Pub Date : 2026-01-05DOI: 10.1016/j.foodhyd.2026.112422
Shihao Cui , Ying Cui , Andreas Blennow , Yuyue Zhong , Xingxun Liu
This study presents an artificial intelligence–driven approach to predicting the printability and textural attributes of 3D-printed food models before the printing process. To enable formulation-based and non-destructive prediction, 12 key features were experimentally extracted from the ink formulation. Building on these data, the research proposes a novel multi-stage deep learning framework, consisting of three specialized neural network models. The first model, a binary classifier, provides an initial screening to determine whether the ink is printable. Upon positive determination, the ink proceeds to the second model, a printability rating classifier that categorizes printability into high, moderate, or low levels, offering a more refined evaluation rarely addressed in previous studies. In parallel, the same input features are used by a third model to simultaneously predict multiple textural properties of the final product — hardness, springiness, gumminess, and cohesiveness — representing a significant advancement toward pre-printing quality assessment. Using a dataset compiled from systematically collected samples, the three models each achieved an average accuracy of nearly 90%. This research streamlined pre-printing evaluations and non-destructive assessments of 3D-printed food items, while also laying the groundwork for future advancements in the field.
{"title":"Artificial intelligence-driven pre-estimation of printability and textural properties of starch-based gels in 3D food printing","authors":"Shihao Cui , Ying Cui , Andreas Blennow , Yuyue Zhong , Xingxun Liu","doi":"10.1016/j.foodhyd.2026.112422","DOIUrl":"10.1016/j.foodhyd.2026.112422","url":null,"abstract":"<div><div>This study presents an artificial intelligence–driven approach to predicting the printability and textural attributes of 3D-printed food models before the printing process. To enable formulation-based and non-destructive prediction, 12 key features were experimentally extracted from the ink formulation. Building on these data, the research proposes a novel multi-stage deep learning framework, consisting of three specialized neural network models. The first model, a binary classifier, provides an initial screening to determine whether the ink is printable. Upon positive determination, the ink proceeds to the second model, a printability rating classifier that categorizes printability into high, moderate, or low levels, offering a more refined evaluation rarely addressed in previous studies. In parallel, the same input features are used by a third model to simultaneously predict multiple textural properties of the final product — hardness, springiness, gumminess, and cohesiveness — representing a significant advancement toward pre-printing quality assessment. Using a dataset compiled from systematically collected samples, the three models each achieved an average accuracy of nearly 90%. This research streamlined pre-printing evaluations and non-destructive assessments of 3D-printed food items, while also laying the groundwork for future advancements in the field.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"175 ","pages":"Article 112422"},"PeriodicalIF":11.0,"publicationDate":"2026-01-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145947898","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 : 2026-01-05DOI: 10.1016/j.foodhyd.2026.112427
Chengpu Chen, Yifei Gao, Hang Xu, Dan Yang, Guanghong Zhou, Keping Ye
Mycoprotein, with high nutritional value and intrinsic fibrous morphology, is a promising ingredient for meat analogs. Yet, achieving stable and well-aligned muscle-like fibers in complex formulations remains challenging. In this study, a full-formulation mycoprotein system—comprising mycoprotein with egg white protein, wheat gluten, dietary fiber, and flavoring agents—was employed to better simulate realistic matrices. The effects of sodium alginate (SA) on the rheological behavior and printability of mycoprotein inks were examined, and subsequent freezing treatment was assessed for its impact on structural stability, texture, and water distribution. Molecular interactions and protein secondary structures were further analyzed to elucidate the underlying mechanisms, including hydrogen bonding enhancement, hydrophobic interaction strengthening, ionic interaction rearrangement, and secondary structure reorganization. Moderate SA addition (0.6–0.8%) significantly enhanced viscoelasticity and structural recovery, improving printing precision and stacking stability. Extrusion induced alignment of mycoprotein hyphae, while SA-supported gelation facilitated the formation of parallel muscle-like fibers. Freezing exerted dual effects: in low-support groups (characterized by low sodium alginate levels and weak gel-supported structural integrity), it highlighted the macroscopic appearance of fibrous structures, whereas in high-SA groups it primarily modulated water distribution while preserving the pre-established fiber continuity and textural properties. Molecular analysis showed SA strengthened hydrogen bonding and hydrophobic interactions and reconstructed ionic bonds, stabilizing the protein network. Correlation analysis confirmed close linkages among molecular forces, water states, and texture. SA combined with 3D printing effectively promoted muscle-like fiber construction in full-formulation mycoprotein, while freezing introduced both structural benefits and textural drawbacks. This study provides theoretical insights and practical guidance for optimizing mycoprotein-based meat analogs under cold-chain conditions.
{"title":"Construction and mechanism of mycoprotein-based meat analogue fibrous structures under the coupled effects of sodium alginate, 3D printing, and freezing","authors":"Chengpu Chen, Yifei Gao, Hang Xu, Dan Yang, Guanghong Zhou, Keping Ye","doi":"10.1016/j.foodhyd.2026.112427","DOIUrl":"10.1016/j.foodhyd.2026.112427","url":null,"abstract":"<div><div>Mycoprotein, with high nutritional value and intrinsic fibrous morphology, is a promising ingredient for meat analogs. Yet, achieving stable and well-aligned muscle-like fibers in complex formulations remains challenging. In this study, a full-formulation mycoprotein system—comprising mycoprotein with egg white protein, wheat gluten, dietary fiber, and flavoring agents—was employed to better simulate realistic matrices. The effects of sodium alginate (SA) on the rheological behavior and printability of mycoprotein inks were examined, and subsequent freezing treatment was assessed for its impact on structural stability, texture, and water distribution. Molecular interactions and protein secondary structures were further analyzed to elucidate the underlying mechanisms, including hydrogen bonding enhancement, hydrophobic interaction strengthening, ionic interaction rearrangement, and secondary structure reorganization. Moderate SA addition (0.6–0.8%) significantly enhanced viscoelasticity and structural recovery, improving printing precision and stacking stability. Extrusion induced alignment of mycoprotein hyphae, while SA-supported gelation facilitated the formation of parallel muscle-like fibers. Freezing exerted dual effects: in low-support groups (characterized by low sodium alginate levels and weak gel-supported structural integrity), it highlighted the macroscopic appearance of fibrous structures, whereas in high-SA groups it primarily modulated water distribution while preserving the pre-established fiber continuity and textural properties. Molecular analysis showed SA strengthened hydrogen bonding and hydrophobic interactions and reconstructed ionic bonds, stabilizing the protein network. Correlation analysis confirmed close linkages among molecular forces, water states, and texture. SA combined with 3D printing effectively promoted muscle-like fiber construction in full-formulation mycoprotein, while freezing introduced both structural benefits and textural drawbacks. This study provides theoretical insights and practical guidance for optimizing mycoprotein-based meat analogs under cold-chain conditions.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"174 ","pages":"Article 112427"},"PeriodicalIF":11.0,"publicationDate":"2026-01-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145921093","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 : 2026-01-05DOI: 10.1016/j.foodhyd.2026.112428
Joana Vieira , Inês E. Silva , Carlos Guerreiro , Carlo Bravo , Alessandra Rinaldi , Rui M. Ramos , Pedro A.R. Fernandes , Manuel A. Coimbra , Virgínia Cruz Fernandes , Victor de Freitas , Elsa Brandão , Susana Soares
Astringency
a complex oral sensation described as dryness, puckering, or tightening - limit consumer acceptance of polyphenol-rich products like black tea, with recognized health benefits. Traditional strategies, such as sugar addition or polyphenol removal, often compromise nutritional quality, highlighting the need for alternative approaches to modulate astringency. One promising strategy involves the use of pectic polysaccharides as modulators of polyphenol-oral constituents interactions.
This study explored two pectic polysaccharides fractions (PPFs) from orange peels with different composition on the interactions between black tea polyphenols and oral constituents, using an advanced oral cell-based quaternary model and trained sensory panel. PPF1 had a high degree of methylesterification (88 %) and high molecular weight (1.004 kDa), while PPF2 had a low degree of methylesterification and low molecular weight (226 kDa). Both fractions exhibited high uronic acid content, 72–80 mol%, respectively.
Results
showed that PPFs decreased black tea polyphenols-oral constituents interactions, particularly in the HSC-3-Mu-SP model (HSC-3 tongue-derived cell line, mucosal pellicle, salivary proteins). Notably, PPF2 showed a greater effect (53 % reduction) of total polyphenols adsorbed (UV–Vis colorimetric assay) and decreased the adsorption of all individual polyphenols, with the stronger effect on theasinensin C (56 % reduction) (HPLC analysis). PPF2 also decreased cystatins–oral component interactions (64 % reduction). Conversely, PPF1 showed a reducing effect on theaflavin-3,3′-digallate adsorption (24 %) and on gRPPs/aPRPs precipitation (33–38 %). Sensory analysis corroborated that both PPFs reduced astringency perception of black tea and contributed to positive astringency subqualities: silkiness associated with high molecular weight and mouthcoating associated with high uronic acid content.
{"title":"Deciphering the potential of orange peel polysaccharides for modulating black tea astringency","authors":"Joana Vieira , Inês E. Silva , Carlos Guerreiro , Carlo Bravo , Alessandra Rinaldi , Rui M. Ramos , Pedro A.R. Fernandes , Manuel A. Coimbra , Virgínia Cruz Fernandes , Victor de Freitas , Elsa Brandão , Susana Soares","doi":"10.1016/j.foodhyd.2026.112428","DOIUrl":"10.1016/j.foodhyd.2026.112428","url":null,"abstract":"<div><h3>Astringency</h3><div>a complex oral sensation described as dryness, puckering, or tightening - limit consumer acceptance of polyphenol-rich products like black tea, with recognized health benefits. Traditional strategies, such as sugar addition or polyphenol removal, often compromise nutritional quality, highlighting the need for alternative approaches to modulate astringency. One promising strategy involves the use of pectic polysaccharides as modulators of polyphenol-oral constituents interactions.</div><div>This study explored two pectic polysaccharides fractions (PPFs) from orange peels with different composition on the interactions between black tea polyphenols and oral constituents, using an advanced oral cell-based quaternary model and trained sensory panel. PPF1 had a high degree of methylesterification (88 %) and high molecular weight (1.004 kDa), while PPF2 had a low degree of methylesterification and low molecular weight (226 kDa). Both fractions exhibited high uronic acid content, 72–80 mol%, respectively.</div></div><div><h3>Results</h3><div>showed that PPFs decreased black tea polyphenols-oral constituents interactions, particularly in the HSC-3-Mu-SP model (HSC-3 tongue-derived cell line, mucosal pellicle, salivary proteins). Notably, PPF2 showed a greater effect (53 % reduction) of total polyphenols adsorbed (UV–Vis colorimetric assay) and decreased the adsorption of all individual polyphenols, with the stronger effect on theasinensin C (56 % reduction) (HPLC analysis). PPF2 also decreased cystatins–oral component interactions (64 % reduction). Conversely, PPF1 showed a reducing effect on theaflavin-3,3′-digallate adsorption (24 %) and on gRPPs/aPRPs precipitation (33–38 %). Sensory analysis corroborated that both PPFs reduced astringency perception of black tea and contributed to positive astringency subqualities: silkiness associated with high molecular weight and mouthcoating associated with high uronic acid content.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"174 ","pages":"Article 112428"},"PeriodicalIF":11.0,"publicationDate":"2026-01-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145920959","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}
Soy protein isolate (SPI) can self-assemble into amyloid-like fibrils with highly ordered β-sheet structures that enhance interfacial and emulsifying properties. However, the influence of protein processing-induced structural variations on fibrillation and interfacial behavior remains unclear. In this study, three SPI samples (SPI2, SPI6, and SPI10) were obtained by neutralizing protein dispersions to different pH values (2, 6, and 10), resulting in distinct molecular conformations. The corresponding soy protein amyloid fibrils (SAF2, SAF6, and SAF10) were prepared by controlled hydrolysis at pH 2 and 85 °C. Structural characterization revealed that SPI2 contained smaller peptides that facilitated β-sheet formation, while SPI10 exhibited extensive unfolding and a slower fibrillation rate. Atomic force microscopy (AFM) observations confirmed morphological differences among SAFs, with SAF2 comprising a mixture of rigid and flexible fibrils, whereas SAF10 primarily formed flexible fibrils prone to aggregation. Interfacial measurements demonstrated that SAF10 adsorbed more rapidly at the oil-water interface, yielding high internal phase emulsions (HIPEs) with the highest interfacial protein content (29.6 %) and a thicker, more elastic interfacial layer. Compared with SPI, SAF-stabilized HIPEs showed smaller droplet sizes and superior storage stability (pH 3–8), while maintaining a gel-like structure even after heating at 90 °C. Remarkably, SAF10-stabilized HIPEs exhibited good freeze-thaw reversibility. These results clarify how protein processing-induced structural variations govern amyloid fibril morphology and interfacial functionality, providing new insights for designing fibrous protein stabilizers to construct stable and functional HIPEs for food applications.
{"title":"Effect of protein pH on acid-thermal induced fibrillation of soy protein: structural characteristics and application in high internal phase emulsions","authors":"Xiaohan Hua , Wenjia Yan , Huilin Luan , Xin Jia , Lijun Yin","doi":"10.1016/j.foodhyd.2026.112424","DOIUrl":"10.1016/j.foodhyd.2026.112424","url":null,"abstract":"<div><div>Soy protein isolate (SPI) can self-assemble into amyloid-like fibrils with highly ordered β-sheet structures that enhance interfacial and emulsifying properties. However, the influence of protein processing-induced structural variations on fibrillation and interfacial behavior remains unclear. In this study, three SPI samples (SPI2, SPI6, and SPI10) were obtained by neutralizing protein dispersions to different pH values (2, 6, and 10), resulting in distinct molecular conformations. The corresponding soy protein amyloid fibrils (SAF2, SAF6, and SAF10) were prepared by controlled hydrolysis at pH 2 and 85 °C. Structural characterization revealed that SPI2 contained smaller peptides that facilitated β-sheet formation, while SPI10 exhibited extensive unfolding and a slower fibrillation rate. Atomic force microscopy (AFM) observations confirmed morphological differences among SAFs, with SAF2 comprising a mixture of rigid and flexible fibrils, whereas SAF10 primarily formed flexible fibrils prone to aggregation. Interfacial measurements demonstrated that SAF10 adsorbed more rapidly at the oil-water interface, yielding high internal phase emulsions (HIPEs) with the highest interfacial protein content (29.6 %) and a thicker, more elastic interfacial layer. Compared with SPI, SAF-stabilized HIPEs showed smaller droplet sizes and superior storage stability (pH 3–8), while maintaining a gel-like structure even after heating at 90 °C. Remarkably, SAF10-stabilized HIPEs exhibited good freeze-thaw reversibility. These results clarify how protein processing-induced structural variations govern amyloid fibril morphology and interfacial functionality, providing new insights for designing fibrous protein stabilizers to construct stable and functional HIPEs for food applications.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"175 ","pages":"Article 112424"},"PeriodicalIF":11.0,"publicationDate":"2026-01-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145975761","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 : 2026-01-02DOI: 10.1016/j.foodhyd.2025.112416
Kun Huang , Xiner Ning , Jianing Cai , Shan Sun , Wanyi Sun , Beiwei Zhu , Xiaoming Guo
Sugar beet pectin (SBP) is a promising food emulsifier, yet its application in food is often limited by insufficient emulsion stability. SBP was crosslinked via MMTM-mediated amidation, establishing covalent bridges between protein-associated amine groups and galacturonic acid carboxyl residues. Successful conjugation was confirmed by a substantial increase in molar mass (5- to 10-fold), the appearance of amide I/II bands in FTIR spectra, and a reduction in lysine content via amino acid analysis. AFM imaging revealed a structural transformation from linear chains to aggregated granular assemblies, accompanied by a moderate increase in surface hydrophobicity. Interfacial characterization showed that the crosslinked SBP (SBPM) attained a higher adsorption capacity (1.94 mg m−2) than native SBP (0.57 mg m−2) and formed a cohesive, viscoelastic film at the n-hexadecane-water interface, as determined by dilatational rheology. Adsorption experiments on polystyrene latex bead surfaces confirmed that the dense SBPM interfacial film confers effective steric stabilization against coalescence. In emulsification assays, SBPM-stabilized emulsions (1 % w/w) exhibited a marked improvement in centrifugal stability, with no visible creaming observed. These results demonstrate that MMTM-driven amidation provides an effective approach for enhancing the emulsion-stabilizing properties of SBP, which holds potential for broadening the industrial applications of SBP in food and products requiring long-term emulsion stability.
{"title":"Enhancing the emulsifying properties of sugar beet pectin through 4-(4, 6-dimethoxy-1, 3, 5-triazin-2-yl)-4-methylmorpholinium chloride-catalyzed crosslinking","authors":"Kun Huang , Xiner Ning , Jianing Cai , Shan Sun , Wanyi Sun , Beiwei Zhu , Xiaoming Guo","doi":"10.1016/j.foodhyd.2025.112416","DOIUrl":"10.1016/j.foodhyd.2025.112416","url":null,"abstract":"<div><div>Sugar beet pectin (SBP) is a promising food emulsifier, yet its application in food is often limited by insufficient emulsion stability. SBP was crosslinked via MMTM-mediated amidation, establishing covalent bridges between protein-associated amine groups and galacturonic acid carboxyl residues. Successful conjugation was confirmed by a substantial increase in molar mass (5- to 10-fold), the appearance of amide I/II bands in FTIR spectra, and a reduction in lysine content via amino acid analysis. AFM imaging revealed a structural transformation from linear chains to aggregated granular assemblies, accompanied by a moderate increase in surface hydrophobicity. Interfacial characterization showed that the crosslinked SBP (SBPM) attained a higher adsorption capacity (1.94 mg m<sup>−2</sup>) than native SBP (0.57 mg m<sup>−2</sup>) and formed a cohesive, viscoelastic film at the <em>n</em>-hexadecane-water interface, as determined by dilatational rheology. Adsorption experiments on polystyrene latex bead surfaces confirmed that the dense SBPM interfacial film confers effective steric stabilization against coalescence. In emulsification assays, SBPM-stabilized emulsions (1 % w/w) exhibited a marked improvement in centrifugal stability, with no visible creaming observed. These results demonstrate that MMTM-driven amidation provides an effective approach for enhancing the emulsion-stabilizing properties of SBP, which holds potential for broadening the industrial applications of SBP in food and products requiring long-term emulsion stability.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"174 ","pages":"Article 112416"},"PeriodicalIF":11.0,"publicationDate":"2026-01-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145921136","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 : 2026-01-02DOI: 10.1016/j.foodhyd.2026.112419
Zipeng Liu , Bin Wang , Chun Cao , Limin Li , Jing Hong , Mei Liu , Jiaying Shang , Chong Liu , Xueling Zheng
The utilization of 3D printing to modulate interactions among food components and develop personalized foods has become a research hotspot. However, studies on multicomponent starch-based foods for 3D printing remain limited, particularly regarding the mechanisms of component interactions and structural evolution. In this work, wheat starch (WS) and soy protein isolate (SP) were used to construct 3D printed gels, and nonlinear rheology was applied to investigate molecular interactions and network evolution during printing. SP addition promoted non-covalent interactions with WS, weakening starch chain interactions and reducing microstructural order, gel viscosity, and b values, while increasing the zero-strain nonlinearity coefficient, thixotropy, and shear-thinning behavior. SP improved the flowability and printing precision of the SP-WS gel, whereas excessive SP (>10 %) led to a bicontinuous phase gel, disrupting the starch network and reducing gel strength. These findings provide guidance for processing foods rich in starch and protein and optimizing formulations for 3D printing. Overall, this study can provide important information for the 3D printing of starch-protein-based foods.
{"title":"Insights into the structural evolution of wheat starch-soy protein isolate gel network during 3D printing based on nonlinear rheology","authors":"Zipeng Liu , Bin Wang , Chun Cao , Limin Li , Jing Hong , Mei Liu , Jiaying Shang , Chong Liu , Xueling Zheng","doi":"10.1016/j.foodhyd.2026.112419","DOIUrl":"10.1016/j.foodhyd.2026.112419","url":null,"abstract":"<div><div>The utilization of 3D printing to modulate interactions among food components and develop personalized foods has become a research hotspot. However, studies on multicomponent starch-based foods for 3D printing remain limited, particularly regarding the mechanisms of component interactions and structural evolution. In this work, wheat starch (WS) and soy protein isolate (SP) were used to construct 3D printed gels, and nonlinear rheology was applied to investigate molecular interactions and network evolution during printing. SP addition promoted non-covalent interactions with WS, weakening starch chain interactions and reducing microstructural order, gel viscosity, and <em>b</em> values, while increasing the zero-strain nonlinearity coefficient, thixotropy, and shear-thinning behavior. SP improved the flowability and printing precision of the SP-WS gel, whereas excessive SP (>10 %) led to a bicontinuous phase gel, disrupting the starch network and reducing gel strength. These findings provide guidance for processing foods rich in starch and protein and optimizing formulations for 3D printing. Overall, this study can provide important information for the 3D printing of starch-protein-based foods.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"174 ","pages":"Article 112419"},"PeriodicalIF":11.0,"publicationDate":"2026-01-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145921134","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 : 2026-01-02DOI: 10.1016/j.foodhyd.2025.112417
Enning Zhou , Kwan You , Lai Wei , Sunandita Ghosh , Jan Ilavsky , Da Chen
Plant proteins typically exhibit inferior gelling capacity compared to their animal counterparts due to limited covalent cross-linking. Seeking native cross-linkers was thus essential to address the limitation with minimal safety concerns. Here, the effects of genipin, a natural pigment and cross-linker, on the rheology, micro-and nanostructure, and digestibility of pea protein (PP) suspensions and their heat-set gels were investigated. Genipin increased the apparent viscosity and storage modulus of PP suspensions in a dose-dependent manner. Functional-group assay and sodium dodecyl sulfate–polyacrylamide gel electrophoresis showed decreases in the free amino and sulfhydryl groups of PP alongside increases in particle size and the proportion of high-molecular-weight aggregates. Upon thermal gelation, geipin elevated PP gel viscoelasticity, characteristic relaxation time, and residual stress with increasing concentration. Confocal laser scanning and scanning electron microscopy showed that genipin addition gradually decreased the cracks and aggregates size, leading to a more continuous and homogenous network with finer walls. Ultra-small and small angle X-ray scattering showed genipin suppressed the formation of large aggregates, stabilized intermediate medium sized aggregates, and introduced nanoscale heterogeneity. Solvent-based dissociation assays showed a continuous decrease in protein extractability as genipin concentration increased, consistent with covalent immobilization. In-vitro digestion showed that apparent protein digestibility was not altered by genipin cross-linking. However, intestinal digesta contained higher-molecular-weight peptides with a lower degree of hydrolysis than genipin-free control. These findings demonstrate that genipin effectively cross-links pea protein to strengthen gel networks across multiple length scales and provides a green approach to enhance the firmness of PP-based foods.
{"title":"Genipin as a natural cross-linker strengthens pea protein gel: a mechanistic study","authors":"Enning Zhou , Kwan You , Lai Wei , Sunandita Ghosh , Jan Ilavsky , Da Chen","doi":"10.1016/j.foodhyd.2025.112417","DOIUrl":"10.1016/j.foodhyd.2025.112417","url":null,"abstract":"<div><div>Plant proteins typically exhibit inferior gelling capacity compared to their animal counterparts due to limited covalent cross-linking. Seeking native cross-linkers was thus essential to address the limitation with minimal safety concerns. Here, the effects of genipin, a natural pigment and cross-linker, on the rheology, micro-and nanostructure, and digestibility of pea protein (PP) suspensions and their heat-set gels were investigated. Genipin increased the apparent viscosity and storage modulus of PP suspensions in a dose-dependent manner. Functional-group assay and sodium dodecyl sulfate–polyacrylamide gel electrophoresis showed decreases in the free amino and sulfhydryl groups of PP alongside increases in particle size and the proportion of high-molecular-weight aggregates. Upon thermal gelation, geipin elevated PP gel viscoelasticity, characteristic relaxation time, and residual stress with increasing concentration. Confocal laser scanning and scanning electron microscopy showed that genipin addition gradually decreased the cracks and aggregates size, leading to a more continuous and homogenous network with finer walls. Ultra-small and small angle X-ray scattering showed genipin suppressed the formation of large aggregates, stabilized intermediate medium sized aggregates, and introduced nanoscale heterogeneity. Solvent-based dissociation assays showed a continuous decrease in protein extractability as genipin concentration increased, consistent with covalent immobilization. <em>In-vitro</em> digestion showed that apparent protein digestibility was not altered by genipin cross-linking. However, intestinal digesta contained higher-molecular-weight peptides with a lower degree of hydrolysis than genipin-free control. These findings demonstrate that genipin effectively cross-links pea protein to strengthen gel networks across multiple length scales and provides a green approach to enhance the firmness of PP-based foods.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"174 ","pages":"Article 112417"},"PeriodicalIF":11.0,"publicationDate":"2026-01-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145880986","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 : 2026-01-02DOI: 10.1016/j.foodhyd.2025.112415
Yaxin Yin , Yingnan Zou , Chin Ping Tan , Deyang Li , Xiaojiao Zheng , Daodong Pan , Maolin Tu
Probiotics demonstrate significant efficacy in regulating gut microbiota and enhancing immune function. However, their sensitivity severely limited their application. This study employed transglutaminase (TGase) to enzymatically cross-link whey protein isolate (WPI) and Gum Arabic (GA), and prepared microgel particles. These were utilized as stabilizers in high internal phase emulsions (HIPEs) to encapsulate Lactobacillus reuteri DSM 17938 (L. reuteri). SDS-PAGE analyses confirmed that TGase-induced polymerization, showing the corresponding formation of high-molecular-weight polymers. This covalent cross-linking inherently altered the microgel structure, leading to significant functional modifications. Particle size and rheological results indicated that HIPEs exhibited excellent viscoelasticity and stability. By investigating the effects of WPI-GA concentration and oil volume fraction, it was found that L. reuteri encapsulated in HIPEs demonstrated outstanding thermal stability and resistance to simulated gastrointestinal digestion. After simulated gastric digestion, the viability of probiotics decreased from 7.6 to 3.0 Lg CFU/mL. The probiotics in the 4% microgel-stabilized HIPEs maintained a higher count of 5.1 Lg CFU/mL. These results show that protein-polysaccharide microgel-stabilized HIPEs can protect probiotics more effectively. The findings also provide useful guidance for developing stable probiotic delivery systems.
益生菌具有显著的调节肠道菌群和增强免疫功能的功效。然而，它们的敏感性严重限制了它们的应用。本研究采用转谷氨酰胺酶（TGase）对乳清分离蛋白（WPI）和阿拉伯胶（GA）进行酶交联，制备微凝胶颗粒。它们被用作高内相乳剂（HIPEs）的稳定剂，以包封罗伊氏乳杆菌DSM 17938 （L. reuteri）。SDS-PAGE分析证实了tgase诱导的聚合，显示出相应的高分子量聚合物的形成。这种共价交联固有地改变了微凝胶结构，导致显著的功能修饰。颗粒大小和流变学结果表明，HIPEs具有优异的粘弹性和稳定性。通过研究WPI-GA浓度和油体积分数的影响，发现HIPEs包封的罗伊氏乳杆菌表现出良好的热稳定性和对模拟胃肠道消化的抗性。模拟胃消化后，益生菌活力从7.6 Lg CFU/mL下降到3.0 Lg CFU/mL。在4%微凝胶稳定的HIPEs中，益生菌数量保持在5.1 Lg CFU/mL。结果表明，蛋白质-多糖微凝胶稳定的HIPEs对益生菌具有较好的保护作用。研究结果也为开发稳定的益生菌输送系统提供了有益的指导。
{"title":"TGase-induced WPI-GA microgels for stabilized HIPEs and encapsulation probiotics with enhanced thermal stability and gastrointestinal survival","authors":"Yaxin Yin , Yingnan Zou , Chin Ping Tan , Deyang Li , Xiaojiao Zheng , Daodong Pan , Maolin Tu","doi":"10.1016/j.foodhyd.2025.112415","DOIUrl":"10.1016/j.foodhyd.2025.112415","url":null,"abstract":"<div><div>Probiotics demonstrate significant efficacy in regulating gut microbiota and enhancing immune function. However, their sensitivity severely limited their application. This study employed transglutaminase (TGase) to enzymatically cross-link whey protein isolate (WPI) and Gum Arabic (GA), and prepared microgel particles. These were utilized as stabilizers in high internal phase emulsions (HIPEs) to encapsulate <em>Lactobacillus reuteri</em> DSM 17938 (<em>L. reuteri</em>). SDS-PAGE analyses confirmed that TGase-induced polymerization, showing the corresponding formation of high-molecular-weight polymers. This covalent cross-linking inherently altered the microgel structure, leading to significant functional modifications. Particle size and rheological results indicated that HIPEs exhibited excellent viscoelasticity and stability. By investigating the effects of WPI-GA concentration and oil volume fraction, it was found that <em>L. reuteri</em> encapsulated in HIPEs demonstrated outstanding thermal stability and resistance to simulated gastrointestinal digestion. After simulated gastric digestion, the viability of probiotics decreased from 7.6 to 3.0 Lg CFU/mL. The probiotics in the 4% microgel-stabilized HIPEs maintained a higher count of 5.1 Lg CFU/mL. These results show that protein-polysaccharide microgel-stabilized HIPEs can protect probiotics more effectively. The findings also provide useful guidance for developing stable probiotic delivery systems.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"175 ","pages":"Article 112415"},"PeriodicalIF":11.0,"publicationDate":"2026-01-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145975755","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}
To enhance the stability and bioavailability of chlorogenic acid (CHA), laccase (LAC)-catalyzed cross-linking was employed to prepare whey protein isolate (WPI)-CHA nanocomposites. The complexes exhibited sensitivity to variation in pH and temperature. This study investigated the effects of pH (3.0–7.0) and temperature (15–45 °C) on the structural, antioxidant, and functional properties of WPI-CHA (WC) and WPI-LAC-CHA (WLC) complexes. Under the optimal catalytic conditions for LAC (pH 5.0, 35 °C), WLC complexes exhibited the highest structural stability, characterized by the smallest particle size (133 ± 3.93 nm), highest surface hydrophobicity (822.79 ± 1.74), and lowest free amino content (209.99 ± 1.09 mM/mL). The 52 % fluorescence quenching, amide I red shift and >180 kDa aggregates formation confirmed tertiary structure unfolding and covalent cross-linking, indicative of efficient protein-polyphenol conjugation. WLC complexes exhibited optimal radical scavenging activity at pH 5.0 and 35 °C, with DPPH and ABTS scavenging rates of 78.33 ± 5.11 (μmoL TE/g) and 83.99 ± 1.92 %, respectively. Following in vitro gastrointestinal digestion, WLC complexes retained superior antioxidant capacity (48.5 ± 2.21 μmoL TE/g for DPPH and 70.5 ± 1.70 % for ABTS) compared to free CHA and WC complexes. WLC complexes exhibited significantly greater UV protective efficiency of CHA, functional characteristics (solubility, EAI, ESI, FC and FS) compared to WC. These findings highlighted LAC-catalyzed cross-linking as an effective strategy to fabricate high-performance WPI-CHA nanocomposites, which might be applied in nano-carriers and packaging materials in the food industry.
{"title":"Covalent cross-linking of whey protein isolate-chlorogenic acid nanoparticles mediated by laccase: Structural, antioxidant and functional characteristics","authors":"Bingjie Xue, Jing Zhang, Sijia Yan, Yanhui Yang, Wupeng Ge, Lili Zhao","doi":"10.1016/j.foodhyd.2025.112418","DOIUrl":"10.1016/j.foodhyd.2025.112418","url":null,"abstract":"<div><div>To enhance the stability and bioavailability of chlorogenic acid (CHA), laccase (LAC)-catalyzed cross-linking was employed to prepare whey protein isolate (WPI)-CHA nanocomposites. The complexes exhibited sensitivity to variation in pH and temperature. This study investigated the effects of pH (3.0–7.0) and temperature (15–45 °C) on the structural, antioxidant, and functional properties of WPI-CHA (WC) and WPI-LAC-CHA (WLC) complexes. Under the optimal catalytic conditions for LAC (pH 5.0, 35 °C), WLC complexes exhibited the highest structural stability, characterized by the smallest particle size (133 ± 3.93 nm), highest surface hydrophobicity (822.79 ± 1.74), and lowest free amino content (209.99 ± 1.09 mM/mL). The 52 % fluorescence quenching, amide I red shift and >180 kDa aggregates formation confirmed tertiary structure unfolding and covalent cross-linking, indicative of efficient protein-polyphenol conjugation. WLC complexes exhibited optimal radical scavenging activity at pH 5.0 and 35 °C, with DPPH and ABTS scavenging rates of 78.33 ± 5.11 (μmoL TE/g) and 83.99 ± 1.92 %, respectively. Following <em>in vitro</em> gastrointestinal digestion, WLC complexes retained superior antioxidant capacity (48.5 ± 2.21 μmoL TE/g for DPPH and 70.5 ± 1.70 % for ABTS) compared to free CHA and WC complexes. WLC complexes exhibited significantly greater UV protective efficiency of CHA, functional characteristics (solubility, EAI, ESI, FC and FS) compared to WC. These findings highlighted LAC-catalyzed cross-linking as an effective strategy to fabricate high-performance WPI-CHA nanocomposites, which might be applied in nano-carriers and packaging materials in the food industry.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"174 ","pages":"Article 112418"},"PeriodicalIF":11.0,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145881029","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 : 2025-12-31DOI: 10.1016/j.foodhyd.2025.112411
K.L. Baltrusch, M.D. Torres, H. Domínguez
Carrageenans are linear sulfated polysaccharides widely used in industry, but their high molecular weight and limited solubility restrict broader biomedical and agricultural applications. This study presents a two-step process combining ultrasonic pretreatment with a H2O2-AH2 redox system to produce low-molecular-weight carrageenan (LMWC) efficiently and controllably. Ultrasonication rapidly reduced molecular weight, homogenized polymer size, and preserved functional groups, as confirmed by HPSEC, rheology, FTIR and 1H NMR. Depolymerization kinetics followed a two-phase model, with the most energy-efficient ultrasonication at 60 % amplitude for 8.67 min (54.2 % MW reduction, 218.8 J/mL). Redox-assisted depolymerization was optimized via a quadratic model, showing strong effects of temperature and time, while intermediate reagent ratios maximized efficiency. Scaling from 150 mL to 2.2 L retained performance, producing ∼9.35 kDa LMWC with lower polydispersity, reduced reagent consumption, and faster processing than mild-acid hydrolysis controls. The purified fraction exhibited enhanced antioxidant activity (IC50 0.96 g/L, 270 mg Trolox equivalents/g). The sequential US, H2O2-AH2 method provides a scalable, controllable route to tailor LMWC for specific applications, outperforming conventional acid treatments and offering a robust alternative to enzymatic depolymerization.
{"title":"Optimized ultrasonication-redox process for controlled production of low molecular weight carrageenan","authors":"K.L. Baltrusch, M.D. Torres, H. Domínguez","doi":"10.1016/j.foodhyd.2025.112411","DOIUrl":"10.1016/j.foodhyd.2025.112411","url":null,"abstract":"<div><div>Carrageenans are linear sulfated polysaccharides widely used in industry, but their high molecular weight and limited solubility restrict broader biomedical and agricultural applications. This study presents a two-step process combining ultrasonic pretreatment with a H<sub>2</sub>O<sub>2</sub>-AH<sub>2</sub> redox system to produce low-molecular-weight carrageenan (LMWC) efficiently and controllably. Ultrasonication rapidly reduced molecular weight, homogenized polymer size, and preserved functional groups, as confirmed by HPSEC, rheology, FTIR and <sup>1</sup>H NMR. Depolymerization kinetics followed a two-phase model, with the most energy-efficient ultrasonication at 60 % amplitude for 8.67 min (54.2 % MW reduction, 218.8 J/mL). Redox-assisted depolymerization was optimized via a quadratic model, showing strong effects of temperature and time, while intermediate reagent ratios maximized efficiency. Scaling from 150 mL to 2.2 L retained performance, producing ∼9.35 kDa LMWC with lower polydispersity, reduced reagent consumption, and faster processing than mild-acid hydrolysis controls. The purified fraction exhibited enhanced antioxidant activity (IC<sub>50</sub> 0.96 g/L, 270 mg Trolox equivalents/g). The sequential US, H<sub>2</sub>O<sub>2</sub>-AH<sub>2</sub> method provides a scalable, controllable route to tailor LMWC for specific applications, outperforming conventional acid treatments and offering a robust alternative to enzymatic depolymerization.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"174 ","pages":"Article 112411"},"PeriodicalIF":11.0,"publicationDate":"2025-12-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145881030","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}
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