrease of G′ of the emulgels, whereas in the case of weak partitioning, G’ was little influenced compared to κ-car in water. Strain sweeps demonstrated distinct non-linear behaviour depending on the partitioning of the κ-car between the dispersed and the continuous phases. Overall, the results highlight the potential to fine-tune the mechanical properties of W/W emulgels for application in food through selection of the polymers and the phase composition.
{"title":"Impact of partitioning of κ-car between phases on the mechanical properties of water-in-water emulsion gels","authors":"Navya Mary Jose, Taco Nicolai, Frédéric Renou, Lazhar Benyahia","doi":"10.1016/j.foodhyd.2025.112297","DOIUrl":"10.1016/j.foodhyd.2025.112297","url":null,"abstract":"<div><div>This study investigates gelation of κ-carrageenan (κ-car) in water-in-water (W/W) emulsions formed by mixing two incompatible polymers. Gelation was induced by cooling in the presence of KCl. Polyethylene oxide (PEO), dextran (Dex), pullulan (Pul), and gelatin (Gel) were used to prepare the W/W emulsions and to form emulsion gels (emulgels) by adding κ-car. In first instance, κ-car was added to solutions of each of these polymers in order to establish the effect of the presence of these polymers on the gelation of κ-car. It was found that the microstructure of the κ-car network was more homogeneous with increasing viscosity of the polymer solution, but their impact on the storage modulus (G′) and gelation temperature (T<sub>g</sub>) was very small. Subsequently, κ-car was added to W/W emulsions where it partitioned between the two phases in a manner that depended on the types of polymers. Strong partitioning to the dispersed phase led to a large decrease of G′ of the emulgels, whereas in the case of weak partitioning, G’ was little influenced compared to κ-car in water. Strain sweeps demonstrated distinct non-linear behaviour depending on the partitioning of the κ-car between the dispersed and the continuous phases. Overall, the results highlight the potential to fine-tune the mechanical properties of W/W emulgels for application in food through selection of the polymers and the phase composition.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"173 ","pages":"Article 112297"},"PeriodicalIF":11.0,"publicationDate":"2025-11-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145621069","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}
Pub Date : 2025-11-25DOI: 10.1016/j.foodhyd.2025.112275
Ri Chen , Jingjing Zhao , Zhongquan Sui , Dganit Danino , Harold Corke
In this study, α-amylase was used to assist starch nanoparticles (SNP) production through debranching and nanoprecipitation. The molecular structure, aggregation behavior, morphological properties, and digestibility of SNP were investigated. α-amylase hydrolysis pretreatment for 4 h increased the short-chain ratio of SNP, with a peak at DP = 13. This facilitated the formation of smaller and more uniform SNP, particularly at higher antisolvent concentrations. With α-amylase pretreatment, the small molecules reduced steric hindrance and interparticle interaction, resulting in a compact structure and well-defined boundaries during nanoprecipitation as indicated by cryo-EM. The crystalline pattern was mostly influenced by the solvent-to-antisolvent ratio. Prolonging α-amylase hydrolysis time led to loss of long-range crystalline order in SNP, while promoting the formation of submicron crystallites. Additionally, pretreatment increased slowly digestible starch and resistant starch ratios, leading to a lower glycemic response, thereby improving their functional performance. These findings offer valuable insights for optimizing the nanoprecipitation to produce SNP with controlled size and morphology, which enhances their potential as carriers in delivery systems.
{"title":"α-amylase-assisted spherical starch nanoparticles production from waxy rice starch by pullulanase debranching and nanoprecipitation: Structural and functional insights","authors":"Ri Chen , Jingjing Zhao , Zhongquan Sui , Dganit Danino , Harold Corke","doi":"10.1016/j.foodhyd.2025.112275","DOIUrl":"10.1016/j.foodhyd.2025.112275","url":null,"abstract":"<div><div>In this study, α-amylase was used to assist starch nanoparticles (SNP) production through debranching and nanoprecipitation. The molecular structure, aggregation behavior, morphological properties, and digestibility of SNP were investigated. α-amylase hydrolysis pretreatment for 4 h increased the short-chain ratio of SNP, with a peak at DP = 13. This facilitated the formation of smaller and more uniform SNP, particularly at higher antisolvent concentrations. With α-amylase pretreatment, the small molecules reduced steric hindrance and interparticle interaction, resulting in a compact structure and well-defined boundaries during nanoprecipitation as indicated by cryo-EM. The crystalline pattern was mostly influenced by the solvent-to-antisolvent ratio. Prolonging α-amylase hydrolysis time led to loss of long-range crystalline order in SNP, while promoting the formation of submicron crystallites. Additionally, pretreatment increased slowly digestible starch and resistant starch ratios, leading to a lower glycemic response, thereby improving their functional performance. These findings offer valuable insights for optimizing the nanoprecipitation to produce SNP with controlled size and morphology, which enhances their potential as carriers in delivery systems.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"173 ","pages":"Article 112275"},"PeriodicalIF":11.0,"publicationDate":"2025-11-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145681225","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}
Pub Date : 2025-11-25DOI: 10.1016/j.foodhyd.2025.112290
Shiyuan Chang , Yingjie Zhu , Yaqi Zhang , Jia He , Runjie Song , Shengxuan Jin , Changcheng Zhao , Pimiao Huang
Grape seed protein (GSP) is a valuable plant-derived protein, while the magnetic induction electric field (MIEF) represents an emerging nonthermal processing technology whose application to GSP modification has not yet been reported. This study investigated the effects of varying MIEF intensities and treatment durations on the aggregation behavior, structural features, and functional properties of GSP. It was found that MIEF treatment at 800 V for 9 min effectively weakened the aggregation behavior of GSP, with the particle size decreasing by 60.4 %. MIEF treatment induced partial unfolding and exposure of internal hydrophobic cavities of GSP, thereby enhancing GSP functionality, including 1.7 times increase in water solubility, 2.9 times increase in water holding capacity, and 2.3 times increase in oil holding capacity. SDS-PAGE confirmed that the primary protein structure remained intact. Circular dichroism spectroscopy revealed a decrease in α-helix content accompanied by increases in β-turn and β-sheet structures following MIEF treatment. Fluorescence spectroscopy indicated substantial alterations in the tertiary structure. Molecular dynamics simulations corroborated the experiments, showing that MIEF could modulate protein aggregation patterns and destabilize protein conformations, thereby contributing to functional improvements. Collectively, these findings highlight MIEF as a promising approach for enhancing the functionality of GSP, while computational simulations provide valuable insights for optimizing processing parameters and elucidating the underlying modification mechanisms.
{"title":"Magnetic induction electric field: A novel physical approach to modulate the structure, aggregation, and functional property of grape seed protein: An integrated experimental and molecular dynamics simulation study","authors":"Shiyuan Chang , Yingjie Zhu , Yaqi Zhang , Jia He , Runjie Song , Shengxuan Jin , Changcheng Zhao , Pimiao Huang","doi":"10.1016/j.foodhyd.2025.112290","DOIUrl":"10.1016/j.foodhyd.2025.112290","url":null,"abstract":"<div><div>Grape seed protein (GSP) is a valuable plant-derived protein, while the magnetic induction electric field (MIEF) represents an emerging nonthermal processing technology whose application to GSP modification has not yet been reported. This study investigated the effects of varying MIEF intensities and treatment durations on the aggregation behavior, structural features, and functional properties of GSP. It was found that MIEF treatment at 800 V for 9 min effectively weakened the aggregation behavior of GSP, with the particle size decreasing by 60.4 %. MIEF treatment induced partial unfolding and exposure of internal hydrophobic cavities of GSP, thereby enhancing GSP functionality, including 1.7 times increase in water solubility, 2.9 times increase in water holding capacity, and 2.3 times increase in oil holding capacity. SDS-PAGE confirmed that the primary protein structure remained intact. Circular dichroism spectroscopy revealed a decrease in <em>α</em>-helix content accompanied by increases in <em>β</em>-turn and <em>β</em>-sheet structures following MIEF treatment. Fluorescence spectroscopy indicated substantial alterations in the tertiary structure. Molecular dynamics simulations corroborated the experiments, showing that MIEF could modulate protein aggregation patterns and destabilize protein conformations, thereby contributing to functional improvements. Collectively, these findings highlight MIEF as a promising approach for enhancing the functionality of GSP, while computational simulations provide valuable insights for optimizing processing parameters and elucidating the underlying modification mechanisms.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"173 ","pages":"Article 112290"},"PeriodicalIF":11.0,"publicationDate":"2025-11-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145620996","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}
Pub Date : 2025-11-25DOI: 10.1016/j.foodhyd.2025.112293
Yeon Ho Kim , Seung Jun Lee , Bum Ju Kil, Yoon Hyuk Chang
The aims of this study were 1) to prepare boiled fish analog (BFA) by mixing soy protein isolate (SPI) and fish gelatin (FG) cross-linked by transglutaminase (TGase) in a non-heat matrix with κ-carrageenan (Car) and locust bean gum (LBG) in a heat-matrix and 2) to analyze a change in chemical, textural, and morphological properties of BFA. The visual appearance, fish muscle fiber shape, and surface color of BFA samples were successfully similar to those of boiled Convict grouper. Furthermore, the results of FE-SEM exhibited increase the fish muscle fiber shape on the surface of BFA with an increase in the concentration of TGase. The chemical characterization of BFA samples using FT-IR and XRD exhibited considerable changes in characteristic peaks due to the interaction of fragment molecules to polysaccharides by heating and long-chain proteins by TGase. The increasing concentrations of TGase in the BFA enhanced the solvent holding capacity, hardness, springiness, and shear force properties of BFA. These phenomena could be explained by the morphological results of CLSM images of BFA samples, which displayed the smaller and denser droplets with increasing concentrations of TGase. Overall, the results of this study suggested that BFA samples can be applied to the first alternative fish meat products by mimicking fish muscle fiber in the food industry.
{"title":"Preparation of multipolymer hydrogel system-based boiled fish analog for mimicking fish muscle fiber: Combination of heat and non-heat matrixes","authors":"Yeon Ho Kim , Seung Jun Lee , Bum Ju Kil, Yoon Hyuk Chang","doi":"10.1016/j.foodhyd.2025.112293","DOIUrl":"10.1016/j.foodhyd.2025.112293","url":null,"abstract":"<div><div>The aims of this study were 1) to prepare boiled fish analog (BFA) by mixing soy protein isolate (SPI) and fish gelatin (FG) cross-linked by transglutaminase (TGase) in a non-heat matrix with κ-carrageenan (Car) and locust bean gum (LBG) in a heat-matrix and 2) to analyze a change in chemical, textural, and morphological properties of BFA. The visual appearance, fish muscle fiber shape, and surface color of BFA samples were successfully similar to those of boiled <em>Convict grouper</em>. Furthermore, the results of FE-SEM exhibited increase the fish muscle fiber shape on the surface of BFA with an increase in the concentration of TGase. The chemical characterization of BFA samples using FT-IR and XRD exhibited considerable changes in characteristic peaks due to the interaction of fragment molecules to polysaccharides by heating and long-chain proteins by TGase. The increasing concentrations of TGase in the BFA enhanced the solvent holding capacity, hardness, springiness, and shear force properties of BFA. These phenomena could be explained by the morphological results of CLSM images of BFA samples, which displayed the smaller and denser droplets with increasing concentrations of TGase. Overall, the results of this study suggested that BFA samples can be applied to the first alternative fish meat products by mimicking fish muscle fiber in the food industry.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"173 ","pages":"Article 112293"},"PeriodicalIF":11.0,"publicationDate":"2025-11-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145621080","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}
Pub Date : 2025-11-25DOI: 10.1016/j.foodhyd.2025.112294
Haifu Jia , Jinghang Zhang , Yuanyuan Li , Zhishan Song , Yatong Ni , Bo Qu , Xinyan Yang , Qianyu Zhao , Yujun Jiang
The viability of probiotics is susceptible to multiple factors during production, processing, storage, and digestion. To maintain probiotic viability, we employed a medicine and food homology polysaccharide, Angelica sinensis polysaccharide (AP), and sodium alginate (SA) crosslinked with Ca2+ to form functional composite microcapsules (SAPG), which were further coated with chitosan (CS) via electrostatic interactions (SAPCG) for encapsulating Lactobacillus paracasei JY062. Results demonstrated that AP incorporation improved the rheological properties, mechanical strength, and probiotic encapsulation efficiency of the microcapsules. Molecular simulations and FTIR spectroscopy confirmed that the -COO- and -OH groups of SA interacted with the -OH groups of AP through hydrogen bonding. The SAPG (8:1) and SAPCG microcapsules exhibited dense network structures, excellent thermal stability, and optimal swelling rates. Additionally, these microcapsules effectively protected probiotics against viability loss induced by lyophilization, heat treatment, simulated digestion, and storage. After 120 min of exposure to simulated gastric fluid (SGF), probiotic viability decreased by only 1.18 and 1.02 log CFU/mL for SAPG and SAPCG, respectively, while enabling controlled probiotic release in the intestinal environment. When incorporated into frozen pear juice, SAPCG-protected probiotics maintains viability above 7 log CFU/mL after pasteurisation. Following 28 days of storage at 4 °C, probiotic viability in frozen pear juice decreased by only 0.20 log CFU/mL, with minimal changes in pH, total acid content, and viscosity within acceptable ranges. In conclusion, SAPCG demonstrates promising potential for probiotic encapsulation, protection, and targeted release, with practical applications in beverage formulations.
{"title":"Fabrication of chitosan/alginate/angelica polysaccharide functional microcapsules: enhancing the viability of Lactobacillus paracasei in digestion, storage and applications","authors":"Haifu Jia , Jinghang Zhang , Yuanyuan Li , Zhishan Song , Yatong Ni , Bo Qu , Xinyan Yang , Qianyu Zhao , Yujun Jiang","doi":"10.1016/j.foodhyd.2025.112294","DOIUrl":"10.1016/j.foodhyd.2025.112294","url":null,"abstract":"<div><div>The viability of probiotics is susceptible to multiple factors during production, processing, storage, and digestion. To maintain probiotic viability, we employed a medicine and food homology polysaccharide, Angelica sinensis polysaccharide (AP), and sodium alginate (SA) crosslinked with Ca<sup>2+</sup> to form functional composite microcapsules (SAPG), which were further coated with chitosan (CS) via electrostatic interactions (SAPCG) for encapsulating <em>Lactobacillus paracasei</em> JY062. Results demonstrated that AP incorporation improved the rheological properties, mechanical strength, and probiotic encapsulation efficiency of the microcapsules. Molecular simulations and FTIR spectroscopy confirmed that the -COO<sup>-</sup> and -OH groups of SA interacted with the -OH groups of AP through hydrogen bonding. The SAPG (8:1) and SAPCG microcapsules exhibited dense network structures, excellent thermal stability, and optimal swelling rates. Additionally, these microcapsules effectively protected probiotics against viability loss induced by lyophilization, heat treatment, simulated digestion, and storage. After 120 min of exposure to simulated gastric fluid (SGF), probiotic viability decreased by only 1.18 and 1.02 log CFU/mL for SAPG and SAPCG, respectively, while enabling controlled probiotic release in the intestinal environment. When incorporated into frozen pear juice, SAPCG-protected probiotics maintains viability above 7 log CFU/mL after pasteurisation. Following 28 days of storage at 4 °C, probiotic viability in frozen pear juice decreased by only 0.20 log CFU/mL, with minimal changes in pH, total acid content, and viscosity within acceptable ranges. In conclusion, SAPCG demonstrates promising potential for probiotic encapsulation, protection, and targeted release, with practical applications in beverage formulations.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"173 ","pages":"Article 112294"},"PeriodicalIF":11.0,"publicationDate":"2025-11-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145621073","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}