Oat proteins have shown potential as sustainable alternatives to animal-derived proteins; however, their extraction efficiency and functional properties are strongly influenced by raw material composition and processing conditions. This study evaluated protein extraction from two oat varieties with contrasting protein, β-glucan, and starch contents using enzymatic, ultrasound, and enzymatic–ultrasound treatments prior to alkaline extraction. Oat protein concentrates (OPCs) were characterized in terms of protein content and yield, structural attributes, and solubility. Ultrasound-assisted extractions, with or without enzymes, improved protein yield in both varieties (from 57 to 68

This comparative study investigated the use of individual treatments and sequential application of high-intensity ultrasound followed by enzymatic hydrolysis to modulate the physicochemical and functional properties of pea and faba bean protein isolates. Enzymatic hydrolysis shifted the peptide profile toward lower-molecular-weight peptides, while ultrasound induced unfolding and disrupted aggregates. These treatments impacted the surface activity and solubility of both isolates. Hydrolysis significantly enhanced solubility of pea (67.9% vs. 8.9%) and faba bean (43.6% vs. 7.3%) proteins; ultrasound was more effective at improving solubility in faba bean protein (64.2% vs. 7.3%) than in pea (19.9% vs. 8.9%). Ultrasound and enzymatic hydrolysis altered emulsifying and foaming properties through different mechanisms in a source-dependent manner. Ultrasound enhanced emulsion stability to a greater extent than enzymatic hydrolysis (100% vs. 73.3% for pea; 100% vs. 50.2% for faba bean) and achieved the smallest droplet sizes (3.1 vs. 5.7 mu m for pea; 2.5 vs. 5.0 mu m for faba bean). Hydrolysis, as well as ultrasound coupled with enzymatic hydrolysis, produced finer but less stable foams, whereas ultrasound promoted coarser foams with slower collapse and greater stability, especially in pea protein systems. Overall, structural rearrangements induced by ultrasound and enzymatic hydrolysis directly influenced both proteins' interfacial interactions, improving solubility and emulsion formation. Foaming behaviour was modulated in both proteins, with overall improvement in stability observed mainly for pea. These findings highlight that tailoring modification strategies according to intrinsic characteristics of each protein source is crucial for adjusting their functionality in plant-based formulations and improving performance for specific applications.

Background and Objectives The goal of this research was to examine the relationship between the composition and functionality of pea flour using the following machine learning algorithms: linear regression, partial least squares regression (PLSR), Gaussian process regression (GPR), support vector regression, gradient-boosted decision trees, and a standard feed-forward neural network.Findings In general, linear models outperformed non-linear models. PLSR provided best fits for prediction of emulsion stability, oil holding capacity, foam stability and foam capacity; but was less effective for solubility and water holding capacity, which were best described by the GPR model. Variable Importance in Projection scores, calculated for each PLSR model, showed that protein and acid detergent fiber were both highly influential in predicting foaming capacity (1.52 and 1.55), foaming stability (1.30 and 1.54), oil holding capacity (1.64 and 1.50), and water holding capacity (1.56 and 1.53). Protein was also highly important in predicting solubility (1.80), alongside starch (1.60) whereas lipid was highly predictive (2.02) for emulsion stability.Conclusion Application of machine learning models was successful in relating compositional features of pea flour to functionality.Significance and Novelty Using machine learning to predict the functional behavior of pea will aid both breeders and product developers in ingredient selection.

BACKGROUND:Increasing interest in incorporating pulses into human diets has increased demand for their fractionation into diverse food ingredients. Air classification has relatively low capital and operating costs, uses no water, and preserves the native protein structure. However, its efficiency in separating protein and starch is lower than that of wet fractionation. This study investigated seed germination of pea and faba bean for 24, 48, and 96 h as a pretreatment to improve the air classification efficiency of pulse flours into fine (protein-rich) and coarse (starch-rich) streams. RESULTS:Scanning electron microscopy revealed that germination disrupted the protein and fiber matrices surrounding starch granules in pea and faba bean seeds, improving subsequent air classification efficiency. Following 24-96 h of soaking and germination, the fine stream yield increased from 251 to 295 g kg⁻¹ for pea and from 274 to 364 g kg⁻¹ for faba bean. Protein retention in the fine stream - the proportion of total protein recovered - also increased, from 620 to 686 g kg⁻¹ for pea and from 702 to 882 g kg⁻¹ for faba bean, both at 48 h of germination. After 96 h, protein retention declined. In contrast, germination had no effect on the starch retention in the coarse stream. CONCLUSION:In conclusion, 48 h of germination of pea and faba bean seeds is sufficient to improve the air classification efficiency of the resulting pulse flours. © 2026 The Author(s). Journal of the Science of Food and Agriculture published by John Wiley & Sons Ltd on behalf of Society of Chemical Industry.

The objective of this study was to develop and characterize texturized vegetable proteins (TVPs) from faba bean protein isolate and concentrate (FIFC), and faba bean protein—oat flour (FO) for their application in vegan chicken burgers under two feed moisture contents (38

The effect of high energy homogenization methods [high speed (HS) vs. high pressure (HP)] and emulsion composition [oil content (0–15

In this study, yellow peas, green lentils, and red lentils were germinated for up to 72 h. The germinated seeds were milled into flour and analyzed for compositional and functional changes, including α-amylase activity, water and oil holding capacity, foaming and emulsifying properties, protein solubility, in vitro protein and starch digestibility, and pasting properties. Overall, germination of pulses had significant impacts on the composition and several functional properties of the flours. The protein content and α-amylase activity increased and the water holding capacity was improved. Germination decreased protein solubility in pea but not in lentils. Germination did not affect the foaming properties or oil holding capacity of the three pulses. The lentil flours from germinated seeds were much lower in pasting viscosity, temperature, and time, while for pea, germination did not have as large of an impact on pasting properties. Germination had minor effects on the nutritional properties of the flours with reduced in-vitro protein digestibility corrected amino acid score (IV-PDCAAS) in lentils and changes in starch digesting properties, mainly in red lentils. The in-vitro protein digestibility (IVPD) was not modified through germination.

The goal of this research was to examine the effect of alcohol washing (ethanol and isopropanol; concentrations of 35

Starch-rich pulse flours are an underutilized, low-value by-product from air classification of pulses. They contain 8 %–20 % proteins with substantial untapped potential. This research aimed to optimize the alkaline extraction/isoelectric precipitation method to produce protein isolates from air-classified starch-rich faba bean and pea flours and to examine their techno-functional characteristics in comparison with commercial pea protein isolate (CPPI). The alkaline extraction was performed over a range of pH (8.5, 9.5, 10.5, and 11.0) and temperatures (25, 30, 40, and 50 °C). Higher pH and temperature increased the yields but reduced the purity of the protein isolates. Fourier transform infrared (FTIR) spectroscopy further revealed that the milder extraction conditions better preserved β-sheet and β-turn structures and led to smaller percentages of unordered α-helices in both faba bean (FPI) and pea protein isolates (PPI). FPI and PPI extracted under yield-optimized condition (designated as FPI-Cyield and PPI-Cyield) exhibited greater denaturation, surface charge, and hydrophobicity than the counterparts from purity-optimized condition (designated as FPI-Cpurity and PPI-Cpurity). Consequently, FPI-Cyield and PPI-Cyield showed reduced water solubility, increased oil-absorption capacity (OAC), and enhanced emulsion stability and foaming capacity as compared to respective FPI-Cpurity and PPI-Cpurity samples. This study revealed that the alkaline extraction conditions influenced not only the purity and yield but also the surface and functional properties of generated protein isolates.

Background and ObjectivesIn the present study, the effect of a pH-shifting method in combination with heat was investigated for its effects on the resulting surface and functional properties of a commercial pea protein isolate. The pH shifting process was performed at both acidic (pH 2) and alkaline (pH 10) pH and then adjusted back to neutrality. The heat-treated samples were further subjected to heating and later neutralized at pH 7.FindingsThe results of these treatments indicated that an alkaline pH shifting, as well as its combination with heat, resulted in a significant increase in the solubility of the proteins, whereas an acidic pH shifting, and in combination with heat, reduced the stability of the proteins in solution. Additionally, some functional properties were enhanced by pH shifting, such as foaming capacity or emulsion stability, while other properties showed no alteration or were negatively impacted, such as foaming stability. Furthermore, analysis of the bubble structure of foams using a dynamic foam analyzer revealed that bubble sizes for samples shifted at pH 2 in combination with heat presented the biggest increase in bubble growth over time, creating a less stable foam.ConclusionsThe application of pH shifting and the use of heat can aid in the improvement of pea protein functionality and allow tailoring of these proteins for specific applications.Significance and NoveltyThis study utilized a simple method to achieve modifications in the protein structures, providing insights into the application of pea proteins into food products as emulsifying and foaming agents.

Pea protein enriched flour was hydrolyzed using both proteases and amylases simultaneously, then it was heated to induce Maillard conjugation between proteins and polysaccharides. The resulting protein-starch conjugates were investigated for their structural, surface, and functional properties. SDS-polyacrylamide gel electrophoresis and scanning electron microscopy analyses showed the presence of different molecular species and altered microstructure in the conjugate preparations. The zeta potentials at pH 7 (− 20.6 to − 32.3 mV) and pH 10 (− 29.2 to − 36.6 mV) were more negative compared to pH 4 (0.2 to 8.6 mV), indicating higher exposure of ionized side chains. All trypsin-hydrolyzed protein-starch conjugates exhibited better foaming and emulsification properties compared to the papain-hydrolyzed protein-starch conjugates. Trypsin-hydrolyzed conjugates with a degree of hydrolysis (24

The aim of this study was to produce texturized vegetable proteins (TVPs) from faba bean protein via low-moisture extrusion. The effect of extrusion variables including temperature (110, 125, and 140 °C at the die), feed moisture content (30, 35, and 40%), and screw speed (200, 300, and 400 rpm) on the TVP properties were investigated. An increase in feed moisture content or extruder temperature reduced the specific mechanical energy and torque by 40–45% during extrusion. An increase in feed moisture created TVPs with lower bulk densities and rehydration ratios while an increase in extruder temperature or screw speed increased the bulk density of the TVPs. An increase in screw speed also caused a decrease in the water holding capacity of the milled TVP flours. The TVP flours had a 33–70% higher oil holding capacity than the raw material. The texture profile showed that an increase in feed moisture influenced TVP hardness, gumminess, and chewiness with higher values compared to the treatments with lower moisture contents. Springiness, cohesiveness, and resilience were more affected by a change in screw speed with higher values at 200 rpm. The best parameters were selected (125 °C, 40% MC, 300 rpm) to produce TVP to use as a partial (hybrid burger) and complete (vegan burger) replacement of beef in a burger patty. The replacement of 25% beef with TVPs in a hybrid burger increased the cooking yield and moisture retention and decreased the thickness and diameter change compared to the beef burger without TVPs. In a vegan formulation, the faba bean TVP burger had lower cooking yield and moisture retention than commercial products.

Twelve GRAS (generally recognized as safe) microorganisms, including seven bacteria (Lactobacillus delbrueckii, Lactobacillus rhamnosus, Weissella confusa, Lactococcus lactis, Leuconostoc pseudomesenteroides, Pediococcus pentosaceus, and Tetragenococcus halophilus), one fungus (Aspergillus oryzae), and four yeasts (Zygosaccharomyces rouxii, Saccharomyces cerevisiae, Kluyveromyces marxianus, and Wickerhamomyces anomalus), were used as starter cultures for solid-state fermentation (SSF) of pea protein isolate (PPI). Improved PPI solubility was found to be the main positive effect of SSF. The greatest improvement in protein solubility, nearly a fourfold increase compared to the solubility of unfermented PPI, was achieved in samples fermented with Z. rouxii. Uninoculated “control” PPI samples, which were fermented solely by indigenous microflora, were found to have nearly threefold higher protein solubility than in unfermented PPI, which was greater than in most samples fermented with starter cultures. Two of the tested strains, W. anomalus and T. halophilus, significantly inhibited the beneficial activity of indigenous microflora, leading to unchanged or diminished protein solubilities after fermentation. Changes in protein solubility following SSF correlated with degrees of protein hydrolysis (DH): most samples, which had protein solubility of > 30

The overall goal of this research was to evaluate the suitability of various plant protein concentrates for 3D printing plant-based meat analogs for the development of dysphagia diets. Initially various protein concentrates from faba bean, chickpea, oat, pea, and mung bean were evaluated for the nutritional composition (i.e., protein quality) and physicochemical properties. The high-water holding capacity of pea (4.6 g/g) and mung bean protein (6.47 g/g) made them unsuitable for 3D printing. Oat and chickpea proteins had moderate water holding capacity (1.67 g/g and 2.07 g/g, respectively) and in vitro protein digestibility corrected amino acid scores of 74.93

Background and ObjectivesThe aim of this study was to investigate the effect of incorporation of different plant-based polysaccharides (pectin, maltodextrin (MD) and gum arabic (GA)) with pea protein isolate (PPI) to obtain maximum encapsulation efficiency (EE), gastrointestinal (GI) stability and yield of probiotic Lactobacillus casei through spray drying. Several characteristics of encapsulated vegan probiotic powders were evaluated including functional, structural, and thermal characteristics.FindingsThe results showed that the highest EE (93.9%) and in vitro GI stability (8.58 log CFU/mL) was obtained with the powder encapsulated with PPI + GA. Variation in particle size was observed for all the samples. Confocal laser micrographs and vital staining revealed the highest viability of probiotic L. casei cells that were obtained with those encapsulated in PPI + GA. Thermal properties showed that the incorporation of GA increased the glass transition temperature up to 189.2 degrees C, which represented a higher thermal stability of the powder.ConclusionsPPI + GA coated powder was found with acceptable powder characteristics and maximum probiotic survivability.Significance and NoveltyIn this study, spray drying was used to encapsulate the probiotic bacteria which is a convenient and effective process for industrial applications. Characterization of the spray-dried encapsulated probiotic powder has been done, which helps to understand the behavior of powder in terms of solubility, flowability, thermal stability, and probiotic viability. PPI was used as carrier material, which bridges the gap between already available spray-dried products containing MD as carrier material, which could spike blood sugar levels if consumed over an extended period of time. As per the results, target product applications could include sports bars, cereals, and baking where dispersibility is not imperative.

Faba beans are a promising protein source, but the functional proteins must be extracted for stable beverage emulsion development. The present study examines the impact of an aqueous-based mild fractionation on the recovery, composition, interfacial and emulsifying behaviour of protein-rich soluble fractions from faba bean flour. Mild fractionation was performed at two different centrifugation speeds (3000 rpm and 4000 rpm) for various time durations (1.5-4 min). Proximate composition revealed enhanced protein recovery at the higher centrifugation speed, with the highest protein concentration of 85.9 % obtained at 4000 rpm for 2.5 min. The speed and duration of centrifugation could be controlled to optimize the extraction and protein yield from faba bean flour. The albumin-to-globulin ratio increased after mild fractionation as the duration of centrifugation increased until a plateau was observed. Interfacial tension of the soluble fractions decreased as the duration of centrifugation increased. Emulsions prepared with 3000 rpm fractions had larger droplet sizes and destabilized rapidly, while the 4000 rpm fractions could produce stable emulsions with much smaller droplet sizes. The albumin-to-globulin ratio and the presence of various minor components (phenolics, saponins and phospholipids) had negligible effects on the emulsion stability. It was found that the higher amount of hydrophobic amino acids and higher surface hydrophobicity of the 4000 rpm fractions led to faster adsorption to the oil-water interface, which could be responsible for their better emulsion stabilization ability than the 3000 rpm fractions. The proposed mild fractionation is a sustainable approach to developing stable emulsions as it can successfully retain the native proteins with their emulsifying behavior.

The overall goal of this research was to develop faba bean protein emulsion-based films with antimicrobial capabilities using oregano essential oil (OEO), nisin, and ethylenediaminetetraacetic acid (EDTA) and to evaluate their efficacy in reducing pathogen survival on artificially inoculated fresh meat (eye-of-round steak). Initial screening of film-forming solutions showed that combining OEO with higher concentrations of nisin and EDTA was most effective in inhibiting Salmonella enteritidis , Escherichia coli , and Staphylococcus aureus . OEO was incorporated into films using either high-shear homogenization (HSH) [0%, 1%, 2%, and 3%, and 1% with 10 mg nisin and 320 mg EDTA] or high-pressure homogenization (HPH) [0%, 1%, and 1% with 10 mg nisin and 320 mg EDTA] to examine the effect of oil droplet size on film characteristics and bactericidal efficacy. A week-long pathogen survival study showed that the viable bacterial load was reduced by 2.5, 4, and 1.9 log for each of the bacteria, respectively, for films produced with HSH, versus 2.2, 2.3, and 1.1 log for those produced with HPH. Nisin and EDTA did not have a significant effect on film characteristics, whereas OEO increased film elasticity (115% for 0% OEO vs. 204% for 3% OEO) and decreased water vapor permeability, but only when HPH was used (0.67 g·mm/kPa·h·m 2 for the 0% OEO films [HSH] vs. 0.63 g·mm/kPa·h·m 2 for the 1% OEO [HSH] vs. 0.48 for the 1% OEO [HPH]). These results suggest that, while HPH can improve certain characteristics of protein-based films, it also reduced their antimicrobial capacity.

Background and ObjectivesMilling practices, otherwise refined for specific uses in cereal-based foods, have not been thoroughly developed for pulses. This study investigates whether scouring and moisture conditioning pretreatments on yellow peas and green lentils can enhance hull removal, and in turn, whether changes in hull removal alter in vitro protein digestibility and quality.FindingsTotal by-product losses were significant in green lentils when subject to scouring, which was altered by high moisture addition in yellow peas. The scouring pretreatment altered both the protein digestibility and amino acid scores of green lentils, which translated to improved protein quality in all streams, but significantly in the break flour stream. Yellow peas similarly demonstrated significant improvements in protein quality from scouring, as a result of altered amino acid scores.ConclusionThe addition of a scouring procedure can improve the protein quality of yellow peas and green lentils.Significance and NoveltyPulse milling procedures are rarely evaluated for optimization of protein quality. This research establishes milling protocols that may be used to enhance the protein quality of yellow peas and green lentils.

Pigeon pea and rice protein concentrates exhibit high protein content exceeding 70

Background and Objectives Cassava leaves represent a significant waste stream in cassava cultivation, currently underutilized in both food and nonfood applications. This study investigates the use of solid-state fermentation with Aspergillus oryzae, Lactobacillus plantarum, and Bacillus subtilis to modify the composition and functional properties of cassava leaf flour (CLF), as well as to serve as a pretreatment for wet fractionation aimed at producing higher protein ingredients.Finds Results showed that fermentation increased the protein content of CLF while reducing anti-nutritional compounds. Fermentation had no significant effect on water-holding capacity or protein digestibility, but it increased oil-holding capacity and decreased solubility. Alkaline extraction followed by isoelectric precipitation was applied to extract proteins from the fermented CLF; however, fermentation did not improve protein availability, as evidenced by the lower protein purity of the concentrates when compared to non-fermented samples. Nevertheless, the functional properties of the protein concentrates obtained from the fermented cassava leaves were improved, demonstrating a positive effect of fermentation on the extracted protein's techno-functional potential.Conclusions Overall, fermentation increased the protein content of CLF, reduced anti-nutritional compounds, and enhanced the functional properties of the extracted protein.Significance and Novelty These findings suggest that fermentation of cassava leaf flour represents a viable biotechnological strategy for sustainable food industry applications, contributing to the development of more sustainable food supply chains.