Regulation of pea protein fibrillation by ultrasound and zinc ions: promotion mechanism, structural evolution, and in vitro implications for astaxanthin delivery.

From stability to application: mechanistic insights into the stability and 3d printing of probiotic-loaded pea protein-based high internal phase pickering emulsions.

Structural modification of pea protein via high-energy fluidic microfluidizer: Mechanistic insights into enhanced solubility and acid-induced gelation properties.

Comparative impacts of physical and chemical modifications on pea protein concentrate: Effects on physicochemical properties.

Insoluble and soluble pea proteins at air-water and oil-water systems: Adsorption and interfacial network formation behavior.

Amelioration of hepatic steatosis in male obese rats by high-protein diet is dependent upon protein source.

Fermentation of dry- and wet-extruded pea protein texturates for flavor development.

Selective precipitation-induced conformational modulation of pea proteins enhances adsorption at the oil-water interface.

Enteral formulas are an essential part of nutrition support to prevent or treat malnutrition and minimize hospital length of stay (LOS). Yet not all formulas are tolerated and may leave nutritional needs unmet. Unique pea protein plant-based formulas (PPPBF) are nutritionally complete and have accumulated evidence of good tolerance, but impact on health economic outcomes (HEO) is largely unknown. Aim: To examine differences in patient and clinical characteristics and HEOs of hospitalized adults using PPPBF versus dairy and/or soy protein (DSP) formulas to inform further research. Materials & methods: Retrospective comparative cohort study examined real-world data (Premier Healthcare Database) from adults (≥18year) admitted to US hospitals who were prescribed a formula between 1 January 2020 and 30 September 2023. Patient and clinical characteristics and HEOs were compared between the PPPBF and DSP groups by unadjusted descriptive analysis. Results: Preliminary analyses were conducted on inpatients (n=65,338 DSP; n=243 PPPBF) from 60 US hospitals. PPPBF (versus DSP) group was younger (mean [SD] 63.6 [17.0] vs 66.7 [17.3]years; p=0.006) and had a higher diagnosis rate for malnutrition, weight loss, food allergies, irritable bowel syndrome and/or inflammatory bowel disease on admission. Overall, formula intake was primarily oral but higher in PPPBF versus DSP (100 vs 78.3%, p<0.001). Charlson Comorbidity Index indicated PPPBF (versus DSP) was sicker (median 4.0 vs 3.0; p<0.001). Yet PPPBF group had shorter LOS (by ∼2days; p<0.001) and lower mortality rate by discharge (5.8% vs 11.5%; p=0.005) without significant difference in 90-day readmission/outpatient visit rates after discharge (unadjusted comparisons). Conclusion: Preliminary evidence in hospitalized adults observed a shorter LOS in PPPBF users, despite higher baseline acuity and without significant difference in readmission/outpatient visit rates compared (unadjusted) to DSP users. Adjusted analyses and further research are needed.

Hospitals increasingly seek to align patient meals with sustainable food policies while ensuring nutritional adequacy and patient acceptance. However, the limited availability of palatable high-protein plant-derived meals with complete amino acid profiles hampers implementation. This study aimed to develop and evaluate fully plant-derived hospital meals for nutritional adequacy, palatability, cost-effectiveness, and feasibility within sustainable food policy frameworks. A multidisciplinary, co-creative study was conducted between April and December 2025 with hospital staff and industry partners. Meal development criteria were derived from clinical guidelines and hospital policies and prioritized by a multidisciplinary team. Recipes were iteratively developed and evaluated through cooking and tasting sessions, then optimized for nutritional composition, amino acid profile, and palatability. Nutritional values were calculated using the Dutch Food Composition Database, and protein quality estimated through weighted mean digestibility and aggregated amino acid scores across meal protein sources. Thirty meal recipes were developed and combined into seven daily menus providing 90-97g protein per day, primarily from soy, lentils, grains, and nuts. To increase protein in breakfast and lunch without enlarging portions, pea protein isolate and soy-based drinks were incorporated. Total daily menu costs ranged from €10.50 to €12.30. Fully plant-derived meals can provide adequate, palatable, and cost-effective protein, suitable for clinical use, although trade-offs between protein quality, taste, cost, and portion size remain. These meals offer a practical blueprint for hospitals seeking to adjust animal-to-plant protein ratios and support the transition toward sustainable nutrition.

To improve the applicability of pea protein isolate (PPI), this work demonstrated that enzymatic hydrolysis effectively mitigates its bitterness, which is primarily driven by specific bitter peptides. Five peptides were validated with low recognition thresholds (0.171-0.586 mmol/L), ranking within the top 30% of reported bitter peptides. Among them, LN-9, VF-5, and VN-10 contribute substantially to PPI bitterness. Molecular docking indicated that hydrophobic interactions and hydrogen bonds primarily mediate peptide binding to bitter taste receptors (TAS2Rs). Critically, in vitro calcium flux assays revealed that the activation of TAS2R14 and TAS2R39, as well as TAS2R4, strongly correlates with perceived sensory bitterness. This work provides an integrated strategy to identify key bitter peptides and pinpoints specific TAS2Rs as primary targets for debittering, offering a robust scientific basis for enhancing the palatability of plant-based proteins in the food industry.

The properties of pea protein isolate (PPI), comprising a sustainable plant-derived protein for which the full functional potential in complex food matrices remains unrealized as a result of inherent limitations in food applications, are investigated in this work under gamma (γ) irradiation (0-10 kGy). The study used non-thermal physical treatment, namely γ irradiation, using ionizing radiation from a 60Co source, which causes controlled structural rearrangements in macromolecules. Fourier transform infrared spectroscopy deconvolution revealed irradiation-induced changes: partial unfolding of secondary structures (α-helix/β-sheet), whereas scanning electron microscopy showed fragmented morphology (4-8 kGy) and aggregated clusters. Functional properties peaked at 8 kGy with solubility, emulsifying activity and water/oil-holding capacity, whereas 10 kGy enhanced emulsion stability but reduced solubility because of disulfide cross-linking. This study establishes 8 kGy as the critical threshold for balancing structural flexibility and functionality of PPI, providing a non-thermal strategy for tailoring plant proteins in next-generation foods. Physicochemical studies linked these changes to disulphide bond breaking, free sulfhydryl dynamics and fluorophore exposure. These results highlight γ irradiation as a flexible approach to modify PPI activity, hence balancing structural changes with particular dietary applications. © 2026 Society of Chemical Industry.

Mechanistic insights into the preparation and stabilisation of supersaturated pea protein isolate-curcumin nanoparticles prepared by a pH-driven method.

Protein intake has shown benefits to mitigate postprandial hyperglycaemic excursions. In particular, whey protein has demonstrated strong potential for postprandial glucose management, and more recent findings highlighted evidence for increased efficacy of whey protein when consumed before, rather than with a carbohydrate-rich meal. Given the strong interest yet limited evidence on plant-based protein, the present study compared the potential of pea protein consumed prior to carbohydrates, on postprandial glucose as well as satiety and blood pressure (BP). In an acute randomized cross-over trial, ten healthy adults consumed a pea protein drink either before (PrePP) or with (PP) a standard carbohydrate-rich meal, compared with a control meal (CHO). Continuous glucose monitoring, satiety levels and BP were recorded over 180min post-meal consumption. Both PP and PrePP significantly reduced postprandial glucose excursion (0.46 vs. 1.125 mmol/L), compared to CHO (1.89 mmol/L). The effect was more pronounced with PrePP, exhibiting a delayed glucose response and a blunted peak beyond 60min. Systolic BP remained unchanged, whereas both PP and PrePP significantly reduced diastolic BP compared to CHO (- 4.2 mmHg at 150min, p < 0.05; -9.2 mmHg at 180min, p < 0.01, respectively). PP significantly increased fullness and reduced hunger after 60 and 180min, respectively, whereas PrePP significantly decreased hunger after 60min of carbohydrate consumption. Given the enhanced efficacy in lowering postprandial glucose when consumed before carbohydrates, pea protein pre-meal consumption could be considered as part of a dietary strategy to manage postprandial glycaemia well comparable to whey protein.

Stropharia rugosoannulata mycelium is a naturally fibrous and sustainable protein source for meat analogs; however, its weak gel-forming ability and poor extrudability limit its printability and structural stability. In this study, extrusion-based 3D-printable composite inks were developed using mechanically fragmented mycelium, pea protein isolate (PPI), and curdlan (CUR). The effects of mycelium and CUR concentrations on printability, rheological properties, water-holding capacity, water distribution, thermal properties, and texture were systematically evaluated. The results showed that mechanical fragmentation for 20 s effectively dispersed the mycelial aggregates while preserving the filamentous network. CUR markedly improved extrusion continuity, print accuracy, and shape fidelity after deposition. All inks exhibited shear-thinning behavior. Increasing CUR concentration enhanced apparent viscosity, storage modulus, thixotropic recovery, water-holding capacity, and thermal stability, while converting part of the immobilized water into bound water within the gel network. In addition, CUR strengthened hydrogen bonding in the composite inks. Texture profile analysis of heated meat analogs showed that hardness, springiness, cohesiveness, gumminess, chewiness, and resilience increased progressively with increasing CUR concentration. Among the tested formulations, the ink containing 50% mycelium, 5% PPI, and 6% CUR exhibited the best balance between printability, structural stability, and meat-like texture, showing the closest textural similarity to boiled chicken breast. These findings provide a practical strategy for fabricating mycelium-based meat analogs with improved printability and meat-like texture.

The growing use of plant-based protein ingredients, particularly pea protein, highlights the need for robust analytical methodologies capable of monitoring emerging contaminants such as per- and polyfluoroalkyl substances (PFAS). In this study, a green and efficient analytical method based on fabric phase sorptive extraction (FPSE) coupled with UHPLC–MS/MS was developed and validated for the determination of four PFAS; perfluorooctanoic acid (PFOA), perfluorooctane sulfonic acid (PFOS), perfluorononanoic acid (PFNA), and perfluorohexane sulfonic acid (PFHxS) in pea protein. The FPSE protocol was optimized to address the challenges associated with high-protein matrices, minimizing matrix effects while ensuring high extraction efficiency. The method demonstrated excellent linearity (R2 > 0.9910) over the range 0.05–10 μg/kg with limits of detection and quantification ranging from 0.003 to 0.020 μg/kg and 0.010 to 0.060 μg/kg, respectively. Recoveries ranged from 96 to 107%, while repeatability (expressed as relative standard deviation) was below 7.8%, confirming the method’s accuracy and precision. The validated method was applied to eleven commercial pea protein samples, where PFOA was detected in nine out of eleven samples at concentrations between 0.01 and 2.76 μg/kg, whereas PFNA was detected in one sample and PFOS and PFHxS were not detected. The proposed method provides a robust and environmentally friendly tool for the determination of PFAS in plant-based protein matrices, contributing to improved food safety monitoring and supporting future risk assessment studies.

This study aimed to encapsulate anthocyanins from black rice bran (an agro-industrial by-product) using pea protein (PR) and maltodextrin (MA) as wall materials. The microcapsules were characterized by determining encapsulation efficiency, structural and thermal characteristics, color and storage stability, and in vitro anthocyanin release. Two formulations were prepared, both containing 2.5% anthocyanin (ANC), one containing 100% PR (PP) and the other containing 50% PR and 50% MA (PM). The encapsulation efficiency(EE)was higher for PM (94.7%) than for PP (90.2%). Furthermore, the particle size was 2.2-fold higher for PM due to the addition of MA. After 60 days, the stability of both microcapsules was significantly higher (approximately 66%-70%) than that of ANC (54%) and did not differ significantly between them (p>0.05). Regarding the evaluation of anthocyanin release, the PM sample in the gastric phase presented a release of 34.7%. In comparison, PP was 29.2%, but at the end of the intestinal phase, the PP sample presented a total of 56.2% anthocyanin release, while PM presented 59.6%, differing from each other (p<0.05). Overall, the addition of PR was essential to increase the storage stability of anthocyanins through encapsulation, presenting high EE and good release during the in vitro digestibility of these compounds. Microcapsules have the potential to be applied in several areas, especially in the food industry. PRACTICAL APPLICATIONS: The key contribution of this research is that the food and supplement industries can use microcapsules as a natural, stable coloring agent and antioxidant booster derived from rice waste. They protect sensitive nutrients during storage and ensure their controlled release in the body, offering a healthier, plant-based alternative to synthetic dyes in functional foods.

Meat quality of a slow-growing chicken breed fed soybean meal-free diets.

• 14 protein snack bars were developed using four different protein sources • Nougat-layer bars were rated most favorably in taste, texture, and appearance • Pea protein with nougat layer achieved top sensory evaluation scores • Two nougat bars showed strong purchase intent from sensory panelists Snack bars are often used to supplement daily protein intake, though these bars are often reported as having bland or unappealing flavors. Therefore, this study aimed to develop a new snack bar using various protein sources while optimizing sensory attributes. Fourteen bars were formulated, and each consisted of a shortbread base, date caramel layer with protein (whey, soy, pea or hemp), a flavor-texture layer (nougat, chocolate truffle, peanut butter or double-date caramel), and a chocolate coating. Sensory evaluations were conducted on a 5-point Likert scale (1 = dislike extremely, 5 = like extremely) and showed that the nougat layer bar with pea protein received the most favorable ratings, with mean scores of 4.23 ± 0.83 for taste, 4.15 ± 0.98 for texture, and 4.60 ± 0.63 for appearance (p<0.05). Bars with a nougat layer, regardless of protein source, were rated significantly higher for all attributes compared to other layer types (p<0.05). Panelists also indicated they would be "likely to purchase" two of the four nougat variations. Proximate analysis confirmed differences in protein content among the nougat bars, with the hemp bars containing the most protein (19.22±0.34%) and pea bars containing the least (13.68±0.09%) (p < 0.05). Penetrometer measurements showed that the whey and soy protein date caramel layers exhibited the greatest hardness (p < 0.05), with mean values of 5.21 ± 1.42 N and 4.64 ± 1.43 N, respectively. The formulations show strong potential for consumer acceptance and could be further optimized to meet nutritional targets for commercial snack bars.

Pea proteins can act not only as interfacial stabilizers of oil-in-water emulsions but also as gelling agents in the continuous phase. Protein gelation, rather than droplet jamming, may be the main mechanism of emulsion stability, providing a physical explanation for the creaminess of high-protein plant-based emulsions. Spin-echo small angle neutron scattering (SESANS) with D2O/H2O contrast variation was used to study 15% pea protein dispersions and emulsions with 40-60% rapeseed oil, 7.5% protein at pH3 to 6.5. SESANS investigates length scales up to tens of micrometres, enabling simultaneous analysis of protein networks and oil droplets without dilution. Complementary small angle X-ray/neutron scattering were used to validate protein aggregate size, and hydration. Protein dispersions at neutral pH formed mass fractal networks with small individual building blocks (radius∼38Å, hydration ∼70%). Emulsions consisted of oil droplets embedded in these networks, with droplet radii decreasing at higher oil fractions due to an effective higher protein concentration in the continuous phase, creating a denser network. Dispersions and emulsions at lower pH contained aggregated clusters of denatured proteins. These coarse and inhomogeneous networks gave increasing droplet radii at lower pH. Contrast variation enabled the separation of protein and oil droplet scattering, demonstrating that protein gelation rather than droplet jamming is the main mechanism of stability. This gives a physical explanation of the high viscosity of high-protein plant-based emulsions and is promising for these plant materials to be used as gelling agents in food applications.