Solid lipid particles (SLPs) are widely used in food emulsification and drug delivery owing to their biocompatibility and controllable release properties. However, the crystallization and interfacial behaviors of emulsifier-modified high-melting lipids remain poorly understood. This study combined experiments and molecular dynamics simulations to examine sodium caseinate (Na-Cas) effects on sugarcane wax SLPs. At 2.0–2.5 wt%, Na-Cas formed a dense surface layer that reduced interfacial tension and improved dispersion through electrostatic and steric stabilization. Differential scanning calorimetry and X-ray diffraction showed that Na-Cas disrupted crystal packing, inhibited grain growth, and lowered crystallization enthalpy, producing uniform microcrystals. Simulations revealed a three-step crystallization process—chain extension, nucleation, and growth—with cooling rate governing defect density and crystal size. Hydrophobic interactions and hydrogen bonding stabilized crystal surfaces. These results clarify the crystallization mechanism of high-melting lipids and support the design of functional SLPs.
{"title":"Molecular dynamics elucidation of the synergistic regulation of thermal kinetics and sodium caseinate on the crystalline and interfacial architecture of solid lipid particles","authors":"Yongbo Gou , Mengli Li , Jiayan Xu , Yuan Cheng , Xingyu Guan , Yongchun Huang , Xiangyi Tang","doi":"10.1016/j.foodhyd.2026.112442","DOIUrl":"10.1016/j.foodhyd.2026.112442","url":null,"abstract":"<div><div>Solid lipid particles (SLPs) are widely used in food emulsification and drug delivery owing to their biocompatibility and controllable release properties. However, the crystallization and interfacial behaviors of emulsifier-modified high-melting lipids remain poorly understood. This study combined experiments and molecular dynamics simulations to examine sodium caseinate (Na-Cas) effects on sugarcane wax SLPs. At 2.0–2.5 wt<em>%</em>, Na-Cas formed a dense surface layer that reduced interfacial tension and improved dispersion through electrostatic and steric stabilization. Differential scanning calorimetry and X-ray diffraction showed that Na-Cas disrupted crystal packing, inhibited grain growth, and lowered crystallization enthalpy, producing uniform microcrystals. Simulations revealed a three-step crystallization process—chain extension, nucleation, and growth—with cooling rate governing defect density and crystal size. Hydrophobic interactions and hydrogen bonding stabilized crystal surfaces. These results clarify the crystallization mechanism of high-melting lipids and support the design of functional SLPs.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"175 ","pages":"Article 112442"},"PeriodicalIF":11.0,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145975757","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 : 2026-06-01Epub Date: 2026-01-13DOI: 10.1016/j.foodhyd.2026.112446
Ge Qiao , Xiao-Wei Chen , Xiao-Yang Luo , Lin-Shang Zhang , Xiao Liu
Driven by growing consumer demand for health and environmental sustainability, the development of nutritionally superior plant-based fat analogs has become a key focus in both research and the food industry. Herein, structuring of edible liquid oil into switchable thermo-triggered soy protein (SPI) soft emulsion gels for 3D-printable fat substitute in plant-based meat patties was investigated. Self-supporting SPI soft emulsion gels were successfully prepared with carrageenan (CG) via a one-pot, heat-induced crosslinking approach. Subsequently, the soft emulsion gels were further fabricated by spatially distributing the SPI-CG complex around dispersed oil droplets, forming a network within the continuous phase. Fourier-transform spectroscopy and microstructural observations revealed that protein cross-linking intensified, leading to the formation of a denser gel network as the CG concentration increased to 0.8 %. Rheologically, the emulsion gels exhibited interesting thermos-reversibility and 3D-printability with over 90 % printing accuracy. As fat substitutes in plant-based patties, the emulsion gels effectively mitigated the undesirable brittleness of liquid oils, imparting a cohesive and elastic texture, and reduced cooking loss to approximately 10 %. Moreover, the increased CG content in the SPI-CG emulsion gels significantly increased the hardness and chewiness of plant-based meat patties. These results confirm that the thermo-responsive soy protein soft emulsion gels are suitable for replacing saturated fat in plant meat products.
{"title":"Switchable thermo-triggered and 3D-printable soy protein soft emulsion gels as fat analogs for plant-based meat","authors":"Ge Qiao , Xiao-Wei Chen , Xiao-Yang Luo , Lin-Shang Zhang , Xiao Liu","doi":"10.1016/j.foodhyd.2026.112446","DOIUrl":"10.1016/j.foodhyd.2026.112446","url":null,"abstract":"<div><div>Driven by growing consumer demand for health and environmental sustainability, the development of nutritionally superior plant-based fat analogs has become a key focus in both research and the food industry. Herein, structuring of edible liquid oil into switchable thermo-triggered soy protein (SPI) soft emulsion gels for 3D-printable fat substitute in plant-based meat patties was investigated. Self-supporting SPI soft emulsion gels were successfully prepared with carrageenan (CG) via a one-pot, heat-induced crosslinking approach. Subsequently, the soft emulsion gels were further fabricated by spatially distributing the SPI-CG complex around dispersed oil droplets, forming a network within the continuous phase. Fourier-transform spectroscopy and microstructural observations revealed that protein cross-linking intensified, leading to the formation of a denser gel network as the CG concentration increased to 0.8 %. Rheologically, the emulsion gels exhibited interesting thermos-reversibility and 3D-printability with over 90 % printing accuracy. As fat substitutes in plant-based patties, the emulsion gels effectively mitigated the undesirable brittleness of liquid oils, imparting a cohesive and elastic texture, and reduced cooking loss to approximately 10 %. Moreover, the increased CG content in the SPI-CG emulsion gels significantly increased the hardness and chewiness of plant-based meat patties. These results confirm that the thermo-responsive soy protein soft emulsion gels are suitable for replacing saturated fat in plant meat products.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"175 ","pages":"Article 112446"},"PeriodicalIF":11.0,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145975759","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 : 2026-06-01Epub Date: 2026-01-19DOI: 10.1016/j.foodhyd.2026.112458
Ulrich Sukop , Katharina Hoefler , Victoria Wiesmann , Philipp L. Fuhrmann , Mario Jekle , Regine Schoenlechner , Konrad J. Domig , Denisse Bender , Stefano D'Amico
The absence of a viscoelastic gluten network remains a major factor limiting the quality of gluten-free (GF) bakery products. This study examined whether arabinoxylans (AX) from maize (alkaline-extracted, M-CEAX; xylanase-extracted, M-XEAX) and wheat (wheat-extracted AX, WEAX), in combination with maize gluten meal (MGM), can form a cohesive joint polymeric network resembling gluten. Cross-linking was enzymatically induced using laccase or glucose oxidase (GOX) with horseradish peroxidase (HRP). Model batters were assessed through rheological tests (amplitude, frequency, time sweep) and physicochemical methods (particle and molecular size, polymer solubility and bound phenolic/ferulic acid) to evaluate AX-protein interactions. Rheological analyses revealed that laccase increased elasticity in M-CEAX systems but failed to promote strong AX-protein interactions. In contrast, GOX-HRP significantly enhanced the storage modulus (G′) in M-CEAX-MGM added model batters, suggesting stronger cross-linking. Particle size results supported this, showing larger d-values and higher span, especially in enzymatically treated M-CEAX formulations. AX solubility increased with M-CEAX alone but remained unchanged with protein addition. Bound phenolic content was higher in laccase-treated than in GOX-HRP-treated systems, indicating weaker cross-linking. Size exclusion chromatography (SEC) showed increased molecular weight in M-CEAX and MGM model batters treated with GOX-HRP, whereas M-CEAX-MGM combinations showed no clear size shift, which can be attributed to large insoluble aggregates not detected by the method. Overall, these findings highlighted the importance of polymer structure and enzyme specificity in modulating network formation. The results suggested that AX-protein interactions can enhance GF batter viscoelasticity and stability, offering a promising strategy to improve the structure of GF bakery products.
{"title":"Characterisation of enzymatically-induced arabinoxylan-protein interactions in gluten-free model batter","authors":"Ulrich Sukop , Katharina Hoefler , Victoria Wiesmann , Philipp L. Fuhrmann , Mario Jekle , Regine Schoenlechner , Konrad J. Domig , Denisse Bender , Stefano D'Amico","doi":"10.1016/j.foodhyd.2026.112458","DOIUrl":"10.1016/j.foodhyd.2026.112458","url":null,"abstract":"<div><div>The absence of a viscoelastic gluten network remains a major factor limiting the quality of gluten-free (GF) bakery products. This study examined whether arabinoxylans (AX) from maize (alkaline-extracted, M-CEAX; xylanase-extracted, M-XEAX) and wheat (wheat-extracted AX, WEAX), in combination with maize gluten meal (MGM), can form a cohesive joint polymeric network resembling gluten. Cross-linking was enzymatically induced using laccase or glucose oxidase (GOX) with horseradish peroxidase (HRP). Model batters were assessed through rheological tests (amplitude, frequency, time sweep) and physicochemical methods (particle and molecular size, polymer solubility and bound phenolic/ferulic acid) to evaluate AX-protein interactions. Rheological analyses revealed that laccase increased elasticity in M-CEAX systems but failed to promote strong AX-protein interactions. In contrast, GOX-HRP significantly enhanced the storage modulus (G′) in M-CEAX-MGM added model batters, suggesting stronger cross-linking. Particle size results supported this, showing larger d-values and higher span, especially in enzymatically treated M-CEAX formulations. AX solubility increased with M-CEAX alone but remained unchanged with protein addition. Bound phenolic content was higher in laccase-treated than in GOX-HRP-treated systems, indicating weaker cross-linking. Size exclusion chromatography (SEC) showed increased molecular weight in M-CEAX and MGM model batters treated with GOX-HRP, whereas M-CEAX-MGM combinations showed no clear size shift, which can be attributed to large insoluble aggregates not detected by the method. Overall, these findings highlighted the importance of polymer structure and enzyme specificity in modulating network formation. The results suggested that AX-protein interactions can enhance GF batter viscoelasticity and stability, offering a promising strategy to improve the structure of GF bakery products.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"175 ","pages":"Article 112458"},"PeriodicalIF":11.0,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146036018","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 : 2026-06-01Epub Date: 2026-01-14DOI: 10.1016/j.foodhyd.2026.112437
Junquan Zheng , Daobang Tang , Xueming Liu , Xuping Wang , Yaosheng Lin , Mingjun Zhu , Jingrong Cheng
Astaxanthin (AST) suffers from poor water solubility, low stability, and limited oral bioavailability, which restrict its practical application. To address these issues, this study developed a whey protein fibril-sodium alginate (WPF/SA) stabilized Pickering emulsion for the co-delivery of AST and piperine (Pip), the latter being a natural bioenhancer known to improve intestinal absorption by inhibiting drug-metabolizing enzymes and efflux transporters. The interaction mechanisms among WPF, SA, and Pip, the emulsion's environmental stability, and the bioavailability-enhancing effect were systematically investigated using molecular docking, spectroscopic analysis, emulsion characterization, and a Caco-2 cell model. Results indicated that Pip binds to WPF via hydrophobic interactions, while SA associates through electrostatic forces at pH 5.0. These interactions led to a reduction in β-sheet content from 28.73 % to 23.58 % and an increase in random coil from 23.18 % to 28.88 %. The SA incorporation significantly improved emulsion stability, raising the absolute zeta potential from +9 mV to −38.5 mV and enhancing rheological properties. Compared to the SA-free system, the W(P)/SA (1:2)-E increased AST retention by 0.85-fold after 90 °C heating and by 1.26-fold after UV irradiation. In Caco-2 cells, Pip was shown to significantly enhance the cellular uptake of AST. The highest uptake level (65.79 ng/μg protein) was observed at a W(P) to SA ratio of 1:2, representing a 1.28-fold increase over the WPF-stabilized emulsion, and indicating a clear synergistic effect between Pip and SA. This study offers an effective strategy for enhancing both the stability and bioavailability of AST, supporting its potential application in functional foods and nutraceuticals.
{"title":"Molecular insights into whey protein fibril-sodium alginate-piperine complexes for stabilizing astaxanthin emulsions with improved bioaccessibility","authors":"Junquan Zheng , Daobang Tang , Xueming Liu , Xuping Wang , Yaosheng Lin , Mingjun Zhu , Jingrong Cheng","doi":"10.1016/j.foodhyd.2026.112437","DOIUrl":"10.1016/j.foodhyd.2026.112437","url":null,"abstract":"<div><div>Astaxanthin (AST) suffers from poor water solubility, low stability, and limited oral bioavailability, which restrict its practical application. To address these issues, this study developed a whey protein fibril-sodium alginate (WPF/SA) stabilized Pickering emulsion for the co-delivery of AST and piperine (Pip), the latter being a natural bioenhancer known to improve intestinal absorption by inhibiting drug-metabolizing enzymes and efflux transporters. The interaction mechanisms among WPF, SA, and Pip, the emulsion's environmental stability, and the bioavailability-enhancing effect were systematically investigated using molecular docking, spectroscopic analysis, emulsion characterization, and a Caco-2 cell model. Results indicated that Pip binds to WPF via hydrophobic interactions, while SA associates through electrostatic forces at pH 5.0. These interactions led to a reduction in β-sheet content from 28.73 % to 23.58 % and an increase in random coil from 23.18 % to 28.88 %. The SA incorporation significantly improved emulsion stability, raising the absolute zeta potential from +9 mV to −38.5 mV and enhancing rheological properties. Compared to the SA-free system, the W(P)/SA (1:2)-E increased AST retention by 0.85-fold after 90 °C heating and by 1.26-fold after UV irradiation. In Caco-2 cells, Pip was shown to significantly enhance the cellular uptake of AST. The highest uptake level (65.79 ng/μg protein) was observed at a W(P) to SA ratio of 1:2, representing a 1.28-fold increase over the WPF-stabilized emulsion, and indicating a clear synergistic effect between Pip and SA. This study offers an effective strategy for enhancing both the stability and bioavailability of AST, supporting its potential application in functional foods and nutraceuticals.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"175 ","pages":"Article 112437"},"PeriodicalIF":11.0,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146035990","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 : 2026-06-01Epub Date: 2026-02-09DOI: 10.1016/j.foodhyd.2026.112539
Shiqi Yang , Donglei Luan , Yahui Wen , Bin Zhao , Tianxi Yang , Juan Yan
Ready-to-eat cooked meat products contain high levels of moisture and nutrients, making them highly vulnerable to microbial contamination and subsequent quality degradation during storage. Therefore, the development of green packaging materials that integrate active preservation functions with freshness indication is of great significance. In this work, a carboxymethyl chitosan (CMCS)/tannic acid (TA)-Fe3+ coordination hydrogel (CMCS/TA-Fe) film with favorable biocompatibility and degradability was fabricated through a facile coordination-driven self-assembly strategy, leveraging the multiple interactions among CMCS, TA, and ferric ions (Fe3+). The introduction of the TA-Fe3+ metal-polyphenol markedly enhanced the mechanical performance of the film, increasing its storage modulus (G′) to approximately 2.4 × 104 Pa, and endowed it with efficient photothermal conversion capability. Under near-infrared irradiation at 808 nm, the film surface temperature rapidly increased to 103 °C within 15 min, enabling complete inactivation of Escherichia coli and Staphylococcus aureus. In addition, the dynamic coordination structure of TA-Fe3+ exhibited pH-responsive chromatic behavior in a model system, resulting in distinct and reversible color changes under different pH conditions. These color variations suggest the potential of the CMCS/TA-Fe film as a visual indicator for freshness-related pH changes. When applied to the refrigerated preservation of cooked chicken breast, the CMCS/TA-Fe film combined with near-infrared irradiation effectively inhibited microbial proliferation, delayed pH increase, reduced moisture loss, and preserved textural and sensory quality. Overall, this study demonstrates a multifunctional and environmentally friendly hydrogel film that integrates photothermal antibacterial activity with a pH-responsive color indication function, offering a promising strategy for intelligent food packaging applications.
{"title":"A CMCS/TA-Fe hydrogel film based on metal-phenolic network coordination for intelligent preservation of cooked meat","authors":"Shiqi Yang , Donglei Luan , Yahui Wen , Bin Zhao , Tianxi Yang , Juan Yan","doi":"10.1016/j.foodhyd.2026.112539","DOIUrl":"10.1016/j.foodhyd.2026.112539","url":null,"abstract":"<div><div>Ready-to-eat cooked meat products contain high levels of moisture and nutrients, making them highly vulnerable to microbial contamination and subsequent quality degradation during storage. Therefore, the development of green packaging materials that integrate active preservation functions with freshness indication is of great significance. In this work, a carboxymethyl chitosan (CMCS)/tannic acid (TA)-Fe<sup>3+</sup> coordination hydrogel (CMCS/TA-Fe) film with favorable biocompatibility and degradability was fabricated through a facile coordination-driven self-assembly strategy, leveraging the multiple interactions among CMCS, TA, and ferric ions (Fe<sup>3+</sup>). The introduction of the TA-Fe<sup>3+</sup> metal-polyphenol markedly enhanced the mechanical performance of the film, increasing its storage modulus (G′) to approximately 2.4 × 10<sup>4</sup> Pa, and endowed it with efficient photothermal conversion capability. Under near-infrared irradiation at 808 nm, the film surface temperature rapidly increased to 103 °C within 15 min, enabling complete inactivation of <em>Escherichia coli</em> and <em>Staphylococcus aureus</em>. In addition, the dynamic coordination structure of TA-Fe<sup>3+</sup> exhibited pH-responsive chromatic behavior in a model system, resulting in distinct and reversible color changes under different pH conditions. These color variations suggest the potential of the CMCS/TA-Fe film as a visual indicator for freshness-related pH changes. When applied to the refrigerated preservation of cooked chicken breast, the CMCS/TA-Fe film combined with near-infrared irradiation effectively inhibited microbial proliferation, delayed pH increase, reduced moisture loss, and preserved textural and sensory quality. Overall, this study demonstrates a multifunctional and environmentally friendly hydrogel film that integrates photothermal antibacterial activity with a pH-responsive color indication function, offering a promising strategy for intelligent food packaging applications.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"175 ","pages":"Article 112539"},"PeriodicalIF":11.0,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146184765","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}
This study investigated the effects of three mill streams (representing distinct parts of wheat grain) and straight run flour (a blend of mill streams) on dough characteristics and steamed bread quality during post-ripening. Throughout the post-ripening period, the mill streams (2M) from the wheat endosperm exhibited a more stable dough stabilization time, while the bran-rich mill streams (2S and 2B) displayed a downward trend. In addition, when mill streams were post-ripened for 20 days, the viscoelasticity and gas retention of dough were enhanced, and internal crumb structure in steamed bread was improved. After mill streams post-ripening, the increase in glutenin macropolymer content promoted formation of a dense and elastic gluten network structure in dough. The results demonstrated that post-ripening promoted protein aggregation of wheat flour mill streams. Among them, 2M streams (the second reduction) showed the slightest changes in protein properties, 2S streams (the second sizing) and 2B streams (the second break) exhibited a significant decline in free sulfhydryl content and gliadin content, and an increase in glutenin content. More pronounced changes in gelatinization properties and peroxidase activity were observed in the 2S and 2B streams. Principal component analysis indicated that the gluten network formation promoted by mill streams post-ripening contributed more obvious to improved quality of steamed bread dough. These results proved the differences in mill streams post-ripening and provided a valuable theoretical basis for improving steamed bread dough with specific mill streams during post-ripening.
{"title":"Physicochemical characteristics changes in post-ripening of wheat flour mill streams: Effects on dough properties and steamed bread quality","authors":"Meng-Li Zhang , Xiao-Na Guo , Xiao-Hong Sun , Ke-Xue Zhu","doi":"10.1016/j.foodhyd.2026.112523","DOIUrl":"10.1016/j.foodhyd.2026.112523","url":null,"abstract":"<div><div>This study investigated the effects of three mill streams (representing distinct parts of wheat grain) and straight run flour (a blend of mill streams) on dough characteristics and steamed bread quality during post-ripening. Throughout the post-ripening period, the mill streams (2M) from the wheat endosperm exhibited a more stable dough stabilization time, while the bran-rich mill streams (2S and 2B) displayed a downward trend. In addition, when mill streams were post-ripened for 20 days, the viscoelasticity and gas retention of dough were enhanced, and internal crumb structure in steamed bread was improved. After mill streams post-ripening, the increase in glutenin macropolymer content promoted formation of a dense and elastic gluten network structure in dough. The results demonstrated that post-ripening promoted protein aggregation of wheat flour mill streams. Among them, 2M streams (the second reduction) showed the slightest changes in protein properties, 2S streams (the second sizing) and 2B streams (the second break) exhibited a significant decline in free sulfhydryl content and gliadin content, and an increase in glutenin content. More pronounced changes in gelatinization properties and peroxidase activity were observed in the 2S and 2B streams. Principal component analysis indicated that the gluten network formation promoted by mill streams post-ripening contributed more obvious to improved quality of steamed bread dough. These results proved the differences in mill streams post-ripening and provided a valuable theoretical basis for improving steamed bread dough with specific mill streams during post-ripening.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"175 ","pages":"Article 112523"},"PeriodicalIF":11.0,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146184809","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 : 2026-06-01Epub Date: 2026-01-31DOI: 10.1016/j.foodhyd.2026.112519
Alexander Fuchs , Enrico Hupfeld , Volker Sieber
Carrageenans are essential texturizers in various dairy products, where they form elastic gel networks through specific interactions with casein micelles, enabling effective structure formation even at low concentrations. Plant-based milk alternatives on the other side, such as almond- or oat-based products, recently experience a rising consumer demand, but are devoid of these protein–polysaccharide interactions, which poses major challenges for their efficient texturization. Consequently, new mild, adaptable, and label-friendly gelation strategies are required to achieve desirable texture and stability in such systems. Here, we present an enzymatic approach to trigger gel formation in non-dairy matrices using the carrageenan sulfatase CaCgS1 from Cellulophaga algicola DSM 14237. The enzyme catalyzes the desulfation of κ-carrageenan to a κ/β-hybrid carrageenan under mild conditions, which triggers the gelation of the reaction product in-situ and yields a homogenous hydrogel with enhanced gel strength and thermal stability by an increased helical aggregation activity of the modified polymer chains. The increased gel strength relies exclusively on the cleavage of sulfate groups without the need to alter the ionic composition or increase the polymer concentration. Applied to plant-based milk formulations, this process enables the generation of homogeneous, stable textures at low polymer concentrations. The concept provides a novel method for structuring plant-based foods and expands the application scope of enzyme-induced gelation in modern food design, and beyond.
{"title":"Sulfatase-induced in situ gelation of κ-carrageenan provides an enzyme-based texturizing solution for plant-based milk systems","authors":"Alexander Fuchs , Enrico Hupfeld , Volker Sieber","doi":"10.1016/j.foodhyd.2026.112519","DOIUrl":"10.1016/j.foodhyd.2026.112519","url":null,"abstract":"<div><div>Carrageenans are essential texturizers in various dairy products, where they form elastic gel networks through specific interactions with casein micelles, enabling effective structure formation even at low concentrations. Plant-based milk alternatives on the other side, such as almond- or oat-based products, recently experience a rising consumer demand, but are devoid of these protein–polysaccharide interactions, which poses major challenges for their efficient texturization. Consequently, new mild, adaptable, and label-friendly gelation strategies are required to achieve desirable texture and stability in such systems. Here, we present an enzymatic approach to trigger gel formation in non-dairy matrices using the carrageenan sulfatase CaCgS1 from <em>Cellulophaga algicola</em> DSM 14237. The enzyme catalyzes the desulfation of κ-carrageenan to a κ/β-hybrid carrageenan under mild conditions, which triggers the gelation of the reaction product in-situ and yields a homogenous hydrogel with enhanced gel strength and thermal stability by an increased helical aggregation activity of the modified polymer chains. The increased gel strength relies exclusively on the cleavage of sulfate groups without the need to alter the ionic composition or increase the polymer concentration. Applied to plant-based milk formulations, this process enables the generation of homogeneous, stable textures at low polymer concentrations. The concept provides a novel method for structuring plant-based foods and expands the application scope of enzyme-induced gelation in modern food design, and beyond.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"175 ","pages":"Article 112519"},"PeriodicalIF":11.0,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146184876","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 : 2026-06-01Epub Date: 2026-01-26DOI: 10.1016/j.foodhyd.2026.112503
Ianne Kong , Benbettaieb Nasreddine , Debeaufort Frédéric , Degraeve Pascal , Liew Phing Pui , Kar Lin Nyam
Natural bioactive compound enriched edible films are increasingly acceptable as environmentally friendly substitutes for traditional plastic packaging. These films can provide antibacterial and antioxidant properties to improve food safety and extend shelf-life in addition to reducing their negative effects on the environment. The impact of incorporating nanoemulsified kesum (Persicaria minor Huds.) essential oil (KEO-NE) into gelatin-chitosan edible films was investigated focusing on structural, thermal, and release properties. Fourier transform infrared spectroscopy (FTIR) revealed no significant changes indicating physical interactions with the biopolymer matrix in FTIR spectra following KEO-NE incorporation. Scanning electron microscopy (SEM) showed KEO-NE induced surface irregularities and internal heterogeneities, with pores and bubbles indicating droplet migration during drying, contrasting control films. Differential scanning calorimetry indicated a decline in the thermal stability after the introduction of KEO-NE that evidenced by diminished endothermic peak and enthalpy values. Release kinetics studies in various food simulants showed that addition of salts in ethanol significantly enhanced KEO-NE release rates, affecting diffusion coefficients and total release amounts. The total KEO release varied from 3426.5 ± 396.7 mg/L to 64129.1 ± 1379.3 mg/L with the maximum release observed in a solution of 50 % ethanol and 1 % of NaCl. Consequently, the diffusion coefficients exhibited considerable variation which was 0.9 ± 0.1 to 15.0 ± 4.2 x 10−12 m2/s implying increased diffusion in salt-infused ethanol attributed to salting-out activities. The proportion of the KEO release varied from 1.1 ± 0.2 % to 18.7 ± 1.8 % with MgCl2 facilitating the most significant release fraction. Higher release rates in ethanol with salts suggest salt-induced changes in film solubility and matrix interactions play a pivotal role in controlling KEO-NE diffusion due to salting-out effects. This study contributes to SDG (Sustainable Development Goal) 12 (Responsible Consumption and Production) by developing biodegradable edible films with controlled release of bioactive compounds, offering a sustainable alternative to conventional food packaging materials.
{"title":"Gelatin-chitosan edible film with kesum essential oil nanoemulsion: Film structure and release kinetics of nanoemulsified kesum essential oil influenced by the presence of different salts in ethanolic food simulants","authors":"Ianne Kong , Benbettaieb Nasreddine , Debeaufort Frédéric , Degraeve Pascal , Liew Phing Pui , Kar Lin Nyam","doi":"10.1016/j.foodhyd.2026.112503","DOIUrl":"10.1016/j.foodhyd.2026.112503","url":null,"abstract":"<div><div>Natural bioactive compound enriched edible films are increasingly acceptable as environmentally friendly substitutes for traditional plastic packaging. These films can provide antibacterial and antioxidant properties to improve food safety and extend shelf-life in addition to reducing their negative effects on the environment. The impact of incorporating nanoemulsified kesum (<em>Persicaria minor</em> Huds.) essential oil (KEO-NE) into gelatin-chitosan edible films was investigated focusing on structural, thermal, and release properties. Fourier transform infrared spectroscopy (FTIR) revealed no significant changes indicating physical interactions with the biopolymer matrix in FTIR spectra following KEO-NE incorporation. Scanning electron microscopy (SEM) showed KEO-NE induced surface irregularities and internal heterogeneities, with pores and bubbles indicating droplet migration during drying, contrasting control films. Differential scanning calorimetry indicated a decline in the thermal stability after the introduction of KEO-NE that evidenced by diminished endothermic peak and enthalpy values. Release kinetics studies in various food simulants showed that addition of salts in ethanol significantly enhanced KEO-NE release rates, affecting diffusion coefficients and total release amounts. The total KEO release varied from 3426.5 ± 396.7 mg/L to 64129.1 ± 1379.3 mg/L with the maximum release observed in a solution of 50 % ethanol and 1 % of NaCl. Consequently, the diffusion coefficients exhibited considerable variation which was 0.9 ± 0.1 to 15.0 ± 4.2 x 10<sup>−12</sup> m<sup>2</sup>/s implying increased diffusion in salt-infused ethanol attributed to salting-out activities. The proportion of the KEO release varied from 1.1 ± 0.2 % to 18.7 ± 1.8 % with MgCl<sub>2</sub> facilitating the most significant release fraction. Higher release rates in ethanol with salts suggest salt-induced changes in film solubility and matrix interactions play a pivotal role in controlling KEO-NE diffusion due to salting-out effects. This study contributes to SDG (Sustainable Development Goal) 12 (Responsible Consumption and Production) by developing biodegradable edible films with controlled release of bioactive compounds, offering a sustainable alternative to conventional food packaging materials.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"175 ","pages":"Article 112503"},"PeriodicalIF":11.0,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146184761","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 : 2026-06-01Epub Date: 2026-01-12DOI: 10.1016/j.foodhyd.2025.112360
Junhong Xie , Li Feng , Fanghui Deng , Wei Yue , Wei Liang , Qiannan Zhao , Wentao Ma , Jianhua Rong , Shanbai Xiong , Yang Hu
Increasing the added value of freshwater fish by-product processing and reducing the economic losses are currently research hotspots in the field of aquatic products. However, the collagen-based products derived from freshwater fish cannot be widely applied due to their disadvantages such as low mechanical properties. Enzymatic cross-linking modification to improve the physicochemical properties of collagen-based materials is a better solution. This study focused on the self-assembly behavior of collagen molecules, investigated the cross-linking of collagen solutions mediated by laccase and proanthocyanidins, and improved their rheological properties and structural characteristics. The results showed that the volume ratio of collagen-proanthocyanidins/laccase (COL-PL) within the range of 1:0.01 to 1:0.4 is more conducive to the stability of collagen molecules. All cross-linked groups exhibited shear thinning properties. Collagen-proanthocyanidins (COL-PA) enhanced the mechanical properties of collagen molecules to a certain extent. However, when the volume ratio of COL-PL is 1:0.02, it not only accelerates the aggregation of collagen molecules, but also generates a complex with the best gel performance. This is mainly because low-concentration laccase can catalyze the generation of proanthocyanidin active groups. The interaction between the C=O bond and the -NH2 bond in the collagen molecule peptide chain provides more sites for the aggregation of collagen molecules, and at the same time, the chemical bond interaction also makes the collagen aggregate more closely. Finally, through atomic force microscopy observation, after 24 h, COL-PL 1:0.02 group collagen molecules formed a dense reticular cross-linked structure. The research provides a new approach to expanding freshwater fish collagen potential application prospects.
{"title":"Proanthocyanidin/laccase-mediated cross-linking enhances the structural stability and rheological properties of collagen solutions","authors":"Junhong Xie , Li Feng , Fanghui Deng , Wei Yue , Wei Liang , Qiannan Zhao , Wentao Ma , Jianhua Rong , Shanbai Xiong , Yang Hu","doi":"10.1016/j.foodhyd.2025.112360","DOIUrl":"10.1016/j.foodhyd.2025.112360","url":null,"abstract":"<div><div>Increasing the added value of freshwater fish by-product processing and reducing the economic losses are currently research hotspots in the field of aquatic products. However, the collagen-based products derived from freshwater fish cannot be widely applied due to their disadvantages such as low mechanical properties. Enzymatic cross-linking modification to improve the physicochemical properties of collagen-based materials is a better solution. This study focused on the self-assembly behavior of collagen molecules, investigated the cross-linking of collagen solutions mediated by laccase and proanthocyanidins, and improved their rheological properties and structural characteristics. The results showed that the volume ratio of collagen-proanthocyanidins/laccase (COL-PL) within the range of 1:0.01 to 1:0.4 is more conducive to the stability of collagen molecules. All cross-linked groups exhibited shear thinning properties. Collagen-proanthocyanidins (COL-PA) enhanced the mechanical properties of collagen molecules to a certain extent. However, when the volume ratio of COL-PL is 1:0.02, it not only accelerates the aggregation of collagen molecules, but also generates a complex with the best gel performance. This is mainly because low-concentration laccase can catalyze the generation of proanthocyanidin active groups. The interaction between the C=O bond and the -NH<sub>2</sub> bond in the collagen molecule peptide chain provides more sites for the aggregation of collagen molecules, and at the same time, the chemical bond interaction also makes the collagen aggregate more closely. Finally, through atomic force microscopy observation, after 24 h, COL-PL 1:0.02 group collagen molecules formed a dense reticular cross-linked structure. The research provides a new approach to expanding freshwater fish collagen potential application prospects.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"175 ","pages":"Article 112360"},"PeriodicalIF":11.0,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146036017","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 : 2026-06-01Epub Date: 2026-01-20DOI: 10.1016/j.foodhyd.2026.112477
Zhihao Xu , Xuemei Lin , Wenzhong Zhao , Xiaoqi Ding , Xianglin Sun , Yuting Ding , Hui Chen , Pengbo Cui
This study developed novel protein-based fish oil oleogels employing protein nanofibrils derived from sodium tripolyphosphate-phosphorylated (STPP) fava bean 11S globulin. X-ray photoelectron spectroscopy confirmed successful phosphorylation through a P2p peak at 133.3 eV, supported by FTIR bands at 972 cm−1 (P–O stretching) and 894 cm−1 (P=O vibration). Phosphorylation disrupted the crystalline structure of 11S globulin, increasing β-turns and reducing random coils as revealed by XRD. Under acid-heat treatment (pH 2.0, 85 °C), phosphorylated 11S (P11S) formed finer and more uniform nanofibrils compared to the heterogeneous network of native 11S. Thioflavin T fluorescence showed faster nucleation and higher intensity for P11S fibrils, indicating enhanced fibrillation kinetics. P11S fibrils also exhibited superior emulsifying activity and emulsion stability. Mass spectrometry identified self-assembling peptide segments and phosphorylation sites, clarifying the molecular mechanism. When incorporated into oleogels, phosphorylated fibril oleogel (P11SG) displayed a softer, cream-like texture than the harder 11S oleogel (11SG). Rheological and texture analyses confirmed that P11SG had a lower storage modulus, hardness, and chewiness, but higher resilience and similar oil-binding capacity. Overall, phosphorylation effectively modulates the self-assembly and functional characteristics of 11S globulin. This providing a promising strategy to design protein-based oleogels with tunable textures and enhanced interfacial performance for food applications.
{"title":"Phosphorylation-modified fava bean 11S protein fibril-based oleogels: A novel strategy to enhance network flexibility and alter rheological and textural properties","authors":"Zhihao Xu , Xuemei Lin , Wenzhong Zhao , Xiaoqi Ding , Xianglin Sun , Yuting Ding , Hui Chen , Pengbo Cui","doi":"10.1016/j.foodhyd.2026.112477","DOIUrl":"10.1016/j.foodhyd.2026.112477","url":null,"abstract":"<div><div>This study developed novel protein-based fish oil oleogels employing protein nanofibrils derived from sodium tripolyphosphate-phosphorylated (STPP) <em>fava bean</em> 11S globulin. X-ray photoelectron spectroscopy confirmed successful phosphorylation through a P<sub>2p</sub> peak at 133.3 eV, supported by FTIR bands at 972 cm<sup>−1</sup> (P–O stretching) and 894 cm<sup>−1</sup> (P=O vibration). Phosphorylation disrupted the crystalline structure of 11S globulin, increasing β-turns and reducing random coils as revealed by XRD. Under acid-heat treatment (pH 2.0, 85 °C), phosphorylated 11S (P11S) formed finer and more uniform nanofibrils compared to the heterogeneous network of native 11S. Thioflavin T fluorescence showed faster nucleation and higher intensity for P11S fibrils, indicating enhanced fibrillation kinetics. P11S fibrils also exhibited superior emulsifying activity and emulsion stability. Mass spectrometry identified self-assembling peptide segments and phosphorylation sites, clarifying the molecular mechanism. When incorporated into oleogels, phosphorylated fibril oleogel (P11SG) displayed a softer, cream-like texture than the harder 11S oleogel (11SG). Rheological and texture analyses confirmed that P11SG had a lower storage modulus, hardness, and chewiness, but higher resilience and similar oil-binding capacity. Overall, phosphorylation effectively modulates the self-assembly and functional characteristics of 11S globulin. This providing a promising strategy to design protein-based oleogels with tunable textures and enhanced interfacial performance for food applications.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"175 ","pages":"Article 112477"},"PeriodicalIF":11.0,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146036019","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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