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Chicken analogs were structured using binary blends of soy protein isolate (SPI) and wheat gluten (WG) or whey protein concentrate (WPC), as well as trinary blends of SPI-WG-WPC via high moisture extrusion. Chicken analogs with anisotropic structures were achieved (anisotropic index >1). Although adding WPC increased hardness, by varying the ratio of SPI to WG in the trinary blends, comparable texture profile properties as cooked chicken breast were achieved. The drivers of the fiber structure formation were non-covalent protein-protein interactions like hydrogen bonds and hydrophobic interactions, and to a lesser extent, inter-protein disulfide bonds formation. β-sheets were the dominant secondary structure, and adding WPC increased the proportion of α-helix while adding WG increased the proportion of β-turns in the meat analog (MA). This study offered strategies on structuring extruded chicken analogs with WPC, a high-quality protein source, and provided insights into mechanisms underlying the formation of fiber structures. • Chicken analogs structured via high moisture extrusion of plant and dairy proteins. • Addition of WG decreased hardness, chewiness, and springiness of chicken analogs. • Non-covalent bonds were the main drivers of structure formation in chicken analogs. • Adding WPC resulted in more compact, but WG resulted in looser protein networks. [ABSTRACT FROM AUTHOR]

Pea protein, a valuable plant-based protein source, is notable for its nutritional value, essential amino acids, and low allergenicity, making it widely applicable in food, medicine, and materials. It consists mainly of globulin and albumin, which influence its functional properties and applications. However, there is a lack of comprehensive reviews on its extraction methods, functional properties, modification techniques, and applications in food. This paper aims to fill these gaps by detailing pea protein composition, extraction methods, functional properties, and modification impacts while summarizing its food applications and proposing future research directions. The goal is to enhance pea protein's functionality and expand its applications through optimized extraction and advanced technology. By improving extraction techniques and adapting pea protein for better functionality, we aim to develop high-quality market applications, ensuring the growth and sustainability of the pea protein industry globally. This approach promises a flourishing future for pea protein, meeting global competition demands and driving industry advancement. [Display omitted] [ABSTRACT FROM AUTHOR]

High moisture extrusion allows the production of plant protein-based products, including meat analogues. Building upon our previous findings showing that zein mixed with rice starch provides the necessary textural properties to formulations, different pea protein-based formulations with varying amounts of zein and rice starch or wheat gluten (as control) were produced using high moisture extrusion and the rheological, textural, and microstructural characteristics were evaluated and associated with the secondary structure of proteins. Samples containing wheat gluten presented desirable rheological and mechanical properties in terms of texturization, which was evidenced by the generation of a layered and three-dimensional viscoelastic network. The addition of rice starch to zein significantly increased the viscoelasticity of the samples due to enhanced development of non-covalent interactions that led to higher and more stable β -sheets content and to the formation of a fibrous and layered microstructure and a 3D network nearly like those obtained with gluten. The sole replacement of pea protein by zein was not enough to develop these desired characteristics, demonstrating the importance of the non-covalent interactions between rice starch and zein for the generation of these properties. Overall, zein and rice starch improved texturization of pea protein-based gluten-free analogues made by high moisture extrusion. [ABSTRACT FROM AUTHOR]

This study explored the relationship between pea protein foaming properties and their structure and physicochemical properties under neutral and acidic pH. Results showed that pH modified the zeta potential, particle size and surface tension due to electrostatic changes. FT-MIR and fluorescence spectra revealed pH-induced conformational changes, exposing hydrophobic groups and increasing sulfhydryl content, promoting protein aggregation. At pH 3, the highest foaming capacity (1.273) and lowest foam expansion (6.967) were observed, associated with increased surface hydrophobicity and net charges, ideal for creating light foams with high liquid incorporation for acidic beverages or fruit-based mousses. Pea protein isolate generated stable foams with foam volume stability between 86.662 % and 94.255 %. Although neutral pH conditions showed the highest foam volume stability, their air bubbles increased in size and transitioned from spherical to polyhedral shape, suitable for visual-centric applications, like cappuccino foam and beer-head retention. Foams at pH 5 exhibited the smallest bubbles and maintained their spherical shape, enhancing drainage resistance, beneficial for whipped toppings. Strong correlations (Pearson correlation coefficient higher than 0.600) were noted between the structure, surface and foaming properties, providing crucial insights into optimizing pea protein functionality across various pH conditions, enabling the development of plant-based foamed products with tailored properties. [Display omitted] • pH altered secondary and tertiary structure, and surface properties of PPI. • Significant impact is noticed on β-sheet, β-turn, A1, A2 and SS bonds contents. • Decreasing pH from neutral to acidic increased surface hydrophobicity. • Neutral pH had highest foam stability; pH 5 produced smaller, more uniform bubbles. • Correlations showed links between structural changes and foaming properties. [ABSTRACT FROM AUTHOR]

The current study was undertaken to synthesize pea protein based films containing fatty acids with various chain lengths. Films namely PFAF1, PFAF2, and PFAF3 were fabricated in the presence of pelargonic acid, margaric acid, and pentacosanoic acid, respectively. Also, negative (PF: film formulated using protein alone) and positive control (PCF: film formulated using mixture of protein and chitosan) control were prepared. Interactions occurring within films were clarified by FTIR. Moreover, morphology and thermal behavior of samples were evaluated by SEM and TGA. Variations in thickness (PF: 0.03 mm, PFAF1: 0.03 mm, PFAF2: 0.04 mm, PFAF3: 0.04 mm, PCF: 0.06 mm) and water content (PF: 28.85 %, PFAF1: 16.20 %, PFAF2: 14.51 %, PFAF3: 12.04 %, PCF: 13.83) were obvious. Superior opacity was identified in PCF, followed by PFAF3, PFAF2, PFAF1, and PF. PFAF3 together with PCF were more successful than others in reducing/protecting oxygen and water permeation. Adding fatty acid or chitosan to protein films led to the decline in tensile strength (TS) and increment in elongation at break (E). As for preservation performances, maximum limitations against shifts in weight and color of bananas during 7-day storage were provided by PFAF3. Also, except for PF, all coatings (especially PFAF3) postponed the rotting of fruits. • A versatile approach to food wrapping field. • Designing eco-friendly innovative natural plant protein based films. • A strategy for enhancing the film forming ability of plant proteins. • Positive correlation between fatty acid chain length and barrier behavior of films. • Packaging for maintaining postharvest quality of fruit over prolonged storage. [ABSTRACT FROM AUTHOR]

Poor dispersibility of curcumin (cur) in aqueous medium and heat instability are common drawbacks preventing its efficiently practical use. Herein, the aim of this work was to reduce the size of cur crystals to the nanoscale through solid dispersion technique and subsequently stabilize them in an amorphous form. In this work, different ratios of pea protein (PP) to cur (6: 1, 12:1, 18:1 and 24:1, w/w) nano-supernatant (NS) in water were prepared via microfluidization. Results showed that particle size, Zeta potential (ZP) and cur concentration of cur in PP-cur NS in optimal conditions reached 357.45 nm, −33.43 mV and 81.68 mg/L, respectively. PP-cur NS showed excellent storage stability within one month and high heat stability of 52.32% at 90 °C after 180 min. Structural analysis including FT-IR, DSC and XRD indicated that cur entered into the hydrophobic pocket of PP by hydrophobic interactions and hydrogen bonds after microfluidization. This study indicated that PP exhibiting as an emulsifier and carrier might significantly reduce the surface tension of NS and in turns prolong their storability. • First reported the preparation of pea-protein (PP) nano-supernatant in water. • Treatment conditions of microfluidization process were statistically optimized. • Physicochemical properties of different ratios of PP-cur nano-supernatant were investigated. • Cur concentration in PP-cur nano-supernatant was higher than previously reported one. • Interaction mechanisms between PP and cur were proposed. [ABSTRACT FROM AUTHOR]

Solution stability of food proteins is a crucial factor determining their shelf-life and sensory properties; yet to obtain stable protein products such as beverages is generally challenged by the growing demand for non-additive foods. Here, we report a facile method stabilizing pea proteins (PPs) by a simple preheating process at a concentration below 4% (w / v) and a temperature >90 °C. Far ultraviolet circular dichroism, fluorescence spectra, together with light scattering analyses demonstrated that the PPs were unfolded and became crosslinked via exposed hydrophobic moieties and disulfide bonds, giving rise to the formation a stable spatio-temporal interconnected system that could withstand the initial nucleation of aggregations. In addition, for reheated samples treated at a sufficiently high concentration of 15% (w / v), rheological characterizations revealed decreased aggregation along with increased preheating temperature and decreased preheating concentration. The robust strategy, along with the stabilized PPs in this study, would give a strong insight into preparation of heat-stable proteins with a wide span of concentrations, which may serve the needs for protein-enriched ingredients and satisfy the demands for cost-effective protocols applied in food industry. [ABSTRACT FROM AUTHOR]

In this study, pea protein isolate (PPI) nanoparticles were fabricated with calcium-induced cross-linking and the potential as a nano-carrier for protecting resveratrol (RES) from degradation as well as improving its antioxidant activities was investigated. Ca2+ ions concentration and pH value had significant impacts on the formation of PPI nanoparticles. Dissociation assays suggested that PPI nanoparticles were mainly formed and stabilized by Ca2+ ions induced salt-bridge, hydrophobic interaction, and hydrogen bonding. Encapsulation efficiency (EE) and Loading amount (LA) of RES in PPI nanoparticles was 74.08%, and 30.24 μg/mg protein, respectively. Fluorescence emission results suggested that the formation of RES-PPI nanoparticles was primarily driven with hydrophobic interaction. AFM results clearly indicated that both RES-PPI nanocomplexes and RES-PPI nanoparticles were nano-scale, spherical shaped and distributed uniformly. RES-PPI nanoparticles exhibited higher physicochemical stability (Z-average diameter stability and RES retention) than RES-SPI nanocomplexes. Antioxidant ability of RES can be remarkably enhanced with both PPI-based nano-delivery systems. Ca2+ ions induced PPI nanoparticles obtained in this study have the great potential as functional delivery systems for hydrophobic nutraceuticals in food, and pharmaceutical industry. Unlabelled Image • PPI nanoparticle was fabricated with calcium-induced cross-linking. • RES-PPI nanoparticles were primarily driven with hydrophobic interaction. • RES retention in PPI nanoparticle is higher than that in PPI nanocomplex. • Antioxidant ability of RES can be enhanced with PPI-based nano-delivery system. [ABSTRACT FROM AUTHOR]

The development of food-grade high internal phase emulsions (HIPEs) for 3D printing and the replacement of animal fats have attracted considerable attention. In this study, in order to improve the rheological properties and stability of pea protein to prepare HIPE, pea protein/carboxymethyl cellulose (pH-PP/CMC) was prepared and subjected to pH cycle treatment to produce HIPEs. The results showed that pH cycle treatment and CMC significantly reduced the droplet size of HIPEs (from 143.33 to 12.10 μm). At higher CMC concentrations, the interfacial tension of the PP solution decreased from 12.84 to 11.71 mN/m without pH cycle treatment and to 10.79 mN/m with pH cycle treatment. The HIPEs with higher CMC concentrations subjected to pH cycle treatment showed shear thinning behavior and higher viscoelasticity and recovered their solid-like properties after being subjected to 50 % strain, indicating that they could be used for 3D printing. The 3D printing results showed that the pH-PP/CMC HIPE with 0.3 % CMC had the finest structure. Our work provides new insights into developing food-grade HIPEs and facilitating their use in 3D printing inks as nutrient delivery systems and animal fat substitutes. • PP-stabilized O/W HIPE reinforced by pH cycle treatment and CMC • CMC and pH cycle reduced surface tension at the oil-water interface and droplet size of HIPEs. • pH cycle treatment gave the PP/CMC-stabilized HIPE better rheology property. • HIPEs showed good physical stability at 0.2 % and 0.3 % CMC concentrations. • The 3D printed objects have high shape fidelity and self-supporting ability. [ABSTRACT FROM AUTHOR]

This study aimed to optimize the formulation of olive oil-in-water (O/W) emulsion gels by incorporating Pea Protein (PP) and Guar Gum (GG) as alternative options for solid fats. The optimum rheological (consistency index, apparent viscosity, recovery) and texture (firmness) properties of the emulsion gels were obtained using a mixture of 2 % PP, 1 % GG, 60 % Olive Oil (OO), and 37 % Water (W). The blend of PP2/GG1 showed the highest results for recovery and firmness, 111.27 % and 33.89 g , respectively. PP/GG blend emulsion gels exhibited higher absolute ζ-potential values, ranging between −72.3 and −77.4 mV. The polydispersity index (PDI) ranged from 0.185 to 0.535, with the most uniform distributions found in the PP/GG blend emulsion gels. Strong phase separation resistance indicated strong stability of PP-GG complex emulsion gels. Higher PP concentrations decreased emulsion oxidation. FTIR and XRD research showed that PP and GG interact strongly, indicating good compatibility. The free binding energy of the most stable configuration of the molecules was −6.8 kcal mol−1, indicating a high affinity. PP interacted with GG through 9 amino acid residues, with notable residues being Asp 224, Thr 235, Ala 332, Ile 334, and Arg 336, and their respective interaction distances ranged between 2.69 Å and 3.87 Å. • The optimal formulation was determined as PP (2 %), GG (1 %), OO (60 %), and W (37 %). • PP-GG complex emulsion gels were stable and phase-resistant. • Hydrogen bonds were the primary form for interaction between PP and GG. [ABSTRACT FROM AUTHOR]

In this study, a composite hydrogel consisting of pea protein and konjac glucomannan (KG) was fabricated using three approaches, namely neutral, salt-set, and alkaline gelation. Hydrogels made from pea protein were brittle and weak. The addition of KG improved the elasticity and water holding capacity of the pea protein hydrogels. Concomitantly, a decrease in syneresis rate and swelling of the composite hydrogels was observed. The alkaline-set hydrogels exhibited the highest resilience to strain. Thixotropicity was found to be less pronounced for salt-set hydrogels. Sulphate had a greater positive effect on the structural recovery and negative effect on hysteresis area than chloride due to the greater salting-out effect of the sulphates. The addition of KG facilitated the formation of an interconnected structure with limited mobility of biopolymer chains. A sharp increase in G' and G" during the temperature ramp indicated the predominance of hydrophobic interactions towards the aggregation of biopolymers. The infrared spectra of the hydrogels revealed a change in secondary structure of proteins on addition of KG. A controlled in vitro release of riboflavin was observed in neutral and salt-set hydrogels. The alkaline-set hydrogels exhibited a prolonged gastric retention time, thereby establishing in vitro antacid activity in the gastric environment. • Konjac glucomannan (KG) improved the structural resilience of composite pea protein (PP) hydrogels. • Alkaline-set hydrogels were more stable than neutral and salt-set hydrogels. • Alteration in secondary structure of the protein due to the addition of KG. • Controlled in-vitro release of riboflavin from the salt-set hydrogels. • Prolonged in-vitro antacid activity of alkaline-set hydrogel, compared to unencapsulated Na 2 CO 3. [ABSTRACT FROM AUTHOR]

This study investigated effects of carboxymethylcellulose sodium (CMC) on the conformational evolution of pea protein during the high moisture extrusion process. The morphological observation showed that the addition of CMC facilitated the formation of fibrous structure of pea protein. In comparison with the pea protein in the melting zone and extrudate, the combination of CMC increased the denaturation enthalpy of pea protein by 2.09 % and 2.34 %. Compared with the material in the mixing zone, the degree of grafting between CMC and pea protein in the die was enhanced by 98.95 %. In general, the supplementation of CMC depressed the exposure of hydrophobic groups in the pea protein. In the extrusion barrel, the CMC increased the unfolding of protein molecular chains while it promoted the refolding of protein chains in the die. For the extrudate, the addition of CMC decreased the contents of α-helix and β-sheet of pea protein by 9.67 % and 6.93 % while the contents of β-turn and random coil were increased, leading to changes in the molecular weight distribution of protein molecules. In conclusion, these results provided new strategies toward producing the high-quality pea protein-based meat analogues by adding CMC. [ABSTRACT FROM AUTHOR]