Food Structure-Netherlands最新文献

{"title":"Application of seaweed polysaccharides in pre-baked frozen bread and their effect on frozen gluten","authors":"Ying Zhu ,&nbsp;Shangyuan Sang ,&nbsp;Maya Fitriyanti ,&nbsp;Xiaohu Luo ,&nbsp;Imran Mahmood Khan ,&nbsp;Xueming Xu","doi":"10.1016/j.foostr.2025.100493","DOIUrl":"10.1016/j.foostr.2025.100493","url":null,"abstract":"<div><div>During the freezing process, the formation and recrystallization of ice crystals can disrupt the gluten structure. This study first investigated the effects of five types of seaweed polysaccharides—sodium alginate, propylene glycol alginate (PGA), κ-carrageenan, ι-carrageenan, and λ-carrageenan on the quality of pre-baked frozen bread. The results showed that seaweed polysaccharides significantly reduced the hardness of pre-baked frozen bread, and PGA significantly increased the bread's volume (P &lt; 0.05). Additionally, the effects of the five seaweed polysaccharides on the physicochemical and structural properties of gluten protein before and after freeze-thaw treatment were investigated. After freeze-thaw treatment, compared with the control group, seaweed polysaccharides increased the proportion of strongly bound water in gluten, reduced the content of weakly bound water, decreased the free sulfhydryl content and surface hydrophobicity index of gluten, and increased the content of α-helix structures. Compared with the other four seaweed polysaccharides, gluten treated with PGA exhibited improved integrity of the gluten network after freeze-thaw treatment. Our results demonstrate the feasibility of employing seaweed polysaccharides as natural cryoprotectants in frozen bakery production.</div></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"47 ","pages":"Article 100493"},"PeriodicalIF":5.9,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145771906","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}

{"title":"Effect of different particle size on microstructure, hydration characteristics, and flow properties of bulb powders from Lanzhou Lily (Lilium davidii var. unicolor)","authors":"Yunqing Yan,&nbsp;Siyi Zhou,&nbsp;Shuwei Tang,&nbsp;Ningning Wang,&nbsp;Xinyu Gao,&nbsp;Yue Wang,&nbsp;Hongguang Zhu,&nbsp;Zichao Li,&nbsp;Haixin Sun","doi":"10.1016/j.foostr.2025.100489","DOIUrl":"10.1016/j.foostr.2025.100489","url":null,"abstract":"<div><div>Lanzhou lily (<em>Lilium davidii</em> var. <em>unicolor</em>) has been well recognized as a domestic food ingredient of food-medicine homology over China, especially gained its popularity in Autumn due to its prominent benefits to the lung and calming the mind. It has been reported that its bulbs are rich in nutrients and bioactive compounds, and micronization can significantly enhance the structural and functional properties of Lanzhou lily for high-value applications. This study employed planetary ball milling to produce lily powders with four distinct particle sizes: plant scale (939.8 μm), tissue scale (145.88 μm), cellular scale (31.92 μm), and subcellular scale (6.85 μm). Comprehensive characterization revealed that subcellular-scale powder (SLB) exhibited superior physicochemical properties, including enhanced brightness (<em>L*</em> = 99.19), elevated soluble dietary fiber content (8.50 g/100 g), improved water solubility index (53.59 %), increased bulk density (0.49 × 10³ kg/m³), higher thermal stability (93.41 J/g), and greater horizontal pore occupancy in cell walls (16.79 %). Pearson correlation analysis demonstrated a significant positive correlation between water soluble index and cellular level (&lt;1 μm) pore occupancy (r = 0.82, p &lt; 0.01), while a strong negative correlation was observed with dietary fiber ratio (r = -0.90, p &lt; 0.01). These findings indicate that micronization-induced structural modifications can effectively optimize the functional characteristics of lily powder, particularly its solubility and thermal stability. The results provide valuable insights for developing advanced Lanzhou lily-based products in the food and pharmaceutical industries.</div></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"46 ","pages":"Article 100489"},"PeriodicalIF":5.9,"publicationDate":"2025-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145417417","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}

{"title":"Pea protein as filler particles in dual-protein hybrid emulsified gels: Focus on the particle reinforcement theory","authors":"Peng Zhong ,&nbsp;Qing Yu ,&nbsp;Zonglin Guo,&nbsp;Hua Zheng,&nbsp;Jie Lin,&nbsp;Hongtao Lei,&nbsp;Yudong Shen,&nbsp;Shaozong Wu","doi":"10.1016/j.foostr.2025.100480","DOIUrl":"10.1016/j.foostr.2025.100480","url":null,"abstract":"<div><div>Due to the health concerns, gel-type hybrid meat products containing plant proteins and the gel formation mechanisms have captured extensive attention. In this work, the effect of pea protein concentrate (4 %-12 %, w/w) on the properties of chicken breast emulsified gels was investigated. The results showed that pea protein formed active filler particles, having strong non-covalent interactions with the chicken protein gel network. With the addition of pea protein concentrate, the whole gel structure became more compact, accompanied by the conversion of α-helices into β-sheets. Pea protein concentrate improved the gel quality through both the gel network reinforcement effect and the particle reinforcement effect. Cooking yield increased from 88.3 % to a maximum of 98.7 % at 8 % addition level; hardness was increased from 3907 g to a maximum of 9191 g at a 12 % addition level, while springiness exhibited no significant change. Moreover, the quality improvement supported the use of pea protein concentrate as a partial substitute for chicken breast without sacrificing gel quality. In conclusion, pea protein concentrate is a promising plant protein for constructing chicken breast-based hybrid emulsified gels, and these findings offer valuable insights for its practical application in the development of dual-protein hybrid emulsified meat products.</div></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"46 ","pages":"Article 100480"},"PeriodicalIF":5.9,"publicationDate":"2025-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145321480","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}

{"title":"Lentil protein isolate suspensions with improved solubility and colloidal stability using high pressure homogenisation treatments","authors":"Nicolas Malterre ,&nbsp;Francesca Bot ,&nbsp;Justyna Tarapata ,&nbsp;Elke K. Arendt ,&nbsp;Emanuele Zannini ,&nbsp;James A. O’Mahony","doi":"10.1016/j.foostr.2025.100469","DOIUrl":"10.1016/j.foostr.2025.100469","url":null,"abstract":"<div><div>Lentil protein has generally good techno-functional properties; however, the limited solubility of lentil protein is a barrier to its wider use in food applications. This study aimed to evaluate the impact of high-pressure homogenisation (HPH), in the range 0–180 MPa, on selected techno-functional properties of lentil protein isolate (LPI) suspensions. The results showed that the low solubility (62.8 %) of LPI is mainly attributed to hydrophobic interactions and hydrogen bonds. Treatment with HPH at 180 MPa was effective in increasing this solubility to 95.3 %. The weighted mean volume diameter of particles in the suspensions decreased from 10.7 ± 1.1 (control) to 0.33 ± 0.06 µm (180 MPa), with this reduction in particle size attributed to physical disruptions/breakage of powder particles and of insoluble protein aggregates. Surface hydrophobicity increased from 614 to 1312 on HPH treatment, due to the exposure of previously-buried hydrophobic groups. The physical stability of the suspensions increased with increasing pressure, as evidenced by the separation rate decreasing from 8.55 % to 4.92 %/h for the control and 180 MPa treatments, respectively. These results indicate that HPH is a promising processing strategy to develop colloidally stable lentil protein suspensions with enhanced solubility and improved techno-functional properties for use of lentil protein ingredients in sustainable food products.</div></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"46 ","pages":"Article 100469"},"PeriodicalIF":5.9,"publicationDate":"2025-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145269065","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}

{"title":"Porous pathways to improve food functionality and sustainability","authors":"Lara Manzocco","doi":"10.1016/j.foostr.2025.100488","DOIUrl":"10.1016/j.foostr.2025.100488","url":null,"abstract":"","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"46 ","pages":"Article 100488"},"PeriodicalIF":5.9,"publicationDate":"2025-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145789912","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}

{"title":"Impact of various enzymes on bran-rich wheat dough properties and sweet bread quality","authors":"Miao Wang ,&nbsp;Man Wang ,&nbsp;Nicola Gasparre ,&nbsp;Zuoqian Yang ,&nbsp;Chunhua Wu ,&nbsp;Chengrong Wen","doi":"10.1016/j.foostr.2025.100490","DOIUrl":"10.1016/j.foostr.2025.100490","url":null,"abstract":"<div><div>Enzymes are important food additives in the bakery industry. This work compared the effects of six enzymes, including maltotetraose amylase (G4), α-amylase (AM), cellulase (CEL), xylanase (XYL), glucose oxidase (GOX), and lignin peroxidase (LiP), on the properties of bran-rich wheat dough (BRWD, a sweet dough) and the quality of bran-rich wheat bread (BRWB, a sweet bread). The results indicated that adding enzymes reduced the water absorption of the mixed flour, along with decreased starch pasting viscosity, setback values, and free sulfhydryl content in the BRWD. Notably, the XYL group exhibited the most pronounced effect (<em>P</em> &lt; 0.05), with the lowest water absorption at 60.73 % and the minimum free sulfhydryl content at 10.19 μmol/g. Dynamic rheological analysis revealed that all used enzymes except LiP reduced the storage modulus (G') and loss modulus (G''), while microscopic observations indicated improved starch coating in most treatments—except for LiP, which showed the opposite trend. In terms of bread quality, both G4 and AM significantly increased specific volume and reduced hardness (<em>P</em> &lt; 0.05), with AM-treated BRWB achieving the highest specific volume (3.95 mL/g) and the lowest hardness (20.23 N). Furthermore, enzymes increased cell density of bread crumb while decreasing retrogradation enthalpy changes of bread during storage. In comparison, the G4 group exhibited the highest crumb cell density (61.58 cells/cm²) and demonstrated the most effective inhibition of starch retrogradation. These findings highlight the potential of enzyme-assisted processing to enhance BRWB quality, offering practical insights for the bakery industry to improve consumer acceptance of whole grain products.</div></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"46 ","pages":"Article 100490"},"PeriodicalIF":5.9,"publicationDate":"2025-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145684131","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}

{"title":"Changes in starch-assisted expansion porous structure of peanut protein via extrusion and impact on textural and rehydration properties","authors":"Feng Guo,&nbsp;Hui Hu,&nbsp;Huan Zhou,&nbsp;Anna Hu,&nbsp;Qiang Wang,&nbsp;Jinchuang Zhang","doi":"10.1016/j.foostr.2025.100474","DOIUrl":"10.1016/j.foostr.2025.100474","url":null,"abstract":"<div><div>Extruded restructured plant proteins for foods are beneficial towards environmental sustainability. Peanut protein is a high-quality source of plant protein that can be utilized towards this goal. However, control of pore structure during extrusion is challenging, leading to poor texture and rehydration properties. In this study, blends of peanut protein and pea starch were subjected to extrusion processing at pea starch inclusion levels of 0 %, 10 %, 15 %, 20 %, 25 %, and 30 % (w/w) to fabricate extrudates possessing a porous structure. Results showed that increased pea starch content raised the expansion ratio of the peanut protein extrudates from 1.47 to 2.80, creating larger pores. This promoted faster water absorption by the extrudates. Protein and starch interacted through hydrogen bonds and hydrophobic interactions, influencing disulfide bonds and free sulfhydryl groups. Higher pea starch content increased protein-starch interactions, resulting in polymer systems with higher viscosity. The results explained the influence of the porous structure of peanut protein and pea starch on the extrudate’s textural and rehydration properties during extrusion.</div></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"46 ","pages":"Article 100474"},"PeriodicalIF":5.9,"publicationDate":"2025-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145269068","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}

{"title":"Whey protein aggregates affect cast film appearance and mechanical properties – Part I: Network formation of straight fibrils and non-amyloid aggregates","authors":"Therese Ruhmlieb ,&nbsp;Achim Overbeck ,&nbsp;Charlotte Ruhmlieb ,&nbsp;Ingo Kampen ,&nbsp;Arno Kwade ,&nbsp;Karin Schwarz ,&nbsp;Anja Steffen-Heins","doi":"10.1016/j.foostr.2025.100464","DOIUrl":"10.1016/j.foostr.2025.100464","url":null,"abstract":"<div><div>The film forming properties of pre-treated whey protein isolate (WPI) were investigated. In part I of this study, WPI was structured into amyloid aggregates <em>via</em> acidic pH-dependent heat treatment. Isolated amyloid fractions (straight fibrils) and non-amyloid fractions containing small aggregates and peptides, or mixtures of both fractions were used for film formation. The films' appearance and mechanical properties were influenced by cohesive and adhesive interactions of mesoscopic materials, affecting delamination, stress control, and peelability. Analysis of surface structure and crack patterns using top-view photographs, scanning electron microscopy, and atomic force microscopy images indicated the interplay between adhesion and cohesion forces, which was supported by measurements of hardness, and elasticity through nanoindentation. Films consisting of straight, long fibrils and non-amyloid aggregates provided the highest mechanical strength and cohesive properties. This was due to the scaffold-forming fibrillar network, in which adhesive non-amyloid aggregates were embedded. Fibrillization led to a more uniform film profile at lower protein concentrations by decreasing vertical and horizontal convection flows. The alignment of aggregates during the drying process demonstrated to play a regulatory role in stress release. As a result, aggregate morphology has been observed to directly affect the nature of the resultant cracks, with straight fibrils resulting in straight and linear cracks. Insights obtained from studying pure amyloid/non-amyloid film networks can optimize WPI film formulations for improved edible film applications. This includes reducing crack formation, enhancing visual appearance, and improving peelability.</div></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"46 ","pages":"Article 100464"},"PeriodicalIF":5.9,"publicationDate":"2025-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145269067","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}

{"title":"Comparison between the microstructure and rheology of heat-set emulsion gels formed with purified rapeseed proteins","authors":"Colleen P.K. Mudau,&nbsp;Maria Moutkane,&nbsp;Gireeshkumar Balakrishnan,&nbsp;Taco Nicolai,&nbsp;Christophe Chassenieux","doi":"10.1016/j.foostr.2025.100485","DOIUrl":"10.1016/j.foostr.2025.100485","url":null,"abstract":"<div><div>There is a current drive to replace animal protein by plant proteins for reasons of sustainability. Rapeseed is cultivated for oil, but is also a promising new source of high quality proteins. Industrial application of these proteins necessitates detailed knowledge of their functionality. Here we investigate their potential for the formation of emulsion gels. Emulsions were formed by mixing rapeseed protein isolate (RPI) at different concentrations up to C = 16.5 wt% with rapeseed oil (RO) up to 50 wt%. The emulsions formed weak gels with an elastic modulus (G’) that increased with increasing RO content. Confocal laser scanning microscopy (CLSM) showed that the droplets clustered forming a system spanning network. Heating caused an initial rapid increase of G’ to a value that increased systematically with increasing protein and oil content, but there was little effect of the pH and the ionic strength. Results with RPI were compared to that with purified cruciferin and napin from which it is concluded that napin plays only a minor role in the formation of the emulsion gels. CLSM images showed that during heating cruciferin forms microgels that adsorb at the oil droplet surface and crosslink into a system spanning network in which the oil droplets act as active fillers. The yield strain of the emulsion gels was determined by measuring the shear moduli as a function of the strain and was found to be close to 100 % independent of the oil and protein content.</div></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"46 ","pages":"Article 100485"},"PeriodicalIF":5.9,"publicationDate":"2025-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145417497","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}

{"title":"Investigating the effect of MAG/(NaPO3)x on the physicochemical and structural properties of rice starch-protein rice and improving the mechanism in each zone during the extrusion process","authors":"Li-shuang Wang ,&nbsp;Jia-Sun ,&nbsp;Jin-hui Jia ,&nbsp;Jin-jie Huo ,&nbsp;Yu-min Duan ,&nbsp;Na-Wang ,&nbsp;Xiao-shuai Yu ,&nbsp;Zhi-gang Xiao ,&nbsp;Ying Wang ,&nbsp;Xiao-ling Tian","doi":"10.1016/j.foostr.2025.100468","DOIUrl":"10.1016/j.foostr.2025.100468","url":null,"abstract":"<div><div>The underlying mechanism of the interactions among rice starch (RS), glutelin (G), and texture improvement, during the formation, physicochemical, and structural properties of ternary reconstituted rice, has not been confirmed systematically. Herein, a comprehensive assessment was conducted to investigate the effects of monoacylglycerol (MAG) and composite phosphate (NaPO₃)x on the characteristics and properties of reconstituted rice in each zone during extrusion processing. The results demonstrated that MAG and (NaPO₃)x contributed to improving the hardness, chewiness, and springiness, while reducing the adhesiveness from 7.9 mJ to 1.07 mJ ( for MAG-rice) and 1.6 mJ (for (NaPO₃)x-rice), respectively. From the mixing zone to the extrudate zone, MAG acted as an embedded entity and was tightly bonded to rice starch-glutelin (RS/G) molecules via hydrogen bonding and hydrophobic interactions, which enhanced the tightness and flexibility of RS/G networks, reducing in a microstructure with smoother surface performance and fewer wrinkled protrusions. Meanwhile, (NaPO₃)x interacted with RS/G by electrostatic interaction, beginning from the melting zone, promoting the formation of the (NaPO₃)x-rice with a more solid and dense performance microstructure. In addition, compared with RS/G-rice, both MAG-rice and (NaPO₃)x-rice exhibited higher viscosity coefficients, storage moduli (G'), and loss moduli (G′'), lower tanδ values (indicating more solid-like behavior), better thermal stability, and larger particle sizes. Furthermore, MAG-rice and (NaPO₃)x-rice showed increased rapid viscosity, setback viscosity, and regularity of intermolecular arrangement. Among them, the improvement effect of MAG on RS/G was more prominent than that of (NaPO₃)x. This study provides theoretical guidance for designing and producing reconstituted rice products with rice starch and glutelin as the skeletal structure.</div></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"46 ","pages":"Article 100468"},"PeriodicalIF":5.9,"publicationDate":"2025-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145221811","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}