Food Hydrocolloids最新文献_第10页

α-Amylase mediated production of modified potato starch with distinct gel properties α-淀粉酶介导的具有不同凝胶性质的马铃薯变性淀粉的制备

IF 11 1区农林科学

Food Hydrocolloids Pub Date : 2025-06-24 DOI: 10.1016/j.foodhyd.2025.111697

Signe Schram Zinck , Stefan Jarl Christensen , Dora Jahola , Christinne Hedberg Hyldgaard , Ole Bandsholm Sørensen , Mohammad Amin Mohammadifar , Anne S. Meyer

{"title":"α-Amylase mediated production of modified potato starch with distinct gel properties","authors":"Signe Schram Zinck , Stefan Jarl Christensen , Dora Jahola , Christinne Hedberg Hyldgaard , Ole Bandsholm Sørensen , Mohammad Amin Mohammadifar , Anne S. Meyer","doi":"10.1016/j.foodhyd.2025.111697","DOIUrl":"10.1016/j.foodhyd.2025.111697","url":null,"abstract":"<div><div>This study examines how seven microbial α-amylases selected from different glycoside hydrolase 13 (GH13) subfamilies (GH13_1, GH13_5, GH13_37, and GH13_42) affect the molecular and physical properties of potato starch with respect to gelation and gel properties. The results revealed distinct degradation profiles, reflecting different preferences for amylose and amylopectin. Rheological analysis of the starch gels revealed that, notably, starch treated with <em>Um</em>-αAmy, a GH13_37 α-amylase from an uncultured marine bacterium, had superior gel properties, while starch treated with catalytically efficient <em>Bacillus-</em>derived α-amylases of GH13_5 exhibited particularly poor gelling abilities. The results suggest that the strong gel properties of <em>Um</em>-αAmy treated starch are likely associated with a preferential, yet controlled, amylose degradation combined with a limited activity on amylopectin. Assessment of the enzyme structure models indicated a possible correlation between active site conformation and starch degradation profiles, with open conformations potentially enabling enhanced amylopectin degrading ability, and thus, poor gelling ability of the resulting starch. Furthermore, the limited thermal stability of <em>Um</em>-αAmy turned out to be a desirable trait, facilitating a more controlled enzymatic starch modification process. Altogether, these findings provide a novel insights into the significance of α-amylase phylogeny and classification in controlled enzymatic starch modification and highlight the potential of selected α-amylases for enzymatic production of modified potato starch with distinct gel properties.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"170 ","pages":"Article 111697"},"PeriodicalIF":11.0,"publicationDate":"2025-06-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144514382","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}

引用次数: 0

Ovalbumin-Rutin complexes as hypoallergenic foaming agents: A dual-effect strategy for protein modification 卵清蛋白-芦丁复合物作为低过敏性发泡剂：蛋白质修饰的双效策略

IF 11 1区农林科学

Food Hydrocolloids Pub Date : 2025-06-24 DOI: 10.1016/j.foodhyd.2025.111692

Zuyue Li , Ran Yang , Mahmoud Abou-Elsoud , Peng Hu , Yijie Li , Long Sheng , Dong Uk Ahn , Xi Huang

{"title":"Ovalbumin-Rutin complexes as hypoallergenic foaming agents: A dual-effect strategy for protein modification","authors":"Zuyue Li , Ran Yang , Mahmoud Abou-Elsoud , Peng Hu , Yijie Li , Long Sheng , Dong Uk Ahn , Xi Huang","doi":"10.1016/j.foodhyd.2025.111692","DOIUrl":"10.1016/j.foodhyd.2025.111692","url":null,"abstract":"<div><div>This study aimed to overcome two inherent limitations of ovalbumin (OVA), specifically its high allergenicity and limited foaming properties, through the formulation of OVA-rutin complexes. Various modification levels of OVA-Rutin complexes were successfully produced, as confirmed by polyphenol binding equivalents and amino acid residues changes. Multispectral analyses collectively demonstrated that rutin promoted structural loosening in OVA and improved its molecular flexibility. At an OVA-Rutin ratio of 1:0.4, the IgE binding capacity diminished by 35.70 %. Meanwhile, the system exhibited superior Fe<sup>2+</sup> chelation ability (50.88 ± 0.31 %), DPPH radical scavenging capability (67.18 ± 2.25 %) and ABTS radical scavenging ability (87.23 ± 0.50 %). The combination of rutin and OVA significantly increased foaming ability by 75.56–155.24 % and foaming stability by up to 1.32-fold. This improved foam performance was attributed to the desirable air-water interfacial activity and rearrangement capacity of the OVA-Rutin complexes. These findings provide an effective strategy for simultaneously enhancing foaming properties of OVA and mitigating its allergenicity.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"170 ","pages":"Article 111692"},"PeriodicalIF":11.0,"publicationDate":"2025-06-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144522277","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}

引用次数: 0

Tribological properties and interfacial adsorption behavior of milk protein-based formulations: Roles of whey protein type and thermal processing 乳蛋白基配方的摩擦学性能和界面吸附行为：乳清蛋白类型和热处理的作用

IF 11 1区农林科学

Food Hydrocolloids Pub Date : 2025-06-23 DOI: 10.1016/j.foodhyd.2025.111695

Junwei Lian , Kun Yang , Jianshe Chen , Yang Zhu

{"title":"Tribological properties and interfacial adsorption behavior of milk protein-based formulations: Roles of whey protein type and thermal processing","authors":"Junwei Lian , Kun Yang , Jianshe Chen , Yang Zhu","doi":"10.1016/j.foodhyd.2025.111695","DOIUrl":"10.1016/j.foodhyd.2025.111695","url":null,"abstract":"<div><div>Whey protein-associated mouthdrying during oral processing is a driving factor for consumers' dislike of high-protein beverages, however, remains mechanistically underexplored in dairy systems. This study investigated the fundamental mechanisms driving powderiness in whey protein-enriched dairy beverages (8 % w/w protein). We conducted a comparative analysis of whey protein concentrate (WPC) versus whey protein isolate (WPI) at various casein-whey ratios (80:20 to 20:80) and evaluated thermal processing effects (63 °C/85 °C for 30 min) from rheological characterization, particle size distribution, tribological properties, and interfacial adsorption kinetics. Results demonstrated that protein composition significantly altered frictional behavior, with WPC-dominated systems (casein-whey protein ratio of 20:80) exhibiting 33.6 % higher friction coefficients versus WPI counterparts at 10 mm/s without heating. Thermal treatment at 85 °C induced substantial aggregation in WPI-dominant systems (hydrodynamic diameter increased from 0.150 μm to 0.167 μm) and reduced adsorption capacity by 30.80 %, correlating with impaired lubrication. Conversely, WPC maintained structural homogeneity and enhanced interfacial coverage post-heating, preserving lubrication functionality. These findings establish composition-specific thermal processing guidelines for optimizing sensory attributes in high-protein dairy beverages.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"170 ","pages":"Article 111695"},"PeriodicalIF":11.0,"publicationDate":"2025-06-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144471936","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}

引用次数: 0

Protein network density and fibrous structure control of soy protein isolate-based high-moisture meat analogs using yeast or rice protein isolates with distinct glass transition temperatures 酵母或大米分离蛋白在不同玻璃化转变温度下对大豆分离蛋白高水分肉类类似物的蛋白质网络密度和纤维结构的控制

IF 11 1区农林科学

Food Hydrocolloids Pub Date : 2025-06-23 DOI: 10.1016/j.foodhyd.2025.111670

Hyun Woo Choi , Jungwoo Hahn , Young Jin Choi

{"title":"Protein network density and fibrous structure control of soy protein isolate-based high-moisture meat analogs using yeast or rice protein isolates with distinct glass transition temperatures","authors":"Hyun Woo Choi , Jungwoo Hahn , Young Jin Choi","doi":"10.1016/j.foodhyd.2025.111670","DOIUrl":"10.1016/j.foodhyd.2025.111670","url":null,"abstract":"<div><div>This study investigates the impact of yeast protein isolate (YPI) and rice protein isolate (RPI) on the structural and functional properties of soy protein isolate (SPI)-based high-moisture meat analogs (HMMA). By leveraging the distinct glass transition temperatures (T<sub>g</sub>) of YPI and RPI, this study examines their roles in modulating SPI network density and fibrous structure formation during high-moisture extrusion (HME). It was revealed that YPI and RPI altered the rheological and microstructural properties of SPI-based gels, leading to differences in hardness, cohesiveness, and texturization index. YPI, with its higher T<sub>g</sub>, maintained particulate form during processing, acting as a physical filler that improved structural anisotropy and enhanced fiber formation. RPI, although more susceptible to thermal denaturation, contributed to a flexible protein network, enhancing textural properties at moderate concentrations. Chemical interaction analysis revealed that while YPI and RPI reduced hydrogen and hydrophobic interactions, they increased disulfide bond formation at optimal levels, promoting a stronger fibrous structure. However, excessive incorporation led to protein aggregation and reduced network stability. Such findings suggest that the strategic incorporation of YPI and RPI enables precise tuning of the SPI-based HMMA texture, providing a novel approach to optimizing plant-based meat structures through targeted protein selection and extrusion processing. These findings not only advance the understanding of protein-protein interactions during extrusion but also provide practical strategies for improving the texture and fibrous structure of plant-based meat products, facilitating their commercial application.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"170 ","pages":"Article 111670"},"PeriodicalIF":11.0,"publicationDate":"2025-06-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144511119","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}

引用次数: 0

Influence of xanthan gum and guar gum on the gelation and structural properties of carboxylated cellulose nanofibers-based emulsion gels 黄原胶和瓜尔胶对羧化纤维素纳米纤维乳液凝胶的凝胶化和结构性能的影响

IF 11 1区农林科学

Food Hydrocolloids Pub Date : 2025-06-23 DOI: 10.1016/j.foodhyd.2025.111694

Yanyan Cheng, Jieqiong Lin, Yi Luo, Jinzhou Xiao, Weiqi Fei, Jiajun Song, Huiliang Wen, Jianhua Xie

{"title":"Influence of xanthan gum and guar gum on the gelation and structural properties of carboxylated cellulose nanofibers-based emulsion gels","authors":"Yanyan Cheng, Jieqiong Lin, Yi Luo, Jinzhou Xiao, Weiqi Fei, Jiajun Song, Huiliang Wen, Jianhua Xie","doi":"10.1016/j.foodhyd.2025.111694","DOIUrl":"10.1016/j.foodhyd.2025.111694","url":null,"abstract":"<div><div>This study investigated the use of carboxylated cellulose nanofibers (CCNF) as stabilizers, for fabricating emulsion gels and the effects of adding hydrophilic colloids (xanthan gum, XG and guar gum, GG) on the properties of the CCNF emulsion. XG and GG are anionic and neutral polysaccharides, respectively. As anionic cellulose derivatives, CCNF has a synergistic effect with XG through electrostatic attraction and hydrogen bonding, whereas interactions with GG are formed mainly through hydrogen bonding and physical entanglement. These two different molecular interaction mechanisms result in a composite emulsion gel system with a stable three-dimensional network structure. Results indicated that the addition of XG/GG significantly enhanced the storage modulus (G′) and loss modulus (G″), and improved the gel strength, hardness and fracture elongation. The emulsion gels exhibited markedly improved water-holding capacity (WHC) and freeze-thaw (F-T) stability, and the WHC after freezing and thawing increased to 78 %–97 % with the addition of XG and GG at various concentrations. These findings demonstrated the promising potential of CCNF-stabilized emulsion gels incorporating XG and GG and provide a basis for expanding the use of CCNF emulsion gels.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"170 ","pages":"Article 111694"},"PeriodicalIF":11.0,"publicationDate":"2025-06-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144481683","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}

引用次数: 0

Enzyme-crosslinked soy protein aerogels: Structural and functional modulations by pre-freezing process 酶交联大豆蛋白气凝胶：预冻过程的结构和功能调节

IF 11 1区农林科学

Food Hydrocolloids Pub Date : 2025-06-23 DOI: 10.1016/j.foodhyd.2025.111698

Tan Hu , Yuan Yuan , Jiyan Wang , Hao Hu

{"title":"Enzyme-crosslinked soy protein aerogels: Structural and functional modulations by pre-freezing process","authors":"Tan Hu , Yuan Yuan , Jiyan Wang , Hao Hu","doi":"10.1016/j.foodhyd.2025.111698","DOIUrl":"10.1016/j.foodhyd.2025.111698","url":null,"abstract":"<div><div>Biopolymer aerogels, particularly protein-based aerogels, have garnered significant attention due to their environmentally friendly nature, high porosity, and unique functional properties. However, the production of soy protein isolate (SPI) aerogels using SPI as the sole precursor material is still challenging, particularly in achieving the desired structural and functional properties. Herein, the effect of different pre-freezing temperature (−20 °C (A20), −80 °C (A80), and −196 °C (A196)) on structural and functional properties of single-component SPI aerogels is investigated. The single-component SPI aerogels are prepared by transglutaminase (TGase)-crosslinked SPI hydrogels as precursors and then pre-frozen at different temperatures. Among three aerogels, A80 aerogel exhibits the highest structural integrity, featuring an interconnected, dendritic pore structure, which results in the most extensive pore size distribution and the highest porosity of 92.67 ± 0.53 %. In contrast, A196 demonstrates the most compact microstructure and the most concentrated pore size distribution, with the lowest porosity of 90.43 ± 0.28 %. Importantly, the pre-freezing treatment significantly influences the structural properties of SPI aerogels. A196 aerogel shows less ordered structures, with a higher presence of β-turns and random coils, compared to the more ordered structures observed in A20 and A80 aerogels. Moreover, A196 aerogel exhibits the best oil adsorption capacity (OAC) and oil holding capacity (OHC), while A80 aerogel demonstrates the highest dye adsorption. These findings provide new insights into the fabrication of single-component TGase-crosslinked SPI aerogels.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"170 ","pages":"Article 111698"},"PeriodicalIF":11.0,"publicationDate":"2025-06-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144481682","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}

引用次数: 0

Tunable self-association of partially dephosphorylated beta-casein 部分去磷酸化β -酪蛋白的可调节自结合

IF 11 1区农林科学

Food Hydrocolloids Pub Date : 2025-06-23 DOI: 10.1016/j.foodhyd.2025.111668

Pernille Lund Rasmussen , Åsmund Rinnan , Søren Bang Nielsen , Anni Bygvrå Hougaard

{"title":"Tunable self-association of partially dephosphorylated beta-casein","authors":"Pernille Lund Rasmussen , Åsmund Rinnan , Søren Bang Nielsen , Anni Bygvrå Hougaard","doi":"10.1016/j.foodhyd.2025.111668","DOIUrl":"10.1016/j.foodhyd.2025.111668","url":null,"abstract":"<div><div>The utilization of bovine casein for creating casein micelles with properties resembling those in human milk presents an opportunity to bridge the nutritional gap between human milk and infant formula. However, the processing of these innovative structures and ingredients remains uncharted territory. While previous studies have examined temperature-induced self-association of dephosphorylated β-casein (β-CN) by varying single factors, the structuring events of industrially manufactured β-CN ingredients have not yet been fully described. In this study, a calcium depleted β-CN was prepared from micellar casein isolate by cold microfiltration. Partial dephosphorylation was carried out using alkaline phosphatase and quantified though intact protein analysis by LC-MS. In situ self-association was investigated during heating (15–75 °C, 1 °C increments) in a multichannel spectrophotometer, with absorbance and static light scattering (SLS) being monitored. An experimental design was employed to investigate the impact of calcium concentration (0–9 mM), β-CN concentration (2.5–10 mg/mL) and degree of dephosphorylation. The results demonstrate that altering the calcium concentration has a significant impact on tuning of the temperature-induced self-association of β-CN. Notably, at 0 mM calcium, irreversible self-association was not observed, and increasing calcium concentration led to a decrease in the temperature of initial self-association. Partial dephosphorylation also had a significant impact, resulting in an increased temperature at initial self-association. The calcium to β-CN ratio exerted a significant impact on the self-association temperature, while the β-CN concentration alone had no pronounced effect. Furthermore, it was demonstrated that calcium-phosphate bridges were not solely responsible for the self-association protein interactions of partially dephosphorylated β-CN.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"170 ","pages":"Article 111668"},"PeriodicalIF":11.0,"publicationDate":"2025-06-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144500914","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}

引用次数: 0

Study on the mechanism of riboflavin/UV induced soy protein nanofibrils hydrogel by photo crosslinking 核黄素/紫外线诱导大豆蛋白纳米原纤维水凝胶的光交联机理研究

IF 11 1区农林科学

Food Hydrocolloids Pub Date : 2025-06-21 DOI: 10.1016/j.foodhyd.2025.111671

Xu Zhang , Hekai Zhao , Yao Lu , Baokun Qi , Yang Li

{"title":"Study on the mechanism of riboflavin/UV induced soy protein nanofibrils hydrogel by photo crosslinking","authors":"Xu Zhang , Hekai Zhao , Yao Lu , Baokun Qi , Yang Li","doi":"10.1016/j.foodhyd.2025.111671","DOIUrl":"10.1016/j.foodhyd.2025.111671","url":null,"abstract":"<div><div>Fibrillar modification significantly enhanced the functional properties of soy protein nanofibrils (SPF). Through acid-heat induction, this study successfully converted soy protein isolate (SPI) into SPF and systematically investigated the gelation mechanism of riboflavin (RF)/UV-induced SPF photo-crosslinked hydrogels. The results demonstrated that RF actively participated in the crosslinking reaction, and fibrillar modification significantly improved the binding ability of SPI with RF. Isothermal titration calorimetry (ITC) revealed that fibrillar modification altered the thermodynamics of the SPI/RF binding, shifting the reaction from endothermic to exothermic, with the binding driving force transitioning from hydrophobic interactions to hydrogen bonding. After UV irradiation at a riboflavin concentration of 0.5 mM, both SPI and SPF samples exhibited optimal rheological properties. Notably, the SPF/RF system was able to stably form a gel, with its storage modulus increasing by 74-fold and 25-fold compared to the SPI/RF system and the native SPF sample, respectively. This enhancement indicates the formation of a more continuous three-dimensional network structure, wherein riboflavin functions as a photocatalyst. Circular dichroism analysis indicated that photo crosslinking did not significantly alter the protein's secondary structure. Additionally, Raman spectroscopy analysis showed a reduction in the characteristic peaks of phenylalanine (970−1055 cm<sup>−1</sup>) and tryptophan (756 cm<sup>−1</sup>) after photo crosslinking, suggesting that synergistic interactions with tyrosine contributed to the formation of the crosslinking network. This study provides a theoretical foundation for the design of light-responsive plant protein-based materials and broadens the application prospects of SPF.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"170 ","pages":"Article 111671"},"PeriodicalIF":11.0,"publicationDate":"2025-06-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144514384","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}

引用次数: 0

Physical properties and microstructure of hybrid processed cheeses formulated with plant protein and milk protein ingredients 植物蛋白和乳蛋白混合加工奶酪的物理特性和微观结构

IF 11 1区农林科学

Food Hydrocolloids Pub Date : 2025-06-21 DOI: 10.1016/j.foodhyd.2025.111688

Di Lu , Debashree Roy , Alejandra Acevedo-Fani , Harjinder Singh , Mark Waterland , Aiqian Ye

{"title":"Physical properties and microstructure of hybrid processed cheeses formulated with plant protein and milk protein ingredients","authors":"Di Lu , Debashree Roy , Alejandra Acevedo-Fani , Harjinder Singh , Mark Waterland , Aiqian Ye","doi":"10.1016/j.foodhyd.2025.111688","DOIUrl":"10.1016/j.foodhyd.2025.111688","url":null,"abstract":"<div><div>Hybrid processed cheese analogues (HPCAs) containing either mung bean (MPI) or hemp protein (HPI) with rennet casein (RC) at various ratios were prepared and analysed to understand their spatial and microstructural distribution and related physical properties, such as rheological properties, texture profile, meltability, and stretchability. In addition, protein composition and secondary protein structure were studied using SDS–PAGE and FTIR spectroscopy, while CLSM and TEM were employed to visualise the microstructure of the cheese matrix. Results indicated that plant protein types and concentration significantly affected the physical properties and microstructure of HPCAs. The addition of 30 % or more plant protein altered the physical and textural properties as well as the microstructure of the cheese analogues, with a decrease in β-sheet content and an increase in random coil structures. Mung bean protein–based HPCAs exhibit greater stretchability (e.g. 93.8 mm in 30 % MPI <em>vs</em> 41.53 mm in 30 % HPI), rheological, and textural properties, but not meltability (e.g. 1 % in 70 % MPI <em>vs</em> 48 % in 70 % HPI), compared with the hemp protein system at the same mixing ratios. This difference can be attributed to the size of the plant protein aggregation. All data were analysed by one-way ANOVA with Tukey's test (p < 0.05). These findings deepen our understanding of plant protein-based and hybrid cheeses, paving the way for optimised plant-based dairy alternatives.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"170 ","pages":"Article 111688"},"PeriodicalIF":11.0,"publicationDate":"2025-06-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144490925","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}

引用次数: 0

Development of whole highland barley ready-to-eat 3D printed dysphagia diet: Effect of heat treatment 全青稞即食3D打印吞咽困难饮食的开发：热处理效果

IF 11 1区农林科学

Food Hydrocolloids Pub Date : 2025-06-21 DOI: 10.1016/j.foodhyd.2025.111661

Delin Kou , Peiyao Zhao , Runkang Qiu , Yifei Li , Bei Fan , Litao Tong , Lili Wang , Liya Liu , Fengzhong Wang

{"title":"Development of whole highland barley ready-to-eat 3D printed dysphagia diet: Effect of heat treatment","authors":"Delin Kou , Peiyao Zhao , Runkang Qiu , Yifei Li , Bei Fan , Litao Tong , Lili Wang , Liya Liu , Fengzhong Wang","doi":"10.1016/j.foodhyd.2025.111661","DOIUrl":"10.1016/j.foodhyd.2025.111661","url":null,"abstract":"<div><div>Highland barley is rarely used as a main material to prepare 3D-printed food for people with dysphagia, mainly because its rich dietary fibers might lead to low printing accuracy and poor taste. This study investigated the impact of heat treatment temperature on the 3D printing properties of highland barley (HB) flour and its potential application in texture-modified foods for individuals with dysphagia. HB flours with varying degrees of gelatinization were used as 3D printing food inks. The effects of heat treatment temperatures on the printability and texture were analyzed. Rheological analysis showed that all printing inks exhibited solid-like behavior, and the ink heated at 200 °C (97.12 % ± 0.99 %) showed the best printing accuracy due to optimal adhesion, resistance to deformation, and extrudability. The ink at this heat treatment temperature also had the highest semi-solid water (<em>T</em><sub><em>22</em></sub>) and appropriate free water (<em>T</em><sub><em>23</em></sub>). Fourier transform infrared spectroscopy revealed that heat treatment altered the molecular structure of starch and proteins, affecting intermolecular forces, with hydrogen bonding being the primary force maintaining ink integrity. Hydrogen bonding and hydrophobic interactions were key factors in print performance, supported by correlation analysis. By adjusting the printing parameter-fill levels, the dough made of pre-heated HB flour could meet the Level-5 dysphagia food according to the framework of International Dysphagia Diet Standardization Initiative (IDDSI). This study gives a solution to overcome the problems caused by post-processing, and produces a new kind of instant highland barley food.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"170 ","pages":"Article 111661"},"PeriodicalIF":11.0,"publicationDate":"2025-06-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144365859","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}

引用次数: 0