Cruciferin, one of the major protein components of rapeseed, can form microgels (CMG) that are shown to be efficient emulsifiers for water-in-water (W/W) emulsions. They spontaneously crosslink at the interface to form stable microcapsules (MC), which can themselves be used to stabilize W/W emulsions. Confocal laser scanning microscopy showed that the microstructure of W/W emulsions stabilized by MC depends on the compatibility of the polymer within the MC with those in the dispersed and continuous phase. Depending on the compatibility, the MC form a layer at the interface that protrudes inward to the droplet phase or outwards to the continuous phase. In the first case stable suspensions of raspberry-like MC can be formed with a shell of small MC. In the latter case the droplets form a network bridged by MC. The pH was found to play a pivotal role as it determines the partition of the CMG and MC between the phases and the attraction between the proteins.
{"title":"Morphology of water in water emulsions stabilized by protein microcapsules","authors":"Maria Moutkane, Colleen P.K. Mudau, Gireeshkumar Balakrishnan, Taco Nicolai, Christophe Chassenieux","doi":"10.1016/j.foodhyd.2025.112353","DOIUrl":"10.1016/j.foodhyd.2025.112353","url":null,"abstract":"<div><div>Cruciferin, one of the major protein components of rapeseed, can form microgels (CMG) that are shown to be efficient emulsifiers for water-in-water (W/W) emulsions. They spontaneously crosslink at the interface to form stable microcapsules (MC), which can themselves be used to stabilize W/W emulsions. Confocal laser scanning microscopy showed that the microstructure of W/W emulsions stabilized by MC depends on the compatibility of the polymer within the MC with those in the dispersed and continuous phase. Depending on the compatibility, the MC form a layer at the interface that protrudes inward to the droplet phase or outwards to the continuous phase. In the first case stable suspensions of raspberry-like MC can be formed with a shell of small MC. In the latter case the droplets form a network bridged by MC. The pH was found to play a pivotal role as it determines the partition of the CMG and MC between the phases and the attraction between the proteins.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"174 ","pages":"Article 112353"},"PeriodicalIF":11.0,"publicationDate":"2025-12-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145735084","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 : 2025-12-10DOI: 10.1016/j.foodhyd.2025.112350
David Pietri , Daniel Diecke , Leonie Jabs , Daniel Dwiggins , Holger Wirz , Christine McBeth
A revolution is currently underway to transform meat production by adapting cultivated animal cells for large-scale use in the food industry. Textured meat products such as beef filet require scaffolds for cellular growth. Many in the industry have turned to bioprinting as the key method for manufacturing scaffolds due to its ability to precisely generate the complex morphologies that have been investigated for regenerative medicine. However, the low-price targets of food manufacturing are unlikely to bear the strain of high-cost methods such as bioprinting. Here, we leveraged methods from the textile industry to produce high volumes of konjac glucomannan monofilaments at production rates of 15 m/min with polymer costs in the range of $0.18USD/kilometer. We show that wet-spun konjac glucomannan fibers exhibited dry tensile strengths in the 35 MPa range which were of sufficient strength to withstand downstream automated circular braiding. Critically, C2C12 muscle cells readily attached, grew, and differentiated on these plant monofilaments. Myotube fusion approached 50 % with strong global alignment with the longitudinal axis of the fiber. More than 20 % of the myotubes were 0.8 mm long, indicating strong differentiation. As fat is an important carrier of flavor, we also demonstrated 3T3-L1 adipocyte attachment and differentiation. With multiple filaments, C2C12 connected tissue across strands suggesting possible paths forward to large, macroscopic constructs. Cultivated meat will require the integration of numerous advances from the tissue engineering field. We demonstrate here that emphasizing the manufacturing constraints of scaffold production rather than precisely mimicking native tissue yields low-cost biocompatible scaffolds.
{"title":"Wet-spun textile-inspired konjac glucomannan scaffolds: cost effective alternative for cultivated meat production","authors":"David Pietri , Daniel Diecke , Leonie Jabs , Daniel Dwiggins , Holger Wirz , Christine McBeth","doi":"10.1016/j.foodhyd.2025.112350","DOIUrl":"10.1016/j.foodhyd.2025.112350","url":null,"abstract":"<div><div>A revolution is currently underway to transform meat production by adapting cultivated animal cells for large-scale use in the food industry. Textured meat products such as beef filet require scaffolds for cellular growth. Many in the industry have turned to bioprinting as the key method for manufacturing scaffolds due to its ability to precisely generate the complex morphologies that have been investigated for regenerative medicine. However, the low-price targets of food manufacturing are unlikely to bear the strain of high-cost methods such as bioprinting. Here, we leveraged methods from the textile industry to produce high volumes of konjac glucomannan monofilaments at production rates of 15 m/min with polymer costs in the range of $0.18USD/kilometer. We show that wet-spun konjac glucomannan fibers exhibited dry tensile strengths in the 35 MPa range which were of sufficient strength to withstand downstream automated circular braiding. Critically, C2C12 muscle cells readily attached, grew, and differentiated on these plant monofilaments. Myotube fusion approached 50 % with strong global alignment with the longitudinal axis of the fiber. More than 20 % of the myotubes were 0.8 mm long, indicating strong differentiation. As fat is an important carrier of flavor, we also demonstrated 3T3-L1 adipocyte attachment and differentiation. With multiple filaments, C2C12 connected tissue across strands suggesting possible paths forward to large, macroscopic constructs. Cultivated meat will require the integration of numerous advances from the tissue engineering field. We demonstrate here that emphasizing the manufacturing constraints of scaffold production rather than precisely mimicking native tissue yields low-cost biocompatible scaffolds.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"174 ","pages":"Article 112350"},"PeriodicalIF":11.0,"publicationDate":"2025-12-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145734576","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 : 2025-12-10DOI: 10.1016/j.foodhyd.2025.112349
Minxin Lu , Ruizi Zhou , Chang Zhang , Shucheng Liu , Hui Teng , Lei Chen
In this work, the myofibrillar protein (MP) of Penaeus vannamei was used to assess the effects of magnetic field-assisted freezing (MF) combined with curdlan (CUR) on its in vitro digestive properties, and to analyze digestive variations between the stomach and intestinal stages. The results showed that compared with gastric digestion, intestinal digestion exhibited a higher protein digestibility (65.37 %) and degree of hydrolysis (12.05 %) under the condition of 600G+0.6 %, indicating that intestinal enzymes were more efficient at degrading MP under this condition. Particle size distribution showed that protein aggregate size decreased significantly to 1.29 nm and 1.5 nm (p < 0.05) under 600G+0.4 % and 600G+0.6 % respectively after intestinal digestion. Fluorescence and Ultraviolet spectra revealed the exposure of the hydrophobic environment of aromatic residues during the intestinal phase, confirming the increased accessibility of active groups. Microstructural observations showed that the intestinal digestion products under 600G+0.4 % and 600G+0.6 % exhibited a more homogeneous, fragmented morphology. SDS-PAGE analysis confirmed a significant increase in the content of small molecule peptides (<11 kDa) during the intestinal phase. In addition, the total amount of free amino acids after intestinal digestion was 10 times higher than that in the gastric stage, indicating that MF-CUR treatment promoted deep hydrolysis of MP. In conclusion, the digestive efficiency of the intestinal stage is significantly higher than that of the gastric stage, and the combination of MF and CUR can maximize the digestive properties of MP. This provides a novel concept for the high-value processing of aquatic products.
{"title":"Effects of magnetic field assisted freezing combined with curdlan in vitro digestion of myofibrillar protein in Penaeus vannamei from the perspective of gel","authors":"Minxin Lu , Ruizi Zhou , Chang Zhang , Shucheng Liu , Hui Teng , Lei Chen","doi":"10.1016/j.foodhyd.2025.112349","DOIUrl":"10.1016/j.foodhyd.2025.112349","url":null,"abstract":"<div><div>In this work, the myofibrillar protein (MP) of <em>Penaeus vannamei</em> was used to assess the effects of magnetic field-assisted freezing (MF) combined with curdlan (CUR) on its in vitro digestive properties, and to analyze digestive variations between the stomach and intestinal stages. The results showed that compared with gastric digestion, intestinal digestion exhibited a higher protein digestibility (65.37 %) and degree of hydrolysis (12.05 %) under the condition of 600G+0.6 %, indicating that intestinal enzymes were more efficient at degrading MP under this condition. Particle size distribution showed that protein aggregate size decreased significantly to 1.29 nm and 1.5 nm (<em>p</em> < 0.05) under 600G+0.4 % and 600G+0.6 % respectively after intestinal digestion. Fluorescence and Ultraviolet spectra revealed the exposure of the hydrophobic environment of aromatic residues during the intestinal phase, confirming the increased accessibility of active groups. Microstructural observations showed that the intestinal digestion products under 600G+0.4 % and 600G+0.6 % exhibited a more homogeneous, fragmented morphology. SDS-PAGE analysis confirmed a significant increase in the content of small molecule peptides (<11 kDa) during the intestinal phase. In addition, the total amount of free amino acids after intestinal digestion was 10 times higher than that in the gastric stage, indicating that MF-CUR treatment promoted deep hydrolysis of MP. In conclusion, the digestive efficiency of the intestinal stage is significantly higher than that of the gastric stage, and the combination of MF and CUR can maximize the digestive properties of MP. This provides a novel concept for the high-value processing of aquatic products.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"174 ","pages":"Article 112349"},"PeriodicalIF":11.0,"publicationDate":"2025-12-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145735078","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 : 2025-12-09DOI: 10.1016/j.foodhyd.2025.112337
Xiaolin An , Zilong Zhao , Zixian Zhu , Dan Huang , Xing Chen , Bowen Yan , Jianlian Huang , Nana Zhang , Daming Fan
Microalgae, as a nutrient-rich emerging food source, play a crucial role in the development of future food, while their consumption forms are limited. To broaden their applications, the chlorella powder was used as the main material and processed with microwave 3D printing to achieve instant molding and curing. The dispersed chlorella particles were blended with κ-carrageenan to establish a network structure, enhancing its compatibility for microwave 3D printing. Stress-strain analysis demonstrated that κ-carrageenan facilitated the instant curing of chlorella under microwave 3D printing and the curing strength increased proportionally with both microwave power and κ-carrageenan concentration. Furthermore, rheological analysis and simulation elucidated the regulatory effects of microwave power and κ-carrageenan on chlorella extrusion and deposition. The combined action of microwave and κ-carrageenan significantly improved the fluid field distribution during extrusion, and the deposited filament exhibited a threefold increase in G′ within 0.30 s. The low-field nuclear magnetic resonance and fourier transform infrared spectroscopy were empolyed to analyze the effects of microwave and phase transition of κ-carrageenan on water distribution and molecular structural changes within the system. Scanning electron microscopy was also utilized to observe the microstructures of chlorella particles crosslinked by κ-carrageenan at different printing temperatures. Based on the instant molding capacity of printed chlorella, the configurations of products were customized, achieving complex designs such as hollowed-out overhanging structures. Additionally, microwave 3D printing could modulate the textural properties of chlorella-based products to a certain extent. Overall, our findings provide a new approach for the design of future microalgae-based foods.
{"title":"κ-Carrageenan facilitates the instant curing of chlorella powders during microwave 3D printing","authors":"Xiaolin An , Zilong Zhao , Zixian Zhu , Dan Huang , Xing Chen , Bowen Yan , Jianlian Huang , Nana Zhang , Daming Fan","doi":"10.1016/j.foodhyd.2025.112337","DOIUrl":"10.1016/j.foodhyd.2025.112337","url":null,"abstract":"<div><div>Microalgae, as a nutrient-rich emerging food source, play a crucial role in the development of future food, while their consumption forms are limited. To broaden their applications, the chlorella powder was used as the main material and processed with microwave 3D printing to achieve instant molding and curing. The dispersed chlorella particles were blended with κ-carrageenan to establish a network structure, enhancing its compatibility for microwave 3D printing. Stress-strain analysis demonstrated that κ-carrageenan facilitated the instant curing of chlorella under microwave 3D printing and the curing strength increased proportionally with both microwave power and κ-carrageenan concentration. Furthermore, rheological analysis and simulation elucidated the regulatory effects of microwave power and κ-carrageenan on chlorella extrusion and deposition. The combined action of microwave and κ-carrageenan significantly improved the fluid field distribution during extrusion, and the deposited filament exhibited a threefold increase in G′ within 0.30 s. The low-field nuclear magnetic resonance and fourier transform infrared spectroscopy were empolyed to analyze the effects of microwave and phase transition of κ-carrageenan on water distribution and molecular structural changes within the system. Scanning electron microscopy was also utilized to observe the microstructures of chlorella particles crosslinked by κ-carrageenan at different printing temperatures. Based on the instant molding capacity of printed chlorella, the configurations of products were customized, achieving complex designs such as hollowed-out overhanging structures. Additionally, microwave 3D printing could modulate the textural properties of chlorella-based products to a certain extent. Overall, our findings provide a new approach for the design of future microalgae-based foods.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"174 ","pages":"Article 112337"},"PeriodicalIF":11.0,"publicationDate":"2025-12-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145735080","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}
Understanding how plant-based ingredients interact and behave structurally is essential for achieving desired qualities in food products. However, investigations into cellulose nanocrystal (CNC)-induced structural modulation in chickpea protein matrices have offered limited insight into the conformational rearrangements occurring within their secondary structural elements. This study examined the effects of CNC concentrations (0.5, 1, and 3 %) on the conformational, secondary structure, and rheological properties of chickpea protein isolate (CPI) suspensions. The incorporation of CNC promoted greater aggregation, surface hydrophobicity, and exposed free sulfhydryl groups in the proteins, resulting in an increased water absorption capacity of the CPI-CNC complexes. Protein solubility improved as the CNC content increased (reaching 51 % with 3 % CNC), possibly because of structural changes that exposed amino acid residues to interact with water. FTIR analysis indicated that hydrogen bonds and electrostatic interactions affected the complexation of CPI and CNC. At low concentrations of CNC (0.5 %–1 %), the content of anti-parallel β-sheets and β-turns was reduced to transform into pseudo-β-sheets, promoting a more disordered conformation. However, the 1:1 protein-to-nanocrystal ratio promoted more pseudo-, anti-parallel-, and parallel β-sheets from α-helices and β-turns than CPI. The viscosity, viscoelasticity, and thixotropy behavior of the protein suspensions were influenced by an increase in CNC. A high CNC content markedly increased the thixotropic response of the CPI–CNC complexes, indicating reinforcement of interparticle bonding and network cohesiveness. These results highlight the importance of nanocrystal concentration in the modulation of plant-based protein structures and microstructure of the formed colloids.
{"title":"Cellulose nanocrystal-mediated modulation of structural conformation and rheological properties of chickpea proteins","authors":"Ingrid Contardo , Sofía Gutiérrez , Valentina Walton , Bastián Hidalgo","doi":"10.1016/j.foodhyd.2025.112341","DOIUrl":"10.1016/j.foodhyd.2025.112341","url":null,"abstract":"<div><div>Understanding how plant-based ingredients interact and behave structurally is essential for achieving desired qualities in food products. However, investigations into cellulose nanocrystal (CNC)-induced structural modulation in chickpea protein matrices have offered limited insight into the conformational rearrangements occurring within their secondary structural elements. This study examined the effects of CNC concentrations (0.5, 1, and 3 %) on the conformational, secondary structure, and rheological properties of chickpea protein isolate (CPI) suspensions. The incorporation of CNC promoted greater aggregation, surface hydrophobicity, and exposed free sulfhydryl groups in the proteins, resulting in an increased water absorption capacity of the CPI-CNC complexes. Protein solubility improved as the CNC content increased (reaching 51 % with 3 % CNC), possibly because of structural changes that exposed amino acid residues to interact with water. FTIR analysis indicated that hydrogen bonds and electrostatic interactions affected the complexation of CPI and CNC. At low concentrations of CNC (0.5 %–1 %), the content of anti-parallel β-sheets and β-turns was reduced to transform into pseudo-β-sheets, promoting a more disordered conformation. However, the 1:1 protein-to-nanocrystal ratio promoted more pseudo-, anti-parallel-, and parallel β-sheets from α-helices and β-turns than CPI. The viscosity, viscoelasticity, and thixotropy behavior of the protein suspensions were influenced by an increase in CNC. A high CNC content markedly increased the thixotropic response of the CPI–CNC complexes, indicating reinforcement of interparticle bonding and network cohesiveness. These results highlight the importance of nanocrystal concentration in the modulation of plant-based protein structures and microstructure of the formed colloids.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"174 ","pages":"Article 112341"},"PeriodicalIF":11.0,"publicationDate":"2025-12-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145735082","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 : 2025-12-08DOI: 10.1016/j.foodhyd.2025.112314
Huan Lin , Mengke Yao , Qing Zhang , Yingying He , Changfeng Qu , Jinlai Miao
Low-molecular-weight carrageenan (LMWC) has attracted much attention due to its bioactivity. Furthermore, films and hard capsules developed using LMWC as the raw materials also possess significant research value. In this study, the chemical structure of LMWC was characterized, and the rheological properties of LMWC, kappa-carrageenan (κ-C), and gelatin were investigated. Additionally, the mechanical and optical properties of films produced from these materials were compared. Finally, Carrageenan hard capsules were prepared using LMWC. The results showed that the molecular weight of LMWC was 15.75 kDa, representing a decrease by 97.42 %, and its viscosity was 3.90 ± 0.14 mPa s, a reduction of 97.32 %. FT-IR analysis indicated that the molecular structure of LMWC remained unchanged and was consistent with that of κ-C. Rheological results demonstrated that LMWC behaved as a pseudoplastic fluid, and its flow curve was more similar to gelatin and distinctly different from κ-C. Furthermore, the viscosity and gelation properties of LMWC solutions resembled those of gelatin than κ-C, and all solutions formed smooth, transparent films. The LMWC films exhibited outstanding mechanical properties, with the highest tensile strength reaching 76.22 ± 3.42 MPa at 3 % and the greatest elongation at break reaching 10.62 ± 1.49 % at 5 %. All films showed very high light transmittance, exceeding 90 % at 800 nm, indicating superior optical qualities. The capsules made from LMWC were clear, smooth-surfaced, and flexible. Therefore, LMWC possesses excellent gel-forming and film-forming properties and has the potential to develop carrageenan-based hard capsules as an alternative for gelatin products.
{"title":"Film and hard capsule formation properties of the low-molecular-weight carrageenan","authors":"Huan Lin , Mengke Yao , Qing Zhang , Yingying He , Changfeng Qu , Jinlai Miao","doi":"10.1016/j.foodhyd.2025.112314","DOIUrl":"10.1016/j.foodhyd.2025.112314","url":null,"abstract":"<div><div>Low-molecular-weight carrageenan (LMWC) has attracted much attention due to its bioactivity. Furthermore, films and hard capsules developed using LMWC as the raw materials also possess significant research value. In this study, the chemical structure of LMWC was characterized, and the rheological properties of LMWC, kappa-carrageenan (κ-C), and gelatin were investigated. Additionally, the mechanical and optical properties of films produced from these materials were compared. Finally, Carrageenan hard capsules were prepared using LMWC. The results showed that the molecular weight of LMWC was 15.75 kDa, representing a decrease by 97.42 %, and its viscosity was 3.90 ± 0.14 mPa s, a reduction of 97.32 %. FT-IR analysis indicated that the molecular structure of LMWC remained unchanged and was consistent with that of κ-C. Rheological results demonstrated that LMWC behaved as a pseudoplastic fluid, and its flow curve was more similar to gelatin and distinctly different from κ-C. Furthermore, the viscosity and gelation properties of LMWC solutions resembled those of gelatin than κ-C, and all solutions formed smooth, transparent films. The LMWC films exhibited outstanding mechanical properties, with the highest tensile strength reaching 76.22 ± 3.42 MPa at 3 % and the greatest elongation at break reaching 10.62 ± 1.49 % at 5 %. All films showed very high light transmittance, exceeding 90 % at 800 nm, indicating superior optical qualities. The capsules made from LMWC were clear, smooth-surfaced, and flexible. Therefore, LMWC possesses excellent gel-forming and film-forming properties and has the potential to develop carrageenan-based hard capsules as an alternative for gelatin products.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"174 ","pages":"Article 112314"},"PeriodicalIF":11.0,"publicationDate":"2025-12-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145734628","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 : 2025-12-07DOI: 10.1016/j.foodhyd.2025.112334
Rulin Jin , Shuangjian Li , Saiya Li , Xiaoyang Li , Yiguo Zhao , Wei Lu , Cuixia Sun , Yapeng Fang , Yiping Cao
Pumpkin seed protein isolate (PSPI) represents an underutilized resource with nutritional value but limited techno-functionality. This study introduced a facile microwave pretreatment to markedly enhance the fibrillization capacity of PSPI. Optimal pretreatment (1 min, denoted as PSPI-M1) followed by heating at 90 °C and pH 2.5 for 5 h yielded fibrils with a high conversion rate, as confirmed by ThT fluorescence, SDS-PAGE, AFM, and TEM. Structural analyses (FTIR, XRD) verified the formation of characteristic cross-β-sheet-rich amyloid fibrils. The resultant fibrils exhibited significantly improved foaming capacity and stability. Furthermore, a synergistic effect was observed when fibrillated PSPI-M1 was combined with co-extracted albumin. Leveraging this enhanced functionality, fibrillated PSPI-M1 was successfully employed as a 100 % replacer for egg white in chiffon cakes, producing cakes with high specific volume and desirable soft texture. This work demonstrates microwave pretreatment as an effective strategy to unlock the functional potential of PSPI, facilitating its application as a high-value, plant-based ingredient in aerated foods.
{"title":"Microwave pretreatment enhances pumpkin seed protein fibrillization for egg white substitution in chiffon cakes","authors":"Rulin Jin , Shuangjian Li , Saiya Li , Xiaoyang Li , Yiguo Zhao , Wei Lu , Cuixia Sun , Yapeng Fang , Yiping Cao","doi":"10.1016/j.foodhyd.2025.112334","DOIUrl":"10.1016/j.foodhyd.2025.112334","url":null,"abstract":"<div><div>Pumpkin seed protein isolate (PSPI) represents an underutilized resource with nutritional value but limited techno-functionality. This study introduced a facile microwave pretreatment to markedly enhance the fibrillization capacity of PSPI. Optimal pretreatment (1 min, denoted as PSPI-M1) followed by heating at 90 °C and pH 2.5 for 5 h yielded fibrils with a high conversion rate, as confirmed by ThT fluorescence, SDS-PAGE, AFM, and TEM. Structural analyses (FTIR, XRD) verified the formation of characteristic cross-β-sheet-rich amyloid fibrils. The resultant fibrils exhibited significantly improved foaming capacity and stability. Furthermore, a synergistic effect was observed when fibrillated PSPI-M1 was combined with co-extracted albumin. Leveraging this enhanced functionality, fibrillated PSPI-M1 was successfully employed as a 100 % replacer for egg white in chiffon cakes, producing cakes with high specific volume and desirable soft texture. This work demonstrates microwave pretreatment as an effective strategy to unlock the functional potential of PSPI, facilitating its application as a high-value, plant-based ingredient in aerated foods.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"174 ","pages":"Article 112334"},"PeriodicalIF":11.0,"publicationDate":"2025-12-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145734577","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 : 2025-12-06DOI: 10.1016/j.foodhyd.2025.112338
Aiting Hui , Wenbiao Lv , Yuqi Xie , Lu Wang , Fengying Xie
This study investigated the effects of different amylose contents on the structural and gel properties of corn starch-sodium alginate hydrogel beads. Compared with the waxy corn starch-sodium alginate (WCS-SA) and normal corn starch-sodium alginate (NCS-SA) hydrogel beads, the high-amylose corn starch-sodium alginate (HCS-SA) hydrogel beads presented more ordered pore structure, lower porosity, and higher relative crystallinity. These structural changes suggested that amylose structure accelerated its recrystallization, leading to the formation of a denser double cross-linking gel network. In low-field nuclear magnetic resonance, a higher content of amylose caused a left-shift in the transverse relaxation time, with an increase in the proportion of immobilized water. Rheological data revealed that the storage modulus (G′) of HCS-SA hydrogel beads exhibited a significant elevation relative to WCS-SA and NCS-SA hydrogel beads with increasing amylose content. Texture profile analysis corroborated these findings, indicating that the hardness, springiness, and gumminess of hydrogel beads significantly increased with amylose content. Among them, the HCS70-SA hydrogel bead reached the maximum value. Furthermore, high-amylose corn starch decreased the water content and markedly restricted the swelling ratio of the hydrogel beads. Thus, the mechanical properties and swelling ratio of starch-based hydrogel beads can be effectively optimized by controlling the amylose content, offering a novel strategy for the development of controlled-release systems in functional foods.
{"title":"Performance valuation of the gel properties of starch-based hydrogel beads: Understanding the interaction between amylose and sodium alginate and the formation mechanism of the double network structure","authors":"Aiting Hui , Wenbiao Lv , Yuqi Xie , Lu Wang , Fengying Xie","doi":"10.1016/j.foodhyd.2025.112338","DOIUrl":"10.1016/j.foodhyd.2025.112338","url":null,"abstract":"<div><div>This study investigated the effects of different amylose contents on the structural and gel properties of corn starch-sodium alginate hydrogel beads. Compared with the waxy corn starch-sodium alginate (WCS-SA) and normal corn starch-sodium alginate (NCS-SA) hydrogel beads, the high-amylose corn starch-sodium alginate (HCS-SA) hydrogel beads presented more ordered pore structure, lower porosity, and higher relative crystallinity. These structural changes suggested that amylose structure accelerated its recrystallization, leading to the formation of a denser double cross-linking gel network. In low-field nuclear magnetic resonance, a higher content of amylose caused a left-shift in the transverse relaxation time, with an increase in the proportion of immobilized water. Rheological data revealed that the storage modulus (G′) of HCS-SA hydrogel beads exhibited a significant elevation relative to WCS-SA and NCS-SA hydrogel beads with increasing amylose content. Texture profile analysis corroborated these findings, indicating that the hardness, springiness, and gumminess of hydrogel beads significantly increased with amylose content. Among them, the HCS70-SA hydrogel bead reached the maximum value. Furthermore, high-amylose corn starch decreased the water content and markedly restricted the swelling ratio of the hydrogel beads. Thus, the mechanical properties and swelling ratio of starch-based hydrogel beads can be effectively optimized by controlling the amylose content, offering a novel strategy for the development of controlled-release systems in functional foods.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"174 ","pages":"Article 112338"},"PeriodicalIF":11.0,"publicationDate":"2025-12-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145734626","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 : 2025-12-06DOI: 10.1016/j.foodhyd.2025.112335
Ning Li , Fengzhang Wang , Yang Li , Dezhi Li , Huanhuan Wang , Yimeng Shan , Mengzi Nie , Jing Wang , Li-Tao Tong
Rice protein has excellent nutritional properties including low allergenicity, balanced amino acid composition, and mild flavor, but its poor solubility significantly limits its potential for high-value applications. This study investigated the interaction mechanism between dipotassium glycyrrhizinate (DG) and rice glutelin (RG) during pH cycling, with a focus on its role in improving RG solubility and modulating protein aggregation behavior. After co-assembly of RG and DG, the solubility of RG increased significantly from 5.81 % to 95.77 % under neutral conditions (pH 7.0), with a 35.76 % elevation in the absolute zeta potential value. Concurrently, the particle size decreased substantially from 4.03 μm to 82.30 nm, along with a significant reduction in turbidity. The results indicated that co-assembly of DG and RG can effectively inhibit self-aggregation of protein, thereby enhancing its solubility. Multi-spectroscopy and molecular dynamics simulations revealed that hydrophobic interaction, electrostatic interaction and hydrogen bonding are the main driving forces behind DG–RG binding. Surface hydrophobicity (H0) and zeta potential results indicated that DG stabilized the structural unfolding of RG by binding to the hydrophobic region of the protein, thereby inhibiting further protein aggregation. Microscopic morphology observation provides further visual evidence that complexes of RG and DG dissociate micrometer-scale aggregates into nanometer-scale spherical particles. In summary, this study presents a promising strategy for enhancing the solubility of RG, with significant implications for broadening the applications of rice protein and modifying insoluble plant-based proteins.
{"title":"The pH-driven binding mechanism of rice glutelin-dipotassium glycyrrhizinate and its effects on protein solubility and aggregation behavior","authors":"Ning Li , Fengzhang Wang , Yang Li , Dezhi Li , Huanhuan Wang , Yimeng Shan , Mengzi Nie , Jing Wang , Li-Tao Tong","doi":"10.1016/j.foodhyd.2025.112335","DOIUrl":"10.1016/j.foodhyd.2025.112335","url":null,"abstract":"<div><div>Rice protein has excellent nutritional properties including low allergenicity, balanced amino acid composition, and mild flavor, but its poor solubility significantly limits its potential for high-value applications. This study investigated the interaction mechanism between dipotassium glycyrrhizinate (DG) and rice glutelin (RG) during pH cycling, with a focus on its role in improving RG solubility and modulating protein aggregation behavior. After co-assembly of RG and DG, the solubility of RG increased significantly from 5.81 % to 95.77 % under neutral conditions (pH 7.0), with a 35.76 % elevation in the absolute zeta potential value. Concurrently, the particle size decreased substantially from 4.03 μm to 82.30 nm, along with a significant reduction in turbidity. The results indicated that co-assembly of DG and RG can effectively inhibit self-aggregation of protein, thereby enhancing its solubility. Multi-spectroscopy and molecular dynamics simulations revealed that hydrophobic interaction, electrostatic interaction and hydrogen bonding are the main driving forces behind DG–RG binding. Surface hydrophobicity (H<sub>0</sub>) and zeta potential results indicated that DG stabilized the structural unfolding of RG by binding to the hydrophobic region of the protein, thereby inhibiting further protein aggregation. Microscopic morphology observation provides further visual evidence that complexes of RG and DG dissociate micrometer-scale aggregates into nanometer-scale spherical particles. In summary, this study presents a promising strategy for enhancing the solubility of RG, with significant implications for broadening the applications of rice protein and modifying insoluble plant-based proteins.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"174 ","pages":"Article 112335"},"PeriodicalIF":11.0,"publicationDate":"2025-12-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145734627","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 : 2025-12-06DOI: 10.1016/j.foodhyd.2025.112339
Shiwen Lin , Yutong Liu , Cheng Li , Baohua Kong , Min Li , Qian Liu , Chuanai Cao
This study aimed to assess the regulatory mechanism by which κ-carrageenan (KC) enhances the water holding capacity (WHC) of myofibrillar protein (MP) gels under different NaCl concentrations during the heating process, focusing on dynamic changes in protein aggregation behaviour and molecular docking. The addition of KC considerably enhanced the WHC and immobilized water content of MP gels, with relatively low porosity distributed throughout the gel matrix—particularly at an NaCl concentration of 0.6 M (P < 0.05). During the heating process, KC facilitated the early denaturation and aggregation of MP at lower temperatures. This resulted in the formation of an irreversible three-dimensional network, as evidenced by the assessment of dynamic rheological behaviour. Moreover, during the heating process, KC significantly increased the surface hydrophobicity and progressively decreased the fluorescence intensity of MP, especially at temperatures of 40°C–60 °C (P < 0.05). This finding suggests that KC facilitated the unfolding of the tertiary structure of MP through heating treatment. It also facilitated a structural transition in MP, resulting in a shift from an α-helix configuration to a β-sheet arrangement. This alteration promoted the aggregation of myosin heads and enhanced cross-linking among myosin tails. Furthermore, disulfide bonding and hydrophobic interactions performed played roles as driving forces in the formation of MP–KC mixed gels during heat treatment, particularly at NaCl concentrations of up to 0.6 M, as verified by the molecular docking results. Our study provides novel theoretical insights into the gelling mechanisms of MP–KC mixed gels. These findings have significant implications for the practical utilization of KC for the development of meat products.
{"title":"Underlying the regulatory mechanism of κ-carrageenan on improving the water holding capacity of myofibrillar protein gels at different NaCl levels: Emphasis on aggregation behaviour and molecular docking during heating process","authors":"Shiwen Lin , Yutong Liu , Cheng Li , Baohua Kong , Min Li , Qian Liu , Chuanai Cao","doi":"10.1016/j.foodhyd.2025.112339","DOIUrl":"10.1016/j.foodhyd.2025.112339","url":null,"abstract":"<div><div>This study aimed to assess the regulatory mechanism by which <em>κ</em>-carrageenan (KC) enhances the water holding capacity (WHC) of myofibrillar protein (MP) gels under different NaCl concentrations during the heating process, focusing on dynamic changes in protein aggregation behaviour and molecular docking. The addition of KC considerably enhanced the WHC and immobilized water content of MP gels, with relatively low porosity distributed throughout the gel matrix—particularly at an NaCl concentration of 0.6 M (<em>P</em> < 0.05). During the heating process, KC facilitated the early denaturation and aggregation of MP at lower temperatures. This resulted in the formation of an irreversible three-dimensional network, as evidenced by the assessment of dynamic rheological behaviour. Moreover, during the heating process, KC significantly increased the surface hydrophobicity and progressively decreased the fluorescence intensity of MP, especially at temperatures of 40°C–60 °C (<em>P</em> < 0.05). This finding suggests that KC facilitated the unfolding of the tertiary structure of MP through heating treatment. It also facilitated a structural transition in MP, resulting in a shift from an <em>α</em>-helix configuration to a β-sheet arrangement. This alteration promoted the aggregation of myosin heads and enhanced cross-linking among myosin tails. Furthermore, disulfide bonding and hydrophobic interactions performed played roles as driving forces in the formation of MP–KC mixed gels during heat treatment, particularly at NaCl concentrations of up to 0.6 M, as verified by the molecular docking results. Our study provides novel theoretical insights into the gelling mechanisms of MP–KC mixed gels. These findings have significant implications for the practical utilization of KC for the development of meat products.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"174 ","pages":"Article 112339"},"PeriodicalIF":11.0,"publicationDate":"2025-12-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145734629","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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