Food Structure-Netherlands最新文献_第2页

Binding kinetics and structural analysis of chickpea protein interactions with spent coffee phenolics under varying pH and concentrations 不同 pH 值和浓度下鹰嘴豆蛋白质与咖啡酚的结合动力学和结构分析

IF 5.6 3区农林科学

Food Structure-Netherlands Pub Date : 2024-10-01 DOI: 10.1016/j.foostr.2024.100401

Beyza Saricaoglu , Hilal Yılmaz , Busra Gultekin Subasi , Mohammad Amin Mohammadifar , Esra Capanoglu

{"title":"Binding kinetics and structural analysis of chickpea protein interactions with spent coffee phenolics under varying pH and concentrations","authors":"Beyza Saricaoglu , Hilal Yılmaz , Busra Gultekin Subasi , Mohammad Amin Mohammadifar , Esra Capanoglu","doi":"10.1016/j.foostr.2024.100401","DOIUrl":"10.1016/j.foostr.2024.100401","url":null,"abstract":"<div><div>Several studies have been performed to improve structural, nutritional and functional properties of proteins through protein-phenolic interactions. In this study, changes in the structure of chickpea protein following interaction with spent coffee phenolics were analyzed. Varying phenolic concentrations (0, 0.5, 1.0, and 1.5) and pH values (7.0 and 9.0) were examined to investigate the effect of different interaction conditions. The results indicated that spent coffee phenolics induced the secondary and tertiary structure of chickpea protein, and this change was affected by the phenolic concentration. The interaction with phenolic compounds resulted in a blue shift in the FTIR spectra in Amide A at both pH values. Chickpea protein isolate (CPI) reacted with phenolic compounds via C-N and N-H bonds and hydrogen bonds were built up between protein-phenolic complexes. Thermodynamic parameter calculations indicated that hydrogen bonding and van der Waals forces were the primary types of interactions between CPI and phenolic extract at both pH conditions (7.0 and 9.0). Besides, irregularity of shapes was observed in morphological analysis after protein-phenolic interaction. In addition to proven structural changes, this study has laid the basis for future studies investigating the effect of phenolics on the functional and nutritional properties of chickpea proteins.</div></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"42 ","pages":"Article 100401"},"PeriodicalIF":5.6,"publicationDate":"2024-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142697932","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

Process-induced protein aggregates influenced pea globulins’ structure formation upon heating 工艺诱导的蛋白质聚集影响豌豆球蛋白加热后的结构形成

IF 5.6 3区农林科学

Food Structure-Netherlands Pub Date : 2024-10-01 DOI: 10.1016/j.foostr.2024.100398

Jarupat Luecha , Jens Saalbrink , José C. Bonilla , Nesli Sozer

{"title":"Process-induced protein aggregates influenced pea globulins’ structure formation upon heating","authors":"Jarupat Luecha , Jens Saalbrink , José C. Bonilla , Nesli Sozer","doi":"10.1016/j.foostr.2024.100398","DOIUrl":"10.1016/j.foostr.2024.100398","url":null,"abstract":"<div><div>Pea protein ingredients play key role in formulations of plant-based foods. However, functional properties of pea ingredients are inconsistent depending on extraction process. Protein aggregation occurs simultaneously during protein extraction, thus examining the protein aggregated states as induced by processing is essential for better process design. This study investigated the influence of process-induced protein aggregated states on structure formation upon heating of pea protein ingredients. Combining rheological, spectroscopic, and microscopic techniques, the mechanisms underlining heat-induced structure formation have been unveiled from microscopic to macroscopic scales. The salt-extracted isolate (PPI*) where protein aggregation was minimized, developed mesh-like structure through intermolecular protein-protein interaction upon gelling similar to commercial protein concentrate (PPC). In turn, commercial isolate (PPI) as appeared as microscopic particles, formed gel through accumulation of protein particles with no structure development. The aggregated states of PPI* and PPI seemed to dictate vicilin and legumin purification by means of anion exchange chromatography. Purification process promoted intermolecular protein aggregate structures. However, these purified fractions regardless of parent isolates showed similar structure development as PPC and PPI* during gelling. Monitoring protein aggregation during extraction process can be a key to limit functional property variation in pea protein ingredients.</div></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"42 ","pages":"Article 100398"},"PeriodicalIF":5.6,"publicationDate":"2024-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142555584","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Enhancing soy protein isolate flexibility through non-covalent ferulic acid modification: Implications for interfacial characteristics and protein-based emulsion performance 通过非共价阿魏酸改性提高大豆分离蛋白的柔韧性：对界面特性和蛋白质乳液性能的影响

IF 5.6 3区农林科学

Food Structure-Netherlands Pub Date : 2024-10-01 DOI: 10.1016/j.foostr.2024.100400

Yurou Chen, Mengyue Zhang, Yuhan Lan, Xibo Wang

{"title":"Enhancing soy protein isolate flexibility through non-covalent ferulic acid modification: Implications for interfacial characteristics and protein-based emulsion performance","authors":"Yurou Chen, Mengyue Zhang, Yuhan Lan, Xibo Wang","doi":"10.1016/j.foostr.2024.100400","DOIUrl":"10.1016/j.foostr.2024.100400","url":null,"abstract":"<div><div>This study aims to enhance the flexibility of soy protein isolate (SPI) to improve its functional properties, focusing on the investigated the effects of ferulic acid (FA) on the structure, interfacial behaviour and emulsification performance of SPI. Our study showed that FA induces SPI structures to depolymerization and unfolding primarily through hydrogen bonding and hydrophobic interactions, thereby increasing the flexible structures (random coils and β-turns) of protein. These changes enhanced the interfacial functional properties of SPI, with 150 μmol/g of FA-modified SPI exhibiting the best molecular flexibility, and its emulsification and emulsification stability were improved by 21.26 % and 39.86 %, respectively, compared to unmodified SPI. In addition, non-covalently modified FA significantly improved emulsions stability. Emulsions stabilized by SPI-FA<sub>150</sub> complexes exhibited better storage, heat, and freeze-thaw stability than SPI, with a significant reduction in oxidation products. This relationship between flexibility and function reveals the importance of structural modification in enhancing protein functionality. These discoveries shed new light on flexible protein processing technologies and the application of FA in protein functional modification.</div></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"42 ","pages":"Article 100400"},"PeriodicalIF":5.6,"publicationDate":"2024-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142663033","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

Changes in the rheological, textural, microstructural and in vitro antioxidant properties of biscuit dough by incorporation of the extract and fiber-rich residue obtained through green extraction of defatted date seeds 通过绿色提取脱脂枣籽获得的提取物和富含纤维的残渣对饼干面团的流变学、质地、微结构和体外抗氧化特性的影响

IF 5.6 3区农林科学

Food Structure-Netherlands Pub Date : 2024-10-01 DOI: 10.1016/j.foostr.2024.100395

Meththa Ranasinghe , Constantinos Stathopoulos , Balan Sundarakani , Sajid Maqsood

{"title":"Changes in the rheological, textural, microstructural and in vitro antioxidant properties of biscuit dough by incorporation of the extract and fiber-rich residue obtained through green extraction of defatted date seeds","authors":"Meththa Ranasinghe , Constantinos Stathopoulos , Balan Sundarakani , Sajid Maqsood","doi":"10.1016/j.foostr.2024.100395","DOIUrl":"10.1016/j.foostr.2024.100395","url":null,"abstract":"<div><div>The present study aimed at utilization of aqueous extract and fiber-rich extraction residue of defatted date seed powder (DDSP) as functional ingredient for improving the quality attributes of biscuit dough. Previously optimized microwave-assisted extraction (MAE) was used to recover the bioactive compounds from small, medium and large sized DDSP particles. Extracts and 2.5 %, 5 % and 7.5 % substitution levels of fiber-rich residue were incorporated in dough formulations, before rheological, physical and bioactive properties of dough were investigated. Smallest particles at 7.5 % substitution level resulted in the highest storage (G′) and loss moduli (G″) and lowest creep strain showing the highest resistance to deformation in the dough. Hardness increased with decreasing particle size and increasing substitution level of extraction residue. Highest substitution level with smallest particle size resulted in the darkest dough. Highest total phenolic content (TPC) of 0.60 mg GAE/g was found in the dough with 7.5 % substitution level by medium sized particles. The highest DPPH radical scavenging activity and Ferric reducing antioxidant power (FRAP) values were 2.00 mmol TE/g and 0.34 mmol TE/g, respectively, for small sized particles and 7.5 % substitution level of extraction residue. Substitution of DDSP fiber-rich extraction residue altered the structural arrangement of gluten in the dough.</div></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"42 ","pages":"Article 100395"},"PeriodicalIF":5.6,"publicationDate":"2024-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142420495","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Development of vitamin D3 and Spirulina platensis protein hydrolysates co-loaded nanoliposomes and coated by sodium caseinate 维生素 D3 和螺旋藻蛋白水解物共载纳米脂质体及酪蛋白酸钠包衣的开发

IF 5.6 3区农林科学

Food Structure-Netherlands Pub Date : 2024-10-01 DOI: 10.1016/j.foostr.2024.100399

Sajed Amjadi , Hadi Almasi , Hamed Hamishehkar , Morteza Kashaninejad , Ali Ehsani , Shirin Jalili

{"title":"Development of vitamin D3 and Spirulina platensis protein hydrolysates co-loaded nanoliposomes and coated by sodium caseinate","authors":"Sajed Amjadi , Hadi Almasi , Hamed Hamishehkar , Morteza Kashaninejad , Ali Ehsani , Shirin Jalili","doi":"10.1016/j.foostr.2024.100399","DOIUrl":"10.1016/j.foostr.2024.100399","url":null,"abstract":"<div><div>The objective of this study was to investigate the co-loading of vitamin D<sub>3</sub> (VitD<sub>3</sub>) and <em>Spirulina platensis</em> protein hydrolysates (SPH) within coated nanoliposomes (NLPs) by sodium caseinate, with the intention of developing a novel nutritional supplement. The coated NLPs exhibited particle size, PDI, and zeta potential values of 185.30 ± 29.62 nm, 0.22±0.04, and +18.70 ± 3.44 mV, respectively. Moreover, the encapsulation efficiencies of the coated NLPs for VitD<sub>3</sub> and SPH were 83.24 ± 4.22 % and 89.41 ± 4.36 %, respectively. The improving effect of the surface coating by sodium caseinate on the stability and function of the NLPs was exhibited through analysis of chemical structure, thermal stability, and crystalline structure. The transmission electron microscopy pictures of the developed NLPs revealed a spherical morphology with a thin layer around the vesicle. The loaded VitD<sub>3</sub> and SPH in the coated NLPs showed controlled release profiles during incubation in the simulated gastrointestinal condition. Moreover, the VitD<sub>3</sub>/SPH co-loaded NLPs and their coated form had no considerable cell toxicity. To conclude, the developed nanosystem demonstrated the suitable characteristics of a nanocarrier for reaping the nutritional benefits of VitD<sub>3</sub> and SPH.</div></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"42 ","pages":"Article 100399"},"PeriodicalIF":5.6,"publicationDate":"2024-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142526538","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

Impact of hydrocolloids on 3D meat analog printing and cooking 水胶体对 3D 肉类模拟打印和烹饪的影响

IF 5.6 3区农林科学

Food Structure-Netherlands Pub Date : 2024-10-01 DOI: 10.1016/j.foostr.2024.100396

Md. Hafizur Rahman Bhuiyan, Nushrat Yeasmen, Michael Ngadi

{"title":"Impact of hydrocolloids on 3D meat analog printing and cooking","authors":"Md. Hafizur Rahman Bhuiyan, Nushrat Yeasmen, Michael Ngadi","doi":"10.1016/j.foostr.2024.100396","DOIUrl":"10.1016/j.foostr.2024.100396","url":null,"abstract":"<div><div>This study investigated the effects of hydrocolloid addition on three-dimensional (3D) printing and cooking of plant ingredients-based meat analog (MA). The MA inks were formulated with soy protein isolate, wheat gluten, canola oil, water, and hydrocolloids (xanthan gum, pectin, hydroxypropyl methylcellulose, guar gum, locust bean gum) at a ratio of 22:12:15:88:2. Formulated inks were used to create a specific 3D cylindrical model geometry and the printed structure were subjected to air frying (AF:180°C, 15 min) and infrared heating (IR:180°C, 15 min). Results showed that the MA ink’s viscosity (3871–5482 Pa. s), 3D printing rate (0.34–0.39 g.sec<sup>−1</sup>), printing error (2.51–10.37 %), and printing precision (81.97–97.27 %) were significantly (p<0.05) impacted by the incorporation of hydrocolloids. The dimensional stability (63.17–98.58 %), and cooking loss (6.70–17.41 %) were greatly impacted by both the hydrocolloids and post-printing cooking methods. Moisture (1.71 db) and fat (0.28 db) content of uncooked 3D printed MA were identical, whereas, differences in color attributes (L value:80.21–98.88, a value:0.01–0.13, b value:0.11–2.11) among the studied hydrocolloid added samples were observed. Moisture, fat, and color traits of 3D printed meat-analogs were significantly (p<0.05) impacted by post-printing cooking methods (AF, IR). During post-printing cooking, the loss of mass (moisture, fat) and changes in color tones were associated with the types of hydrocolloids incorporated in formulating the 3D printing ink. Surfaces and internal structure, mass loss, chemical profile, and glass-transition-temperature of 3D printed meat-analogs were significantly (p<0.05) impacted by both the type of incorporated hydrocolloids and post-printing cooking methods.</div></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"42 ","pages":"Article 100396"},"PeriodicalIF":5.6,"publicationDate":"2024-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142442294","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Quantifying the distribution of proteins at the interface of oil-in-water food emulsions 量化蛋白质在水包油食品乳剂界面上的分布

IF 5.6 3区农林科学

Food Structure-Netherlands Pub Date : 2024-10-01 DOI: 10.1016/j.foostr.2024.100393

Abbas Jabermoradi , John P.M. van Duynhoven , Johannes Hohlbein

{"title":"Quantifying the distribution of proteins at the interface of oil-in-water food emulsions","authors":"Abbas Jabermoradi , John P.M. van Duynhoven , Johannes Hohlbein","doi":"10.1016/j.foostr.2024.100393","DOIUrl":"10.1016/j.foostr.2024.100393","url":null,"abstract":"<div><div>Emulsifiers play an essential role in ensuring the physiochemical stability of food emulsions. In the case of mayonnaise, proteins contained in egg yolk act as emulsifiers. Here, we employed stochastic optical reconstruction microscopy (STORM) to localize proteins at the oil/water droplet interface using fluorescently labeled antibodies. To quantitatively analyze the distribution of proteins, we first simulated homogeneous and heterogeneous distributions. We then implemented the relative position distribution (RPD) analysis to extract the histogram of relative distances between all neighboring localizations. By analyzing the local maxima of the histogram, we could classify distributions at droplet interfaces as homogeneous, partially heterogeneous, and heterogeneous. The model fitting over the RPD histogram using a 2D probability function further provided a localization precision amplitude consistent with the analysis of the local maxima. As a model system for mayonnaise, we used emulsions prepared with combinations of phosvitin, phospholipids, apolipoprotein B (apoB), and sodium dodecyl sulfate (SDS) as emulsifiers. The binary phosvitin/SDS model emulsion showed a partially heterogeneous distribution of phosvitin around the droplets. The ternary phosvitin/phospholipid/SDS and apoB/phospholipid/SDS emulsions showed increased heterogeneity of phosvitin and apoB. Quantification of heterogeneity at droplet interfaces may provide insights in factors determining the physical and chemical stability of emulsions.</div></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"42 ","pages":"Article 100393"},"PeriodicalIF":5.6,"publicationDate":"2024-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142420496","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

Capillary flow-MRI of micronized fat crystal dispersions: Effect of shear history on microstructure and flow 微粉化脂肪晶体分散体的毛细管流-MRI：剪切历史对微观结构和流动的影响

IF 5.6 3区农林科学

Food Structure-Netherlands Pub Date : 2024-10-01 DOI: 10.1016/j.foostr.2024.100392

Klaudia W. Milc , Joshua A. Dijksman , Ruud den Adel , John P.M. van Duynhoven , Camilla Terenzi

{"title":"Capillary flow-MRI of micronized fat crystal dispersions: Effect of shear history on microstructure and flow","authors":"Klaudia W. Milc , Joshua A. Dijksman , Ruud den Adel , John P.M. van Duynhoven , Camilla Terenzi","doi":"10.1016/j.foostr.2024.100392","DOIUrl":"10.1016/j.foostr.2024.100392","url":null,"abstract":"<div><div>Micronized fat crystal (MFC) dispersions are a novel food ingredient enabling more efficient manufacturing of fat-based products as compared to established melt-cool processing. Yet, predicting rheological properties of MFC dispersions, remains a challenge. Here, we demonstrate how a capillary-flow Magnetic Resonance Imaging (MRI) platform provides quantitative measurements of local flow of MFC dispersions, inaccessible by global rheology. The measured 2D <sup>1</sup>H MRI velocity maps unveiled a 5-fold velocity enhancement, and corresponding increase in wall slip, upon increasing the pre-shear time within 0–5 h, due to the 14 % increase in thickness of the crystalline nanoplatelets via recrystallization and aggregation of nanoplatelets. In the absence of pre-shearing, MFC dispersions exhibit an unsheared band at the walls of the capillary, likely arising from fouling and migration of thin nanoplatelets. In contrast to FCDs, flow cooperativity could not be observed for MFC dispersions due to the non-fractality of the fat crystal network. These results demonstrate that, by varying the pre-shear duration, the flow-microstructure properties of the MFC dispersions can be altered in a controlled manner. The approach presented here will allow for rapid assessment of shear-history dependence of flow properties of MFC dispersions under industrially relevant flow conditions.</div></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"42 ","pages":"Article 100392"},"PeriodicalIF":5.6,"publicationDate":"2024-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142420585","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Effectiveness of supercooled freezing in suppressing ice recrystallization during frozen storage 过冷冷冻对抑制冷冻储存过程中冰再结晶的效果

IF 5.6 3区农林科学

Food Structure-Netherlands Pub Date : 2024-09-23 DOI: 10.1016/j.foostr.2024.100391

Rajib Lochan Poudyal , Mark Anthony Redo , Yasuho Ishikawa , Tsukasa Miyake , Toru Suzuki , Manabu Watanabe

{"title":"Effectiveness of supercooled freezing in suppressing ice recrystallization during frozen storage","authors":"Rajib Lochan Poudyal , Mark Anthony Redo , Yasuho Ishikawa , Tsukasa Miyake , Toru Suzuki , Manabu Watanabe","doi":"10.1016/j.foostr.2024.100391","DOIUrl":"10.1016/j.foostr.2024.100391","url":null,"abstract":"<div><div>Ice recrystallization often occurs during frozen food storage, an undesirable occurrence that can cause further damage to food cells and tissues. One factor that triggers its occurrence is the initial structure of the ice crystals formed during the freezing phase. During frozen storage, small ice crystals may recrystallize due to their high surface-to-volume ratio and excess free energy. In this study, the ice recrystallization of supercooled frozen tofu was evaluated during a 12-week frozen storage period and compared with that of slowly and rapidly frozen tofu. The storage temperature was at − 10 ± 2 ℃. Slow freezing at − 10 ℃ static air has produced large crystals up to 0.6 mm before storage and tended not to grow further. Rapid freezing at − 80 ℃ static air with elongated ice crystals exhibits the highest recrystallization rate, especially on the surface of the sample, where the maximum ice crystals grew from 0.23 mm before storage to 0.45 mm after 12 weeks. Supercooled freezing has produced small and homogeneous ice crystals, the largest being 0.15 mm, but their spherical shape tends to have a low affinity for recrystallization, which has allowed the crystals to maintain their size and structure during the frozen storage.</div></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"42 ","pages":"Article 100391"},"PeriodicalIF":5.6,"publicationDate":"2024-09-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142327268","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

Microstructural analysis of network formation in milk protein-polysaccharide mixtures by timelapse confocal laser scanning microscopy 利用定时共焦激光扫描显微镜分析牛奶蛋白-多糖混合物中网络形成的微观结构

IF 5.6 3区农林科学

Food Structure-Netherlands Pub Date : 2024-09-16 DOI: 10.1016/j.foostr.2024.100390

Mariska Brüls-Gill , Sanam Foroutanparsa , Théo Merland , C. Elizabeth P. Maljaars , Maurien Olsthoorn , Roderick P. Tas , Ilja K. Voets

{"title":"Microstructural analysis of network formation in milk protein-polysaccharide mixtures by timelapse confocal laser scanning microscopy","authors":"Mariska Brüls-Gill , Sanam Foroutanparsa , Théo Merland , C. Elizabeth P. Maljaars , Maurien Olsthoorn , Roderick P. Tas , Ilja K. Voets","doi":"10.1016/j.foostr.2024.100390","DOIUrl":"10.1016/j.foostr.2024.100390","url":null,"abstract":"<div><p>To improve the firmness and viscosity of yogurt, a widely consumed dairy product, polysaccharides are frequently utilized. Polysaccharides can modify the formation of the protein networks that make up yogurt by interacting with the milk proteins via electrostatic forces and depletion mechanisms. The interactions between milk proteins and polysaccharides during yogurt fermentation are difficult to study, because they evolve over time due to the decrease in pH. To overcome this, we examine the impact of five different types of polysaccharides (low acyl gellan, high acyl gellan, xanthan, guar gum, ι-Carrageenan) during acid-induced milk gelation using Confocal Laser-Scanning Microscopy. Additionally, we employ Fourier space analysis, time-dependent oscillatory rheology, and cross-correlation image analysis to quantitatively understand how the different polysaccharides affect yogurt microstructure and properties. Our results show that addition of xanthan, guar gum, and ι-carrageenan results in faster structure formation, at pH values above the onset of gelation. Furthermore, while having identical charge density, low acyl gellan associates faster with the protein network compared to more acetylated high acyl gellan or highly branched xanthan. In summary, this study highlights the benefits of integrating timelapse imaging with quantitative image analysis to gain insights into the influence of polysaccharides during milk gelation.</p></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"42 ","pages":"Article 100390"},"PeriodicalIF":5.6,"publicationDate":"2024-09-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2213329124000261/pdfft?md5=a46028b1467b01aedd75659fb2b776bc&pid=1-s2.0-S2213329124000261-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142274806","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0