Food Structure-Netherlands最新文献_第6页

Variation in HMW-GSs at Glu-D1 locus causes differences in protein behaviors and starch structures during noodle cooking and retrogradation Glu-D1基因座HMW-GSs的变异导致面条在煮熟和退化过程中蛋白质行为和淀粉结构的差异

IF 5.9 3区农林科学

Food Structure-Netherlands Pub Date : 2026-01-01 Epub Date: 2025-12-24 DOI: 10.1016/j.foostr.2025.100499

Pai Peng, Xiaolong Wang, Xinyu Zhang, Xinrui Ren, Xinzhong Hu

{"title":"Variation in HMW-GSs at Glu-D1 locus causes differences in protein behaviors and starch structures during noodle cooking and retrogradation","authors":"Pai Peng, Xiaolong Wang, Xinyu Zhang, Xinrui Ren, Xinzhong Hu","doi":"10.1016/j.foostr.2025.100499","DOIUrl":"10.1016/j.foostr.2025.100499","url":null,"abstract":"<div><div>To study the effect of gluten strength on starch structure and digestibility during noodle processing, two gluten samples containing HMW-GSs N/17 + 18/5 + 10 and N/17 + 18/2 + 12, respectively, were separated from wheat near-isogenic lines and combined with identical wheat starch to prepare two recombinant noodles. The structural changes in protein, starch, and their interactions during noodle cooking and retrogradation were investigated. The results indicated that the noodles with 5 + 10 subunits exhibited better cooking and textural characteristics compared to 2 + 12. Cooking and retrogradation led to protein aggregation, with the 5 + 10 noodles displaying higher levels of SDS-unextractable polymeric proteins characterized by increased disulfide bonds, hydrophobic interactions, and β-sheets. Meanwhile, the double helices within starch were disrupted, producing more single helices rich in inclusion complexes. The dense and extensive gluten matrix in 5 + 10 noodles inhibited the destruction of starch granules during cooking, and promoted starch recrystallization and the formation of starch-protein complexes, which contributed to a higher RS content (29.13 %). In contrast, the 2 + 12 noodle exhibited greater release of short-chain starches and monomeric proteins during cooking, leading to a disordered structure that impeded starch recrystallization and improved starch digestibility. The findings support improving noodle quality and starch digestion resistance through the incorporation of suitable HMW-GSs.</div></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"47 ","pages":"Article 100499"},"PeriodicalIF":5.9,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145841632","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"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

Microrheological mechanisms of casein-whey protein ratio regulating protein-dominated gel networks and quality correlation in yogurt 酪蛋白-乳清蛋白比例调节蛋白主导凝胶网络和酸奶质量相关性的微流变机制

IF 5.9 3区农林科学

Food Structure-Netherlands Pub Date : 2026-01-01 Epub Date: 2025-12-22 DOI: 10.1016/j.foostr.2025.100498

Hairan Ma , Xiuying Wu , Jiajie Hu , Huifang Cai , Hui Li , Hongliang Li , Xiaoxia Bai

{"title":"Microrheological mechanisms of casein-whey protein ratio regulating protein-dominated gel networks and quality correlation in yogurt","authors":"Hairan Ma , Xiuying Wu , Jiajie Hu , Huifang Cai , Hui Li , Hongliang Li , Xiaoxia Bai","doi":"10.1016/j.foostr.2025.100498","DOIUrl":"10.1016/j.foostr.2025.100498","url":null,"abstract":"<div><div>This study systematically investigated the effects of varying casein-to-whey protein (CN:WP) ratios on the microrheological properties of protein gels and the quality characteristics of yogurt. Eight sets of protein gel and yogurt samples were prepared, with CN:WP ratios adjusted to 10:0, 9:1, 8:2, 7:2, 8:3, 5:2, 4:2, and 3:2, respectively. For protein gels, key parameters measured included microrheological properties (mean squared displacement, MSD; Elasticity Index, EI; Solid-Liquid Balance, SLB; Macroscopic Viscosity Index, MVI) and gel strength; for yogurt, analyses encompassed particle size distribution, water-holding capacity (WHC), textural properties, and sensory attributes. Results revealed that casein is pivotal for the formation and structural integrity of protein gel networks. When the CN:WP ratio was < 8:2, the elasticity, viscosity, and strength of protein gels increased with increasing CN:WP ratio—this was attributed to the enhanced formation of a continuous casein-dominated network. For yogurt, samples with a CN:WP ratio > 8:2 exhibited superior WHC and consistency. Within the CN:WP range of 8:2–8:3, a higher casein proportion promoted the formation of a more robust gel structure. Consequently, the corresponding yogurt showed smaller and more uniform particle size (22.59–31.11 μm), further improved WHC (73.99 %–77.04 %), and enhanced textural properties. Specifically, controlling the CN:WP ratio within 8:2–8:3 yielded yogurt with a smooth mouthfeel (sensory score +1.2) and uniform texture, which are desirable quality attributes for commercial products.</div></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"47 ","pages":"Article 100498"},"PeriodicalIF":5.9,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145841633","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"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

Precooking and rehydration strategies of common bean seeds (Phaseolus vulgaris L.) determine their regeneration properties 菜豆种子的预熟和复水化策略决定了其再生特性

IF 5.9 3区农林科学

Food Structure-Netherlands Pub Date : 2026-01-01 Epub Date: 2026-03-07 DOI: 10.1016/j.foostr.2026.100510

Nguyen T.H. An , Annu Mathew , Henry Tafiire , Ann Van Loey , Marc E. Hendrickx

{"title":"Precooking and rehydration strategies of common bean seeds (Phaseolus vulgaris L.) determine their regeneration properties","authors":"Nguyen T.H. An , Annu Mathew , Henry Tafiire , Ann Van Loey , Marc E. Hendrickx","doi":"10.1016/j.foostr.2026.100510","DOIUrl":"10.1016/j.foostr.2026.100510","url":null,"abstract":"<div><div>Precooking beans prior to drying enables the production of shelf-stable products, prevents the hard-to-cook defect associated with storage of raw beans, and enhances consumer convenience through reduced preparation time. This study aimed at mechanistic insights into how precooking and rehydration strategies influence the regeneration behavior of precooked dehydrated beans. Beans were precooked under different conditions: conventional cooking (30, 45, and 120 min), and limited-water cooking (120 min), to generate varying (micro)structures. Bean microstructure and hardness after each processing step were evaluated and linked to rehydration performance under direct (23 °C, 90 °C) and two-step (23 °C followed by 90 °C) approaches. Extensively precooked beans showed lower hardness, pronounced cell separation, and cell wall thinning. After dehydration (40 °C), these structural changes resulted in a more porous structure with weakened cell wall integrity, which significantly enhanced rehydration capacity and rates (<span><math><msub><mrow><mi>D</mi></mrow><mrow><mi>eff</mi></mrow></msub></math></span> 2–6 times higher at 90 °C). Two-step rehydration (23 °C/7 h, then 90 °C/10 min) was recommended to avoid grainy texture and white cores, indicative of insufficient hydration. Modeling of rehydration kinetics indicated that at 23 °C, both surface-controlled mass transfer and diffusion governed water uptake, while at 90 °C, diffusion (without surface resistance) was the dominant mechanism. Bean texture after rehydration did not change/soften beyond that established during precooking, despite greater pectin solubilization (an increase in hot-water-extractable pectin), suggesting that pectin solubilization may not contribute to the softening of precooked dehydrated beans. Therefore, beans must be precooked to a palatable level for consumption before dehydration, suggesting a processing criterion to attain desirable texture after rehydration.</div></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"47 ","pages":"Article 100510"},"PeriodicalIF":5.9,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147384846","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"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

High-pressure homogenization improves functional properties of pea protein isolates 高压均质提高了豌豆分离蛋白的功能特性

IF 5.9 3区农林科学

Food Structure-Netherlands Pub Date : 2026-01-01 Epub Date: 2026-02-27 DOI: 10.1016/j.foostr.2026.100507

Laura Scheuer , Veronika Mair , Katrin Hasenkopf , Stephanie Bader-Mittermaier , Ute Schweiggert-Weisz , Susanne Gola

{"title":"High-pressure homogenization improves functional properties of pea protein isolates","authors":"Laura Scheuer , Veronika Mair , Katrin Hasenkopf , Stephanie Bader-Mittermaier , Ute Schweiggert-Weisz , Susanne Gola","doi":"10.1016/j.foostr.2026.100507","DOIUrl":"10.1016/j.foostr.2026.100507","url":null,"abstract":"<div><div>The growing demand for sustainable plant-based proteins has led to intensified efforts to enhance their functional performance in food systems. This study systematically investigated the effects of high-pressure homogenization (HPH) on the functional properties (techno-functional and physico-chemical characteristics, <em>in vitro</em> digestibility) of two distinct commercial pea protein isolates (PPI). Protein dispersions were subjected to HPH at pressures of 60 MPa and 120 MPa, using either one or three passes. HPH significantly reduced particle size by disaggregating large protein aggregates, leading to smaller and more soluble particles. At pH 7, protein solubility rose by up to 142% (PPI 1) and 158% (PPI 2), with pronounced improvements in emulsifying properties and foaming activity. Consistent with this, water binding capacity declined markedly. Although higher pressure enhanced techno-functional properties, the number of passes exerted an even stronger influence than pressure alone. Mild HPH-treatment improved gelation in one of the two pea protein isolates. <em>In vitro</em> digestibility, however, remained unaffected. The untreated PPI differed in their techno-functional properties and responded differently to HPH. This suggests that the initial characteristics, which are likely shaped by the intensity of the processing during protein isolation, play a decisive role in HPH responsiveness. Principal component analysis confirmed these raw material-specific differences and showed that HPH-treatment significantly altered the functional profile compared to the untreated samples. Overall, integrating HPH during protein production or as an in-line step in manufacturing offers a scalable, cost-effective route to tailor functionality in liquid applications such as dairy alternatives and beverages.</div></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"47 ","pages":"Article 100507"},"PeriodicalIF":5.9,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147384847","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"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

Elucidating protein–lipid microstructure and interactions in hybrid processed cheeses using synchrotron macro ATR-FTIR microspectroscopy 利用同步加速器宏ATR-FTIR显微光谱分析混合加工奶酪中的蛋白质-脂质微观结构和相互作用

IF 5.9 3区农林科学

Food Structure-Netherlands Pub Date : 2026-01-01 Epub Date: 2026-03-07 DOI: 10.1016/j.foostr.2026.100511

Di Lu , Jitraporn Vongsvivut , Annaleise R. Klein , Cushla McGoverin , Mark Waterland , Yi Zheng , Alejandra Acevedo–Fani , Debashree Roy , Harjinder Singh , Aiqian Ye

{"title":"Elucidating protein–lipid microstructure and interactions in hybrid processed cheeses using synchrotron macro ATR-FTIR microspectroscopy","authors":"Di Lu , Jitraporn Vongsvivut , Annaleise R. Klein , Cushla McGoverin , Mark Waterland , Yi Zheng , Alejandra Acevedo–Fani , Debashree Roy , Harjinder Singh , Aiqian Ye","doi":"10.1016/j.foostr.2026.100511","DOIUrl":"10.1016/j.foostr.2026.100511","url":null,"abstract":"<div><div>Herein, synchrotron-based Fourier-transform infrared (S-FTIR) microspectroscopy was used to investigate the spatial distribution and molecular interactions within hybrid processed cheeses (HPCs) that contain casein and plant proteins. Unsupervised hierarchical cluster analysis (HCA) and k-means clustering provided consistent spatial differentiation, effectively separating the regions that were dominated by plant protein from those dominated by casein. Spectral analysis revealed protein–protein and protein–lipid interactions based on the type of plant protein used across plant-based cheeses and hybrid formulations. Cheese samples that contained only hemp protein isolate (HPI) were dominated by β-sheets (50%) and β-turns (21%), while mung bean protein isolate (MPI)-based cheeses exhibited considerable α-helix (35%) and β-sheet (48%) contents. In HPI–casein hybrid cheeses, hydrogen bonds predominated, with the amide II mode of proteins as the key discriminating component. By contrast, the amide I secondary protein structure was the primary marker that distinguished MPI from casein in MPI–casein cheeses. Increasing the casein content reduced plant protein aggregation and created a more heterogeneous environment, thereby supporting a flexible and disordered protein network. Furthermore, the S-FTIR map of lipids indicated that coconut oil was preferentially associated with casein rather than with plant proteins. Overall, these results highlight the role of S-FTIR microspectroscopy in resolving compositional and molecular-level interactions in hybrid cheese matrices.</div></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"47 ","pages":"Article 100511"},"PeriodicalIF":5.9,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147384845","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"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

Understanding the Impact of high-voltage cold plasma on physicochemical, rheological and structural properties of soybean protein 高压冷等离子体对大豆蛋白理化、流变学和结构特性的影响

IF 5.9 3区农林科学

Food Structure-Netherlands Pub Date : 2026-01-01 Epub Date: 2026-02-02 DOI: 10.1016/j.foostr.2026.100505

Behdad Shokrollahi Yancheshmeh , Mehdi Varidi , Seyed Mohammad Ali Razavi , Farshad Sohbatzadeh , Mohammad Amin Mohammadifar

{"title":"Understanding the Impact of high-voltage cold plasma on physicochemical, rheological and structural properties of soybean protein","authors":"Behdad Shokrollahi Yancheshmeh , Mehdi Varidi , Seyed Mohammad Ali Razavi , Farshad Sohbatzadeh , Mohammad Amin Mohammadifar","doi":"10.1016/j.foostr.2026.100505","DOIUrl":"10.1016/j.foostr.2026.100505","url":null,"abstract":"<div><div>This study was implemented to modify the physicochemical, rheological and microstructural properties of soy protein isolate (SPI) using dielectric barrier discharge (DBD) plasma. For this purpose, SPI powder was treated with DBD plasma for 3 and 6 min at 20 and 26 kV. Then, color, pH, FTIR, amino acid composition, droplet size, polydispersity index (PDI), zeta potential, surface hydrophobicity, sulfhydryl groups, solubility, water holding capacity (WHC), secondary structure of the protein, protein structures, physical stability, as well as rheological properties were evaluated. Results indicated that sulfhydryl group, surface hydrophobicity, solubility, and WHC of SPI were enhanced by the plasma treatment in comparison with the control, and the highest values were obtained after plasma treatment at 26 kV for 6 min. The results of FTIR and circular dichroism (CD) analysis also showed that the 26 kV-3 min plasma exposure caused partial denaturation and unfolding of the α-helix structure of SPI. Intrinsic fluorescence and SDS-PAGE analyses revealed treatment-dependent alterations in protein conformation and subunit patterns, indicating structural modifications of SPI under different plasma conditions. microscopic images also confirmed these results. Rheological results indicated that plasma treatment improved the rheological properties of SPI by increasing significantly (p < 0.05) zero shear viscosity (η0) from 0.906 to 1.420 Pa.s and decreasing flow behavior index (m) from 0.950 to 0.803. The present study indicated successful modification of the physicochemical and rheological properties of SPI treated with DBD plasma.</div></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"47 ","pages":"Article 100505"},"PeriodicalIF":5.9,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146173453","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"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

In situ ultrastructural analyses of proteins and starch in rice, barley, and quinoa during cooking 大米、大麦和藜麦烹饪过程中蛋白质和淀粉的原位超微结构分析

IF 5.9 3区农林科学

Food Structure-Netherlands Pub Date : 2026-01-01 Epub Date: 2026-02-21 DOI: 10.1016/j.foostr.2026.100506

Ling Zhu , Xiaoyu Chen , Jiali Hu , Guohua Zhang , Hui Zhang

{"title":"In situ ultrastructural analyses of proteins and starch in rice, barley, and quinoa during cooking","authors":"Ling Zhu , Xiaoyu Chen , Jiali Hu , Guohua Zhang , Hui Zhang","doi":"10.1016/j.foostr.2026.100506","DOIUrl":"10.1016/j.foostr.2026.100506","url":null,"abstract":"<div><div>The textural contribution of protein morphology and protein-starch interactions in cooked grains remains limited to correlational analysis and is subject to debate. In this study, <em>in situ</em> ultrastructural analyses of proteins and starch in rice, barley, and quinoa during cooking were conducted using multiple microscopy techniques, including electron microscopy and X-ray tomography. Microscopic analyses revealed that cereal proteins were organized as discrete protein bodies along cell walls of rice and quinoa, whereas barley proteins formed continuous amorphous matrices within the endosperm. While rice protein bodies and the barley protein matrix remained unchanged after cooking, quinoa proteins were transformed from discrete bodies into a continuous matrix. X-ray tomography demonstrated that rice protein bodies contribute to spatial hindrance, barley proteins serve as physical barriers that impede starch gelatinization and leaching, and quinoa proteins shift from hindrance to barrier during cooking. These findings elucidate the ultrastructure of proteins in different cereals, along with protein-starch interactions, and clarify the structural roles of these components, thereby providing insights for developing cereal-based products with desired properties.</div></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"47 ","pages":"Article 100506"},"PeriodicalIF":5.9,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147384730","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"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

Effects of transglutaminase on structural properties and in vitro digestibility of plant protein blend high-moisture extrudates 谷氨酰胺转胺酶对高水分植物蛋白混合挤出物结构特性和体外消化率的影响

IF 5.9 3区农林科学

Food Structure-Netherlands Pub Date : 2026-01-01 Epub Date: 2026-02-01 DOI: 10.1016/j.foostr.2026.100504

Yichao Chen , Tiange Li , Qiuyan Zhao , Hongxiao Li , Tianlin Wang , Xianqing Huang , Jiansheng Zhao

{"title":"Effects of transglutaminase on structural properties and in vitro digestibility of plant protein blend high-moisture extrudates","authors":"Yichao Chen , Tiange Li , Qiuyan Zhao , Hongxiao Li , Tianlin Wang , Xianqing Huang , Jiansheng Zhao","doi":"10.1016/j.foostr.2026.100504","DOIUrl":"10.1016/j.foostr.2026.100504","url":null,"abstract":"<div><div>The combination of multiple plant proteins for high-moisture extrusion (HME) is a feasible solution used to improve the nutritional characteristics of plant-based meat alternatives, attracting considerable research interest. However, the structure and nutritional characteristics of plant-based meat alternatives obtained by modifying mixed plant proteins with transglutaminase (TG) are still unknown. In this study, pea protein isolate and wheat protein blend (PPI/WP) was covalently modified using different levels of TG (0 %, 0.5 %, 1 %, and 2 %), and the effects of TG on the structural and digestive properties of high-moisture extrudates were systematically investigated. The findings revealed that PPI/WP extrudates modified with 1 % TG exhibited a more compact fibrous structure and meat-like texture. Fourier transform infrared spectroscopy (FTIR) analysis showed that 1 % TG crosslinking increased the content of β-sheet in the secondary structure of PPI/WP protein from 37 % to 40 %, which contributes to the stability of the protein structure. <em>In vitro</em> digestion studies have shown that 1 % TG increases the total amount of free amino acids during gastrointestinal digestion from 4.075 mg/mL to 4.678 mg/mL (<em>P</em> ≤ 0.05), and significantly enhances hypoglycemic and antioxidant capacities (<em>P</em> ≤ 0.05). These findings provide a solid evidence base for TG to optimize the fiber structure and nutritional reinforcement of extruded materials.</div></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"47 ","pages":"Article 100504"},"PeriodicalIF":5.9,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146173454","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"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

Hybrid yoghurt-like gels from Nannochloropsis oceanica and bovine proteins structured with glucono-δ-lactone: Rheological, physicochemical, and microstructural insights 由海洋纳米绿藻和用葡萄糖-δ-内酯结构的牛蛋白制成的混合酸奶样凝胶：流变学、物理化学和微观结构的见解

IF 5.9 3区农林科学

Food Structure-Netherlands Pub Date : 2026-01-01 Epub Date: 2026-01-19 DOI: 10.1016/j.foostr.2026.100502

Jayani Samarathunga , Thi Phuong Linh Le , Katrina Strazdins , Jeroen Rens , Benu Adhikari

{"title":"Hybrid yoghurt-like gels from Nannochloropsis oceanica and bovine proteins structured with glucono-δ-lactone: Rheological, physicochemical, and microstructural insights","authors":"Jayani Samarathunga , Thi Phuong Linh Le , Katrina Strazdins , Jeroen Rens , Benu Adhikari","doi":"10.1016/j.foostr.2026.100502","DOIUrl":"10.1016/j.foostr.2026.100502","url":null,"abstract":"<div><div>This study developed and characterized set-type hybrid yoghurt-like gels by combining <em>Nannochloropsis oceanica</em> protein (NP) with milk protein concentrate (MPC). The proportion of NP in the NP–MPC hybrid yoghurt-like gel formulations was 25 %, 50 %, 75 %, or 100 % of the total protein content (4.2 % w/w), with 100 % MPC gel serving as the benchmark. The yoghurt-like gel-forming premix was acidified with 2 % (w/w) glucono-δ-lactone (GDL) to induce gelation while avoiding fermentation-related complications. Variations in the buffering capacity of NP–MPC blends modulated the rate of GDL-induced acidification, affecting gelation time and gel strength, as reflected by changes in storage and loss moduli. The lower buffering capacity of NP led to a faster pH drop and reduced gel strength, with lower moduli values observed in NP-rich formulations compared to the more robust networks formed in MPC-rich systems. Increasing the NP proportion decreased viscosity and hardness while increasing syneresis. Gelation during acidification significantly reduced the browning index and increased the whiteness index. Formulations containing 50–100 % NP displayed an olive-green color. Among the formulations, the 25 % NP (75 % MPC) sample exhibited gelation, microstructure, textural, rheological, and syneresis characteristics closest to those of 100 % MPC, indicating it as an optimal formulation. The NP-rich formulation also exhibited a consistency resembling pourable yoghurt. Overall, this study provides new insights into the development of yoghurt-like gels from dairy–algal protein hybrids, with potential to balance nutritional quality and sustainability.</div></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"47 ","pages":"Article 100502"},"PeriodicalIF":5.9,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146023604","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"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

Structure–function relationships in industrial bread enriched with insoluble dietary fiber 富含不溶性膳食纤维的工业面包的结构-功能关系

IF 5.9 3区农林科学

Food Structure-Netherlands Pub Date : 2026-01-01 Epub Date: 2026-03-02 DOI: 10.1016/j.foostr.2026.100508

E. Bruno , P. Cuda , F.R. Lupi , A. D’Agostino , N. Baldino , D. Gabriele

{"title":"Structure–function relationships in industrial bread enriched with insoluble dietary fiber","authors":"E. Bruno , P. Cuda , F.R. Lupi , A. D’Agostino , N. Baldino , D. Gabriele","doi":"10.1016/j.foostr.2026.100508","DOIUrl":"10.1016/j.foostr.2026.100508","url":null,"abstract":"<div><div>The growing demand for functional foods has led to the exploration of alternative fiber sources for bread enrichment. This study examined how highly–insoluble citrus fiber (Vitacel CF 312®), known for its nutritional benefits to consumers, such as reducing the intestinal absorption of fatty acids and glucose, modifies the structure–function relationships of industrial bread doughs focusing on their rheological and microstructural behavior. Dough formulations were prepared varying fiber content (1–6% w/w) and hydration level (50–84% w/w), and their viscoelastic behavior was assessed under shear and uniaxial extension. Epifluorescence microscopy revealed a progressive disruption of gluten network continuity in the case of recipes with similar hydration and reduced starch granule swelling due to competitive water uptake by fiber. These structural changes were directly linked to increased dough consistency and toughness, while enhanced hydration mitigated these effects through partial recovery of gluten–starch interactions. Among all formulations, doughs containing 4.5% fiber at elevated hydration exhibited microstructural and rheological properties closest to the commercial benchmark. Even if lower fiber fractions can perform similarly under optimized hydration conditions, the sample with 4.5% fiber was considered as the best choice, among the tested samples, because it yields the highest fiber apport, offering a superior nutritional profile, with minimal compromise to technological performance.</div></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"47 ","pages":"Article 100508"},"PeriodicalIF":5.9,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147384729","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"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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