Innovative Food Science & Emerging Technologies最新文献

{"title":"Enhancing quinoa protein properties: Pulsed electric fields as a sustainable green innovation for structural and functional excellence","authors":"Atefeh Farahmand ,&nbsp;Sara Naji-Tabasi ,&nbsp;Behrouz Ghorani ,&nbsp;Bahareh Emadzadeh ,&nbsp;Atena Modiri-Dovom ,&nbsp;Omer Said Toker","doi":"10.1016/j.ifset.2026.104433","DOIUrl":"10.1016/j.ifset.2026.104433","url":null,"abstract":"<div><div>Pulsed electric field (PEF) processing is an emerging non-thermal technology capable of modifying plant protein functionality through controlled structural rearrangements. This study systematically investigated the effects of electric field strength (3, 5, and 7 kV/cm) and pulse number (80, 100, and 120) on the structural, techno-functional, thermal, and rheological properties of quinoa protein concentrate (QPC). The results demonstrated that pulse number was the primary factor governing protein functionality, exerting a stronger influence than electric field strength. Compared with the control sample, moderate PEF treatment (5 kV/cm-80 pulses) significantly increased protein solubility (43.75 %), foaming capacity (36 %), and emulsion stability during centrifugation (14 %), while reducing surface tension and improving viscoelastic behavior. Structural analyses revealed a marked increase in free sulfhydryl groups (up to 27.6 μmol/g), a decrease in α-helix content accompanied by a corresponding increase in β-sheet structures, and reduced crystallinity, indicating partial protein unfolding without alteration of the primary structure, as confirmed by SDS-PAGE. Thermal analysis showed a substantial increase in denaturation enthalpy (9.24 J/g), reflecting enhanced structural ordering. In contrast, higher pulse numbers (120 pulses) promoted protein aggregation, leading to reduced solubility, foaming stability, and water-holding capacity. Microscopy revealed a smoother surface with cracks and sheet-like features in PEF-treated proteins compared to the control. These findings demonstrate that moderate PEF treatment improves QPC functionality by balancing molecular unfolding and aggregation, providing mechanistic insight into PEF-induced protein modification and highlighting its potential as a sustainable green technology for the development of high-performance plant-based food ingredients.</div></div>","PeriodicalId":329,"journal":{"name":"Innovative Food Science & Emerging Technologies","volume":"109 ","pages":"Article 104433"},"PeriodicalIF":6.8,"publicationDate":"2026-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146184907","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}

{"title":"Dual-frequency ultrasound pretreatment enhances nutritional quality and protein digestibility of germinated grass pea (Lathyrus sativus L.) flour","authors":"Zhijuan Zhang ,&nbsp;Jiayu Yin ,&nbsp;Huicong Xu ,&nbsp;Bin Dai ,&nbsp;Yuqing Duan ,&nbsp;Kai Hu ,&nbsp;Meihong Cai ,&nbsp;Haihui Zhang","doi":"10.1016/j.ifset.2026.104463","DOIUrl":"10.1016/j.ifset.2026.104463","url":null,"abstract":"<div><div>To enhance the nutritional and functional properties of germinated grass pea (<em>Lathyrus sativus</em> L.) flour, this study applied dual-frequency ultrasound pretreatment to grass pea seeds. Compared with untreated groups (CWF) and single-frequency ultrasound treatment (SWF), dual-frequency ultrasound (DWF) significantly increased protein accumulation and reduced total sugar content in grass peas. Dual-frequency ultrasound treatment promoted the accumulation of total phenolics, total flavonoids, and vitamin C during germination, with increases of 8.43%, 11.94%, and 14.92%, respectively, compared to the control group. Tannins and β-ODAP exhibited an initial decrease followed by an increase during germination. Throughout this process, the tannin content in DWF remained significantly lower than that in CWF and SWF (<em>p</em> &lt; 0.05). During the first 48 h of germination, DWF accelerated the degradation of β-ODAP, <!--> <!-->resulting in a 26.39% reduction in its content<!--> <!-->. However, after 48 h, DWF promoted the accumulation of β-ODAP, reaching 244.55 mg/100 g at 144 h. Furthermore, dual-frequency ultrasound pretreatment notably improved the water absorption capacity, oil absorption capacity, and gel hydration properties of grass pea flour (<em>p</em> &lt; 0.05), while reducing crystallinity(<em>p</em> &lt; 0.05). It was proved that structural modifications in primary and tertiary protein structures of DWF enhanced its in vitro digestibility by 25.22% and 8.72% compared to CWF and SWF. Thus, dual-frequency ultrasound is an efficient and economical method for improving the nutritional and functional characteristics of germinated grass pea flour, providing a novel strategy for high-value utilization of grass peas.</div></div>","PeriodicalId":329,"journal":{"name":"Innovative Food Science & Emerging Technologies","volume":"109 ","pages":"Article 104463"},"PeriodicalIF":6.8,"publicationDate":"2026-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146034860","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}

{"title":"From isolate to concentrate: Insights into the texturization of pea protein systems during high-moisture extrusion","authors":"Maria Gräfenhahn,&nbsp;Michael Beyrer","doi":"10.1016/j.ifset.2026.104457","DOIUrl":"10.1016/j.ifset.2026.104457","url":null,"abstract":"<div><div>Pea protein ingredients vary widely in composition and functional properties depending on their processing history, which strongly affects their behavior during high-moisture extrusion. This study compared pea protein isolate (PPI, 81% protein), pea protein concentrate (PPC, 52% protein), and a 1:1 blend (PPC–PPI, 67% protein) to elucidate how raw material properties influence protein aggregation and the resulting texture of meat analogues processed at high moisture contents (50–60%). PPI exhibited low solubility, high water-holding capacity (WHC), and a partially denatured protein state, whereas PPC contained higher levels of carbohydrates and fiber, showed greater solubility, and retained a more native protein structure. These differences resulted in distinct rheological responses: PPI dispersions formed dense, elastic networks at ambient temperature, while PPC showed limited initial structure but pronounced heat-induced gelation; the blend exhibited comparatively low viscosity and elasticity. During extrusion, PPI formed predominantly disulfide-stabilized networks, resulting in high hardness and anisotropy at low moisture (50%). In contrast, PPC aggregated mainly via non-disulfide covalent bonds, producing stiff but brittle structures. The PPC–PPI blend showed moisture-dependent behavior: at high moisture (60%), enhanced non-covalent interactions promoted molecular mobility and alignment, whereas at low moisture increased non-disulfide covalent cross-linking strengthened the network but constrained anisotropy.</div><div>Correlation analysis confirmed that aggregation pathway, rather than protein content alone, governs extrudate texture. Overall, controlling the balance between disulfide, non-disulfide, and non-covalent interactions is critical for optimizing strength and alignment during high-moisture extrusion of pea proteins, highlighting blending as a practical strategy to tailor texture while leveraging the sustainability advantages of dry-fractionated proteins.</div></div>","PeriodicalId":329,"journal":{"name":"Innovative Food Science & Emerging Technologies","volume":"109 ","pages":"Article 104457"},"PeriodicalIF":6.8,"publicationDate":"2026-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146034858","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}

{"title":"Different strategies to obtain laccase-based time-temperature indicator for monitoring of cold chain storage and management","authors":"Camila Regina Hackenhaar ,&nbsp;Vinicius Zimmermann ,&nbsp;Lucas dos Santos Linares ,&nbsp;Victor Moreira Cannavon ,&nbsp;Juan M. Bolivar ,&nbsp;Roberto Fernandez-Lafuente ,&nbsp;Rafael C. Rodrigues","doi":"10.1016/j.ifset.2026.104454","DOIUrl":"10.1016/j.ifset.2026.104454","url":null,"abstract":"<div><div>In this work, we have developed a battery of enzymatic time-temperature indicators (TTIs) based on the oxidation of 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) catalyzed by laccase from <em>Trametes versicolor</em>. For this, enzyme concentration, pH value, and addition of sodium azide (a non-competitive inhibitor of the enzyme) were utilized to modulate the apparent activation energy of the reaction catalyzed by the biocatalyst (E_a) and the reaction rate constant, tailoring them to match specific product requirements. The color change (∆E) was used as the response parameter. To check the feasibility of this biosensor, ∆E was modeled using a modified Arrhenius equation to extract kinetic parameters for each TTI formulation. TTI prototypes were evaluated under a wide range of isothermal (4–45 °C) and dynamic temperature conditions (4–30 °C). The results showed that enzyme concentration primarily influenced the (∆E) rate, while reaction E_a was significantly affected by pH and laccase inhibitor concentration. Under dynamic conditions simulating real cold chain scenarios, the model accurately predicted the TTI response, demonstrating high correlation between experimental and simulated data (R² &gt; 0.94). These findings confirm the feasibility of customizing TTIs for different perishable products. These enzymatic TTIs offer a scalable and cost-effective tool for integration into intelligent packaging systems, enhancing cold chain management and reducing food waste.</div></div>","PeriodicalId":329,"journal":{"name":"Innovative Food Science & Emerging Technologies","volume":"109 ","pages":"Article 104454"},"PeriodicalIF":6.8,"publicationDate":"2026-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146034861","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}

{"title":"Mitigating Cronobacter sakazakii safety risks associated with non-uniform reconstitution of infant formula using silica-immobilized phenolic compounds","authors":"Oumaima Moumane ,&nbsp;Héctor Gómez-Llorente ,&nbsp;José Manuel Barat ,&nbsp;Édgar Pérez-Esteve ,&nbsp;Alejandro Rivas","doi":"10.1016/j.ifset.2026.104484","DOIUrl":"10.1016/j.ifset.2026.104484","url":null,"abstract":"<div><div><em>Cronobacter sakazakii</em> is a foodborne pathogen of major concern in powdered infant formula (PIF) due to its persistence, desiccation tolerance, and severe health impact on neonates. Although WHO/FAO guidelines recommend reconstituting PIF with water at ≥70 °C to inactivate potential contaminants, studies have shown substantial variability in domestic preparation practices, including suboptimal temperatures and inaccurate powder-to-water ratios. This lack of uniformity in reconstitution represents a critical safety gap that may allow <em>C. sakazakii</em> to survive and proliferate in reconstituted infant formula. This study evaluated the antimicrobial potential of silica particles functionalized with thymol or carvacrol against <em>C. sakazakii</em>, both when applied as dispersed system (1 × MIC and 2 × MIC) and as processing aids in packed beds of different heights (up to 14 cm). Experiments were conducted in phosphate-buffered saline and reconstituted infant formula at incubation temperatures up to 60 °C, to assess the intrinsic antimicrobial response of the functionalized particles and their performance under realistic application conditions, respectively. When applied as dispersed system in PBS or infant formula, functionalized particles (2xMIC) produced strong inactivation of <em>C. sakazakii</em> (&gt; 3 log₁₀ reductions), combining lethal and sublethal damage. Filtration assays confirmed that higher bed heights (14 cm) and elevated temperatures (60 °C) enhanced antimicrobial performance. Importantly, these results demonstrate that functionalized particles could complement existing hygienic practices and mitigate the safety risks derived from non-uniform formula reconstitution, exploiting the mild thermal conditions already present during preparation.</div></div>","PeriodicalId":329,"journal":{"name":"Innovative Food Science & Emerging Technologies","volume":"109 ","pages":"Article 104484"},"PeriodicalIF":6.8,"publicationDate":"2026-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146184821","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}

{"title":"Defatting coconut protein: Influence of solvent polarity and emerging technologies on structural and colloidal properties","authors":"Yuyang Sun ,&nbsp;Lucas Sales Queiroz ,&nbsp;Aberham Hailu Feyissa ,&nbsp;Heidi Olander Petersen ,&nbsp;Adane Tilahun Getachew ,&nbsp;Shuntang Guo ,&nbsp;Federico Casanova","doi":"10.1016/j.ifset.2025.104430","DOIUrl":"10.1016/j.ifset.2025.104430","url":null,"abstract":"<div><div>Defatting is a crucial pretreatment step in extracting plant proteins from food industry by-products. This study investigated the effects of several defatting methods (EtOH (ET), hexane (HX), supercritical fluid CO₂ (SCO₂), and high intensity ultrasound (HIUS) combined with EtOH) on the recovery, structure, functional and colloidal properties of coconut albumin and globulin. The total protein extraction recovery increased from 36.4 % in the non-defatted group (ND) to up to 39.2 % (<em>p</em> &lt; 0.05) after defatting, mainly driven by the higher globulin recovery (24.9 % in ND to 28.4 % with HIUS, <em>p</em> &lt; 0.05), whereas albumin recovery remained statistically unchanged (11.0 % – 11.9 %, <em>p</em> &gt; 0.05) and was slightly reduced under HIUS (10.8 %, <em>p</em> &lt; 0.05). Defatting had minor effects on secondary and tertiary structures but markedly enhanced protein surface hydrophobicity. Globulin showed increased exposure of hydrophobic groups (204 arbitrary units (a.u.) in ND <em>versus</em> 222–274 a.u. in treated groups, <em>p</em> &lt; 0.05). In albumin, HIUS further amplified this effect compared with EtOH (58 <em>versus</em> 66 a.u., <em>p</em> &lt; 0.05), improving emulsifying capacity. Solvent polarity was directly correlated with protein colloidal and functional properties (|R| &gt; 0.7). Defatting reduced globulin solubility (90 % in ND <em>versus</em> 76–90 % in treated groups, <em>p</em> &lt; 0.05), due to increased surface hydrophobicity. EtOH enhanced the emulsifying properties of albumin compared with ND (22.9 <em>versus</em> 26.8 m²/g, <em>p</em> &lt; 0.05). In globulin, however, HIUS promoted intermolecular disulfide bond formation, leading to aggregation and reduced flexibility, which slightly decreased emulsifying performance. In contrast, SCO₂ caused minimal functional changes, comparable to hexane and closest to ND (<em>p</em> &gt; 0.05). Overall, SCO₂ and EtOH combined or not with emerging technologies present a more environmentally friendly and promising alternative to conventional hexane-based defatting.</div></div>","PeriodicalId":329,"journal":{"name":"Innovative Food Science & Emerging Technologies","volume":"109 ","pages":"Article 104430"},"PeriodicalIF":6.8,"publicationDate":"2026-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145923272","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}

{"title":"Controlled ozonation as a sustainable decontamination strategy: Modeling kinetics, microbial inactivation and qualitative changes in black pepper","authors":"Eugénio da Piedade Edmundo Sitoe,&nbsp;Patrícia Monteiro Evangelista,&nbsp;Max Suel Alves dos Santos,&nbsp;Anderson S. Sant'Ana","doi":"10.1016/j.ifset.2026.104453","DOIUrl":"10.1016/j.ifset.2026.104453","url":null,"abstract":"<div><div>This study investigated how controlled ozone (O₃) application flow rates influence reaction and decomposition kinetics, microbial inactivation, and the physicochemical quality of black pepper. Samples of 2.50 kg of whole (unmilled) black pepper grains were exposed to O₃ applied at a concentration of 20.00 mg·L⁻¹, at specific flow rates of 0.20 and 0.40 m³·min⁻¹·t⁻¹. Untreated grains served as controls. Physical-chemical parameters consisting of water content, water activity, weight of 100 grains, pH, and color were evaluated. The effect of flow rate was significant (<em>p</em> &lt; 0.05) on the reaction and decomposition kinetics of O₃, as well as on microbial inactivation and physical-chemical parameters. At a rate of 0.20 m³·min⁻¹·t⁻¹, the saturation time was 5.97 h and the half-life was 19.14 min, while a flow rate of 0.40 m³·min⁻¹·t⁻¹ reduced these values to 4.19 h and 17.07 min, respectively. The decomposition of O₃ was adequately described by a first-order model (R² = 0.99). The lower flow rate reduced mesophiles, molds, and yeasts by 0.75, 1.37, and 1.74 logs, while the higher flow rate showed reductions of 0.68, 1.09, and 0.57 logs, respectively. The pH decreased significantly from 6.91 ± 0.09 (control) to 5.67 ± 0.34 at a flow rate of 0.20 m³·min⁻¹·t⁻¹. The effect of O₃ applied at both flow rates did not significantly affect (<em>p</em> &gt; 0.05) water content, water activity<em>,</em> hundred-grain weight, and color. These results indicate that O₃ can be applied in a controlled manner to increase microbiological safety while maintaining grain quality. This behavior represents a practical and sustainable solution for the post-harvest industry.</div></div>","PeriodicalId":329,"journal":{"name":"Innovative Food Science & Emerging Technologies","volume":"109 ","pages":"Article 104453"},"PeriodicalIF":6.8,"publicationDate":"2026-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145974161","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}

{"title":"Multiscale analysis on the fibrillation of whey protein isolate induced by cold plasma treatment: regulation mechanism of aggregation morphology and its emulsifying properties","authors":"Gongshuai Song ,&nbsp;Ziming Xu ,&nbsp;Zhen Xu ,&nbsp;Mingwei Zeng ,&nbsp;Mengna Zhang ,&nbsp;Jinyan Gong","doi":"10.1016/j.ifset.2026.104467","DOIUrl":"10.1016/j.ifset.2026.104467","url":null,"abstract":"<div><div>Cold plasma (CP) treatment can alter the structure of proteins and modify the physicochemical property. However, the mechanism of CP-assisted acidic-thermal protein fibrillation during different fibrillation degrees is essential to explore. This study aimed to investigate the effect of CP-assisted acidic-thermal fibrillation on the structural, physicochemical, and emulsifying characteristics of whey protein isolate (WPI) and its ability to stabilize high internal phase emulsions (HIPEs). Results indicated CP exhibited significant potential for promoting the formation of WPI fibrils (WFs), as evidenced by a 1.84-fold increase in Thioflavin T fluorescence intensity and enhanced β-sheet content from 13.72% to 43.77%. FTIR and SEM analyses confirmed that CP induced unfolding of the WPI structure and the formation of highly ordered, filamentous aggregates. The fibrils induced by CP exhibited superior emulsifying activity index (32.66 m²/g) and emulsion stability index (89.24 min), representing 2.1- and 1.8-fold increases over the native WPI, respectively. Moreover, the CP-induced WF stabilized HIPEs with the smaller droplet sizes, higher apparent viscosity, and enhanced storage stability. The driving force of CP-assisted self-assembly fibrillation mainly involved hydrogen bonds and electrostatic interactions. The HIPEs stabilized by PWFs exhibited the superior thermal and ultraviolet stability of encapsulated lycopene. The highest retention rate (56.10%) was obtained in the HIPEs. This work revealed that CP-assisted fibrillation provided an efficient, green, and controllable strategy to tailor the structure and interfacial functionality of proteins, revealing the important role of CP in regulating the protein fibrillation process.</div></div>","PeriodicalId":329,"journal":{"name":"Innovative Food Science & Emerging Technologies","volume":"109 ","pages":"Article 104467"},"PeriodicalIF":6.8,"publicationDate":"2026-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146073596","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}

{"title":"Ultrasound-assisted enzymatic construction of sodium caseinate-arabinoxylan covalent conjugates for stabilizing high internal phase emulsions and efficient delivery of curcumin","authors":"Peizhu Liu ,&nbsp;Xuenan Gao ,&nbsp;Olayemi Eyituoyo Dudu ,&nbsp;Luodi Xu ,&nbsp;Yingying Sui ,&nbsp;Mingrui Zhang ,&nbsp;Yue Sun ,&nbsp;Jinju Cheng ,&nbsp;Yujun Jiang","doi":"10.1016/j.ifset.2025.104408","DOIUrl":"10.1016/j.ifset.2025.104408","url":null,"abstract":"<div><div>In this study, sodium caseinate (CAS) and arabinoxylan (AX) were used as substrates, and covalent conjugates (AX-CAS) were constructed via ultrasound-assisted (0, 100, 200, 400 W) enzymatic glycosylation technology. Based on these conjugates, high internal phase emulsions (HIPEs) with different oil phase volume fractions (70%, 75%, 80%) were prepared to improve emulsion stability, curcumin encapsulation efficiency and bioavailability. Ultraviolet, fluorescence, and infrared spectroscopic analyses were employed to identify the optimal reaction mass ratio of AX to CAS, which was found to be 2:2. Following pretreatment with 400 W ultrasound, the enzymatic cross-linking between CAS and AX led to remarkable improvements in the structural and functional characteristics of CAS, its particle size was reduced, while its surface hydrophobicity, secondary structure stability, solubility, foaming capacity, emulsifying activity, and interfacial properties were all enhanced. HIPEs with an 80% oil phase volume fraction, prepared using the AX-CAS conjugate, demonstrated the most favorable performance. These HIPEs featured small droplet sizes, high absolute zeta potential, a compact and ordered microstructure, and a high-elastic three-dimensional network compared with CAS- and AX/CAS-stabilized HIPEs. Furthermore, they displayed outstanding stability under both long-term storage and high-temperature conditions, and were also capable of effectively inhibiting lipid oxidation and phase separation. After curcumin was loaded into the HIPEs, the encapsulation efficiency reached approximately 90%. During in vitro gastrointestinal digestion, the system maintained high stability characterized by smaller droplet size, the release rate of free fatty acids was 39.1%, and the bioaccessibility of curcumin stood at 59%.</div></div>","PeriodicalId":329,"journal":{"name":"Innovative Food Science & Emerging Technologies","volume":"108 ","pages":"Article 104408"},"PeriodicalIF":6.8,"publicationDate":"2026-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145735072","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}

{"title":"From ingredients to integration: Exploring the processing technologies and ingredients for pea and wheat-based meat alternatives and their social implications","authors":"Ann-Marie Kalla-Bertholdt ,&nbsp;Dagmara Weckowska ,&nbsp;Anna Laux ,&nbsp;Sarah Voss ,&nbsp;Carsten Dreher ,&nbsp;Cornelia Rauh","doi":"10.1016/j.ifset.2025.104384","DOIUrl":"10.1016/j.ifset.2025.104384","url":null,"abstract":"<div><div>Plant-based meat alternatives (PBMA) are one of the solutions proposed for diversifying protein production and changing consumption patterns. This study presents the first step towards creating an innovation radar for PBMA. Following an innovation radar method, the study reviews the extant literature on PBMA production, focusing on studies on pea and wheat proteins, to identify technologies and ingredients used in key stages of the PBMA value chain, namely in crop development, pre-treatment, protein extraction and fractionation, functionalization, product formulation, texturization, and final product modification. The social implications of the technologies and ingredients, especially potential impacts on inclusion in consumption and production are proposed, alongside environmental, economic and legal aspects. The study finds alternative production technologies/ingredient options at each stage of the value chain. Their implications for sensory characteristics of PBMA products and consequent consumer acceptance are widely considered in the literature, indicating a strong focus on imitation of meat products. The implications for production costs and health are also debated, and concerns about nutritional aspects are raised in the literature. The normative aspects of the technological and ingredient choices as well as implications for affordability, availability or accessibility of PBMA products are rarely discussed. The study makes a first step towards developing an innovation radar for PBMA and concludes with the reflection on the usefulness of the radar method.</div></div>","PeriodicalId":329,"journal":{"name":"Innovative Food Science & Emerging Technologies","volume":"108 ","pages":"Article 104384"},"PeriodicalIF":6.8,"publicationDate":"2026-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145735105","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}