Food Structure-Netherlands最新文献

{"title":"Nutraceutical and toxicological evaluation of hydrogels architected using resistant starch nanoparticles and gum acacia for controlled release of kaempferol","authors":"Nairah Noor ,&nbsp;Faiza Jhan ,&nbsp;Adil Gani ,&nbsp;Irfan Ahmad Raina ,&nbsp;Mohammad Ashraf Shah","doi":"10.1016/j.foostr.2022.100307","DOIUrl":"10.1016/j.foostr.2022.100307","url":null,"abstract":"<div><p><span><span>Resistant starch<span> nanoparticles (RSN) were obtained using ultrasonication. RSN displayed a hydrodynamic diameter of 345.12 ± 0.01 nm and </span></span>zeta potential of 16.78 ± 0.04 mV. A bio composite hydrogel (RSNG) was formed by incorporating RSN of varying concentration (0.2%, 0.4% and 0.8%) in gum acacia (GA) to form resistant starch nanoparticle - gum acacia hydrogel, RSNG (0.2), RSNG (0.4) and RSNG (0.8), respectively. Kaempferol was nano encapsulated in RSNG (0.2%, 0.4% and 0.8%) for its controlled release. RSNG (0.4) displayed highest encapsulation efficiency of 61.23 ± 0.56% and in vitro release of kaempferol followed Higuchi model. Toxicity evaluation of RSN and RSNG revealed no effect on calf thymus DNA and human embryonic kidney (HEK-293 T) cells. The nutraceutical potential of RSNG showed retention of anti-oxidant, anti-diabetic, anti-hypertensive, anti-lipidemic and anti-microbial properties in simulated gastro-intestinal conditions (SGID). RSNG can efficiently encapsulate </span>flavonoids<span> and retain bioactivity in human digestive conditions that can be applied in food and pharmaceutical areas.</span></p></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"35 ","pages":"Article 100307"},"PeriodicalIF":4.7,"publicationDate":"2023-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"44750153","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Structural and colloidal properties of whey protein aggregates produced by indirect tubular heating and direct steam injection","authors":"Xiuju Wang,&nbsp;Zhengtao Zhao","doi":"10.1016/j.foostr.2022.100301","DOIUrl":"10.1016/j.foostr.2022.100301","url":null,"abstract":"<div><p>This research aimed to compare the structural and colloidal properties of whey protein aggregates (WPA) produced by indirect tubular heating and direct steam injection methods. The results illustrated that WPA produced from direct steam injection had better colloidal stability and functionality compared to those produced by indirect heating. WPA obtained from direct steam injection had smaller sizes and higher surface hydrophobicity, although they had a similar surface negative charge. More importantly, WPA from direct steam injection had much better colloidal stability. Especially for the sample produced by the direct steam injection containing a higher concentration of 30 %, which remained stable during 20 days’ storage. In comparison, precipitation was noticed after ten days for the sample with a lower concentration of 10 %, indicating the functionality and colloidal stability of WPA were also affected by the protein concentration. Those results demonstrated that the functionality of WPA can be tailored by selecting appropriate materials and manufacturing techniques.</p></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"35 ","pages":"Article 100301"},"PeriodicalIF":4.7,"publicationDate":"2023-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"46238817","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Editorial for 4th FSFS 2020","authors":"","doi":"10.1016/j.foostr.2022.100300","DOIUrl":"https://doi.org/10.1016/j.foostr.2022.100300","url":null,"abstract":"","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":" ","pages":""},"PeriodicalIF":4.7,"publicationDate":"2022-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"44127994","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Functionalising insoluble pea protein aggregates using high-pressure homogenisation: Effects on physicochemical, microstructural and functional properties","authors":"Kian Siang Ong ,&nbsp;Jie Hong Chiang ,&nbsp;Shaun Yong Jie Sim ,&nbsp;David Liebl ,&nbsp;Mufeeda Madathummal ,&nbsp;Christiani Jeyakumar Henry","doi":"10.1016/j.foostr.2022.100298","DOIUrl":"10.1016/j.foostr.2022.100298","url":null,"abstract":"<div><p>Commercial plant protein isolates contain a large fraction of non-functional proteins due to the harsh processing conditions used. Therefore, greater value can be unlocked by functionalising these “inert” plant proteins. Using commercial insoluble pea protein isolate (I-PPI) as an example, this study demonstrates the application of high-pressure homogenisation (HPH) as a physical method to improve the techno-functionality of I-PPI. The dispersions were HPH-treated at 60, 120, or 180 MPa for one, three, and five pressure cycles. HPH treatments resulted in decreased particle size (from 16.7 ± 1.3–9.4 ± 0.2 µm at 60 MPa) and increased zeta-potential. Microstructural observations revealed the formation of smaller aggregate clusters and flake-like structures after HPH treatments. The protein solubility of I-PPI (15.9 ± 2.0 %) under acidic conditions (pH 2) significantly increased at all HPH treatment levels, with the greatest increase at 120 MPa for 5 passes (27.2 ± 2.0 %). Remarkably, the non-gelling I-PPI was able to form self-standing gels (15 % w/w) after HPH treatments, with the greatest gel strength observed at 180 MPa. The emulsifying and foaming stability of HPH-treated I-PPI increased from 60 to 120 MPa but decreased at 180 MPa. Overall, our results demonstrate a key paradigm in protein modification: transforming insoluble plant proteins into functional protein ingredients.</p></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"34 ","pages":"Article 100298"},"PeriodicalIF":4.7,"publicationDate":"2022-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"49223909","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Editorial for 4th FSFS 2021","authors":"Andre Brodkorb","doi":"10.1016/j.foostr.2022.100300","DOIUrl":"https://doi.org/10.1016/j.foostr.2022.100300","url":null,"abstract":"","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"34 ","pages":"Article 100300"},"PeriodicalIF":4.7,"publicationDate":"2022-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71854037","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Ultrasonography assessment of gastric emptying for different emulsion microstructures was superior to acetaminophen marker method","authors":"Samar Hamad,&nbsp;Jacqueline Maw,&nbsp;Amanda J. Wright","doi":"10.1016/j.foostr.2022.100299","DOIUrl":"10.1016/j.foostr.2022.100299","url":null,"abstract":"<div><p>Gastric emptying (GE) influences postprandial metabolism, including satiety and is partially mediated by food structure. Tools for routine GE assessment and suitable for a range of food structures in metabolic studies are warranted. This study compared GE results from the acetaminophen absorption (plasma concentration) versus ultrasonography (US, gastric antrum area) methods when 15 healthy men consumed four oil-in-water emulsions differing in lipid physical state and emulsifier acid stability, meaning gastric phase behaviours differed. Plasma acetaminophen was only correlated with antrum measurements for the intragastrically stable emulsion with liquid lipid droplets (P = 0.041, r = −0.69). The US results support the role of colloidal stability in delaying GE and the images showed different gastric phase behaviours. In contrast, acetaminophen solubility confounded the results when the emulsions were susceptible to acidic flocculation. US antrum measurements (but not the acetaminophen results) were also correlated with participant subjective satiety (P &lt; 0.0001), supporting the close mediation of satiety perception by antral distention. Overall, US was superior to the acetaminophen method for assessing GE. It was easily implemented, provided visual insights into gastric phase behaviour, and predicted subjective satiety responses, allowing us to relate food structure and changes therein during digestion to metabolic response.</p></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"34 ","pages":"Article 100299"},"PeriodicalIF":4.7,"publicationDate":"2022-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"45228185","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Study of gellan gum films reinforced with eggshell nanoparticles for the elaboration of eco-friendly packaging","authors":"Benjamín Arredondo-Tamayo ,&nbsp;Juan Vicente Méndez-Méndez ,&nbsp;José Jorge Chanona-Pérez ,&nbsp;Josué David Hernández-Varela ,&nbsp;Lizbeth González-Victoriano ,&nbsp;Susana Dianey Gallegos-Cerda ,&nbsp;Eduardo Martínez-Mercado","doi":"10.1016/j.foostr.2022.100297","DOIUrl":"10.1016/j.foostr.2022.100297","url":null,"abstract":"<div><p><span>Development of eco-friendly materials based on biopolymers and agro-food waste has increased due to severe pollution caused using plastic materials. The aim of this work was to obtain nanoparticles by high-energy milling at different times (1–3 h) from eggshells as they are a source of </span>calcium carbonate<span><span> and was study using microscopy and spectroscopy techniques. Particle size distribution and mean particle size were determined. After 2 h of milling, the smallest particles (84 ± 40 nm, with 91 % ≤ 100 nm) were obtained. The effect of the addition of eggshell nanoparticles (ENP) at different concentrations (1–3 wt%) on different functional properties of gellan gum (GG) films was studied. The results indicated that addition of ENP (3 wt%) improves hydrophobic, water barrier, mechanical, and thermogravimetric properties of the ENP/GG film in comparison with GG film. X-ray diffraction analysis and infrared spectroscopy provided information to propose a descriptive model to explain the chemical interactions between ENP and GG. Consequently, the films could be used to fabricate eco-friendly materials for use in the </span>food sector in the elaboration of dishes and shockproof protective netting for delicate fruits.</span></p></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"34 ","pages":"Article 100297"},"PeriodicalIF":4.7,"publicationDate":"2022-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"43383675","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Complex coacervation of α-lactalbumin with gum arabic: Effect of environmental condition, mass ratio, and biopolymer concentration","authors":"Jiang Yi ,&nbsp;Dixue Luo ,&nbsp;Qingyu He ,&nbsp;Zhen Wen ,&nbsp;Yujuan Lu","doi":"10.1016/j.foostr.2022.100296","DOIUrl":"https://doi.org/10.1016/j.foostr.2022.100296","url":null,"abstract":"<div><p><span><span>The coacervate formation and interaction between α-lactalbumin (ALA) and gum arabic (GA) was investigated with turbidimetric analysis, fluorescence spectroscopy, atom force microscopy (AFM), and isothermal titration </span>calorimetry (ITC). Critical pH values (pH</span>_c, pH_φ1, pH_opt and pH_φ2<span><span>) of phase transitions for ALA-GA complexes (1:1, 0.1%, w/v) without NaCl, representing the formation of soluble and insoluble complexes, were 4.95, 3.85, 3.70, and 2.30, respectively. pH and NaCl concentrations are dominant in influencing the formation of ALA-GA complexes. AFM graphs evidently indicated the formation, association, and dissociation of ALA-GA complex. ITC results confirmed that the formation of soluble ALA/GA complex was a spontaneous exothermic process, and the electrostatic interaction between ALA and GA was stronger at pH 3.0 than that at pH 4.9 and 5.6. The obtained information of this study provides insights into the interaction between ALA and GA and expands the application of ALA-based formulations in </span>food systems with desirable functionality.</span></p></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"34 ","pages":"Article 100296"},"PeriodicalIF":4.7,"publicationDate":"2022-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71854038","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Structural, functional, and anti-cancer properties of conjugates of quinoa protein isolate and olive leaf polyphenolic extract: Application in production of bread","authors":"Mohammad Amin Aliyari ,&nbsp;Seyedeh Fatemeh Sadeghian Motahar ,&nbsp;Maryam Salami ,&nbsp;Mirko Betti ,&nbsp;Elnaz Hosseini ,&nbsp;Zahra Habibi-Kelishomi ,&nbsp;Bahram Goliaei ,&nbsp;Atiyeh Ghasemi","doi":"10.1016/j.foostr.2022.100292","DOIUrl":"10.1016/j.foostr.2022.100292","url":null,"abstract":"<div><p><span><span>Plant-based proteins are of growing interest in the food industry as an alternative to replace animal based ones, however, their functional properties are limited and research is needed in order to improve emulsifying, foaming, solubility properties. The objectives of the present study were to investigate the impacts of complexation between quinoa protein isolate (QPI) and different concentrations of olive leaf polyphenolic extract (OLE) (0.1 %, 0.2 %, 0.3 %, 0.4 %, and 0.5 %) on the structural changes, functional properties, and in-vitro gastric digestion of QPI. The cytotoxicity of the hydrolyzed QPI/OLE complex, in which proteins turn to </span>bioactive peptides<span>, was evaluated using human stomach cancer cell lines. Additionally, bread using optimum QPI/OLE complex was produced and textural, sensorial, and color properties were evaluated. Fluorescence quenching and surface hydrophobicity measurements showed that QPI and OLE were complexed mainly through hydrophobic interactions. SDS-PAGE revealed that the complexation between the protein and phenolic compounds<span> was appropriate and also complexes were highly digestible in stomach-like conditions. Additionally, OLE could enhance solubility, foaming as well as emulsification properties of QPI significantly. The rate of lipid hydroperoxide formation in QPI/OLE samples containing greater amounts of OLE was also reduced significantly. QPI/OLE complexes also exhibited a large potential to scavenge free radicals. </span></span></span><em>In-vitro</em> digestion experiment showed that the addition of OLE to the QPI solution promoted the production of bioactive peptides. According to the anti-cancer results, hydrolyzed QPI/OLE complexes exhibited a greater cell survival reduction in comparison to the OLE alone. Analysis of produced bread also revealed that the hardness of samples decreased with addition of QPI/OLE complexes. This study demonstrated that QPI/OLE complex shows the potential to be developed by food industry as a tailor-made functional food with health benefits.</p></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"33 ","pages":"Article 100292"},"PeriodicalIF":4.7,"publicationDate":"2022-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"46062582","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Effect of bleaching and defatting treatment of camel skin on the color, structural and interfacial properties of extracted gelatin","authors":"Samson Olumide Fawale ,&nbsp;Tholkappiyan Ramachandran ,&nbsp;Hamed Fathalla ,&nbsp;Sajid Maqsood","doi":"10.1016/j.foostr.2022.100275","DOIUrl":"https://doi.org/10.1016/j.foostr.2022.100275","url":null,"abstract":"<div><p>The effect of defatting and bleaching of camel skin on gel-forming, structural, and interfacial properties of extracted gelatin was studied. Gelatin defatted for 6 h and bleached for 48 h (48BD-6 h) gave the highest yield (28.44%) while gelatin bleached for 24 h (24 BC) gave the highest gel strength (423.3 g). Electrophoretic analysis showed that all gelatin samples had α-chains as the predominant protein type. Fourier transformation infrared (FTIR) spectroscopy showed that all gelatin samples possessed major peaks in the amide region with reduced peak intensity recorded in defatted and bleached samples because of the loss of the triple helix state of the gelatin. X-ray diffraction analysis indicated that all the gelatin samples are basically amorphous with both weak and sharp peaks observed around 7° and broad peaks at ~19–22°. Microstructural analysis revealed highly cross-linked network with less voids in all the gelatin samples which correlated with high gel strength recorded. Colour of the gelatin powder samples were significantly improved by bleaching with an increase in the <em>L</em>^∗-value and decrease in the <em>a</em>^∗-value. These results indicates that with bleaching, gelatin molecules were oxidized, resulting in the production of gelatin cross-links, giving gelatin an improved gel strength, colour, and functionality.</p></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"33 ","pages":"Article 100275"},"PeriodicalIF":4.7,"publicationDate":"2022-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71815027","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}