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.
{"title":"Pea protein as filler particles in dual-protein hybrid emulsified gels: Focus on the particle reinforcement theory","authors":"Peng Zhong , Qing Yu , Zonglin Guo, Hua Zheng, Jie Lin, Hongtao Lei, Yudong Shen, 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}
Lanzhou lily (Lilium davidii var. unicolor) 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 (L* = 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 (<1 μm) pore occupancy (r = 0.82, p < 0.01), while a strong negative correlation was observed with dietary fiber ratio (r = -0.90, p < 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.
{"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, Siyi Zhou, Shuwei Tang, Ningning Wang, Xinyu Gao, Yue Wang, Hongguang Zhu, Zichao Li, 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 × 10<sup>3</sup> 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 (<1 μm) pore occupancy (r = 0.82, p < 0.01), while a strong negative correlation was observed with dietary fiber ratio (r = -0.90, p < 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}
Pub Date : 2025-10-01DOI: 10.1016/j.foostr.2025.100464
Therese Ruhmlieb , Achim Overbeck , Charlotte Ruhmlieb , Ingo Kampen , Arno Kwade , Karin Schwarz , Anja Steffen-Heins
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 via 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.
{"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 , Achim Overbeck , Charlotte Ruhmlieb , Ingo Kampen , Arno Kwade , Karin Schwarz , 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}
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.
{"title":"Changes in starch-assisted expansion porous structure of peanut protein via extrusion and impact on textural and rehydration properties","authors":"Feng Guo, Hui Hu, Huan Zhou, Anna Hu, Qiang Wang, 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}
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.
{"title":"Comparison between the microstructure and rheology of heat-set emulsion gels formed with purified rapeseed proteins","authors":"Colleen P.K. Mudau, Maria Moutkane, Gireeshkumar Balakrishnan, Taco Nicolai, 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}
Pub Date : 2025-10-01DOI: 10.1016/j.foostr.2025.100468
Li-shuang Wang , Jia-Sun , Jin-hui Jia , Jin-jie Huo , Yu-min Duan , Na-Wang , Xiao-shuai Yu , Zhi-gang Xiao , Ying Wang , Xiao-ling Tian
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.
{"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 , Jia-Sun , Jin-hui Jia , Jin-jie Huo , Yu-min Duan , Na-Wang , Xiao-shuai Yu , Zhi-gang Xiao , Ying Wang , 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 (NaPO<sub>3</sub>)x on the characteristics and properties of reconstituted rice in each zone during extrusion processing. The results demonstrated that MAG and (NaPO<sub>3</sub>)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 (NaPO<sub>3</sub>)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, (NaPO<sub>3</sub>)x interacted with RS/G by electrostatic interaction, beginning from the melting zone, promoting the formation of the (NaPO<sub>3</sub>)x-rice with a more solid and dense performance microstructure. In addition, compared with RS/G-rice, both MAG-rice and (NaPO<sub>3</sub>)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 (NaPO<sub>3</sub>)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 (NaPO<sub>3</sub>)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}
Pub Date : 2025-10-01DOI: 10.1016/j.foostr.2025.100490
Miao Wang , Man Wang , Nicola Gasparre , Zuoqian Yang , Chunhua Wu , Chengrong Wen
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 (P < 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 (P < 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.
{"title":"Impact of various enzymes on bran-rich wheat dough properties and sweet bread quality","authors":"Miao Wang , Man Wang , Nicola Gasparre , Zuoqian Yang , Chunhua Wu , 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> < 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> < 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/cm<sup>2</sup>) 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}
Pub Date : 2025-10-01DOI: 10.1016/j.foostr.2025.100472
Peipei Zhang , Bitao Li , Jiacheng Li , Hongwei Ji , Liqing Zhang
Despite the widespread use of hot air drying in seed processing, the mechanisms of drying-induced deformation behavior and microstructural response in pumpkin seeds is not well understood. The moisture content evolution, strain field distribution, and cellular structural responses of seeds under varying drying temperatures (35℃, 40℃, 45℃, 50℃, 55℃, 60℃, 65℃, and 70℃) were systematically analyzed using digital image correlation method (DIC) and cell morphology analysis. The results showed that the drying time to the safe moisture content (9.0 ± 0.5 %) at 70℃ was only 2/9 of that at 35℃. The deformation of pumpkin seeds showed obvious anisotropy, with higher absolute value of strain in the minor axis direction (from −0.017 ∼ −0.056 at 35°C to −0.011 ∼ −0.072 at 70°C) compared to the major axis (from −0.016 to −0.036 at 35°C to −0.029 ∼ −0.056 at 70°C). The pumpkin seeds were dominated by reversible elastic contraction at 50°C or less, and entered the plastic deformation stage when the drying temperature was 50–70°C. The intensified heterogeneity of the strain field reflected the synergistic interaction between the core and edge of seed. The porosity showed a continuous increasing trend with rising temperature, while the average cell area, Feret diameter, and perimeter decreased. The transition from elastic to plastic deformation was observed to occur at around 50°C, which serves as a critical threshold. This study provides a basis for optimizing the hot air drying process of pumpkin seeds, which offering practical guidance for damage-minimized seed and food drying in agricultural applications.
{"title":"Thermal deformation behavior and microstructural response of pumpkin seeds during drying","authors":"Peipei Zhang , Bitao Li , Jiacheng Li , Hongwei Ji , Liqing Zhang","doi":"10.1016/j.foostr.2025.100472","DOIUrl":"10.1016/j.foostr.2025.100472","url":null,"abstract":"<div><div>Despite the widespread use of hot air drying in seed processing, the mechanisms of drying-induced deformation behavior and microstructural response in pumpkin seeds is not well understood. The moisture content evolution, strain field distribution, and cellular structural responses of seeds under varying drying temperatures (35℃, 40℃, 45℃, 50℃, 55℃, 60℃, 65℃, and 70℃) were systematically analyzed using digital image correlation method (DIC) and cell morphology analysis. The results showed that the drying time to the safe moisture content (9.0 ± 0.5 %) at 70℃ was only 2/9 of that at 35℃. The deformation of pumpkin seeds showed obvious anisotropy, with higher absolute value of strain in the minor axis direction <span><math><msub><mrow><mi>ε</mi></mrow><mrow><mi>x</mi></mrow></msub></math></span> (from −0.017 ∼ −0.056 at 35°C to −0.011 ∼ −0.072 at 70°C) compared to the major axis <span><math><msub><mrow><mi>ε</mi></mrow><mrow><mi>y</mi></mrow></msub></math></span> (from −0.016 to −0.036 at 35°C to −0.029 ∼ −0.056 at 70°C). The pumpkin seeds were dominated by reversible elastic contraction at 50°C or less, and entered the plastic deformation stage when the drying temperature was 50–70°C. The intensified heterogeneity of the strain field reflected the synergistic interaction between the core and edge of seed. The porosity showed a continuous increasing trend with rising temperature, while the average cell area, Feret diameter, and perimeter decreased. The transition from elastic to plastic deformation was observed to occur at around 50°C, which serves as a critical threshold. This study provides a basis for optimizing the hot air drying process of pumpkin seeds, which offering practical guidance for damage-minimized seed and food drying in agricultural applications.</div></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"46 ","pages":"Article 100472"},"PeriodicalIF":5.9,"publicationDate":"2025-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145221810","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}
Pub Date : 2025-10-01DOI: 10.1016/j.foostr.2025.100476
Megan Holdstock , Brent S. Murray , Paraskevi Paximada , Michael Rappolt , Isabel Celigueta Torres , Anwesha Sarkar
The effects of pea protein isolate (PPI) particles on the crystallisation and rheological properties of cocoa butter (CB) were evaluated. PPI particles were milled to produce two size classes, coarse and fine. Milled PPI particles were found to aggregate in molten CB, increasing the viscosity of the system and forming an elastic network. Greater aggregation was observed as the size of PPI particles was reduced. PPI particles had no effect on the crystal structure of CB, or the polymorphic transition pathway. However, the induction time of crystallisation was shorter, and the crystalline domain size in the α-phase was smaller for CB crystals + PPI, indicating heterogeneous nucleation effects. PPI particles increased the elasticity of the system by an order of magnitude only during the early stages of CB crystallisation. This study demonstrates that PPI particles can be incorporated into fat-based systems without disrupting fat crystal structure, with the potential to enhance mechanical strength. This highlights their potential as functional rheological modifiers upon milling in confectionery applications.
{"title":"Rheology and crystallisation of cocoa butter in the presence of pea protein","authors":"Megan Holdstock , Brent S. Murray , Paraskevi Paximada , Michael Rappolt , Isabel Celigueta Torres , Anwesha Sarkar","doi":"10.1016/j.foostr.2025.100476","DOIUrl":"10.1016/j.foostr.2025.100476","url":null,"abstract":"<div><div>The effects of pea protein isolate (PPI) particles on the crystallisation and rheological properties of cocoa butter (CB) were evaluated. PPI particles were milled to produce two size classes, coarse and fine. Milled PPI particles were found to aggregate in molten CB, increasing the viscosity of the system and forming an elastic network. Greater aggregation was observed as the size of PPI particles was reduced. PPI particles had no effect on the crystal structure of CB, or the polymorphic transition pathway. However, the induction time of crystallisation was shorter, and the crystalline domain size in the α-phase was smaller for CB crystals + PPI, indicating heterogeneous nucleation effects. PPI particles increased the elasticity of the system by an order of magnitude only during the early stages of CB crystallisation. This study demonstrates that PPI particles can be incorporated into fat-based systems without disrupting fat crystal structure, with the potential to enhance mechanical strength. This highlights their potential as functional rheological modifiers upon milling in confectionery applications.</div></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"46 ","pages":"Article 100476"},"PeriodicalIF":5.9,"publicationDate":"2025-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145269064","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}
Pub Date : 2025-10-01DOI: 10.1016/j.foostr.2025.100483
Oluwafemi Jeremiah Coker, Phyllis J. Shand, Supratim Ghosh
Protein-stabilized emulsion gels are structured soft materials formed by an aggregated network of protein-coated oil droplets holding the aqueous phase immobile. In this study, faba bean protein was physically modified by thermal and high-pressure homogenization before being used to prepare highly stable 30 wt% canola oil-in-water emulsions. The stability and gelation behaviour of the emulsions were characterized by droplet size, charge, small and large deformation rheology and freeze-thaw stability. The effect of protein modification was negligible on droplet size but significant in terms of large deformation rheology and freeze-thaw stability. Heat treatment (90 °C, 30 min) and salt addition (0–3 wt%) resulted in droplet aggregation, converting viscous emulsions into strong, viscoelastic, self-supporting gels. Large deformation rheology revealed that heat treatment significantly increased fracture stress but reduced fracture strain, indicating brittleness in the structure. The emulsions were freeze/thaw stable without any droplet destabilization, except that the unsalted emulsions showed some oiling-off. The microstructure of the emulsion gels revealed an extensive droplet and protein network, which was enhanced by protein modification and salt addition. Investigation of gelation mechanism revealed that the hydrophobic interaction among the interfacial proteins around the oil droplets was the most dominant, followed by hydrogen bonds and disulphide bonds in the heated protein emulsion gels. The stable, self-supporting, strong elastic emulsion gels containing only 30 wt% oil and stabilized using faba protein, created with the selective addition of salt and heat treatment of the emulsions, can be utilized in the development of sustainable, plant-based fat replacers in food formulations.
{"title":"Influence of salt, thermal treatment and protein physical modification on the development of faba bean protein-stabilized elastic emulsion gel","authors":"Oluwafemi Jeremiah Coker, Phyllis J. Shand, Supratim Ghosh","doi":"10.1016/j.foostr.2025.100483","DOIUrl":"10.1016/j.foostr.2025.100483","url":null,"abstract":"<div><div>Protein-stabilized emulsion gels are structured soft materials formed by an aggregated network of protein-coated oil droplets holding the aqueous phase immobile. In this study, faba bean protein was physically modified by thermal and high-pressure homogenization before being used to prepare highly stable 30 wt% canola oil-in-water emulsions. The stability and gelation behaviour of the emulsions were characterized by droplet size, charge, small and large deformation rheology and freeze-thaw stability. The effect of protein modification was negligible on droplet size but significant in terms of large deformation rheology and freeze-thaw stability. Heat treatment (90 °C, 30 min) and salt addition (0–3 wt%) resulted in droplet aggregation, converting viscous emulsions into strong, viscoelastic, self-supporting gels. Large deformation rheology revealed that heat treatment significantly increased fracture stress but reduced fracture strain, indicating brittleness in the structure. The emulsions were freeze/thaw stable without any droplet destabilization, except that the unsalted emulsions showed some oiling-off. The microstructure of the emulsion gels revealed an extensive droplet and protein network, which was enhanced by protein modification and salt addition. Investigation of gelation mechanism revealed that the hydrophobic interaction among the interfacial proteins around the oil droplets was the most dominant, followed by hydrogen bonds and disulphide bonds in the heated protein emulsion gels. The stable, self-supporting, strong elastic emulsion gels containing only 30 wt% oil and stabilized using faba protein, created with the selective addition of salt and heat treatment of the emulsions, can be utilized in the development of sustainable, plant-based fat replacers in food formulations.</div></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"46 ","pages":"Article 100483"},"PeriodicalIF":5.9,"publicationDate":"2025-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145417416","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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