Pub Date : 2024-11-08DOI: 10.1016/j.foodhyd.2024.110827
Tao Yang , Bo Wang , Tian Lv , Pei Wang , Qin Zhou , Dong Jiang , Hao Jiang
This study investigates the impact of various salts (NaCl, KCl, CaCl₂, MgCl₂) on gluten aggregation, with an emphasis on the role of high-molecular-weight glutenin subunits (HMW-GS) in modulating these impacts. The results demonstrated that NaCl significantly improved dough springiness and adhesiveness, while divalent salts like CaCl₂ and MgCl₂ had a greater effect on increasing dough hardness, with KCl showing the least impact among all salts. Differential responses were observed in HMW-GS deletion lines, where Bx7 was more responsive to NaCl and CaCl₂, whereas By8 showed stronger interactions with KCl and CaCl₂. The observed reductions in zeta potential and decrements in ionic bond content during salt-induced gluten aggregation supported the ‘electrostatic shielding’ mechanism, with hydrophobic interactions and hydrogen bonding emerging as key contributors to aggregate stability. Molecular dynamics simulations further corroborated these findings, revealing stronger Coulomb-SR interactions and enhanced binding affinities for divalent ions, in agreement with experimental data. These insights provide a theoretical foundation for optimizing low-sodium formulations in wheat-based products.
{"title":"Influence of high-molecular-weight glutenin subunits and salt types on dough rheology and gluten aggregation: A combined experimental and computational approach","authors":"Tao Yang , Bo Wang , Tian Lv , Pei Wang , Qin Zhou , Dong Jiang , Hao Jiang","doi":"10.1016/j.foodhyd.2024.110827","DOIUrl":"10.1016/j.foodhyd.2024.110827","url":null,"abstract":"<div><div>This study investigates the impact of various salts (NaCl, KCl, CaCl₂, MgCl₂) on gluten aggregation, with an emphasis on the role of high-molecular-weight glutenin subunits (HMW-GS) in modulating these impacts. The results demonstrated that NaCl significantly improved dough springiness and adhesiveness, while divalent salts like CaCl₂ and MgCl₂ had a greater effect on increasing dough hardness, with KCl showing the least impact among all salts. Differential responses were observed in HMW-GS deletion lines, where <em>Bx7</em> was more responsive to NaCl and CaCl₂, whereas <em>By8</em> showed stronger interactions with KCl and CaCl₂. The observed reductions in zeta potential and decrements in ionic bond content during salt-induced gluten aggregation supported the ‘electrostatic shielding’ mechanism, with hydrophobic interactions and hydrogen bonding emerging as key contributors to aggregate stability. Molecular dynamics simulations further corroborated these findings, revealing stronger Coulomb-SR interactions and enhanced binding affinities for divalent ions, in agreement with experimental data. These insights provide a theoretical foundation for optimizing low-sodium formulations in wheat-based products.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"160 ","pages":"Article 110827"},"PeriodicalIF":11.0,"publicationDate":"2024-11-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142697667","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-11-07DOI: 10.1016/j.foodhyd.2024.110826
Samira Forghani, Hadi Almasi
This study aimed to fabricate a food freshness halochromic aerogel based on alginate, gellan, and Echium amoenum anthocyanins (EA). The porosity and morphological properties of the aerogels (AG2, AG6, and AG10) were regulated by varying the concentration of CaCl2 (2, 6, 10 %). FE-SEM analysis revealed that increasing the CaCl2 content led to the formation of aerogels with enhanced overall porosity and larger pore sizes. The AG6 aerogel, characterized by a density of 23.44 ± 0.04 mg/cm³, a porosity of 91.66 ± 0.06%, and an average pore size of 306.93 ± 122.89 μm, was identified as the optimal support for the incorporation of the EA pigment. FT-IR analysis verified the formation of hydrogen bonds between the AG6 aerogel and EA molecules. Incorporating anthocyanin increased the crystallinity and thermal stability of the aerogel, as evidenced by XRD and DSC analyses. The AG6EA aerogel displayed a color shift from red to yellow over a pH range of 2–12. The AG6EA aerogel demonstrated high sensitivity to ammonia vapor and proper color stability and reversibility. The AG6EA aerogel color transitioned from purple to blue and then green through rainbow trout storage, correlating with changes in pH, total volatile basic nitrogen (TVB-N), and total viable microbial count (TVC and TPC) of the fish samples. This research extends a new insight to develop cutting-edge, susceptible, and accurate pH indicators capable of quality assessment of protein-based food products.
{"title":"Halochromic aerogels with Ca2⁺-induced tailored porosity based on alginate/gellan integrated with Echium amoenum anthocyanins: Characterization and application for freshness monitoring of rainbow trout fillet","authors":"Samira Forghani, Hadi Almasi","doi":"10.1016/j.foodhyd.2024.110826","DOIUrl":"10.1016/j.foodhyd.2024.110826","url":null,"abstract":"<div><div>This study aimed to fabricate a food freshness halochromic aerogel based on alginate, gellan, and <em>Echium amoenum</em> anthocyanins (EA). The porosity and morphological properties of the aerogels (AG2, AG6, and AG10) were regulated by varying the concentration of CaCl<sub>2</sub> (2, 6, 10 %). FE-SEM analysis revealed that increasing the CaCl<sub>2</sub> content led to the formation of aerogels with enhanced overall porosity and larger pore sizes. The AG6 aerogel, characterized by a density of 23.44 ± 0.04 mg/cm³, a porosity of 91.66 ± 0.06%, and an average pore size of 306.93 ± 122.89 μm, was identified as the optimal support for the incorporation of the EA pigment. FT-IR analysis verified the formation of hydrogen bonds between the AG6 aerogel and EA molecules. Incorporating anthocyanin increased the crystallinity and thermal stability of the aerogel, as evidenced by XRD and DSC analyses. The AG6EA aerogel displayed a color shift from red to yellow over a pH range of 2–12. The AG6EA aerogel demonstrated high sensitivity to ammonia vapor and proper color stability and reversibility. The AG6EA aerogel color transitioned from purple to blue and then green through rainbow trout storage, correlating with changes in pH, total volatile basic nitrogen (TVB-N), and total viable microbial count (TVC and TPC) of the fish samples. This research extends a new insight to develop cutting-edge, susceptible, and accurate pH indicators capable of quality assessment of protein-based food products.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"160 ","pages":"Article 110826"},"PeriodicalIF":11.0,"publicationDate":"2024-11-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142697951","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-11-07DOI: 10.1016/j.foodhyd.2024.110804
Tao Yang , Tian Lv , Bo Wang , Pei Wang , Qin Zhou , Dong Jiang , Hao Jiang
This study explored how high-molecular-weight glutenin subunits (HMW-GS) at the Glu-B1 locus impact gluten deterioration during dough frozen storage and freeze-thaw (F/T) cycles. Using deletion lines, we found that the deletion of specific HMW-GS, particularly Bx7, led to a greater reduction in glutenin macropolymer (GMP) wet weight during storage, especially under F/T cycles. The frozen conditions triggered more dissociation of hydrogen and disulfide bonds, generating more protein monomers and resulting in severe gluten deterioration in the Bx7 deletion. Additionally, protein structures in these lines were more vulnerable to damage during F/T cycles due to temperature fluctuations. In silico analysis further confirmed that Bx7 had better stability and antifreeze activity compared to By8, explaining why its deletion had a more pronounced effect on gluten stability. These findings offer significant implications for the food industry, particularly in enhancing the quality, shelf-life, and commercial viability of frozen dough products by providing a deeper understanding of the mechanisms behind gluten deterioration, specifically the role of high-molecular-weight glutenin subunits.
{"title":"Unveiling the mechanism of high-molecular-weight glutenin subunit deletions at the Glu-B1 locus affecting gluten deterioration during dough frozen storage and freeze-thaw cycles: An integrative experimental and in silico study","authors":"Tao Yang , Tian Lv , Bo Wang , Pei Wang , Qin Zhou , Dong Jiang , Hao Jiang","doi":"10.1016/j.foodhyd.2024.110804","DOIUrl":"10.1016/j.foodhyd.2024.110804","url":null,"abstract":"<div><div>This study explored how high-molecular-weight glutenin subunits (HMW-GS) at the Glu-B1 locus impact gluten deterioration during dough frozen storage and freeze-thaw (F/T) cycles. Using deletion lines, we found that the deletion of specific HMW-GS, particularly <em>Bx7</em>, led to a greater reduction in glutenin macropolymer (GMP) wet weight during storage, especially under F/T cycles. The frozen conditions triggered more dissociation of hydrogen and disulfide bonds, generating more protein monomers and resulting in severe gluten deterioration in the <em>Bx7</em> deletion. Additionally, protein structures in these lines were more vulnerable to damage during F/T cycles due to temperature fluctuations. In silico analysis further confirmed that <em>Bx7</em> had better stability and antifreeze activity compared to <em>By8</em>, explaining why its deletion had a more pronounced effect on gluten stability. These findings offer significant implications for the food industry, particularly in enhancing the quality, shelf-life, and commercial viability of frozen dough products by providing a deeper understanding of the mechanisms behind gluten deterioration, specifically the role of high-molecular-weight glutenin subunits.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"160 ","pages":"Article 110804"},"PeriodicalIF":11.0,"publicationDate":"2024-11-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142697952","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
This study investigates the structural changes and covalent interactions of rice glutelin and egg white proteins with ferulic acid, considering the effects of germination and whisking times. Using ternary phase diagrams, we analyzed the antioxidant properties and in vitro digestive behaviors of these protein-ferulic acid conjugates. Increased germination time enhanced the conjugate potential of rice glutelin, while prolonged whisking time increased the molecular flexibility of egg white proteins. The optimal ratio of rice glutelin to egg white proteins (6:4) resulted in higher surface hydrophobicity. In vitro digestion showed that a higher proportion of rice glutelin aids gastric digestion, while more egg white protein supports intestinal hydrolysis. Extended germination time reduced particle size and antioxidant capacities during digestion but negatively impacted calcium loading from eggshells. These findings highlight the potential of tailored protein-ferulic acid conjugates for improved functional properties and food applications.
{"title":"Designing ferulic acid-functionalized dual protein conjugates: Process-induced changes, structural interplays, and sustainable calcium fortification","authors":"Kefan Ouyang , Yufeng Wang , Hexiang Xie , Yuanyuan Feng , Hua Xiong , Qiang Zhao","doi":"10.1016/j.foodhyd.2024.110824","DOIUrl":"10.1016/j.foodhyd.2024.110824","url":null,"abstract":"<div><div>This study investigates the structural changes and covalent interactions of rice glutelin and egg white proteins with ferulic acid, considering the effects of germination and whisking times. Using ternary phase diagrams, we analyzed the antioxidant properties and <em>in vitro</em> digestive behaviors of these protein-ferulic acid conjugates. Increased germination time enhanced the conjugate potential of rice glutelin, while prolonged whisking time increased the molecular flexibility of egg white proteins. The optimal ratio of rice glutelin to egg white proteins (6:4) resulted in higher surface hydrophobicity. <em>In vitro</em> digestion showed that a higher proportion of rice glutelin aids gastric digestion, while more egg white protein supports intestinal hydrolysis. Extended germination time reduced particle size and antioxidant capacities during digestion but negatively impacted calcium loading from eggshells. These findings highlight the potential of tailored protein-ferulic acid conjugates for improved functional properties and food applications.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"160 ","pages":"Article 110824"},"PeriodicalIF":11.0,"publicationDate":"2024-11-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142697950","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-11-06DOI: 10.1016/j.foodhyd.2024.110825
Tao Wang , Xin Wu , Xuyuan Li , Wei Feng , Ren Wang , Kai Huang
Fungi proteins represent a potential alternative to animal proteins, which are regarded as a prospective source of edible proteins due to more sustainable and efficient cultivation of fungi. Nevertheless, the extraction of fungi proteins typically involves alkali extraction combined with acid precipitation (AEAP), yielding considerable amounts of salt that causes aggregation and inferior functional properties of proteins. In this study, we put forward a novel extraction method by direct filtration of Na+ and OH− from the alkaline extraction solutions using ceramic membranes. This method enabled the continuous, efficient and cost-effective production of Pleurotus eryngii protein (PEP). The PEP prepared by this technology featured a uniform distribution of nanoparticles (∼129.5 nm) with higher water dispersity, colloidal stability and surface active properties as compared to that prepared by the AEAP method. Moreover, the microstructures of PEP can be tailored with various nanoparticle sizes and size distribution profiles, allowing for the adjustment of long-term stabilities and surface activities. Our study renovated the production technology of fungi proteins to enhance their functionalities as well as the application prospects in the future food industry.
真菌蛋白质是动物蛋白质的潜在替代品，由于真菌的栽培更可持续、更高效，因此被视为可食用蛋白质的未来来源。然而，真菌蛋白质的提取通常采用碱提取结合酸沉淀（AEAP）的方法，会产生大量盐分，导致蛋白质聚集，降低蛋白质的功能特性。在这项研究中，我们提出了一种新型提取方法，即利用陶瓷膜直接过滤碱性提取液中的 Na+ 和 OH-。这种方法能够连续、高效、低成本地生产红球藻蛋白（PEP）。与 AEAP 方法相比，该技术制备的 PEP 纳米粒子分布均匀（129.5 nm），具有更高的水分散性、胶体稳定性和表面活性。此外，PEP 的微观结构可根据不同的纳米颗粒大小和粒度分布曲线进行定制，从而调节长期稳定性和表面活性。我们的研究革新了真菌蛋白质的生产技术，增强了其功能性，并为未来食品工业的发展提供了应用前景。
{"title":"Preparation of salt-free Pleurotus eryngii protein with enhanced colloidal stability and emulsifying properties by ceramic membrane filtration","authors":"Tao Wang , Xin Wu , Xuyuan Li , Wei Feng , Ren Wang , Kai Huang","doi":"10.1016/j.foodhyd.2024.110825","DOIUrl":"10.1016/j.foodhyd.2024.110825","url":null,"abstract":"<div><div>Fungi proteins represent a potential alternative to animal proteins, which are regarded as a prospective source of edible proteins due to more sustainable and efficient cultivation of fungi. Nevertheless, the extraction of fungi proteins typically involves alkali extraction combined with acid precipitation (AEAP), yielding considerable amounts of salt that causes aggregation and inferior functional properties of proteins. In this study, we put forward a novel extraction method by direct filtration of Na<sup>+</sup> and OH<sup>−</sup> from the alkaline extraction solutions using ceramic membranes. This method enabled the continuous, efficient and cost-effective production of <em>Pleurotus eryngii</em> protein (PEP). The PEP prepared by this technology featured a uniform distribution of nanoparticles (∼129.5 nm) with higher water dispersity, colloidal stability and surface active properties as compared to that prepared by the AEAP method. Moreover, the microstructures of PEP can be tailored with various nanoparticle sizes and size distribution profiles, allowing for the adjustment of long-term stabilities and surface activities. Our study renovated the production technology of fungi proteins to enhance their functionalities as well as the application prospects in the future food industry.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"160 ","pages":"Article 110825"},"PeriodicalIF":11.0,"publicationDate":"2024-11-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142697954","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-11-06DOI: 10.1016/j.foodhyd.2024.110823
Woo-Ju Kim , Yoonbin Kim , Yixing Lu , Reza Ovissipour , Nitin Nitin
This study aimed to evaluate plant-based 3D scaffolds for supporting the cultivation of animal cells for cultivated meat. The physical and chemical characteristics of pectin and composite gels (pectin + soy protein isolate [SPI] or pea protein isolate [PPI]) were analyzed. Rheological property analysis revealed that all materials exhibited viscoelastic solid behavior, shear thinning, and micro-structure recovery behavior, essential properties for 3D printing. Texture profile analysis (TPA) of composite gels demonstrated that some of the textural properties of these composite materials were in the range of mechanical properties of meat products including pork, poultry, and fish. The cytocompatibility and proliferative potential of these scaffold gels were evaluated using C2C12 (myoblast cells) as a model cell line, indicating their potential to support the growth of the animal cell without apparent toxicity. In examining 3D printability, incorporating protein into the pectin gel resulted in enhanced printability, characterized by reduced surface roughness and thinner thickness. Based on these analyses, a 3D printed scaffold was generated by using pectin, 30% SPI, and 10% PPI. Remarkably, the scaffolds with pectin and 10% PPI supported the growth of the cells, comparable to the cells grown on a tissue culture plate (positive control) demonstrating its potential to support animal cell growth. These findings highlight the promising potential of the formulated materials for applications within the cultivated meat industry.
本研究旨在评估植物基三维支架对培养肉类动物细胞的支持作用。研究分析了果胶和复合凝胶（果胶+大豆分离蛋白[SPI]或豌豆分离蛋白[PPI]）的物理和化学特性。流变特性分析表明，所有材料都表现出粘弹性固体行为、剪切稀化和微结构恢复行为，这些都是三维打印的基本特性。复合凝胶的纹理轮廓分析（TPA）表明，这些复合材料的某些纹理特性与猪肉、禽肉和鱼肉等肉类产品的机械特性相符。以 C2C12（肌母细胞）为模型细胞系，对这些支架凝胶的细胞相容性和增殖潜力进行了评估，结果表明它们具有支持动物细胞生长的潜力，且无明显毒性。在检测三维打印性能时，将蛋白质加入果胶凝胶可提高打印性能，其特点是表面粗糙度降低，厚度变薄。根据这些分析，使用果胶、30% SPI 和 10% PPI 生成了 3D 打印支架。值得注意的是，含有果胶和 10% PPI 的支架支持细胞生长，与在组织培养板（阳性对照）上生长的细胞相当，这表明它具有支持动物细胞生长的潜力。这些发现凸显了配制材料在肉类养殖业中的应用潜力。
{"title":"Evaluation of plant-based composite materials as 3D printed scaffolds for cell growth and proliferation in cultivated meat applications","authors":"Woo-Ju Kim , Yoonbin Kim , Yixing Lu , Reza Ovissipour , Nitin Nitin","doi":"10.1016/j.foodhyd.2024.110823","DOIUrl":"10.1016/j.foodhyd.2024.110823","url":null,"abstract":"<div><div>This study aimed to evaluate plant-based 3D scaffolds for supporting the cultivation of animal cells for cultivated meat. The physical and chemical characteristics of pectin and composite gels (pectin + soy protein isolate [SPI] or pea protein isolate [PPI]) were analyzed. Rheological property analysis revealed that all materials exhibited viscoelastic solid behavior, shear thinning, and micro-structure recovery behavior, essential properties for 3D printing. Texture profile analysis (TPA) of composite gels demonstrated that some of the textural properties of these composite materials were in the range of mechanical properties of meat products including pork, poultry, and fish. The cytocompatibility and proliferative potential of these scaffold gels were evaluated using C2C12 (myoblast cells) as a model cell line, indicating their potential to support the growth of the animal cell without apparent toxicity. In examining 3D printability, incorporating protein into the pectin gel resulted in enhanced printability, characterized by reduced surface roughness and thinner thickness. Based on these analyses, a 3D printed scaffold was generated by using pectin, 30% SPI, and 10% PPI. Remarkably, the scaffolds with pectin and 10% PPI supported the growth of the cells, comparable to the cells grown on a tissue culture plate (positive control) demonstrating its potential to support animal cell growth. These findings highlight the promising potential of the formulated materials for applications within the cultivated meat industry.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"160 ","pages":"Article 110823"},"PeriodicalIF":11.0,"publicationDate":"2024-11-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142707106","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-11-06DOI: 10.1016/j.foodhyd.2024.110815
Manwinder Kaur Sidhu , Felicity Whitehead , Stefan Kasapis
In this investigation, whey protein and agarose were employed as the phase-separated biopolymer system, with vitamin B6 acting as the diffusant. Fourier-transform infrared (FTIR) spectroscopy affirmed the absence of chemical interactions among all constituents within the experimental parameters. X-ray diffraction (XRD) analysis corroborated the uniform dissolution of vitamin B6 within the composite low-solid mixtures. Confocal scanning laser microscopy elucidated the topology of the matrix, providing tangible evidence of the phase-separated whey protein-agarose networks. Small-deformation dynamic oscillation in-shear was employed to establish a rheological blending law model, predicting the phase volume and effective concentration of the individual components (whey protein and agarose) within their respective domains. Subsequently, a diffusion study was conducted, advocating a novel blending law for molecular transport to estimate the theoretical diffusion coefficient of vitamin B6 in the composite gel by leveraging the effective concentration of each polymer within its phase. The outcomes were positively compared to the observed diffusion coefficient of the vitamin from the composite gel using UV–vis spectroscopy. These results underscore the viability of the blending-law diffusion theory in elucidating the molecular transport of hydrophilic vitamins released from aqueous biopolymer composite gels.
{"title":"Molecular transport of vitamin B6 from whey protein and agarose composite gels using diffusion blending law modelling","authors":"Manwinder Kaur Sidhu , Felicity Whitehead , Stefan Kasapis","doi":"10.1016/j.foodhyd.2024.110815","DOIUrl":"10.1016/j.foodhyd.2024.110815","url":null,"abstract":"<div><div>In this investigation, whey protein and agarose were employed as the phase-separated biopolymer system, with vitamin B6 acting as the diffusant. Fourier-transform infrared (FTIR) spectroscopy affirmed the absence of chemical interactions among all constituents within the experimental parameters. X-ray diffraction (XRD) analysis corroborated the uniform dissolution of vitamin B6 within the composite low-solid mixtures. Confocal scanning laser microscopy elucidated the topology of the matrix, providing tangible evidence of the phase-separated whey protein-agarose networks. Small-deformation dynamic oscillation in-shear was employed to establish a rheological blending law model, predicting the phase volume and effective concentration of the individual components (whey protein and agarose) within their respective domains. Subsequently, a diffusion study was conducted, advocating a novel blending law for molecular transport to estimate the theoretical diffusion coefficient of vitamin B6 in the composite gel by leveraging the effective concentration of each polymer within its phase. The outcomes were positively compared to the observed diffusion coefficient of the vitamin from the composite gel using UV–<em>vis</em> spectroscopy. These results underscore the viability of the blending-law diffusion theory in elucidating the molecular transport of hydrophilic vitamins released from aqueous biopolymer composite gels.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"160 ","pages":"Article 110815"},"PeriodicalIF":11.0,"publicationDate":"2024-11-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142697949","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-11-05DOI: 10.1016/j.foodhyd.2024.110821
Dingkui Qin , Jiani Bao , Zhiyun Zhang , Zhihao Zhou , David Julian McClements , Jiakai Lu
The growing demand for sustainable and functional ingredients in the food, pharmaceutical, and cosmetic industries has heightened interest in plant proteins as foaming agents. However, a knowledge gap persists regarding how transient material properties, influenced by foaming conditions, impact foam stability. This study investigates foam formation and stability of dilute pea protein solutions (0.1–1 wt%) using a gas sparging method. We examine the impact of protein properties, including bulk viscosity, adsorption kinetics, and foaming conditions like sparging flow rate, initial liquid volume, and sparging time. By correlating foam half-life (t1/2) with surface pressure at various time scales, we observed that transient surface pressure at residence time (πr) strongly correlated with t1/2 (R2 = 0.94) over a wide range of foaming processing parameters (flow rate of 0.2–0.4 L/min, liquid volume of 30–150 mL, and sparging time of 5–10 s) and protein concentrations, unlike equilibrium surface pressure or surface pressure at sparging time. This highlights the significance of πr, as it directly relates to initial bubble size, in controlling foam stability for dilute protein solutions. Our results reveal key insights into how transient surface properties, influenced by foaming processing parameters, govern foam stability. These findings contribute to the broader understanding of plant protein functionality and offer potential strategies for enhancing their use in both food and non-food applications.
{"title":"What determines the foam stability of dilute protein solutions in sparging systems?","authors":"Dingkui Qin , Jiani Bao , Zhiyun Zhang , Zhihao Zhou , David Julian McClements , Jiakai Lu","doi":"10.1016/j.foodhyd.2024.110821","DOIUrl":"10.1016/j.foodhyd.2024.110821","url":null,"abstract":"<div><div>The growing demand for sustainable and functional ingredients in the food, pharmaceutical, and cosmetic industries has heightened interest in plant proteins as foaming agents. However, a knowledge gap persists regarding how transient material properties, influenced by foaming conditions, impact foam stability. This study investigates foam formation and stability of dilute pea protein solutions (0.1–1 wt%) using a gas sparging method. We examine the impact of protein properties, including bulk viscosity, adsorption kinetics, and foaming conditions like sparging flow rate, initial liquid volume, and sparging time. By correlating foam half-life (t<sub>1/2</sub>) with surface pressure at various time scales, we observed that transient surface pressure at residence time (π<sub>r</sub>) strongly correlated with t<sub>1/2</sub> (R<sup>2</sup> = 0.94) over a wide range of foaming processing parameters (flow rate of 0.2–0.4 L/min, liquid volume of 30–150 mL, and sparging time of 5–10 s) and protein concentrations, unlike equilibrium surface pressure or surface pressure at sparging time. This highlights the significance of π<sub>r</sub>, as it directly relates to initial bubble size, in controlling foam stability for dilute protein solutions. Our results reveal key insights into how transient surface properties, influenced by foaming processing parameters, govern foam stability. These findings contribute to the broader understanding of plant protein functionality and offer potential strategies for enhancing their use in both food and non-food applications.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"160 ","pages":"Article 110821"},"PeriodicalIF":11.0,"publicationDate":"2024-11-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142697942","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-11-05DOI: 10.1016/j.foodhyd.2024.110819
Yiqiang Dai , Yifei Liu , Zhe Wang , Weimin Xu , Mingsheng Dong , Xiudong Xia , Daoying Wang
Novel naturally sourced polysaccharides are gaining attention for their safety and improvement in food texture. This study investigated the correlations between the structural characteristics and physicochemical properties of dextran GS128 derived from Leuconostoc citreum SH12, and assessed its applicability in three-dimensional (3D) printed whole grain and legume-based (whole grain oat, chickpea and soybean) foods designed for dysphagia patients. The findings revealed that GS128 had a non-crystalline amorphous nature and high thermostability, suggesting its food processing potential. GS128 aqueous solution showed shear thinning and elastic gel behavior, and excellent thixotropic and structural recovery properties, and their effects were positive dose-dependent at the concentration of 4∼10 wt%, which were determined by its nearly linear structure mainly composed of 87.74% α-(1 → 6) linkages with a high molecular weight of 3.02 × 108 Da. Moreover, the addition of 4∼10 wt% GS128 not only retained the shape of 3D printed whole grain and legume food, but also improved the swallowability by 33.26–74.60% compared with food without GS128, indicating the usage potential for dysphagia people. Overall, GS128 as a texture modifier has significant potential for application in the food industry, especially in the development of 3D-printed dysphagia diets.
{"title":"The use of dextran in 3D printing for dysphagia foods: Relationships between its structure and physicochemical properties","authors":"Yiqiang Dai , Yifei Liu , Zhe Wang , Weimin Xu , Mingsheng Dong , Xiudong Xia , Daoying Wang","doi":"10.1016/j.foodhyd.2024.110819","DOIUrl":"10.1016/j.foodhyd.2024.110819","url":null,"abstract":"<div><div>Novel naturally sourced polysaccharides are gaining attention for their safety and improvement in food texture. This study investigated the correlations between the structural characteristics and physicochemical properties of dextran GS128 derived from <em>Leuconostoc citreum</em> SH12, and assessed its applicability in three-dimensional (3D) printed whole grain and legume-based (whole grain oat, chickpea and soybean) foods designed for dysphagia patients. The findings revealed that GS128 had a non-crystalline amorphous nature and high thermostability, suggesting its food processing potential. GS128 aqueous solution showed shear thinning and elastic gel behavior, and excellent thixotropic and structural recovery properties, and their effects were positive dose-dependent at the concentration of 4∼10 wt%, which were determined by its nearly linear structure mainly composed of 87.74% α-(1 → 6) linkages with a high molecular weight of 3.02 × 10<sup>8</sup> Da. Moreover, the addition of 4∼10 wt% GS128 not only retained the shape of 3D printed whole grain and legume food, but also improved the swallowability by 33.26–74.60% compared with food without GS128, indicating the usage potential for dysphagia people. Overall, GS128 as a texture modifier has significant potential for application in the food industry, especially in the development of 3D-printed dysphagia diets.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"160 ","pages":"Article 110819"},"PeriodicalIF":11.0,"publicationDate":"2024-11-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142653412","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-11-05DOI: 10.1016/j.foodhyd.2024.110817
Ruiling Li , Ningzhe Wang , Chao Ma , Jiacheng Wang , Jing Wang , Xin Yang
With the development of the intelligent direction of food 3D printing, people have a strong aesthetic interest in food printing prototypes. In order to investigate the ability of food-based materials to print complex structures and fine patterns simultaneously, three phase-change hydrocolloids with different mechanical strengths after cooling were selected: xanthan gums (Xg), low acyl gellan gums (Gg), and starches (Ss) with ovalbumin to form Xg-ovalbumin emulsion gel (Xg-OEG), Gg-ovalbumin emulsion gel (Gg-OEG), and Ss-ovalbumin emulsion gel (Ss-OEG), respectively. Ss-OEG printed fine patterns with a minimum size of 1.5 mm accurately at a Ss concentration of 1.5%, and was able to print suspended structures, had continuous filament strips and tight layer-to-layer stacking, with the ability to print complex structures and fine patterns simultaneously. Compared with Xg-OEG and Gg-OEG, Ss-OEG had high viscoelasticity and mechanical strength, suitable fluidity, small size of oil droplets without aggregation, dense network structure, and high surface hydrophobicity and amide A peak intensity and the low free sulfhydryl content. Thus, Ss endowed OEG with a certain viscoelasticity and mechanical strength, and caused massive aggregation of proteins through forming disulfide bonds, hydrophobic interactions, and hydrogen bonds. Aggregated ovalbumin and Ss formed a stable and strong network structure, emulsified oil droplets filled in the network, the three tightly crosslinked together to form an emulsion gel with excellent printing ability. This research offered the possibility of simultaneously printing complex structures, high-resolution patterns using food-based materials, also providing a theoretical basis for the design of complex and fine printed products.
随着食品3D打印智能化方向的发展，人们对食品打印原型产生了浓厚的审美兴趣。为了研究食品基材料同时打印复杂结构和精细图案的能力，我们选择了三种冷却后机械强度不同的相变水胶体：黄原胶（Xg）、低酰基结冷胶（Gg）和淀粉（Ss）与卵清蛋白分别形成Xg-卵清蛋白乳液凝胶（Xg-OEG）、Gg-卵清蛋白乳液凝胶（Gg-OEG）和Ss-卵清蛋白乳液凝胶（Ss-OEG）。在 Ss 浓度为 1.5% 的条件下，Ss-OEG 能准确地打印出最小尺寸为 1.5 mm 的精细图案，并能打印出悬浮结构、连续的丝带和紧密的层间堆叠，具有同时打印复杂结构和精细图案的能力。与 Xg-OEG 和 Gg-OEG 相比，Ss-OEG 具有较高的粘弹性和机械强度、适宜的流动性、油滴粒径小且不聚集、致密的网络结构、较高的表面疏水性和酰胺 A 峰强度以及较低的游离巯基含量。因此，Ss 赋予了 OEG 一定的粘弹性和机械强度，并通过形成二硫键、疏水作用和氢键，使蛋白质大量聚集。聚集的卵清蛋白和 Ss 形成了稳定而坚固的网络结构，乳化油滴填充在网络中，三者紧密交联在一起，形成了具有出色印刷能力的乳化凝胶。这项研究为利用食品基材料同时印刷复杂结构和高分辨率图案提供了可能，也为设计复杂精细的印刷产品提供了理论依据。
{"title":"Construction and formation mechanism of phase-change polysaccharide–protein composite emulsion gels: For simultaneous printing of food products with complex structures and fine patterns","authors":"Ruiling Li , Ningzhe Wang , Chao Ma , Jiacheng Wang , Jing Wang , Xin Yang","doi":"10.1016/j.foodhyd.2024.110817","DOIUrl":"10.1016/j.foodhyd.2024.110817","url":null,"abstract":"<div><div>With the development of the intelligent direction of food 3D printing, people have a strong aesthetic interest in food printing prototypes. In order to investigate the ability of food-based materials to print complex structures and fine patterns simultaneously, three phase-change hydrocolloids with different mechanical strengths after cooling were selected: xanthan gums (Xg), low acyl gellan gums (Gg), and starches (Ss) with ovalbumin to form Xg-ovalbumin emulsion gel (Xg-OEG), Gg-ovalbumin emulsion gel (Gg-OEG), and Ss-ovalbumin emulsion gel (Ss-OEG), respectively. Ss-OEG printed fine patterns with a minimum size of 1.5 mm accurately at a Ss concentration of 1.5%, and was able to print suspended structures, had continuous filament strips and tight layer-to-layer stacking, with the ability to print complex structures and fine patterns simultaneously. Compared with Xg-OEG and Gg-OEG, Ss-OEG had high viscoelasticity and mechanical strength, suitable fluidity, small size of oil droplets without aggregation, dense network structure, and high surface hydrophobicity and amide A peak intensity and the low free sulfhydryl content. Thus, Ss endowed OEG with a certain viscoelasticity and mechanical strength, and caused massive aggregation of proteins through forming disulfide bonds, hydrophobic interactions, and hydrogen bonds. Aggregated ovalbumin and Ss formed a stable and strong network structure, emulsified oil droplets filled in the network, the three tightly crosslinked together to form an emulsion gel with excellent printing ability. This research offered the possibility of simultaneously printing complex structures, high-resolution patterns using food-based materials, also providing a theoretical basis for the design of complex and fine printed products.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"160 ","pages":"Article 110817"},"PeriodicalIF":11.0,"publicationDate":"2024-11-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142697944","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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