Food Structure-Netherlands最新文献

{"title":"Production of 3D-printed meat analogues using pea, fava, and mung bean proteins: A comparison study","authors":"Saphal Ghimire ,&nbsp;Chaiwut Gamonpilas ,&nbsp;Muhammad Umar ,&nbsp;Anil Kumar Anal","doi":"10.1016/j.foostr.2025.100419","DOIUrl":"10.1016/j.foostr.2025.100419","url":null,"abstract":"<div><div>The demand of plant-based proteins has increased in the last decade due to several factors such as sustainability, nutritional value, health, and cost concerns. This study aims to assess the functional, rheological, and 3D printing performances of pea protein isolate (PPI), fava protein isolate (FPI), and mung bean protein isolate (MPI)-based edible inks to develop plant-based meat analogues. The water and oil absorption capacity and water solubility index of all samples were significantly different (<em>p</em> &lt; 0.05). The storage modulus, loss modulus, yield stress, and gel strength increased for all inks with increasing the protein concentration. The values of loss tangent within the linear viscoelastic region were in the range of 0.21–0.27 for all samples, indicating the elastic behavior of these inks. The flow behavior index for all edible inks was less than 1, confirming the shear-thinning behavior. The sample with a protein-to-water ratio of 1:2.5, exhibited optimal rheological characteristics for all proteins in terms of printing smoothness and design retention post-processing. Specifically, the mung bean protein-based samples exhibited superior characteristics of elasticity, shear thinning behavior, printing performance, frying stability, and textural properties. All these formulations possess the potential to cater to the growing demand in the alternative proteins market.</div></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"44 ","pages":"Article 100419"},"PeriodicalIF":5.6,"publicationDate":"2025-03-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143725674","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":"Extraction and functional properties modification of guar protein isolates by ultrasound: A promising alternative protein","authors":"Geetarani Liklam Loushigam ,&nbsp;T.P. Sari ,&nbsp;Prarabdh C. Badgujar ,&nbsp;Mahesh Shivanand Dige ,&nbsp;Sunil Pareek","doi":"10.1016/j.foostr.2025.100420","DOIUrl":"10.1016/j.foostr.2025.100420","url":null,"abstract":"<div><div>This study investigated the potential of ultrasound-assisted extraction (UAE) (at 150 W, 250 W, and 350 W for 5–15 min) to isolate proteins from guar meal and its impact on structural and functional modifications of guar protein isolate (GPI). The optimized UAE treatment at 250W-10 min enhanced protein yield (14.36–16.62 %), solubility (22.27–44.55 %), foaming stability (50.95–78.77 %), emulsion activity (130.69–163.36 m²/g), and stability (26.95–56.44 min) compared with control. Surface hydrophobicity and total sulfhydryl content increased (3471–5183 and 28.90–36.76 μmol/g); while, particle size (402.5–298.36 nm) and zeta potential (–16.53 to –38.23 mV) decreased evincing significant improvements (<em>P &lt; 0.05</em>) over the control. Secondary and tertiary structural alterations evident in GPI treated at 250W-10min were further validated by SEM and SDS-PAGE results. Optimized UAE treatment exhibited significantly improved protein digestibility (70.51–85.19 %) with consequently enhanced PDCAAS (44.63–52.29 %) compared to control GPI. UAE treatment did not negatively change GPI’s chemical structure ensuing 100 % cell viability in cytotoxicity assay. These findings demonstrated effectiveness of ultrasonication in enhancing GPI’s functional properties, paving way for its potential applications in human food/nutraceuticals than the current use as low value cattle feed byproduct.</div></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"44 ","pages":"Article 100420"},"PeriodicalIF":5.6,"publicationDate":"2025-03-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143698039","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":"How differences in rice texture and oral physiology affect sensory preference and eating behavior of consumers: A generalized additive models (GAMs) approach","authors":"Zhen Zhao ,&nbsp;Zuo Wang ,&nbsp;Jingye Zhu ,&nbsp;Ancha Xu ,&nbsp;David Julian McClements ,&nbsp;Jianshe Chen ,&nbsp;Yong Chen","doi":"10.1016/j.foostr.2025.100418","DOIUrl":"10.1016/j.foostr.2025.100418","url":null,"abstract":"<div><div>Both food texture and human oral physiology impact consumer preferences and eating behavior. However, the complex relationships between these factors are difficult to explain using simple mathematical models. For this reason, the potential of a generalized additive model (GAM) to relate food texture to oral physiology during the development of healthier foods was investigated. This semiparametric model combines the advantages of both parametric and nonparametric models. The oral behavior of a modified Japonica rice (JM), a low glycemic index (GI) food rich in resistant starch, was compared to that of regular Japonica rice (JR). Both JM and JR were cooked at three water-to-rice (W/R) ratios (low, recommended, high) to obtain samples with different textural properties. The oral physiological parameters of seventeen participants were measured, including biting force and saliva properties. Furthermore, time-intensity (TI) analysis, video recording and electromyography (EMG) were used to provide multiple dynamic sensory analyses. JM required more chewing cycles and longer chewing durations than JR, due to its firmer textural attributes. Linear GAM analysis demonstrated that high hardness and low stickiness of rice led to more chews, chewing duration, and muscle activities, raising the oral processing load and lowering consumer overall liking scores. Additionally, nonlinear GAM analysis indicated that average saliva flow rate and mucin concentration were negatively correlated with both chewing frequency and duration. A simulated gastrointestinal model showed that JM was digested more slowly than JR. In summary, this study provided valuable insights for optimizing the sensory attributes of high-resistant starch rice to enhance its palatability and consumer acceptance.</div></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"44 ","pages":"Article 100418"},"PeriodicalIF":5.6,"publicationDate":"2025-03-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143686790","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":"Plant proteins as substitutes for egg white protein in food foams: Meringues as a model system","authors":"Nadia Flarup Laursen ,&nbsp;Gil Makiel Nielsen ,&nbsp;Magnus Bergholdt Jul Christiansen ,&nbsp;Ruifen Li ,&nbsp;Milena Corredig ,&nbsp;Claus Hviid Christensen","doi":"10.1016/j.foostr.2025.100417","DOIUrl":"10.1016/j.foostr.2025.100417","url":null,"abstract":"<div><div>This study evaluated the properties of selected plant proteins as substitutes for egg white proteins in a model meringue batter. Different protein ingredients, namely wheat protein hydrolysate, potato protein, and aquafaba, were evaluated and compared with traditional egg whites. Both individual and mixed systems were investigated to assess the potential for partial or full replacement of egg white protein. Meringue batters made with egg white protein exhibited lower densities and greater overrun than those made solely with plant protein alternatives. However, when egg white protein was partially replaced with aquafaba and potato protein, comparable foaming properties were observed. A meringue batter composed purely of wheat protein hydrolysate displayed rapid foam formation but low stability. Foaming studies were conducted with and without sucrose, revealing important differences in the presence of sugar. With potato protein and aquafaba, foam volume decreased faster in the presence of sucrose. In contrast, sucrose enhanced foam stability in egg white protein and wheat protein hydrolysate solutions. These findings highlight the potential of plant proteins as substitutes for egg white protein in food foams, providing a foundation for further fundamental research. While promising, more comprehensive analyses and clearer guidance for practical applications would help strengthen both the academic and applied relevance of this work, particularly for future applications in bakery and confectionery products.</div></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"44 ","pages":"Article 100417"},"PeriodicalIF":5.6,"publicationDate":"2025-03-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143644919","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Behavior of common beans under two conditions of water accessibility during cooking: Essential role of pectin solubilization in bean softening","authors":"Nguyen T.H. An ,&nbsp;Annu Mathew ,&nbsp;Henry Tafiire ,&nbsp;Ann Van Loey ,&nbsp;Marc E. Hendrickx","doi":"10.1016/j.foostr.2025.100416","DOIUrl":"10.1016/j.foostr.2025.100416","url":null,"abstract":"<div><div>This study explores the softening behavior of beans during cooking at 95 °C under two conditions of water accessibility during the cooking process: water limited to the level attained in fully soaked beans and excess water (conventional cooking). We examined changes in texture (hardness) and pectin solubilization, where strongly bound pectin is converted to loosely bound pectin. Limited-water cooking (LWC) reduced pectin solubilization by half compared to conventional cooking, resulting in a (s)lower decline in bean hardness. A strong negative correlation (<em>r</em> = −0.977; <em>p</em> &lt; 0.0001) between relative pectin solubilization and relative hardness emphasizes the critical role of pectin solubilization in regulating softening behavior. Despite the difference in water accessibility, both cooking methods required pectin solubilization to a similar extent to obtain comparable bean hardness. Microscopic analysis revealed LWC beans had minimal cell separation (6.84 %) and limited cell expansion (6829 µm²). In contrast, excess water in conventional cooking promoted substantial cell separation (12.43 %) and cell expansion (8716 µm²). Conventional cooking also causes swelling and disruption of starch granules, evidenced by the partial starch leaching into the cellular content. The study demonstrates that water accessibility critically influences pectin solubilization during cooking, directly impacting both the micro- and macroscopic structural properties of beans.</div></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"44 ","pages":"Article 100416"},"PeriodicalIF":5.6,"publicationDate":"2025-03-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143644918","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":"Properties of processed cheese made from cagliata cheese: Influence of fat content and ripening of cagliata cheese and homogenization of cheese milk","authors":"Gaurav Kr Deshwal ,&nbsp;Liesbeth van der Meulen ,&nbsp;Mark Fenelon ,&nbsp;Laura G. Gómez-Mascaraque ,&nbsp;Thom Huppertz","doi":"10.1016/j.foostr.2025.100406","DOIUrl":"10.1016/j.foostr.2025.100406","url":null,"abstract":"<div><div>This study investigated the role of fat in processed cheese. The fat content in the PC samples was either partially or wholly contributed by Cagliata cheese curd, and remaining amount was added in the form of anhydrous milk fat (AMF). The effect hereof on the textural, rheological and microstructural changes while heating from 5 to 95°C in PC was evaluated. The effect of homogenizing milk and ripening duration on the properties of Cagliata cheese and PC prepared therefrom was also evaluated. PC prepared with all the fat added as AMF showed the highest hardness and lowest tendency to melt. PC prepared from full-fat Cagliata cheese made from homogenized milk showed lower tendency to melt as compared to when prepared from Cagliata cheese made from unhomogenised milk. CLSM images of PC prepared with externally added anhydrous milk fat showed formation of fat pools at temperature above 75°C.</div></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"43 ","pages":"Article 100406"},"PeriodicalIF":5.6,"publicationDate":"2025-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143180460","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Investigating the impact of enzyme diversity in producing edible bird nest protein hydrolysates: Techno-functional, structural, molecular docking, and in vitro digestibility","authors":"Rabia Kanwal ,&nbsp;Abdur Rehman ,&nbsp;Muhammad Irfan ,&nbsp;Mian Shamas Murtaza ,&nbsp;Tabussam Tufail ,&nbsp;Mian Anjum Murtaza ,&nbsp;Tawfiq Alsulami ,&nbsp;Ibrahim Khalifa ,&nbsp;Song Miao","doi":"10.1016/j.foostr.2025.100415","DOIUrl":"10.1016/j.foostr.2025.100415","url":null,"abstract":"<div><div>This study investigated the impact of different enzymes, including trypsin, papain, and pepsin, on the physiochemical, structural, and techno-functional characteristics of edible bird’s nest protein (EBNP) and its hydrolysate (EBNPH) over a period of 1–4 h. The aim was to determine the optimal hydrolysis conditions for releasing peptides and evaluate their antioxidant activities. It was reported that trypsin produced the highest degree of hydrolysis (DH) value (19.21 %), followed by papain (15.6 %). EBNPH produced using trypsin showed a higher ability to scavenge oxidizing radicals (72.5 ± 0.2 %) compared to papain (63.7 ± 0.3 %) and pepsin (57.5 ± 0.2 %). Additionally, trypsin demonstrated significantly higher ABTS scavenging activities for EBNPH (76.3 ± 0.6 %) than papain (60.0 ± 0.2 %) and pepsin (67.0 ± 0.3 %), indicating that trypsin produced the highest amount of EBNPH with the highest antioxidant activity. Furthermore, spectral analyses by FTIR and X-ray diffraction (XRD) indicated that a higher flexibility and mobility of the secondary structures had occurred in EBNPH. Moreover, SEM images provide convincing evidence that enzymolysis improves and speeds up the breakdown of proteins’ structures. In addition, EBNPH was more susceptible to digestion by pepsin (74.15 %) and papain (67.83 %) than with trypsin, resulting in significantly higher values for the digestibility of EBNPH with trypsin (84.14 %). This indicates that the enzyme modification effectively improved the digestibility of the hydrolysate. Molecular docking research provides a comprehensive explanation of the entire process of the interaction between a glycoprotein and trypsin. The aforementioned localized enzymolysis, thus, might change protein conformation between EBNP or intermolecular interaction between EBNP and EBNPH to enhance functionality and increase food processing capacity.</div></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"43 ","pages":"Article 100415"},"PeriodicalIF":5.6,"publicationDate":"2025-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143609493","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":"Iron dextran-loaded alginate-calcium multi-vesicular microparticles as an intramuscular supplement: A new approach for in situ prolonged iron release.","authors":"Emerson Durán ,&nbsp;Patricio Romero-Hasler ,&nbsp;María Gabriela Villamizar Sarmiento ,&nbsp;Gonzalo Álvarez-Acevedo ,&nbsp;Eduardo Soto-Bustamante ,&nbsp;Andrónico Neira-Carrillo ,&nbsp;Felipe Oyarzun-Ampuero ,&nbsp;Diane Burgess ,&nbsp;Carolina Valenzuela","doi":"10.1016/j.foostr.2025.100411","DOIUrl":"10.1016/j.foostr.2025.100411","url":null,"abstract":"<div><div>The aim of the present study was to synthesize crosslinked alginate particles (CAPs) loaded with of iron dextran particles (IDP) using the emulsion-crosslinking technique and evaluate them as a potential intramuscular (IM) prolonged-release iron supplement for mammals as humans and pigs. This method presents a potential solution for IM iron supplementation in mammals, offering a controlled and efficient approach to combat iron deficiency. Multi-vesicular CAPs of 25–30 µm were developed with ascending IDP content, obtaining ∼120–200 mg iron/g CAP, distributed mostly in inner and outer layer walls. The encapsulation efficiency, yield and loading capacity values ranged from 22 % to 28 %, 70–76 % and 12–20 %, respectively. IDPs are trapped in alginate-calcium networks without evidence of chemical bonding according to FTIR. XRD analysis suggests a new calcium alginate structure without IDP structural modifications. The release time resulted in 4 h (for commercial iron dextran formulation, CIDF) in contrast with the 120 h observed in the CAP4 formulation. This prolonged release, driven by concentration gradients and hindered by physical barriers, indicates an effective containment and prolonged release of IDP, representing a novel and promising strategy for IM iron supplementation to prevent iron deficiency anemia in mammals, including humans and pigs.</div></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"43 ","pages":"Article 100411"},"PeriodicalIF":5.6,"publicationDate":"2025-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143180461","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":"Enhancing rheological and textural properties of pea protein-collagen gels via transglutaminase crosslinking","authors":"Parisa Eslami ,&nbsp;Victoria Haritos ,&nbsp;Simon Crawford ,&nbsp;Leonie van ‘t Hag","doi":"10.1016/j.foostr.2025.100409","DOIUrl":"10.1016/j.foostr.2025.100409","url":null,"abstract":"<div><div>Plant-based proteins are gaining attention in the food industry as a healthier and more sustainable alternative to animal proteins due to health concerns, growing global population, water scarcity and climate change. However, controlling their structural and textural characteristics is still a challenge. Combining plant-based proteins with other substances is an effective method for modifying their gelation and textural properties. An enzymatic crosslinking agent, transglutaminase (TG), was herein employed to enhance the gel strength of a mixture consisting of pea protein isolate (PPI) (50 mg/mL) and collagen (3 mg/mL). Rheological oscillatory time sweep analysis showed an enhancement in gel strength of the PPI and collagen gel compared to PPI alone, and even more so after treatment with the cross-linking enzyme. Scanning electron microscopy imaging provided evidence for the formation of gel networks and crosslinks when the protein mixture was treated with low concentrations (2.5 U/mL) of TG, whereas high TG loading (18 U/mL) caused protein phase separation. Sodium dodecyl-sulfate polyacrylamide gel electrophoresis analysis also showed formation of higher molecular weight bands after TG crosslinking. Particle sizes of the PPI and collagen mixture after TG treatment were larger than without TG. In addition, sodium chloride (150 mM) addition significantly improved the gel strength of PPI collagen gels crosslinked by TG. In conclusion, TG with or without salt can be utilized to enhance the strength of PPI and low concentration collagen gels.</div></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"43 ","pages":"Article 100409"},"PeriodicalIF":5.6,"publicationDate":"2025-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143180462","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Formation mechanism of thermomechanically stabilized whey protein-pectin complexes: Contribution of pectin and protein to complex structure","authors":"Jessica M. Filla,&nbsp;Shirin Heck,&nbsp;Jörg Hinrichs","doi":"10.1016/j.foostr.2025.100412","DOIUrl":"10.1016/j.foostr.2025.100412","url":null,"abstract":"<div><div>Whey protein pectin complexes (WPPC) processed at the technical scale in the particle size range of 1–40 µm have the potential to be utilized as fat replacers. WPPC are formed via thermomechanical treatment at a specific pH level, which allows for the interaction between the biopolymers. In the pH range of 4.75 to 5.75, whey protein and pectin form coacervates or soluble complexes. The diverse interactions result in WPPC with particle sizes <em>d</em>_<em>3.2</em> between 0.2 and 40 µm after thermomechanical treatment on a scraped surface heat exchanger. The pectin contributes to the WPPC structure in three distinct forms, dependent on the pH, as determined via mass balance. The pectin is present in three forms: (i) 50–80 % free, (ii) 15–30 % electrostatically stabilized, and (iii) 5–10 % incorporated pectin. Approximately 20 % of the whey protein with particle sizes below 1 µm was electrostatically stabilized. The addition of pectin-degrading enzymes resulted in a multimodal particle size distribution, indicating that pectin is connecting larger aggregate structures. Based on the core-shell model, a revised model for the WPPC formation at the technical scale on a scraped surface heat exchanger is proposed.</div></div>","PeriodicalId":48640,"journal":{"name":"Food Structure-Netherlands","volume":"43 ","pages":"Article 100412"},"PeriodicalIF":5.6,"publicationDate":"2025-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143314300","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}