Food Hydrocolloids最新文献

{"title":"Acidic-heating induced protein fibrils derived from perilla seed residues: spotlight on assembly behavior, conformational changes and structure-function relationships","authors":"Xiquan Li ,&nbsp;Jun Yang ,&nbsp;Liting Feng ,&nbsp;Hao Guo ,&nbsp;Xiaochen Liu ,&nbsp;Xiuling Zhang ,&nbsp;Wentao Zhang","doi":"10.1016/j.foodhyd.2025.111709","DOIUrl":"10.1016/j.foodhyd.2025.111709","url":null,"abstract":"<div><div><em>In vitro</em> fibrillation of food-derived proteins is increasingly accepted as a promising strategy to prepare new food ingredients, which have broader functional properties than natural protein. In current study, acidic-heating (90 °C, pH 2.0) was performed for perilla seed protein isolate (PSPI) derived from oilseed residues to evaluate the feasibility to produce protein fibrils. TEM images revealed that PSPI were hydrolyzed and reassembled a fundamental linear structure of fibrils after 6 h of heating, as reflected by the variation in particle size distribution. And the branching effects were observed with prolonged time. The conformational changes of PSPI were systematically assessed by electrophoresis, fourier transform infrared spectroscopy, fluorescence spectroscopy, circular dichroism, molecular dynamics simulations. Together with the results of surface hydrophobicity, zeta-potential confirmed that the self-assembly behavior of PSPI based fibrils was dominated by hydrophobic and electrostatic interactions. In addition, correlation analysis was combined to reflect the dynamical variation on emulsification, foaming, viscosity, interfacial and antioxidant properties during the structural evolution of PSPI. Overall, in-depth insights on the potential of perilla residues to convert into protein fibers will provide theoretical support for the regulation of functional properties of plant proteins and expand the potential applications of oilseed residues in the food field.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"170 ","pages":"Article 111709"},"PeriodicalIF":11.0,"publicationDate":"2025-06-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144519126","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}

{"title":"Potential enhancement of thermal stability in soy protein nanofibrils by metal ions","authors":"Hekai Zhao ,&nbsp;Yao Lu ,&nbsp;Yuyang Huang ,&nbsp;Baokun Qi ,&nbsp;Yang Li","doi":"10.1016/j.foodhyd.2025.111714","DOIUrl":"10.1016/j.foodhyd.2025.111714","url":null,"abstract":"<div><div>Fibrillation, a universal property of proteins, serves as an effective strategy to enhance the functional properties of food-derived proteins. However, certain protein fibrils are susceptible to degradation at elevated temperatures, which limits their application. This study investigates the thermal destabilization behavior of soy protein nanofibril (SPNF) during prolonged heating (85 °C, 0–72 h) and explores the role of Na⁺ and Ca²⁺ in enhancing fibril thermal stability. The aggregation, morphology, and structural properties of the fibril systems were analyzed, revealing that all fibril systems developed weak gels after 24 h of incubation. SPNF and Na⁺-induced SPNF experienced gel network disruption and aggregation during prolonged heating, leading to increased particle size, turbidity, and reduced storage modulus, transitioning to fluid state at 36 h. Meanwhile, both exhibited a rapid decrease in ThT fluorescence and a transition from linear fibrils to particulate aggregates within 60 h. CD and FTIR indicated that as fibrils degraded, the β-sheet structure converted to β-turns, with a significant reduction in hydrogen bonding. Conversely, SPNF induced by 100 and 33 mM Ca²⁺ effectively resisted aggregation, maintaining gelation at 60 and 48 h, respectively. The ThT fluorescence, β-sheet structure, and hydrogen bonding decreased relatively slowly with prolonged heating, and the fibril morphology remained intact at 60 h. Thermogravimetric analysis confirmed that 100 mM Ca²⁺-induced fibrils had a higher thermal degradation temperature (341 °C). These findings suggest that Ca²⁺ enhances SPNF thermal stability, providing a theoretical basis for its application in high-temperature environments in food processing.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"170 ","pages":"Article 111714"},"PeriodicalIF":11.0,"publicationDate":"2025-06-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144519127","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}

{"title":"From agro-waste to functional emulsifiers: Length-optimized cellulose nanocrystals from jujube seeds enhance curcumin delivery in pickering emulsions","authors":"Xingchen Gao ,&nbsp;Yakun Hou ,&nbsp;Yajun Deng ,&nbsp;Shiyu Sun ,&nbsp;Lianfeng Zhao ,&nbsp;Sheng Liu ,&nbsp;Yaxin Sang ,&nbsp;Bing Yang","doi":"10.1016/j.foodhyd.2025.111704","DOIUrl":"10.1016/j.foodhyd.2025.111704","url":null,"abstract":"<div><div>Curcumin, a polyphenolic compound with strong antioxidant and antidiabetic effects, faces limited application due to its lipophilicity and chemical instability. This study investigated the use of cellulose nanocrystals (CNCs), derived from jujube seed waste, to stabilize Pickering emulsions for curcumin encapsulation and assess its digestive behavior. CNCs with varying lengths were produced via acid hydrolysis, ammonium persulfate oxidation, and ultrasonic treatment. Structural and functional properties were characterized, and the influence of CNC length, concentration, and oil-to-water ratio on emulsion formation and curcumin digestibility was examined. Ultrasonication reduced CNC length, increased hydrophobicity, and improved network formation without altering crystallinity. All CNC variants effectively stabilized emulsions, which remained stable during storage. Emulsions with CNC concentrations above 0.9 % formed dense three-dimensional networks that enhanced overall emulsion stability. In vitro digestion revealed that longer CNCs provided better protection for encapsulated curcumin but reduced its bioavailability. Higher oil phase ratios suppressed free fatty acid (FFA) release by limiting lipase access to lipid droplets. Overall, this study demonstrates that adjusting CNC length and oil content provides an effective approach for controlling lipid digestion and optimizing curcumin bioavailability in Pickering emulsions, supporting their use as functional delivery systems.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"170 ","pages":"Article 111704"},"PeriodicalIF":11.0,"publicationDate":"2025-06-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144519122","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}

{"title":"Influence of extrusion processing conditions on fibrous structure, texture, and digestibility of plant-based meat analogues incorporating faba bean protein and brewers’ spent grain","authors":"Yue Fan ,&nbsp;Pratheep K. Annamalai ,&nbsp;Jingjing Wang ,&nbsp;Biao Gu ,&nbsp;Xiao Dong Chen ,&nbsp;Bhesh Bhandari ,&nbsp;Sangeeta Prakash","doi":"10.1016/j.foodhyd.2025.111706","DOIUrl":"10.1016/j.foodhyd.2025.111706","url":null,"abstract":"<div><div>High-moisture extrusion is the most cost-effective method for producing meat analogues with desired microstructure and textural characteristics, owing to its combined unit operations and customisable process conditions. An appropriate combination of extrusion conditions is crucial for obtaining high-moisture meat analogue (HMMA) products with the desired characteristics. In this study, we systematically investigated the effects of varying extrusion conditions, specifically temperature (130–160 °C) and screw speed (100–300 rpm), on the formation of fibrous structure of faba bean protein-based HMMA in the presence of brewers’ spent grain. Our findings indicate that higher screw speeds and temperatures significantly enhanced the phase separation, physical cross-linking, and fibrous structure formation, which improved textural attributes and increased water retention capacity. Importantly, the fibrous structure achieved through adjusting extrusion conditions did not adversely affect the digestibility of faba bean protein-based HMMA. By reporting the efficacy of the extrusion conditions in structuring fibrous meat analogues similar to chicken meat, this study demonstrates that a high-quality meat alternative product can be efficiently produced using two sustainable ingredients (faba bean protein and brewers’ spent grain) without any external modifiers.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"170 ","pages":"Article 111706"},"PeriodicalIF":11.0,"publicationDate":"2025-06-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144522278","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}

{"title":"Development of alginate-based active edible coating with Brassica juncea and Raphanus sativus sprout extracts to extend tomato shelf-life","authors":"Arash Moeini ,&nbsp;Sarai Agustin Salazar ,&nbsp;Luca Gargiulo ,&nbsp;Roméo Arago Dougué Kentsop ,&nbsp;Monica Mattana ,&nbsp;Annamaria Genga ,&nbsp;Christin Josi ,&nbsp;Parisa Pedram ,&nbsp;Gustavo Cabrera-Barjas ,&nbsp;Simona Guerra ,&nbsp;Massimiliano Marvasi ,&nbsp;Thomas Becker ,&nbsp;Pierfrancesco Cerruti","doi":"10.1016/j.foodhyd.2025.111693","DOIUrl":"10.1016/j.foodhyd.2025.111693","url":null,"abstract":"<div><div>Extending the shelf life of fresh produce using sustainable, bio-based preservation methods is an exciting and rapidly growing area of research, driven by the need to reduce food waste and meet consumer demand for chemical-free alternatives. This study presents the development of an alginate-based active edible coating incorporating <em>Brassica juncea</em> (GM) and <em>Raphanus sativus</em> (RT) sprout extracts to prolong tomato shelf life. The coating was prepared by modifying glycerol-plasticized alginate (A) with zein/chitosan (Z/CH) microparticles (MPs) containing the sprout extracts as bioactive antimicrobial and antioxidant agents. The physicochemical properties of the films were characterized using FTIR, SEM, TGA/DSC, contact angle, water vapor permeability, and tensile testing. FTIR analysis revealed interactions between alginate and MPs, TGA confirmed thermal stability, SEM showed uniform MP dispersion, and tensile tests indicated improved flexibility with extract addition, enhancing coating suitability. Encapsulated extracts increased antioxidant activity, achieving 52 % DPPH inhibition for GM and 70 % for RT. The antimicrobial assay demonstrated that RT-formulated films showed moderate biocidal activity against <em>Bacillus cereus</em> and <em>Salmonella enterica</em>, highlighting their potential to improve food safety. Furthermore, tomato shelf-life testing revealed a 30-day extension using RT-loaded MPs, with no visible changes in appearance or texture. These findings suggest that encapsulating RT in plasticized alginate coatings enhances tomato longevity and quality, supporting the use of edible films for active food packaging applications.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"170 ","pages":"Article 111693"},"PeriodicalIF":11.0,"publicationDate":"2025-06-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144514385","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}

{"title":"Insights into the foaming properties of adzuki bean protein isolate as an alternative to egg white protein: Physicochemical and interfacial behaviors in foam decay mechanisms","authors":"June Lee ,&nbsp;Jinhee Kang ,&nbsp;Jee-Young Imm ,&nbsp;Hee Yang","doi":"10.1016/j.foodhyd.2025.111678","DOIUrl":"10.1016/j.foodhyd.2025.111678","url":null,"abstract":"<div><div>As the demand for egg white protein (EWP) alternatives grows due to concerns such as <em>Salmonella</em> contamination, avian influenza, and the increasing environmental awareness, plant-based proteins have gained attention as a promising solution. Compared to other legumes, adzuki beans are rich in sulfur-containing and hydrophobic aromatic amino acids, which may contribute to improved foaming properties. However, their functional potential remains largely unexplored. This study examined the foaming performance of adzuki bean protein isolate (API) relative to EWPs and soy protein isolate (SPI) under varying thermal and temporal conditions. API exhibited foam thickness and drainage comparable with those of EWPs and superior to SPI across 4°C, 25°C, and 83°C. Confocal laser scanning microscopy (CLSM) and scanning electron microscopy revealed that API formed finer, more spherical foam structures with fewer ruptures, while SPI showed larger, unstable bubbles. Zeta potential and dual-fluorescent CLSM analysis indicated greater interfacial rearrangement in API, supported by its lower surface hydrophobicity and higher free sulfhydryl (–SH) content, which enhanced interfacial stiffness in rheology. Fourier-transform infrared spectroscopy analysis further revealed that API, like EWPs, showed increased β-sheet formation under heat, contributing to thermal foam stability, whereas SPI exhibited the opposite trend. In a meringue cookie application, API showed a lighter batter with greater air incorporation than SPI, highlighting its practical potential. Overall, this study offers new insight into the structural and interfacial mechanisms governing foam formation and decay, supporting API’s potential as a promising plant-based alternative for aerated food systems.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"170 ","pages":"Article 111678"},"PeriodicalIF":11.0,"publicationDate":"2025-06-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144514386","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}

{"title":"Thermo-reversible/thermo-irreversible curdlan enhanced rheological behaviours and gelling properties of meat batters containing transglutaminase before and after thermal treatment","authors":"Dongxue Yuan ,&nbsp;Cheng Li ,&nbsp;Yutong Liu ,&nbsp;Chuanai Cao ,&nbsp;Baohua Kong ,&nbsp;Fangda Sun ,&nbsp;Qian Liu ,&nbsp;Yangyang Feng","doi":"10.1016/j.foodhyd.2025.111699","DOIUrl":"10.1016/j.foodhyd.2025.111699","url":null,"abstract":"<div><div>This study investigated combined effects of transglutaminase (TG) and thermo-reversible curdlan (TRC) or thermo-irreversible curdlan (TIRC) on the rheological behaviours, gelling properties and microstructures of meat batters before and after thermal treatment. The results revealed that compared to TG alone, the combination of TRC/TIRC and TG could increase the apparent viscosity and decrease the creep-recovery compliance of uncooked meat batters. Meanwhile, TRC/TIRC and TG could improve the viscoelasticity of meat batters, facilitating the development of a robust gel network structure during heating process, which can be confirmed by the temperature sweep analysis. Moreover, when compared with the control group, the hardness of cooked meat batters significantly increased from 134.92 g to 165.08 g in the TG + TRC-0.5 % group and to 158.69 g in the TG + TIRC-0.5 % group, while resilience increased from 84.62 g to 122.90 g and 113.51 g, respectively (<em>P</em> &lt; 0.05). Furthermore, both TRC and TIRC promoted the formation of a more compact and denser gel network structure in cooked meat batters, reducing pore size by 1.29 μm and 1.05 μm, respectively, compared to the control group. Therefore, our results found that the combination of TRC/TIRC and TG could improve the rheological behaviours of meat batters and facilitate the development of emulsified meat products with superior gelling properties. This study provided a theoretical foundation for the potential application of TRC/TIRC combined with TG in meat products.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"170 ","pages":"Article 111699"},"PeriodicalIF":11.0,"publicationDate":"2025-06-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144511120","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}

{"title":"Deciphering the key interfacial molecules and core structure contributing to fat globule stability in UHT Milk: Omics analysis and computer simulation","authors":"Yi Wang ,&nbsp;Jinghua Yu ,&nbsp;Fazheng Ren ,&nbsp;Pengjie Wang ,&nbsp;Peipei Wu ,&nbsp;Mengyuan Guo ,&nbsp;Wentao Qian ,&nbsp;Menghui Wang ,&nbsp;Jinhui Yang ,&nbsp;Jie Luo","doi":"10.1016/j.foodhyd.2025.111702","DOIUrl":"10.1016/j.foodhyd.2025.111702","url":null,"abstract":"<div><div>Creaming is an issue in UHT milk due to extended storage periods and higher storage temperatures. Therefore, this study aims to unravel the key interfacial molecules and core structure behind the stability of UHT milk fat globules. Raw milk from Holstein, Jersey, and goat breeds, which differ in interfacial components, was selected. The fat globules were standardized for particle size using the UHT system, and stability analysis was performed using Turbiscan to establish high, medium, and low stability fat globule models. Omics analysis revealed that the abundance of 3 interfacial proteins (butyrophilin, adipophilin, and xanthine oxidoreductase) and 2 interfacial phospholipids (phosphatidylserine and sphingomyelin) significantly increased as the fat globule stability increased. Support vector machine was used to identify key interfacial molecules. The results showed that the high abundance of butyrophilin, adipophilin, phosphatidylserine, and sphingomyelin contributed to fat globule stability. Molecular docking and CHARMM-GUI further determined that butyrophilin interacted with adipophilin mainly through hydrogen bonds (ΔG = −47.8 kcal/mol and interaction area = 3088.4 Å²). The abundance of this complex in high-stability fat globules was 2.2 times greater than that in medium-stability fat globules and 4.9 times greater than that in low-stability fat globules, respectively. We hypothesize that the butyrophilin-adipophilin complex may anchor both the inner monolayer and the outer bilayer, forming the backbone of the entire interface. Therefore, this study first reveals that the key molecules contributing to the stability of UHT milk fat globules are butyrophilin, adipophilin, phosphatidylserine, and sphingomyelin, with the butyrophilin-adipophilin complex serving as the core structure.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"170 ","pages":"Article 111702"},"PeriodicalIF":11.0,"publicationDate":"2025-06-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144490927","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}

{"title":"Insights into the highly selective and efficient adsorption of Pb2+ by fish skin collagen-enabled sodium alginate-based composite gel spheres: adsorption and interference mechanisms","authors":"Zuomiao Yang ,&nbsp;Yu Liu ,&nbsp;Enze Wang ,&nbsp;Wei Yin ,&nbsp;Yujiao Wang ,&nbsp;Yicheng Guo ,&nbsp;Wentao Zhang ,&nbsp;Hang Qi","doi":"10.1016/j.foodhyd.2025.111700","DOIUrl":"10.1016/j.foodhyd.2025.111700","url":null,"abstract":"&lt;div&gt;&lt;div&gt;Excessive lead content in wastewater and seaweed products is an urgent scientific problem to be solved. Sodium alginate (SA) is often used as a synthetic gel material to adsorb Pb&lt;sup&gt;2+&lt;/sup&gt; due to its good biocompatibility and affinity for metal ions. However, simple SA gels suffer from poor mechanical stability and limited adsorption capacity for Pb&lt;sup&gt;2+&lt;/sup&gt;. Therefore, there is a need to develop a stable composite SA gel material with high adsorption capacity for Pb&lt;sup&gt;2+&lt;/sup&gt;. Fish skin collagen (FC), as a by-product, is not highly utilized at present, and its own rich amino and carboxyl groups, is a natural and environmentally friendly food-grade adsorbent alternative material. Sodium carboxymethyl cellulose (CMC), a polysaccharide rich in carboxyl groups, is also a good raw material for the preparation of new and safe composite SA gels. Therefore, in this study, a green and non-toxic CMC-FC-SA composite gel sphere was developed to adsorb Pb&lt;sup&gt;2+&lt;/sup&gt; efficiently by physically mixing SA/CMC/FC in the framework of a one-pot method with Ca&lt;sup&gt;2+&lt;/sup&gt; cross-linking. The prepared porous composite gel spheres not only had good swelling and thermal stability, but also showed excellent specific adsorption capacity for Pb&lt;sup&gt;2+&lt;/sup&gt;. The results revealed that the adsorption process of CMC-FC-SA on Pb&lt;sup&gt;2+&lt;/sup&gt; was more consistent with the proposed secondary kinetic model and Langmuir isothermal adsorption model, suggesting that the adsorption process was governed by monolayer chemisorption. The maximum theoretical value of Qm for Pb&lt;sup&gt;2+&lt;/sup&gt; adsorption was determined to be 586.56 mg/g, and the thermodynamic results indicated that the adsorption of Pb&lt;sup&gt;2+&lt;/sup&gt; was an unprompted exothermal reaction. However, the adsorption mechanism of the composite spheres is not yet clear. Therefore, the adsorption mechanism of Pb&lt;sup&gt;2+&lt;/sup&gt; on CMC-FC-SA was revealed to be dominated by ion-exchange reactions and ligand interactions, supplemented by physical adsorption by characterization such as FTIR and XPS. Notably, the CMC-FC-SA spheres displayed good removal efficiency (&gt;88 %, under the Pb&lt;sup&gt;2+&lt;/sup&gt; residue limit of GB.) for Pb&lt;sup&gt;2+&lt;/sup&gt; in the five seaweed concentrates and could maintain the quality of seaweed concentrates. The effect of coexisting organic matter fractions in seaweed concentrates on adsorption has not been evaluated. Therefore, interference tests revealed that SA, phlorotannins and fucoxanthin antagonized Pb&lt;sup&gt;2+&lt;/sup&gt; adsorption through hydrogel diffusion blocking, hydrophobic cluster competition for coordination and micelle adsorption, respectively. While mannitol, glutamate and aspartate enhanced the removal rate by solubilization via -OH/-COOH complexation, synergistic mass transfer via bidentate chelation and hydrophilic optimization. The green strategy proposed in this study provides an efficient adsorbent for treating water and regulating heavy metal content in seaweed products.&lt;/div&gt;&lt;/div","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"170 ","pages":"Article 111700"},"PeriodicalIF":11.0,"publicationDate":"2025-06-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144500916","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}

{"title":"Synergistic enhancement of gelation and protein interactions in low-salt shrimp gels by static magnetic field and microcrystalline cellulose","authors":"Chunyu Li ,&nbsp;Siyang Liu ,&nbsp;Yingying Yang ,&nbsp;Chunhong Yuan ,&nbsp;Tong Zhang ,&nbsp;Changrong Ou ,&nbsp;Wenge Yang ,&nbsp;Huamao Wei","doi":"10.1016/j.foodhyd.2025.111696","DOIUrl":"10.1016/j.foodhyd.2025.111696","url":null,"abstract":"<div><div>With the purpose of developing low-salt shrimp gel products, the present study explored the influence of the low-temperature static magnetic field (LT-SMF) pre-gelation process combined with the additions of microcrystalline cellulose (MCC) on the gel quality enhancement and its mechanism. LT-SMF process was used to treat the shrimp gels, and different proportions of MCC were added to evaluate the gels via textural properties, drip loss and water distribution, protein properties, and microstructure with molecular docking method. The results suggested that an MCC addition of 0.6 % significantly enhanced the hardness, chewiness, and springiness of the shrimp gels, reduced drip loss, and improved water holding capacity. SDS-PAGE analyses and FTIR analysis indicated that the combined LT-SMF and MCC treatment synergistically promoted the formation of β-sheet structures in proteins and facilitated the cross-linking of the myosin heavy chain (MHC), thereby leading the stability of the gel network enhanced. The microstructural results indicated that the collaborative-treated gel network became more uniform and denser. Molecular docking simulations further revealed the stable binding mechanism between biosaccharides in MCC and MHC in shrimp. This study provides a new insight into the development of low-salt shrimp gel products and offers significant theoretical and practical value.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"170 ","pages":"Article 111696"},"PeriodicalIF":11.0,"publicationDate":"2025-06-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144490926","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}