Pub Date : 2026-01-07DOI: 10.1016/j.foodhyd.2026.112432
Yuanda Sun , Shiyu Jia , Shasha Cheng , Wentao Su , Haitao Wang , Mingqian Tan
Biodegradable polysaccharides have attracted increasing interest as sustainable food packaging materials; however, their practical application is limited by inadequate mechanical properties, barrier properties, and antimicrobial activity. To address these challenges, we developed a multifunctional composite film using sodium alginate (SA) and carboxymethyl cellulose (CMC) as the polymer matrix, incorporating zeolite imidazolate framework-L (ZIF-L) for its antimicrobial functionality. The antimicrobial mechanism of ZIF-L against Pseudomonas was elucidated through transcriptomic and metabolomic analyses, revealing disruption of carbohydrate and nucleotide metabolism as the primary cause of bacterial inactivation. Mechanical reinforcement was achieved through iron ion cross-linking, resulting in SA/CMC (SC) composite films that are cross-linked by iron ions and embedded with ZIF-L (SC/ZIF-L/Fe films). Characterization demonstrated that the composite film exhibited enhanced hydrophobicity (water contact angle increased from 44.7° to 106.2°), superior UV shielding, improved tensile strength, and reduced water permeability. Furthermore, the synergistic effect of ZIF-L incorporation and iron cross-linking resulted in significantly enhanced antimicrobial activity compared with unmodified SC composite films. Application tests using salmon demonstrated effective inhibition of microbial growth and prolonged shelf life. Overall, this study highlights the potential of SC/ZIF-L/Fe films as multifunctional candidates for active food packaging.
可生物降解多糖作为可持续食品包装材料引起了越来越多的兴趣;然而,它们的实际应用受到机械性能、屏障性能和抗菌活性不足的限制。为了解决这些挑战,我们开发了一种多功能复合膜,以海藻酸钠(SA)和羧甲基纤维素(CMC)为聚合物基质,加入咪唑酸分子筛框架- l (ZIF-L)的抗菌功能。通过转录组学和代谢组学分析阐明了ZIF-L对假单胞菌的抗菌机制,揭示了碳水化合物和核苷酸代谢的破坏是细菌失活的主要原因。通过铁离子交联实现机械增强,形成由铁离子交联并包埋ZIF-L (SC/ZIF-L/Fe膜)的SA/CMC (SC)复合膜。表征表明,复合膜具有增强的疏水性(水接触角从44.7°增加到106.2°),良好的紫外线屏蔽,提高拉伸强度,降低透水性。此外,与未改性的SC复合膜相比,ZIF-L掺入和铁交联的协同作用显著提高了复合膜的抗菌活性。应用试验表明,鲑鱼有效抑制微生物生长和延长保质期。总的来说,本研究突出了SC/ZIF-L/Fe薄膜作为活性食品包装的多功能候选材料的潜力。
{"title":"Development of iron-crosslinked sodium alginate/carboxymethyl cellulose films functionalized with zeolite imidazolate framework-L for salmon preservation","authors":"Yuanda Sun , Shiyu Jia , Shasha Cheng , Wentao Su , Haitao Wang , Mingqian Tan","doi":"10.1016/j.foodhyd.2026.112432","DOIUrl":"10.1016/j.foodhyd.2026.112432","url":null,"abstract":"<div><div>Biodegradable polysaccharides have attracted increasing interest as sustainable food packaging materials; however, their practical application is limited by inadequate mechanical properties, barrier properties, and antimicrobial activity. To address these challenges, we developed a multifunctional composite film using sodium alginate (SA) and carboxymethyl cellulose (CMC) as the polymer matrix, incorporating zeolite imidazolate framework-L (ZIF-L) for its antimicrobial functionality. The antimicrobial mechanism of ZIF-L against <em>Pseudomonas</em> was elucidated through transcriptomic and metabolomic analyses, revealing disruption of carbohydrate and nucleotide metabolism as the primary cause of bacterial inactivation. Mechanical reinforcement was achieved through iron ion cross-linking, resulting in SA/CMC (SC) composite films that are cross-linked by iron ions and embedded with ZIF-L (SC/ZIF-L/Fe films). Characterization demonstrated that the composite film exhibited enhanced hydrophobicity (water contact angle increased from 44.7° to 106.2°), superior UV shielding, improved tensile strength, and reduced water permeability. Furthermore, the synergistic effect of ZIF-L incorporation and iron cross-linking resulted in significantly enhanced antimicrobial activity compared with unmodified SC composite films. Application tests using salmon demonstrated effective inhibition of microbial growth and prolonged shelf life. Overall, this study highlights the potential of SC/ZIF-L/Fe films as multifunctional candidates for active food packaging.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"175 ","pages":"Article 112432"},"PeriodicalIF":11.0,"publicationDate":"2026-01-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145975803","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 : 2026-01-06DOI: 10.1016/j.foodhyd.2026.112429
Xuanyu He , Yuting Fan , Jiang Yi
The air-water interfacial and foaming properties of three mung bean protein fractions (albumin (ALB), globulin (GLO) and mung bean protein isolate (MPI)) as a function of pH values (3.0, 5.0, 7.0, and 9.0) and ion strengths (10, 100, 500, and 1000 mM) were investigated here. We used interfacial dilatational rheology, characterized the physicochemical properties, and linked the outcomes to the foaming properties of three mung bean protein fractions. At neutral pH (7.0), the mean particle diameter was in the following order: MPI > GLO > ALB. Mean particle size was highly dependent on the pH value. Under identical pH conditions, the surface hydrophobicity of various mung bean protein fractions followed the order: GLO > MPI > ALB. For GLO and MPI, surface hydrophobicity progressively increased with rising ionic strength from 10 to 1000 mM. Proteins at pH values close to their isoelectric point (IEP) can provide the highest surface pressure during the initial adsorption stage (0–10 s). The elastic modulus initially decreased and then increased with rising pH, reaching its minimum at pH 5.0. Foamability was in the following order: ALB > MPI > GLO, varied remarkably with pH, with the effect being more pronounced for GLO. The foamability of both MPI and GLO at pH 5.0 was significantly higher than that at pH 7.0. Compared to GLO, ALB exhibited relatively lower foam stability, likely due to weak interfacial interactions, which failed to prevent particle coalescence. Rising pH from 3.0 to 9.0 continuously reduced the foam stability of ALB, due to enhanced electrostatic repulsion between protein molecules and potential excessive unfolding. The findings gained from this study may provide some useful information to expand the application of mung bean proteins as effective air-water interfacial and foaming stabilizers.
{"title":"Air-water interfacial and foaming properties of various mung bean protein fractions: Effects of pH and salt concentration","authors":"Xuanyu He , Yuting Fan , Jiang Yi","doi":"10.1016/j.foodhyd.2026.112429","DOIUrl":"10.1016/j.foodhyd.2026.112429","url":null,"abstract":"<div><div>The air-water interfacial and foaming properties of three mung bean protein fractions (albumin (ALB), globulin (GLO) and mung bean protein isolate (MPI)) as a function of pH values (3.0, 5.0, 7.0, and 9.0) and ion strengths (10, 100, 500, and 1000 mM) were investigated here. We used interfacial dilatational rheology, characterized the physicochemical properties, and linked the outcomes to the foaming properties of three mung bean protein fractions. At neutral pH (7.0), the mean particle diameter was in the following order: MPI > GLO > ALB. Mean particle size was highly dependent on the pH value. Under identical pH conditions, the surface hydrophobicity of various mung bean protein fractions followed the order: GLO > MPI > ALB. For GLO and MPI, surface hydrophobicity progressively increased with rising ionic strength from 10 to 1000 mM. Proteins at pH values close to their isoelectric point (IEP) can provide the highest surface pressure during the initial adsorption stage (0–10 s). The elastic modulus initially decreased and then increased with rising pH, reaching its minimum at pH 5.0. Foamability was in the following order: ALB > MPI > GLO, varied remarkably with pH, with the effect being more pronounced for GLO. The foamability of both MPI and GLO at pH 5.0 was significantly higher than that at pH 7.0. Compared to GLO, ALB exhibited relatively lower foam stability, likely due to weak interfacial interactions, which failed to prevent particle coalescence. Rising pH from 3.0 to 9.0 continuously reduced the foam stability of ALB, due to enhanced electrostatic repulsion between protein molecules and potential excessive unfolding. The findings gained from this study may provide some useful information to expand the application of mung bean proteins as effective air-water interfacial and foaming stabilizers.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"174 ","pages":"Article 112429"},"PeriodicalIF":11.0,"publicationDate":"2026-01-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145921086","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 : 2026-01-06DOI: 10.1016/j.foodhyd.2026.112421
Wenyuan Li , Wenhuan Xu , Bodun Zhao , Wenting Yang , Bowen Han , Xiaoju Tian , Weigang Chang , Xiaxia Zhang , Xiaobo Dong
Natural sourced hydrocolloids have always gained increasing attention, particularly microbial-derived polysaccharide. Naematelia aurantialba is a gelatinous edible mushroom rich in polysaccharides, however, colloidal properties of its polysaccharides (NAP) remain unclear. In this study, functional properties, rheological behavior, structural characteristic and aggregation behavior of NAP were investigated. The results showed that the functional properties of NAP, including thickening, solubility, swelling power, water retention, and emulsification properties, were comparable or superior to those of most of the 12 commercial polysaccharides. The rheological behavior demonstrated that NAP solution was a typical non-Newtonian fluid, pH adjustment and the presence of salt ions reduced the viscoelasticity, and its rheological property was stable at 4–50 °C. NAP, predominantly composed of mannose (47.51 %), was a homogeneous acidic heteropolysaccharide with high molecular weight (7.98 × 106 Da) and rigid chain conformation. NAP could be aggregated in solution via physical cross-linking of rigid chains and various molecular interactions predominated by hydrophobic interactions. This study provides valuable insights for the potential development and utilization of NAP as a promising hydrocolloid in the food industry.
{"title":"Characterisation of a novel hydrocolloid from gelatinous Naematelia aurantialba","authors":"Wenyuan Li , Wenhuan Xu , Bodun Zhao , Wenting Yang , Bowen Han , Xiaoju Tian , Weigang Chang , Xiaxia Zhang , Xiaobo Dong","doi":"10.1016/j.foodhyd.2026.112421","DOIUrl":"10.1016/j.foodhyd.2026.112421","url":null,"abstract":"<div><div>Natural sourced hydrocolloids have always gained increasing attention, particularly microbial-derived polysaccharide. <em>Naematelia aurantialba</em> is a gelatinous edible mushroom rich in polysaccharides, however, colloidal properties of its polysaccharides (NAP) remain unclear. In this study, functional properties, rheological behavior, structural characteristic and aggregation behavior of NAP were investigated. The results showed that the functional properties of NAP, including thickening, solubility, swelling power, water retention, and emulsification properties, were comparable or superior to those of most of the 12 commercial polysaccharides. The rheological behavior demonstrated that NAP solution was a typical non-Newtonian fluid, pH adjustment and the presence of salt ions reduced the viscoelasticity, and its rheological property was stable at 4–50 °C. NAP, predominantly composed of mannose (47.51 %), was a homogeneous acidic heteropolysaccharide with high molecular weight (7.98 × 10<sup>6</sup> Da) and rigid chain conformation. NAP could be aggregated in solution via physical cross-linking of rigid chains and various molecular interactions predominated by hydrophobic interactions. This study provides valuable insights for the potential development and utilization of NAP as a promising hydrocolloid in the food industry.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"175 ","pages":"Article 112421"},"PeriodicalIF":11.0,"publicationDate":"2026-01-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145947904","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.2026.112426
Mohammad Mahdi Rostamabadi , Fuat Topuz , Elham Assadpour , Hadis Rostamabadi , Seid Mahdi Jafari
Continuous electrospinning (ES) of high-quality natural polymers is essentially dictated by their natural chain entanglement and viscoelastic behavior. By adjusting polymer chain interactions and promoting solution stability, cross-linking (Clink) offers an adaptable route of widening the ES window and attaining fiber morphologies with more uniformity, quality, and consistency. Here, in this review, a structured summary of the principles/techniques of physico-chemical and dynamic Clink methodologies for biopolymers (e.g., alginate, chitosan, gelatin, etc.), is highlighted. Mechanistic influences on how Clink fine-tunes spinnability, jet stability, and fiber morphology are discussed, alongside practical guidance for solution preparation, ES protocols, and polymer selection. Recent progress connecting Clink circumstances to fiber quality/performance are illustrated, with architecture-feature relationships crucial for application-oriented design. The review further outlines novel applications across biomedical scaffolds, functional packaging, and environmental approaches, addressing current challenges and future opportunities. By pairing translational strategies with mechanistic insights, this work offers a robust framework for advancing the electro-spinnability of biopolymers via Clink control.
{"title":"Role of cross-linking in improving the spinnability of biopolymers for production of electrospun fibers/nanofibers","authors":"Mohammad Mahdi Rostamabadi , Fuat Topuz , Elham Assadpour , Hadis Rostamabadi , Seid Mahdi Jafari","doi":"10.1016/j.foodhyd.2026.112426","DOIUrl":"10.1016/j.foodhyd.2026.112426","url":null,"abstract":"<div><div>Continuous electrospinning (ES) of high-quality natural polymers is essentially dictated by their natural chain entanglement and viscoelastic behavior. By adjusting polymer chain interactions and promoting solution stability, cross-linking (C<sub>link</sub>) offers an adaptable route of widening the ES window and attaining fiber morphologies with more uniformity, quality, and consistency. Here, in this review, a structured summary of the principles/techniques of physico-chemical and dynamic C<sub>link</sub> methodologies for biopolymers (e.g., alginate, chitosan, gelatin, etc.), is highlighted. Mechanistic influences on how C<sub>link</sub> fine-tunes spinnability, jet stability, and fiber morphology are discussed, alongside practical guidance for solution preparation, ES protocols, and polymer selection. Recent progress connecting C<sub>link</sub> circumstances to fiber quality/performance are illustrated, with architecture-feature relationships crucial for application-oriented design. The review further outlines novel applications across biomedical scaffolds, functional packaging, and environmental approaches, addressing current challenges and future opportunities. By pairing translational strategies with mechanistic insights, this work offers a robust framework for advancing the electro-spinnability of biopolymers <em>via</em> C<sub>link</sub> control.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"175 ","pages":"Article 112426"},"PeriodicalIF":11.0,"publicationDate":"2026-01-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146035997","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.2026.112422
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}
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 : 2026-01-05DOI: 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}
Pub Date : 2026-01-02DOI: 10.1016/j.foodhyd.2026.112420
Shunan Jia , Xiaoshuai Wang , Hongyan Jin , Yingxue Chang , Yan Zhang , Zejian Xu , Xiaonan Sui
Functional polyphenol, such as tannic acid (TA), possesses numerous desirable characteristics for food applications. However, their instability and resulting low bioavailability currently limit their use within the food industry. Amyloid fibrils represent a desired food matrix for improving the bioavailability and bioaccessibility of polyphenols, owing to their highly ordered structure and abundant functional groups on their surface. In the present work, soy protein amyloid fibrils (SAFs), β-conglycinin (7S globulin) amyloid fibrils (7SAFs) and glycinin (11S globulin) amyloid fibrils (11SAFs) loaded with high content of TA were successfully prepared and the evolution of fibrils polymorphic structure was investigated. Structural analysis revealed that the incorporation of TA induced the cracking of long rigid fibrils and the formation of thicker and more clustered of short-curved fibrils. Concurrently, TA induced an increase in β-sheet contents, from 55.12 % to 65.84 % in SAFs and from 52.64 % to 60.33 % in 7SAFs. 11SAFs showed the highest TA loading rate of 94.76 % compared to that of SAFs and 7SAFs. However, SAFs and 7SAFs showed high TA retention rate of about 79.02 % and 78.89 % in ultraviolet experiment, respectively. In addition, the formed complexes demonstrated high antioxidant activity (ABTS: 76.98 %), offering a promising approach for designing amyloid fibril-based antioxidant materials. This research shed lights into the structural rational modulation of SAFs, 7SAFs and 11SAFs with TA, and paved the way for the preparation of value-added food ingredient composed of food protein amyloid fibrils and TA.
{"title":"Formation of soy protein amyloid fibrils-tannic acid complexes: structure remodeling of fibrils and enhanced antioxidant properties","authors":"Shunan Jia , Xiaoshuai Wang , Hongyan Jin , Yingxue Chang , Yan Zhang , Zejian Xu , Xiaonan Sui","doi":"10.1016/j.foodhyd.2026.112420","DOIUrl":"10.1016/j.foodhyd.2026.112420","url":null,"abstract":"<div><div>Functional polyphenol, such as tannic acid (TA), possesses numerous desirable characteristics for food applications. However, their instability and resulting low bioavailability currently limit their use within the food industry. Amyloid fibrils represent a desired food matrix for improving the bioavailability and bioaccessibility of polyphenols, owing to their highly ordered structure and abundant functional groups on their surface. In the present work, soy protein amyloid fibrils (SAFs), <em>β</em>-conglycinin (7S globulin) amyloid fibrils (7SAFs) and glycinin (11S globulin) amyloid fibrils (11SAFs) loaded with high content of TA were successfully prepared and the evolution of fibrils polymorphic structure was investigated. Structural analysis revealed that the incorporation of TA induced the cracking of long rigid fibrils and the formation of thicker and more clustered of short-curved fibrils. Concurrently, TA induced an increase in <em>β</em>-sheet contents, from 55.12 % to 65.84 % in SAFs and from 52.64 % to 60.33 % in 7SAFs. 11SAFs showed the highest TA loading rate of 94.76 % compared to that of SAFs and 7SAFs. However, SAFs and 7SAFs showed high TA retention rate of about 79.02 % and 78.89 % in ultraviolet experiment, respectively. In addition, the formed complexes demonstrated high antioxidant activity (ABTS: 76.98 %), offering a promising approach for designing amyloid fibril-based antioxidant materials. This research shed lights into the structural rational modulation of SAFs, 7SAFs and 11SAFs with TA, and paved the way for the preparation of value-added food ingredient composed of food protein amyloid fibrils and TA.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"175 ","pages":"Article 112420"},"PeriodicalIF":11.0,"publicationDate":"2026-01-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146074507","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}