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Sum-weighted casein micelle AF4-UV-SAXS data disentangled - A new method for characterization and evaluation of widely size distributed samples 总加权酪蛋白胶束 AF4-UV-SAXS 数据分解 - 表征和评估粒度分布广泛的样品的新方法
IF 11 1区 农林科学 Q1 CHEMISTRY, APPLIED Pub Date : 2025-03-24 DOI: 10.1016/j.foodhyd.2025.111377
Hans Bolinsson , Martin Cramer Pedersen , Maria Glantz , Fátima Herranz-Trillo , Jacob Judas Kain Kirkensgaard , Lars Nilsson
Casein micelles are key structures in milk, influencing stability, nutritional properties, and functionality. Their hierarchical architecture, which is dynamic and responsive to environmental conditions, plays a crucial role in dairy processing. Understanding the structural and dynamic properties of casein micelles is essential for optimizing dairy products and processing techniques. This study presents a novel method for characterizing and evaluating casein micelles using a combination of Asymmetrical Flow Field-Flow Fractionation (AF4) and Small-Angle X-ray Scattering (SAXS) at synchrotron facilities. By coupling AF4 with SAXS, we can fractionate milk samples according to micelle size and gain insights into their structural organization. However, the high-throughput data generated in such experiments pose challenges for traditional data analysis. We introduce an automated data processing pipeline utilizing the McSAS software in combination with Indirect Fourier Transformation, allowing for efficient fitting of SAXS data and extraction of structural parameters such as radius of gyration (Rg) and maximum particle dimension (Dmax). This integrated approach provides a more detailed understanding of the heterogeneity and structural dynamics of casein micelles, revealing distinct features of their size distribution, internal cavities, and overall micelle structure across different fractions. The method offers a powerful tool for future investigations into the behavior of casein micelles under varying environmental conditions, with potential applications in optimizing dairy product formulations and studying casein micelle dynamics.
{"title":"Sum-weighted casein micelle AF4-UV-SAXS data disentangled - A new method for characterization and evaluation of widely size distributed samples","authors":"Hans Bolinsson ,&nbsp;Martin Cramer Pedersen ,&nbsp;Maria Glantz ,&nbsp;Fátima Herranz-Trillo ,&nbsp;Jacob Judas Kain Kirkensgaard ,&nbsp;Lars Nilsson","doi":"10.1016/j.foodhyd.2025.111377","DOIUrl":"10.1016/j.foodhyd.2025.111377","url":null,"abstract":"<div><div>Casein micelles are key structures in milk, influencing stability, nutritional properties, and functionality. Their hierarchical architecture, which is dynamic and responsive to environmental conditions, plays a crucial role in dairy processing. Understanding the structural and dynamic properties of casein micelles is essential for optimizing dairy products and processing techniques. This study presents a novel method for characterizing and evaluating casein micelles using a combination of Asymmetrical Flow Field-Flow Fractionation (AF4) and Small-Angle X-ray Scattering (SAXS) at synchrotron facilities. By coupling AF4 with SAXS, we can fractionate milk samples according to micelle size and gain insights into their structural organization. However, the high-throughput data generated in such experiments pose challenges for traditional data analysis. We introduce an automated data processing pipeline utilizing the McSAS software in combination with Indirect Fourier Transformation, allowing for efficient fitting of SAXS data and extraction of structural parameters such as radius of gyration (<em>R</em><sub><em>g</em></sub>) and maximum particle dimension (<em>D</em><sub><em>max</em></sub>). This integrated approach provides a more detailed understanding of the heterogeneity and structural dynamics of casein micelles, revealing distinct features of their size distribution, internal cavities, and overall micelle structure across different fractions. The method offers a powerful tool for future investigations into the behavior of casein micelles under varying environmental conditions, with potential applications in optimizing dairy product formulations and studying casein micelle dynamics.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"166 ","pages":"Article 111377"},"PeriodicalIF":11.0,"publicationDate":"2025-03-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143734512","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Physicochemical and functional comparison of food-grade and precision-fermented bovine lactoferrin
IF 11 1区 农林科学 Q1 CHEMISTRY, APPLIED Pub Date : 2025-03-24 DOI: 10.1016/j.foodhyd.2025.111380
Jonathan Cavallo, Jared Raynes , Samuel Mandacaru , Deepa Agarwal , Lloyd Condict, Stefan Kasapis
This study provided a comprehensive physicochemical and functional comparison between food-grade, commercially available bovine lactoferrin (cLF) and two precision-fermented variants (pfLF_highFe and pfLF_lowFe) at varying iron saturation levels. LC-MS and FTIR/CD spectroscopy confirmed high purity and structural fidelity at primary and secondary levels, while UV–vis analysis revealed comparable molar absorptivity across all preparations. Fluorescence spectroscopy demonstrated tertiary structural variability with redshifts observed as a result of iron binding. Molecular weight (Mw) comparisons made using SDS-PAGE showed pfLF_highFe and pfLF_lowFe closely resembled cLF, while glycosylation analysis demonstrated very similar N-glycan compositions and site occupancy across low iron samples. The isoelectric points (pI) of pfLF_highFe and pfLF_lowFe were similar to cLF; however, varied slightly as a function of iron saturation, as did surface hydrophobicity (S0) measurements. Thermal denaturation analyses revealed characteristic behaviour of bovine lactoferrin preparations, with differences again observed according to the preparation's iron saturation. Functional studies highlighted the iron chelating ability of native-LF preparations, cLF and pfLF_lowFe, and accompanying antimicrobial activity, but comparable interaction capacity with Lipid A (LPS) demonstrates preservation of structural and certain functional capabilities in precision-fermented bovine lactoferrin irrespective of iron saturation levels.
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引用次数: 0
Microfibrillated cellulose derived from Gelidium amansii controls the thermo-physical properties of emulsion gel composite as the base for cheese alternative 从鹅掌楸中提取的微纤维素可控制作为奶酪替代品基质的乳液凝胶复合材料的热物理性质
IF 11 1区 农林科学 Q1 CHEMISTRY, APPLIED Pub Date : 2025-03-24 DOI: 10.1016/j.foodhyd.2025.111376
Nur Istianah , Ju Hyun Min , Teti Estiasih , Widya Dwi Rukmi Putri , Sri Suhartini , Young Hoon Jung
The utilization of microfibrillated cellulose (MFC) in a Pickering emulsion has become popular recently. However, its application on semi-solid emulsion gel (EG) for cheese structuring has not been invented yet. This study aimed to investigate the effect of Gelidium amansii-derived MFC addition on the thermo-physical properties of EG composite as the ingredient for vegan cheese manufacture. MFC and isolated soy protein (ISP) were incorporated in the EG composites at the concentration levels of 0–1.0 % wt. and 5–30 % wt. accordingly. As a result, the interaction of MFC and ISP could increase the emulsion gel network through the oil droplets bridging and stabilizing under the microfibrillar network of MFC. Higher MFC concentration improves gel stability and texture but reduces the lightness and meltability at a particular ISP level. The prepared cheese model using the selected EG composite (MFC 0.25 % - ISP 15 %) and corn starch hydrogel has a close color, texture, and meltability compared to the commercial dairy sliced cheese. In conclusion, MFC has a critical role in regulating the thermo-physical properties of EG–based cheese alternatives.
近来,在皮克林乳液中使用微纤维素(MFC)已成为一种流行趋势。然而,将其应用于奶酪结构的半固态乳液凝胶(EG)还没有被发明出来。本研究旨在探究添加 Gelidium amansii 衍生的 MFC 对 EG 复合材料热物理性质的影响。MFC 和分离大豆蛋白(ISP)在 EG 复合材料中的添加浓度分别为 0-1.0 %(重量百分比)和 5-30 %(重量百分比)。结果表明,MFC 和 ISP 的相互作用可通过油滴在 MFC 的微纤维网络下架桥和稳定来增加乳液凝胶网络。MFC 浓度越高,凝胶稳定性和质地越好,但在特定的 ISP 水平下,轻度和可熔性会降低。使用选定的 EG 复合材料(MFC 0.25 % - ISP 15 %)和玉米淀粉水凝胶制备的奶酪模型在颜色、质地和可熔性方面与商用乳制品切片奶酪非常接近。总之,MFC 在调节基于 EG 的奶酪替代品的热物理性质方面起着至关重要的作用。
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引用次数: 0
Exploring the interfacial behavior and foam characteristics of various soy protein aggregates: Insights of morphology and conformational flexibility
IF 11 1区 农林科学 Q1 CHEMISTRY, APPLIED Pub Date : 2025-03-22 DOI: 10.1016/j.foodhyd.2025.111362
Ruihan Su , Xueqing Zhang , Jia Cao , Tianhe Xu , Shi Liu , Huriga Zhang , Di Wu , Zhe Wang , Xiaohong Tong , Huan Wang , Lianzhou Jiang
This study investigates the morphology differences and structural flexibility of different soy protein aggregates, and examines their disparities in interfacial and foam characteristics at across pH levels. The results indicated substantial variations in the morphology of the aggregates, resulting in a notable alteration in their flexibility. The soy protein fibrils (SPF) demonstrated superior molecular flexibility relative to the other aggregates, demonstrating maximum flexibility (A280 nm = 0.35) at pH 9. Soy protein fractal aggregates (SPA) exhibited a rigid structure at all pH levels because of the elevated presence of disulfide bonds, α-helixs, and β-sheets. The reduced particle size and elevated presence of irregular convolutions resulted in significantly greater molecular flexibility of the soy protein nanoparticles (SPN) in comparison to SPI. SPN exhibited the second highest flexibility following SPF, was distinguished by tiny particle size and homogenous dispersion, and demonstrated optimal flexibility at pH 9. Furthermore, SPF-9 displayed the lowest interfacial tension (39.29 mN/m), the best solubility (97.54 %), and the foaming ability (180.00 %). And SPN-9 demonstrated the best foam stability. It was ascertained that the interfacial properties and foaming ability of aggregates were positively correlated with their molecular flexibility and that alterations in the morphology and structure of aggregates could impact the flexibility of proteins and thereby enhance the interfacial functional properties. The outcomes of this study establish a theoretical foundation for the application of soy protein in foam-based meals.
本研究调查了不同大豆蛋白聚合体的形态差异和结构灵活性,并研究了它们在不同 pH 值下的界面和泡沫特性差异。研究结果表明,聚合体的形态存在很大差异,导致其柔韧性发生显著变化。大豆蛋白纤维(SPF)的分子柔韧性优于其他聚合体,在 pH 值为 9 时表现出最大柔韧性(A280 nm = 0.35)。 大豆蛋白分形聚合体(SPA)由于二硫键、α-螺旋和 β-片的含量增加,在所有 pH 值下都表现出刚性结构。与 SPI 相比,大豆蛋白纳米粒子(SPN)的粒径减小,不规则卷曲增加,因此分子柔韧性明显提高。此外,SPF-9 显示出最低的界面张力(39.29 mN/m)、最佳的溶解度(97.54 %)和发泡能力(180.00 %)。SPN-9 的泡沫稳定性最好。研究结果表明,聚合体的界面特性和发泡能力与其分子柔韧性呈正相关,聚合体形态和结构的改变会影响蛋白质的柔韧性,从而提高界面功能特性。这项研究成果为大豆蛋白在泡沫膳食中的应用奠定了理论基础。
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引用次数: 0
Seaweeds biorefinery into pigments and carrageenans: Testing a sequential extractions approach
IF 11 1区 农林科学 Q1 CHEMISTRY, APPLIED Pub Date : 2025-03-22 DOI: 10.1016/j.foodhyd.2025.111374
Gabriela Gonçalves , Izabel Cristina Freitas Moraes , Bruno Faria , Loic Hilliou
This study aims to test a sequential extraction (SE) method for red seaweeds (Chondrus crispus, Mastocarpus stellatus, Gigartina pistillata). The tested SE is a preliminary screening step towards the extrusion-based biorefinery (E2B2) of carrageenophytes into various natural products, a concept that still needs to be established. Phycobiliproteins, chlorophyll-a, carotenoids, and hybrid-carrageenans (HK) were isolated with the following sequence: cold-water extraction (CWE), ethanolic extraction (EE), hot water extraction (HWE), and hot alkaline extraction (HAE). HK chemical structures and gelling properties were systematically compared with those of carrageenans isolated from direct extractions (controls). Such comparison, which is critically missing in earlier SE studies, allows to assess the impact of prior extraction sequences on such HK properties. SE effectively separated algal components, facilitating the recovery of HK, particularly with M. stellatus and G. pistillata, with superior gel elasticity and viscosity compared to the controls. HWE yielded less sulphated HK with higher molecular masses and enhanced gelling properties. HAE extracts exhibited lower molecular masses and reduced gelation potential due to the prior HWE sequence. Prolonged extraction generally improved molecular masses and gels elasticity, although a distinct trend was found with C. crispus. The results from this preliminary screening suggest that M. stellatus is not a good candidate for testing in E2B2.
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引用次数: 0
Food-grade 3D-Printable porous scaffolds with advanced stem cell microenvironments enabled by bilayer emulgel
IF 11 1区 农林科学 Q1 CHEMISTRY, APPLIED Pub Date : 2025-03-21 DOI: 10.1016/j.foodhyd.2025.111373
Yuxing Gao , Hongwei Zheng , Qing Kong , Xianchao Feng , Zhaojie Li , Changhu Xue
Porous scaffolds represent promising materials for applications in tissue engineering and cell-cultured meat production. Nevertheless, existing efforts have struggled to achieve a satisfactory balance between edibility, scaffold stiffness, and the behavior of stem cells cultured on these scaffolds. In this study, we introduce bilayer emulgel as a mean of creating 3D-printable porous scaffolds using bio-based materials derived from nature, specifically pea protein and chitin. By incorporating the spray of CaCl2 solution during the 3D printing process, we achieve exceptional fidelity in the precursor architecture of the scaffolds. The resulting scaffolds, with adjustable pore structures, effectively support the cellular behaviors such as adhesion, proliferation, and differentiation of stem cells. Interestingly, apart from the advancement of emulsifying capability, the addition of chitin nanocrystals can significantly enhance the physical properties and biological performance of the scaffolds based on 11S amyloid fibrils. These 3D-printed scaffolds, serving as ideal materials, offer advanced microenvironments for stem cells, thereby advancing the fields of tissue engineering and cell-cultured meat production.
多孔支架是应用于组织工程和细胞培养肉类生产的前景广阔的材料。然而,现有的研究一直在努力实现可食性、支架硬度和在这些支架上培养的干细胞行为之间令人满意的平衡。在本研究中,我们引入了双层凝胶,利用从大自然中提取的生物基材料(特别是豌豆蛋白和甲壳素)来创建可三维打印的多孔支架。通过在三维打印过程中喷洒 CaCl2 溶液,我们实现了支架前体结构的卓越保真度。由此产生的支架具有可调节的孔隙结构,能有效支持干细胞的粘附、增殖和分化等细胞行为。有趣的是,除了提高乳化能力外,添加甲壳素纳米晶体还能显著提高基于11S淀粉样纤维的支架的物理性质和生物学性能。这些三维打印支架作为理想的材料,为干细胞提供了先进的微环境,从而推动了组织工程和细胞培养肉类生产领域的发展。
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引用次数: 0
Tailored zein-polysaccharide nanoparticles for anthocyanin encapsulation: Insights into preparation and characterization
IF 11 1区 农林科学 Q1 CHEMISTRY, APPLIED Pub Date : 2025-03-21 DOI: 10.1016/j.foodhyd.2025.111365
Wen Tao , Isabel M.P.L.V.O. Ferreira , Jingren He , Victor de Freitas , Nuno Mateus , Hélder Oliveira , Ana Fernandes
Encapsulation is a promising strategy to increase the physicochemical stability of anthocyanins (ACNs). In this work, red cabbage anthocyanins-loaded composite nanoparticles were prepared by the self-assembly of zein protein and anionic polysaccharides. Three anionic polysaccharides and two types of preparation approaches were used to form different ACNs-loaded zein/polysaccharide nanoparticles. Results revealed that ACNs-loaded zein/polysaccharide nanoparticles showed spherical morphology with an average particle size in the range of 102.6–360.4 nm, polydispersity index of 0.214–0.415, zeta potential of - (26.7–42.6) mV and the total ACNs encapsulation efficiency (EE) of 68.03–80.55 %, depending on the type of polysaccharides and the different adding sequences of the raw materials. Polysaccharides coating increased the EEs of ACNs as compared to the zein alone. ACNs monomers with acylated groups presented higher EEs. ATR-FTIR spectrum indicated hydrogen bonds, hydrophobic and electrostatic interactions were the dominant forces among ACNs, zein and polysaccharides. In addition, ACNs-loaded zein/polysaccharide nanoparticles showed good colloidal stability to different pH, ionic strength and storage conditions as compared to ACNs-loaded zein nanoparticles due to the electrostatic and steric repulsion from the polysaccharide coating on the nanoparticle surface.
{"title":"Tailored zein-polysaccharide nanoparticles for anthocyanin encapsulation: Insights into preparation and characterization","authors":"Wen Tao ,&nbsp;Isabel M.P.L.V.O. Ferreira ,&nbsp;Jingren He ,&nbsp;Victor de Freitas ,&nbsp;Nuno Mateus ,&nbsp;Hélder Oliveira ,&nbsp;Ana Fernandes","doi":"10.1016/j.foodhyd.2025.111365","DOIUrl":"10.1016/j.foodhyd.2025.111365","url":null,"abstract":"<div><div>Encapsulation is a promising strategy to increase the physicochemical stability of anthocyanins (ACNs). In this work, red cabbage anthocyanins-loaded composite nanoparticles were prepared by the self-assembly of zein protein and anionic polysaccharides. Three anionic polysaccharides and two types of preparation approaches were used to form different ACNs-loaded zein/polysaccharide nanoparticles. Results revealed that ACNs-loaded zein/polysaccharide nanoparticles showed spherical morphology with an average particle size in the range of 102.6–360.4 nm, polydispersity index of 0.214–0.415, zeta potential of - (26.7–42.6) mV and the total ACNs encapsulation efficiency (EE) of 68.03–80.55 %, depending on the type of polysaccharides and the different adding sequences of the raw materials. Polysaccharides coating increased the EEs of ACNs as compared to the zein alone. ACNs monomers with acylated groups presented higher EEs. ATR-FTIR spectrum indicated hydrogen bonds, hydrophobic and electrostatic interactions were the dominant forces among ACNs, zein and polysaccharides. In addition, ACNs-loaded zein/polysaccharide nanoparticles showed good colloidal stability to different pH, ionic strength and storage conditions as compared to ACNs-loaded zein nanoparticles due to the electrostatic and steric repulsion from the polysaccharide coating on the nanoparticle surface.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"166 ","pages":"Article 111365"},"PeriodicalIF":11.0,"publicationDate":"2025-03-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143724376","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Heat-induced dissociation and association of proteins in hempseed protein bodies
IF 11 1区 农林科学 Q1 CHEMISTRY, APPLIED Pub Date : 2025-03-21 DOI: 10.1016/j.foodhyd.2025.111372
Duc Toan Do, Aiqian Ye, Harjinder Singh, Alejandra Acevedo-Fani
Protein bodies (PBs) are naturally occurring storage organelles in seeds. In hempseeds, the major storage proteins, including edestin (11S globulin) and albumin, are primarily located in the crystalloids and proteinaceous matrices of hemp protein bodies (HPBs), respectively. The retention of native PB structures in flours and dry-fractionated protein ingredients has important implications for protein functionality and digestibility, especially when heat treatment is applied during processing. While the thermal behaviour of hempseed proteins has been studied in protein isolate systems, to the best of our knowledge, it has not yet been explored in HPB systems. In this study, we isolated native HPBs using an enzymatic method. Aqueous suspensions of HPBs (4 % protein, w/w) were heated at selected temperatures (60–100 °C) and pH 7 for 20 min, followed by hydrolysis with trypsin at pH 7 and 37 °C for 120 min. The thermal aggregation of proteins in HPBs was characterised using confocal laser scanning microscopy (CLSM) and sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE). The hydrolysis of HPBs by trypsin was monitored over 120 min by measuring the degree of protein hydrolysis (DH) and analysing SDS-PAGE. Aggregation of edestin in HPBs, primarily driven by disulfide bond formation, occurred upon heating, most noticeably at temperatures above 80 °C. Heating increased DH and altered protein degradation patterns of both acidic and basic subunits of edestin. This may be related to conformational changes in the HPB structure resulting from heat-induced dissociation-association of multiple HPB protein fractions, including 11S edestin, 7S globulin, and 2S albumin. These findings contribute to our understanding of the structure-hydrolysis relationships of HPBs, potentially leading to their use as a new plant-based material for food applications.
{"title":"Heat-induced dissociation and association of proteins in hempseed protein bodies","authors":"Duc Toan Do,&nbsp;Aiqian Ye,&nbsp;Harjinder Singh,&nbsp;Alejandra Acevedo-Fani","doi":"10.1016/j.foodhyd.2025.111372","DOIUrl":"10.1016/j.foodhyd.2025.111372","url":null,"abstract":"<div><div>Protein bodies (PBs) are naturally occurring storage organelles in seeds. In hempseeds, the major storage proteins, including edestin (11S globulin) and albumin, are primarily located in the crystalloids and proteinaceous matrices of hemp protein bodies (HPBs), respectively. The retention of native PB structures in flours and dry-fractionated protein ingredients has important implications for protein functionality and digestibility, especially when heat treatment is applied during processing. While the thermal behaviour of hempseed proteins has been studied in protein isolate systems, to the best of our knowledge, it has not yet been explored in HPB systems. In this study, we isolated native HPBs using an enzymatic method. Aqueous suspensions of HPBs (4 % protein, w/w) were heated at selected temperatures (60–100 °C) and pH 7 for 20 min, followed by hydrolysis with trypsin at pH 7 and 37 °C for 120 min. The thermal aggregation of proteins in HPBs was characterised using confocal laser scanning microscopy (CLSM) and sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE). The hydrolysis of HPBs by trypsin was monitored over 120 min by measuring the degree of protein hydrolysis (DH) and analysing SDS-PAGE. Aggregation of edestin in HPBs, primarily driven by disulfide bond formation, occurred upon heating, most noticeably at temperatures above 80 °C. Heating increased DH and altered protein degradation patterns of both acidic and basic subunits of edestin. This may be related to conformational changes in the HPB structure resulting from heat-induced dissociation-association of multiple HPB protein fractions, including 11S edestin, 7S globulin, and 2S albumin. These findings contribute to our understanding of the structure-hydrolysis relationships of HPBs, potentially leading to their use as a new plant-based material for food applications.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"166 ","pages":"Article 111372"},"PeriodicalIF":11.0,"publicationDate":"2025-03-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143706261","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}
引用次数: 0
Conjugation of flaxseed protein and plant polysaccharides: Process optimization, structural characterization and technical-function evaluation
IF 11 1区 农林科学 Q1 CHEMISTRY, APPLIED Pub Date : 2025-03-20 DOI: 10.1016/j.foodhyd.2025.111371
Ziqin Ye , Shengrui Gan , Jinying Wang, Furong Yang, Guoxin Dong
In this study, the covalent conjugation conditions of flaxseed protein isolate (FPI) with flaxseed gum (FG), oat β-glucan (BG), and soybean polysaccharide (SP) were optimized separately using the ultrasound-assisted (U) method. The effects of the conjugation on the structure, function, and antioxidant properties of FPI were explored based on the optimal conditions. The results showed that the infrared absorption peaks of FPI in each sample changed and shifted in amide I and II bands after conjugation, indicating the progression of the Maillard reaction. Fluorescence intensity decreased and red-shifted emission peaks (10–15 nm), suggesting increased protein unfolding and improved hydrophilic interactions. Moreover, conjugation decreased the intensity of the UV absorption peaks, with the maximum absorption shifting to shorter wavelengths. Further validated the structural modifications associated with the Maillard reaction. Ultrasound-assisted conjugation also improved the functional properties in all samples, especially FPI-FG-U showed the best foaming capacity (improved to 80.39 %) and emulsification activity and stability (increased to 64.95 m2/g and 51.80 %), confirmed the correlation between structural changes and functional improvements. ABTS+ and DPPH radical scavenging experiments showed that the antioxidant capacity of FPI was enhanced by covalent conjugation. This study shows that the functional performance of FPI can be extended by covalently linking a combination of sonication, thus broadening their potential uses in the food sector and beyond.
{"title":"Conjugation of flaxseed protein and plant polysaccharides: Process optimization, structural characterization and technical-function evaluation","authors":"Ziqin Ye ,&nbsp;Shengrui Gan ,&nbsp;Jinying Wang,&nbsp;Furong Yang,&nbsp;Guoxin Dong","doi":"10.1016/j.foodhyd.2025.111371","DOIUrl":"10.1016/j.foodhyd.2025.111371","url":null,"abstract":"<div><div>In this study, the covalent conjugation conditions of flaxseed protein isolate (FPI) with flaxseed gum (FG), oat β-glucan (BG), and soybean polysaccharide (SP) were optimized separately using the ultrasound-assisted (U) method. The effects of the conjugation on the structure, function, and antioxidant properties of FPI were explored based on the optimal conditions. The results showed that the infrared absorption peaks of FPI in each sample changed and shifted in amide I and II bands after conjugation, indicating the progression of the Maillard reaction. Fluorescence intensity decreased and red-shifted emission peaks (10–15 nm), suggesting increased protein unfolding and improved hydrophilic interactions. Moreover, conjugation decreased the intensity of the UV absorption peaks, with the maximum absorption shifting to shorter wavelengths. Further validated the structural modifications associated with the Maillard reaction. Ultrasound-assisted conjugation also improved the functional properties in all samples, especially FPI-FG-U showed the best foaming capacity (improved to 80.39 %) and emulsification activity and stability (increased to 64.95 m<sup>2</sup>/g and 51.80 %), confirmed the correlation between structural changes and functional improvements. ABTS<sup>+</sup> and DPPH radical scavenging experiments showed that the antioxidant capacity of FPI was enhanced by covalent conjugation. This study shows that the functional performance of FPI can be extended by covalently linking a combination of sonication, thus broadening their potential uses in the food sector and beyond.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"166 ","pages":"Article 111371"},"PeriodicalIF":11.0,"publicationDate":"2025-03-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143706259","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}
引用次数: 0
Improving rheology and 3D printability of pea, fava and mung bean proteins with raw and fermented millet flour
IF 11 1区 农林科学 Q1 CHEMISTRY, APPLIED Pub Date : 2025-03-20 DOI: 10.1016/j.foodhyd.2025.111369
Saphal Ghimire , Muhammad Umar , Chaiwut Gamonpilas , Anil Kumar Anal
This study aims to enhance the rheological, 3D printing, textural, and nutritional properties of meat analogs by adding the raw and fermented finger millet (RFM and FFM) flour in pea, fava, and mung bean protein isolates (PPI, FPI, and MPI). The gel strength of all samples increased significantly by increasing the protein concentration. The tanδ values for all samples were below 1 (0.16–0.26) indicating elastic and solid-like behavior (G’ > G″). Frequency index increased for FPI (0.09–0.12), PPI (0.10–0.12), and MPI (from 0.10 to 0.13 for) based samples containing both RFM and FFM. The yield stress increased for FPR (111.34–128.47 Pa), FPF (122.73–132.1 Pa), PPR (93.37–166.39 Pa), PPF (126.31–180.4 Pa), MPR (46.17–162.93 Pa), MPF (86.12–189.28 Pa). The optimal formulation in terms of printing, smoothness, texture, and post-processing design retention for all protein-based inks was at finger millet flour to protein ratio of 1:4. However, the MPI-based samples exhibited superior characteristics of elasticity, shear thinning behavior, printing performance, frying stability, and texture. The structural analysis confirmed the higher interactions between FFM flour and proteins, enhancing rheological and textural properties. The protein digestibility values of the analogs ranged from 81.8 % to 91.2 %, with MPI samples exhibiting the highest protein digestibility. This research highlights the potential of utilizing lesser-known cereals to create edible and nutritious analogs through 3D printing.
{"title":"Improving rheology and 3D printability of pea, fava and mung bean proteins with raw and fermented millet flour","authors":"Saphal Ghimire ,&nbsp;Muhammad Umar ,&nbsp;Chaiwut Gamonpilas ,&nbsp;Anil Kumar Anal","doi":"10.1016/j.foodhyd.2025.111369","DOIUrl":"10.1016/j.foodhyd.2025.111369","url":null,"abstract":"<div><div>This study aims to enhance the rheological, 3D printing, textural, and nutritional properties of meat analogs by adding the raw and fermented finger millet (RFM and FFM) flour in pea, fava, and mung bean protein isolates (PPI, FPI, and MPI). The gel strength of all samples increased significantly by increasing the protein concentration. The tanδ values for all samples were below 1 (0.16–0.26) indicating elastic and solid-like behavior (G’ &gt; G″). Frequency index increased for FPI (0.09–0.12), PPI (0.10–0.12), and MPI (from 0.10 to 0.13 for) based samples containing both RFM and FFM. The yield stress increased for FPR (111.34–128.47 Pa), FPF (122.73–132.1 Pa), PPR (93.37–166.39 Pa), PPF (126.31–180.4 Pa), MPR (46.17–162.93 Pa), MPF (86.12–189.28 Pa). The optimal formulation in terms of printing, smoothness, texture, and post-processing design retention for all protein-based inks was at finger millet flour to protein ratio of 1:4. However, the MPI-based samples exhibited superior characteristics of elasticity, shear thinning behavior, printing performance, frying stability, and texture. The structural analysis confirmed the higher interactions between FFM flour and proteins, enhancing rheological and textural properties. The protein digestibility values of the analogs ranged from 81.8 % to 91.2 %, with MPI samples exhibiting the highest protein digestibility. This research highlights the potential of utilizing lesser-known cereals to create edible and nutritious analogs through 3D printing.</div></div>","PeriodicalId":320,"journal":{"name":"Food Hydrocolloids","volume":"166 ","pages":"Article 111369"},"PeriodicalIF":11.0,"publicationDate":"2025-03-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143682578","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}
引用次数: 0
期刊
Food Hydrocolloids
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