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BACKGROUND RESULTS CONCLUSION Pea protein isolate (PPI) is gaining increasing popularity in the food industry. It provides a diverse range of health benefits, such as hypoallergenic and gluten‐free characteristics. However, the functional performance of PPI is hindered by its low solubility and poor stability. Therefore, in this article, PPI and dextran (DX) of different molecular weights were grafted to investigate the effects of grafting DX with different molecular weights on the interface properties and antioxidant properties of PPI. Additionally, the stability and digestive properties of the glycated PPI nanoemulsion system were explored.The result showed that the grafting degree of PPI–DX conjugates (PPI–DC) decreased with an increase in the molecular weight of DX. Surface hydrophobicity, antioxidant activity and solubility of PPI–DC were significantly improved after grafting compared with PPI and PPI–DX mixtures (PPI–DM). Astaxanthin‐loaded emulsions stabilized by grafted conjugates had smaller droplets and higher astaxanthin encapsulation rate compared to PPI emulsions. In vitro digestion demonstrated that the bioavailability of PPI–DC emulsions was higher than of PPI emulsion. Furthermore, after 24 days of storage, retention rate of astaxanthin‐loaded emulsions prepared by conjugates remained above 70%, surpassing that of PPI emulsion.These results indicated that DX grafting can improve the emulsion properties of PPI. In addition, the DX with a molecular weight of 5 kDa showed the most significant improvement. This study contributes to the advancement of natural emulsifiers by modifying PPI through glycation, and furnishes a valuable reference for its utilization in functional foods. © 2024 Society of Chemical Industry. [ABSTRACT FROM AUTHOR]

Summary: This study examined the rheological and textural properties of gels produced through emulsion gelation using pea protein isolate (PPI). Emulsions were prepared with varying PPI concentrations (2%–10%) and 0.25 oil fraction, followed by heat treatment. Higher PPI concentrations improved encapsulation efficiency (EE), but heat slightly reduced it, though EE remained above 90%. Droplet size decreased with higher PPI. The emulsion was then gelled with different kappa‐carrageenan (KC) concentrations (1%–2%) and pH levels (4–7). Gel hardness increased with KC content, while adhesiveness decreased. Springiness, cohesiveness and water‐holding capacity (WHC) rose with pH and KC, while meltability decreased. Rheological tests showed stronger gels with higher KC and lower pH. Storage time generally increased gel strength, except at pH 4. This work highlights the interplay between PPI, KC, pH and storage time in shaping the properties of pea protein‐based emulsions and gels. [ABSTRACT FROM AUTHOR]

Summary: Milk proteins are known for their exceptional nutritional and technological attributes, making them a staple in the food industry. Nonetheless, the partial substitution of milk proteins with plant‐based proteins in dairy products may be an effective strategy to meet the increasing consumer demand for a reduction in the consumption of animal‐derived proteins. This study aimed to evaluate the impact of partial substitution (25% and 50%) of milk proteins with pea protein on the manufacturing and technological attributes of high‐protein yogurt during refrigerated storage. The replacement of up to 50% of the milk proteins with pea protein did not alter the fermentation time and all yogurts had a total lactic acid bacteria count greater than 107 CFU g−1 after manufacturing. However, replacing 50% of milk proteins with pea protein affected the pH, syneresis, water holding capacity, consistency, firmness, viscosity index, and cohesiveness of the yogurts. In turn, no effect was observed on the pH, syneresis, water holding capacity, firmness, and cohesiveness of the product after replacing 25% of the dairy base with pea protein (P >0.05). Hence, the findings indicate that substituting 25% of the milk protein with pea protein in high‐protein yogurts can be achieved without compromising the product's stability. [ABSTRACT FROM AUTHOR]

Summary: The aim of this study was to investigate the effects of microbial transglutaminase (MTGase) on the textural properties and meltability of vegan cheese formulated using cashew paste, tapioca starch, coconut oil, and pea protein. The parameters were evaluated at various MTGase concentrations (0.1, 0.25, 0.5, 0.75, and 1%) and different incubation times (30, 60, and 90 min). A MTGase concentration of 0.25% resulted in higher meltability Index of 3.02 ± 0.14 and acceptable hardness of 3479.44 ± 14.49 g at 30 min of incubation time. However, prolonged incubation times were found to adversely affect the texture and meltability of the cheese. A similar adverse effect on texture was observed at an MTGase concentration of 0.1% at 60 and 90 min of incubation. The results revealed that lower MTGase concentrations with longer incubation times produced similar effects as higher MTGase concentrations with shorter incubation times. However, at a lower enzyme concentration of 0.1%, meltability was significantly higher (3.24 ± 0.33, P < 0.05) at 60 min of incubation compared to 90 min. The findings suggest that vegan cheese with improved texture, meltability, and sensory properties can be developed by combining cashew, tapioca starch, coconut oil, and pea protein in a ratio of 50:25:20:10, with 1% each of carrageenan and agar, and 60% water, and incubating the mixture with 0.25% MTGase for 30 min at 40 °C. [ABSTRACT FROM AUTHOR]

ABSTRACT Fat and protein derived from milk are prime ingredients in a frozen dessert such as ice cream conferring multiple desirable functionalities. However, this frozen dairy dessert is not suitable for individuals having lactose intolerance, cow milk allergy, or vegans. Hence, the study aimed to formulate dairy‐free frozen desserts using plant oils and plant proteins and compare their physicochemical characteristics and sensory acceptance against an ice cream containing milk fat and milk protein. Results indicated that the types of protein significantly influenced the physicochemical properties and sensory acceptance of the frozen dessert samples. Frozen desserts containing brown rice, pea, and soy protein showed greater resistance to melting (0.29, 0.12, and 0.19%/min vs. 1.95%/min), but they scored lower in sensory quality than ice cream made with milk protein; although they remained at an acceptable level. When compared among the plant proteins, the physicochemical characteristics of frozen desserts containing brown rice, pea, and soy protein varied because of the differences in the respective protein composition. Frozen dessert with brown rice protein showed higher overrun (47.50% vs. 40.78% and 37.8%), lower hardness (20.02 N vs. 22.24 and 26.37 N), and higher melting rate (0.29%/min vs. 0.19 and 0.12%/min) than frozen desserts containing soy and pea protein. Additionally, the brown rice protein frozen dessert received lower sensory acceptance than soy and pea protein frozen desserts. In summary, brown rice, pea, and soy proteins showed potential to be used as viable alternatives to milk protein for dairy‐free frozen dessert applications. [ABSTRACT FROM AUTHOR]

BACKGROUND RESULTS CONCLUSION The design of plant‐based microgels provides a platform for food ingredients to enhance palatability and functionality. This work aimed to explore the modifying effect of salt addition (KCl) on the structure of pea protein microgel particles (PPI MPs), on the interfacial adsorption and characteristics of formed emulsions as fat analogues.Salt addition (0–200 mmol L−1) promoted a structural transformation from α‐helix to β‐sheet, increased the surface hydrophobicity (from 1160.8 to 2280.7), and increased the contact angle (from 56.73° to 96.47°) of PPI MPs. The electrostatic shielding effect led to the tighter packing of MPs with irregular structures and lowered the adsorption energy barrier. Notably, salt‐treated PPI MPs could adjust their adsorption state at the interface. The discernible adsorption of PPI MPs with 200 mmol L−1 salt addition that possessed enhanced anti‐deformation ability dominated the interfacial stabilization, whereas a relatively rougher stretched continuous interfacial film formed after spreading and deformation of 0 mmol L−1 MPs. A tribological test suggested that emulsion stabilized by MPs at 0 (0.0053) and 80 mmol L−1 (0.0068) had similar friction coefficients to commercial mayonnaise (0.0058), whereas a higher salt concentration (200 mmol L−1) lowered its oral sensation due to the adsorption layer and enhanced the resistance to droplet coalescence during oral processing.Salt could be a modifier to tune the structure of microgels, and further promote the formation and attributes of emulsions. This study would improve application attributes of PPI MPs in the design of realistic fat analogues. © 2024 Society of Chemical Industry. [ABSTRACT FROM AUTHOR]

Oil‐in‐water emulsions are widely used as the base flavoring or clouding agents in various beverages. Pulse proteins can play a major role as a natural emulsifier in beverages. However, the presence of insoluble components greatly minimizes their potential application in beverage emulsions. In this work, pea protein concentrate was mildly fractionated by aqueous centrifugation to recover a soluble fraction with 71% protein yield, which was then used to develop 5% oil‐in‐water emulsions using a high‐pressure homogenizer. Emulsion stability was tested by heat treatment (90°C, 30 min) in the presence of NaCl (0–1 M) at pH 7.0 and 2.0. Stability increased upon the addition of salt at pH 7, while at pH 2, proteins and droplets aggregated. Heat treatment led to extensive aggregation at both pH values, which was further worsened by salt. To prevent thermal destabilization, the proteins were heat‐treated at 75°C for 30 min for partial denaturation before emulsification under hot conditions. The heat‐treated protein‐stabilized emulsions at pH 7 had superior thermal stability at all salt concentrations without aggregation. However, a similar improvement was not observed at pH 2. Pre‐heating the soluble protein exposed the hydrophobic patches, leading to better adsorption on the droplet surface, which did not show additional aggregation upon further heating the emulsions at pH 7. Interestingly, heat‐treated protein‐stabilized emulsions showed a 44% drop in lipid digestibility compared to the original emulsions. The proposed approach could be a valuable addition to the utilization of pea proteins in beverage emulsions that could withstand heat treatment during food processing. [ABSTRACT FROM AUTHOR]

Pea proteins have garnered attention as a viable alternative to animal proteins, offering health, and sustainability benefits. However, their functional limitations, such as poor solubility, hinder their application in plant‐based food products. This review details the specific physical, chemical, and biological methods employed to enhance pea protein functionality. Chemical methods have been the most effective, particularly in improving solubility, emulsification, and foaming properties, which are essential for food applications like dairy alternatives and meat analogues. Biological methods significantly enhance water and oil retention, contributing to better food texture. Physical methods, including ultrasound and heat treatment, also show promise but require careful application to avoid protein denaturation. While chemical methods are efficacious, they raise concerns about cost‐effectiveness and environmental impact. The review identifies combined treatment approaches as a fertile area for future research, suggesting that a multi‐faceted strategy may provide comprehensive improvements to pea protein functionality. [ABSTRACT FROM AUTHOR]

Food emulsion is one of the major systems in the food industry, which exists in spreads, dressings, creams, sauces, dips, and beverages. Recently, there has been an active search for suitable plant protein sources to replace animal proteins for the fabrication of advanced emulsion systems in the food industry. Pea protein is getting more and more attention as a good emulsifier in the food industry because of its low cost, low allergy, rich nutrition, and good functionality. This review summarizes recent studies on the fabrication and utilization of these advanced emulsions with pea proteins, including nanoemulsions, Pickering emulsions, high internal phase emulsions, and double emulsions. A brief description of emulsifying property of pea protein is given, then the formation and properties of each type of pea protein emulsions are described, and finally, the potential applications of pea protein as an emulsifier in commercial food products are introduced. A particular emphasis is given to the utilization of pea protein as an emulsifier and these advanced pea protein emulsions for the delivery of bioactive components, 3D printing, and production of market products. [ABSTRACT FROM AUTHOR]

Food industry has partially replaced animal proteins with plant‐derived alternatives, and effects of combining these two types on properties of food systems need to be elucidated. This study fabricated and characterised emulsion gels of mixed whey and pea protein, varying protein mass ratios from 100:0 to 0:100 and oil volumes from 30% to 45%, induced by transglutaminase cross‐linking. An increase in pea protein led to larger particle size and reduced surface charge in the solutions. Emulsion droplet size ranged from 0.60 to 15.17 μm, increasing with higher levels of pea protein and oil. Mixed protein gels exhibited significantly greater hardness compared to gels with individual proteins. Water‐holding capacity of pure whey protein emulsion gels exceeded 90%, while the value remained above 80% when pea protein was less than 50%. Partially replacing whey protein with pea protein may have potential applications in food products such as salad dressings and cheese. [ABSTRACT FROM AUTHOR]

BACKGROUND RESULT CONCLUSION Plant‐based beverages have recently seen a significant increase in market demand. However, many of these products suffer from poor emulsion stability and low protein content. Gums have commonly been used to enhance emulsion stability but they do not improve the amino acid profile. This study investigated the use of multiples plant proteins to enhance both the stability and nutritional value of plant‐based beverages.Pea and rice bran proteins both enhanced emulsion stability. Pea protein enhanced the viscosity of the continuous phase whereas rice bran protein lowered interfacial tension. When applied synergistically, competitive adhesion occurred. Rice bran protein gradually displaced pea protein from the oil droplet surface as its concentration increased, leading to emulsion destabilization due to the displaced pea protein. The use of high‐pressure homogenization further enhanced the stability of the emulsion by unfolding protein partially. However, increasing homogenization pressure (>500 Bar) and homogenization cycle (>2 cycles) led to protein aggregation due to excessive exposure of its hydrophobic core. The emulsion formed was resistant to coalescence at 4 °C for 28 days and was stable under high pH and low ionic conditions.The synergistic combination of plant proteins and the effective utilization of co‐processing (homogenization) can enhance the functionality of the individual proteins significantly, leading to the formation of a stable emulsion. The use of plant protein mixture as a stabilizer not only improved the emulsion stability but also ensured a plant‐based beverage with a complete amino acid profile for the vegan community. © 2024 The Author(s). Journal of the Science of Food and Agriculture published by John Wiley & Sons Ltd on behalf of Society of Chemical Industry. [ABSTRACT FROM AUTHOR]

BACKGROUND RESULTS CONCLUSION Construction of meat analogs based on pea protein isolate (PPI) alone by high moisture extrusion (HME) is diffocult as a result of the lack of anisotropic structures. In the present study, 0%–15% of whey protein (WP) was introduced to PPI to make hybrid blends, which were used to construct HME extrudates.WP enhanced the hardness, adhesive, cohesiveness and gumminess of the extrudates and facilitated the formation of a distinct anisotropic structure of PPI. The fibrous degrees of the extrudates containing 10% and 15% WP were around 1.50. The addition of WP, which has more ‐SH groups, increased the disulfide bonds and hydrogen bonding in the extrudates, leading to a denser cross‐linked structure. Particle size distribution and Fourier transform infrared analysis showed that WP induced more compact structured aggregates and more β‐sheet structures in the extrudates. Furthermore, the higher hydration capacity of WP may also help form a dilute melt and generate a more pronounced plug flow, assisting the formation of fiber structures of PPI.The present study demonstrates that WP is a potential modifier, which could be used to improve the structure of PPI‐based meat analogs. © 2024 Society of Chemical Industry. [ABSTRACT FROM AUTHOR]

Summary: Our study focuses on the gelling properties of pea protein (PP), which are comparatively weaker than those of other plant proteins, thereby limiting its application. However, we found that the addition of κ‐carrageenan (κ‐CAR) significantly (P < 0.05) increased PP gels' hardness and water‐holding capacity irrespective of gel formation temperature (80 or 95 °C). Rheological and microstructural analysis confirmed a synergistic effect between PP and κ‐CAR, with higher synergy values observed in hydrogels formulated at 95 °C. Molecular force studies revealed that non‐covalent interactions were dominant, with disulphide bonds contributing only to the structure of gels formed at 95 °C. These promising findings not only enhance our understanding of the PP and κ‐CAR gel formation mechanism but also hold practical implications, potentially leading to improved gelling properties of PP and expanding its applications in the food industry. [ABSTRACT FROM AUTHOR]

BACKGROUND: In past years, thousands of protein‐polysaccharide complexes have been investigated to modify protein characteristics and functionality in food systems. However, the interaction between pea protein isolate (PPI) and soluble soybean polysaccharide (SSPS) has not been thoroughly characterized yet. RESULTS: In the present study, the phase behavior of PPI and SSPS mixtures was analyzed as a function of PPI:SSPS mixing ratio (1:1 to 1:0.10) and pH (7.0 to 2.0), showing that these biopolymers could be electrostatically assembled at 1:1 to 1:0.25 mixing ratios and 4.0 to 3.0 pH values. Then, the characteristics of the PPI–SSPS complexes were studied before and after heating (90 °C and 30 min) by ζ‐potential, surface hydrophobicity, protein solubility, particle size distribution and physical stability for 56 days. By lowering the pH and PPI:SSPS mixing ratio, the complexes showed increased solubility, changed 휁‐potential and higher physical stability. By heating, the complexes presented increased hydrophobicity and physical stability. CONCLUSION: Overall, PPI–SSPS complexes increased the protein solubility, reduced the particle size, and changed both the ζ‐potential and the surface hydrophobicity with respect to PPI control, allowing stabilization of the colloidal system and broadening the possible applications of these high‐quality proteins in acidic food systems. © 2024 Society of Chemical Industry. [ABSTRACT FROM AUTHOR]

BACKGROUND: Understanding the interactions between protein and starch is crucial in revealing the mechanisms by which protein influences starch digestibility. The present study investigated the impact of different contents of pea protein isolate (PPI) on the physicochemical properties and digestibility of pea starch (PS). RESULTS: The results demonstrated that as the content of PPI increased from 0% to 12%, and the digestion of PS decreased by 12.3%. Rheological analysis indicated that PPI primarily interacted with molecular chains of PS through hydrogen bonds. Increasing the content of PPI resulted in a 30.6% decrease in the hardness of the composite gels, accompanied by a 10% reduction in the short‐ordered structure of PS. This hindered the formation of molecular aggregation and resulted in a loose and disordered gel network structure. The microstructure confirmed that the attachment of PPI to PS served as a physical barrier, impeding starch digestibility. CONCLUSION: In summary, the primary mechanism by which PPI inhibited PS digestion involved steric hindrance exerted by PPI and its interaction with PS via hydrogen bonds. These findings contribute to a better understanding of the interaction mechanisms between PS and PPI and offer insights for the optimal utilization of pea resources. © 2024 Society of Chemical Industry. [ABSTRACT FROM AUTHOR]

Summary: This research explores the development of high‐moisture meat analogues (HMMA) by blending wheat gluten (WG) and rice protein (RP) with pea protein isolate (PPI) in a twin‐screw extruder under high‐moisture extrusion conditions. The study investigates the effects of incorporating RP and WG with PPI on textural, rheological and colour properties, as well as the underlying protein–protein interactions through protein solubility. From the compositional analysis of these secondary ingredients, there was no significant difference between them. However, results from the extrusion indicated that WG‐PPI showed good fibration and higher instrumental anisotropy than RP‐PPI blend extrudates. RP‐PPI blends exhibit inferior textural and rheological properties, attributed to RP's limited crosslinking ability within the protein matrix. This has resulted in a poor structure and lower textural values at higher incorporation of RP (50%) in the pea protein matrix. This was due to the insoluble protein fraction of the RP resulting in a non‐melting in the extrusion barrel. These findings underscore the importance of understanding protein interactions in developing optimised HMMA formulations, paving the way for further exploration into developing modified RP with improved physiochemical properties which can be integrated into meat analogues. [ABSTRACT FROM AUTHOR]

There is an increasing demand for plant‐based burger patties owing to the health and sustainability issues raised from the consumption of meat. This study aimed to develop plant‐based burger patties from pea protein isolates (PPIs) and barnyard millet flour (BMF) through high‐moisture extrusion cooking. The extrudates for plant‐based burger patties were developed with a blend ratio of 90:10 PPIs:BMF with different screw speeds ranging from 40 to 120 rpm. The extrudates produced with different screw speeds were analyzed, followed by the analysis of the plant‐based burger patties. Commercial plant‐based burger patties were used as a control. The optimized plant‐based burger patties were then stored in aerobic or vacuum packaging for 12 days under refrigerated condition and analyzed. The optimized extrudates produced using screw speed of 80 rpm displayed moderate water absorption index (3.33%), high hardness (4143–4390 g), and high adhesion (0.47 mJ). The plant‐based burger patties produced using the optimized extrudates had 2006–2608‐g hardness, 0.17 cohesiveness, and 6.70% cooking loss. In comparison to aerobic packaging, the plant‐based burger patties stored in vacuum packaging demonstrated lower cooking loss (8.46%), moisture content (18.03%), total color difference (3.02), and total plate count (8.65 log10 cfu/g) after 12 days of refrigerated storage. The protein content of plant‐based burger patties was not affected throughout the refrigerated storage. This shows the potential of PPIs and BMF mixtures as meat analogue ingredients and the suitability of vacuum packaging for the storage of plant‐based meat. [ABSTRACT FROM AUTHOR]

Lipid oxidation deteriorates the sensory and nutritional quality of food emulsions containing polyunsaturated fatty acids. Classically, different extraction solvents are used as a first step to measure lipid oxidation in emulsions. However, it is unclear how the applied extraction method influences the measured lipid oxidation values. In this work, we systematically examined the performance of common solvent mixtures such as chloroform, methanol, and hexane (or isooctane)–isopropanol on lipid extraction from emulsions stabilized with different emulsifiers (Tween 20 (T20), whey proteins, and pea proteins) and oxidation levels, and how this, in turn, affected the measured hydroperoxide concentrations. Chloroform–methanol was the most effective solvent (lipid yield >93 wt.%). When using hexane–isopropanol, extraction yields were consistently high for T20‐ and pea protein‐based emulsions (>60 wt.%), but in whey protein‐based emulsions, values as low as 26 wt.% were measured. In case of incomplete extraction, hydroperoxide concentrations measured by colorimetric methods need to be corrected for this effect. When using 1H NMR to assess lipid oxidation, the actual amount of extracted lipids is intrinsically taken into account. This highlights not only the importance of the extraction method in determining lipid oxidation in emulsions but also that of the actual analysis method. Practical application: This study highlights that the lipid extraction yield can vary depending not only on the emulsion composition (e.g., type of emulsifier) but also on the oxidative state of the emulsion and the extraction solvent used. If this is overlooked, errors can be made in the hydroperoxide determination. Although these effects can be corrected for, this is not standard procedure, which implies that awareness on this matter should be increased. It is also important to point out that depending on the solvent used, the different lipid classes (including various lipid oxidation products) may be extracted at different levels. Chloroform–methanol should be preferred for extraction of all lipid and lipid oxidation‐derived molecules, including aldehydes. [ABSTRACT FROM AUTHOR]

In recent years, intensive efforts made to harness tissue engineering techniques to develop cultivated meat. Sustainable meat substitutes are a promising solution for the expected world food shortage; however, multiple challenges still pose barriers to the mass, low‐cost production of nutritious cultivated meat. This work is focused on the development of edible nutritious 3D scaffolds for the production of bovine muscle tissue for cultivated meat. Protein‐rich scaffolds composed of pea protein are prepared using mold‐casting and bioprinting techniques. The plant‐based scaffolds supported bovine satellite cells' attachment, growth, and differentiation into muscle tissue without the need for coating agents or high‐cost components. The presented pea‐protein‐rich scaffolds are of high nutritional value, with low allergenicity, and can be processed under low fabrication costs, which can significantly advance the commercial production of nutritious and sustainable cultivated meat. [ABSTRACT FROM AUTHOR]

The special issue of the Journal of the American Oil Chemists' Society (JAOCS) focuses on the advancements in plant protein-based emulsions due to the increasing demand for plant-based foods. The issue includes research on utilizing plant proteins from pulses and oil seeds in various food products like mayonnaise, salad dressings, and dairy-free ice cream. The articles in the special issue cover topics such as protein modification techniques, sustainable extraction methods, and the development of functional foods using plant proteins. The research aims to improve the functionality and stability of plant protein-based emulsions for future food applications. [Extracted from the article]

Sodium carboxymethyl cellulose (CMC) is cross‐linked with pea protein isolate (PPI) to prepare pea protein isolate/sodium carboxymethyl cellulose (PPI/CMC) composite film by the diffusion method. The effects of the mass fraction of CMC on the mechanical properties and water resistance of PPI/CMC composite film are investigated. In the film containing 0.4% CMC, the water vapor permeability (1.43 × 10−7 g m (m2∙h∙Pa)−1) is significantly decreased, while the water contact angle value is elevated (55.76°). The tensile strength of the composite film is enhanced by 54.45%, while the elongation at break is increased by 23.30%. The film has excellent thermal stability and a homogenous structure. The remarkable changes may be attributed to new chemical interactions (hydrogen bonds) between CMC and PPI as revealed by Fourier transform infrared spectroscopy. Further, the composite film has great advantages in water resistance after comparison. The film is applied to the fresh bean skin, effectively blocking and reducing the tearing force between the fresh bean skin, and consequently easy separation after soaking in water for 20 min. Overall, the inclusion of CMC effectively solves the functional limitation caused by the hydrophilicity of PPI film, paving the way for its effective application as a novel edible packaging film in conventional foods. [ABSTRACT FROM AUTHOR]

Interest in plant‐based meat analogues has increased and can be expected to be applied to pet foods, which necessitates the understanding of the nutrient supply in those foods. Our primary aim was to advance our understanding of the digestive properties of sterilized plant‐based meat analogues. The impact of the preparatory processing steps on the solubility of meat analogues was studied. Meat analogues were made by mixing water, salt, and wheat gluten with soy protein isolate, pea protein isolate, or faba bean concentrate. Mixed materials were processed into model meat analogues using shear cell technology. Products were canned in water or gravy and sterilized. An animal‐based canned pet food was made as a reference. Products sampled at the processing steps (mixing, shearing, sterilization) were digested in vitro. Samples of digestate were taken at the gastric phase (0 and 120 min) and small intestinal phase (120, 200, 280, and 360 min) for analysis of protein hydrolysis. The extent digestion of nitrogen and dry matter was determined at the end of incubation. Total phosphorus, soluble phosphorus after acid treatment, and after acid and enzymatic treatment were determined. The degree of hydrolysis after gastric digestion was low but increased immediately in the small intestinal phase; products based on pea had the highest values (56%). Nitrogen digestibility was above 90% for all materials at each processing step, indicating that bioactive compounds were absent or inactivated in the protein isolates and concentrate. Phytate seemed to play a minor role in meat analogues, but phosphorus solubility was influenced by processing. Shearing decreased soluble phosphorus, but this effect was partly reversed by sterilization. Nutrient digestibility as well as phosphorus solubility in plant‐based products was higher than or comparable with the reference pet food. These findings show that the digestive properties of the tested plant‐based meat analogues do not limit the supply of amino acids and phosphorus. [ABSTRACT FROM AUTHOR]

Background: Interaction between plant‐based proteins and polysaccharides depends on several factors. This work reports the influence of pH and biopolymer ratios on the protein (pea protein isolate, PPI)‐polysaccharide (locust bean gum, LBG) coacervates. Electrostatic interaction and hydrogen bond between the biopolymers strongly influenced the formation of the coacervates. Results: The optimum coacervate conditions were observed at pH 4.5 and PPI:LBG ratio of 5:1. The coacervates showed a honeycomb porous architecture having an amorphous nature. Complex coacervates showed a significant elevation of denaturation temperature as compared to biopolymers alone. Conclusion: These results indicates that PPI‐LBG coacervates can be used as an effective biomaterial for encapsulating heat‐sensitive bioactive compounds and other multiple uses in food processing. [ABSTRACT FROM AUTHOR]

BACKGROUND: The application of curcumin (Cur) in the food industry is usually limited by its low water solubility and poor stability. This study aimed to fabricate self‐assembled nanoparticles using pea vicilin (7S) through a pH‐shifting method (pH 7–pH 12–pH 7) to develop water‐soluble nanocarriers of Cur. RESULTS: Intrinsic fluorescence, far‐UV circular dichroism spectra and transmission electron microscopy analysis demonstrated that the structure of 7S could be unfolded at pH 12.0 and refolded when the pH shifted to 7.0. The assembled 7S–Cur exhibited a high loading ability of 81.63 μg mg−1 for Cur and homogeneous particle distribution. Cur was encapsulated in the 7S hydrophobic nucleus in an amorphous form and combined through hydrophobic interactions and hydrogen bonding, resulting in the static fluorescence quenching of 7S. Compared with free Cur, the retention rates of Cur in 7S–Cur were approximately 1.12 and 1.70 times higher under UV exposure at 365 nm or heating at 75 °C for 120 min, respectively, as well as 7S–Cur showing approximately 1.50 times higher antioxidant activity. During simulated gastrointestinal experiments, 7S–Cur exhibited a better sustained‐release property than free Cur. CONCLUSION: The self‐assembled 7S nanocarriers prepared using a pH‐shifting method effectively improved the antioxidant activity, environmental stability and sustained‐release property of Cur. Therefore, 7S isolated from pea protein could be used as potential nanocarriers for Cur. © 2023 Society of Chemical Industry. [ABSTRACT FROM AUTHOR]

Summary: Chlorogenic acid (CA) is a natural antioxidant with multiple biological activities, but its stability is poor. In this article, CA‐load pea protein nanoparticles (PPCNPs) were constructed by an anti‐solvent method to enhance CA stability and characterised by multiple technologies. The results exhibited that the particle size of PPCNPs ranged from 211.62 to 429.79 nm, and the zeta potential ranged from −41.21 to −35.85 mV. PPCNPs had the highest encapsulation efficiency (61.2%) at the CA/pea protein isolate (PPI) mass ratio of 1:20. The loading capacity increased with the ratio of CA/PPI ranging from 1.3% to 3.8%. SEM showed that the nanoparticle surface was an irregular lamellar structure. FTIR showed that O–H and C–H functional group interactions occurred between CA and PPI. DSC results showed that CA was encapsulated in PPCNPs with an amorphous structure. During in vitro digestion, the ABTS radical scavenging ability and retention ratio of CA in PPCNPs was higher than that of free CA. Moreover, PPCNPs increased the bio‐accessibility of CA in vitro by 7.75%, compared with unencapsulated CA. These results suggested that PPCNPs constructed by the anti‐solvent method can reduce the degradation of CA and improve the biological activity of CA. [ABSTRACT FROM AUTHOR]

To explore the effect of plant protein hydrolysate (PPHS, soy and pea protein hydrolysate) on the characteristics of low‐fat Mozzarella cheeses (LFCs), samples incorporating PPHS were prepared and analysed for pizza bake performance, texture, meltability, sensory attributes and microstructure. Upon addition of an appropriate amount of PPHS to cheese milk, the pizza bake performance, stretch performance and sensory properties of LFC were improved, while the texture values (hardness, stickiness and stretch force) decreased gradually. Cheese matrix exhibited an irregular honeycomb structure as the PPHS content increased. Therefore, PPHS holds promise as substitute for milk protein, and LFC containing PPHS represents a highly promising low‐fat dairy product with improved quality and diversified ingredients. [ABSTRACT FROM AUTHOR]

Summary: This study aimed to assess the physical properties of pea‐based texturised vegetable proteins (TVPs) and TVP function as a meat extender (20%–40% w/w) in beef burgers. TVPs were produced with varying protein blend formulas (PBFs) (70%, 76%, 82% protein on a dry basis), extrusion screw speeds (350–450 r.p.m.) and feed moisture contents (FMCs) (38% and 42%, db). Increasing PBF raised TVP hydration time and integrity index, while FMC and screw speed had no discernable trend on these properties. A select group of TVPs were applied as extenders in beef burgers which were tested for their cooking properties and textural quality. Higher FMC lowered total cooking loss (TCL) for some burgers but overall did not impact burger cooking properties or texture. Increasing the extension level reduced TCL and change in burger diameter (CBD). TVPs produced at the lowest PBF and higher FMC studied had the greatest potential in meat extender applications, as they decreased TCL and CBD while maintaining comparable texture to burgers without TVP addition. These lower protein TVPs with enhanced cooking quality can be economically advantageous for the vegetarian and flexitarian applications of plant‐based extenders. [ABSTRACT FROM AUTHOR]

Thickened soup formulations were created with different proteins (hemp, soy, pea, and whey) to improve protein and fluid intake. The formulations consisted of a control soup, and soups with 6% whey protein, 6% hemp protein, 6% pea protein, and 6% soy protein by volume. The suitability of the samples for those living with dysphagia was evaluated using the international dysphagia diet standardization initiative (IDDSI) spoon tilt test and a sensory trial (51 older adults and 51 younger adults). The sensory trial used nine‐point hedonic scales and check‐all‐that‐apply to evaluate the different formulations. The sample with the whey addition was not significantly different than the control in terms of liking of flavor and texture, but it decreased the participants' overall liking. The hemp, pea, and soy decreased overall liking as well as liking of flavor and texture. They were associated with off‐flavors, aftertaste, and astringency. The responses from the older and younger adults were compared and significant differences were found in their liking of the texture, with the older adults finding the formulations' texture significantly more acceptable. Overall, the study identified that hemp, pea, and soy did not create acceptable thickened soup formulations and the hemp and pea formulations did not achieve a consistency level that is acceptable for those living with dysphagia. [ABSTRACT FROM AUTHOR]

A desirable quality of plant‐based meat analogues is to resemble the fibrous structure of cooked muscle meat. While texture analysis can characterize fibrous structures mechanically, assessment of visual fibrous structures remains subjective. Quantitative assessment of visual fibrous structures of meat analogues relies on expert knowledge, is resource‐intensive, and time‐consuming. In this study, a novel image‐based method (Fiberlyzer) is developed to provide automated, quantitative, and standardized assessment of visual fibrousness of meat analogues. The Fiberlyzer method segments fibrous regions from 2D images and extracts fiber shape features to characterize the fibrous structure of meat analogues made from mung bean, soy, and pea protein. The computed fiber scores (the ratio between fiber length and width) demonstrate a strong correlation with expert panel evaluations, particularly on a per‐formulation basis (r2 = 0.93). Additionally, the Fiberlyzer method generates fiber shape features including fiber score, fiber area, and the number of fiber branches, facilitating comparisons of structural similarity between meat analogue samples and cooked chicken meat as a benchmark. With a simple measurement setup and user‐friendly interface, the Fiberlyzer method can become a standard tool integrated into formulation development, quality control, and production routines of plant‐based meat analogue. This method offers rapid, cheap, and standardized quantification of visual fibrousness, minimizing the need for expert knowledge in the process of quality control. [ABSTRACT FROM AUTHOR]

BACKGROUND: Pea protein, as a by‐product of peas (Pisum sativum L.), is rich in a variety of essential amino acids that can meet the body's protein needs and is a valuable source of protein. Since the function of pea protein is closely related to its structure, pea protein has been subjected to different modifications in recent years to improve its application in food and to develop new products. RESULTS: The effects of sonication frequency (primary and secondary time) on pea protein isolate's (PPI's) structural and functional properties were investigated. Sodium dodecyl sulfate polyacrylamide gel electrophoresis demonstrated that different sonication frequencies at the same power (600 W) treatment had no effect on PPI's molecular weight. Fourier‐transform infrared spectroscopy revealed that treatment at different sonication frequencies caused secondary structural changes in PPI. The particle size distribution, foaming, stability, surface hydrophobicity, emulsification, and oxidation resistance of PPI were improved after primary and secondary sonication, but secondary sonication was not more effective than primary sonication for an extended period of time. CONCLUSION: Overall, ultrasound is able to improve the structural and functional properties of pea proteins within a suitable range. It provides a theoretical basis for elucidating the modification of the structure and function of plant proteins by ultrasound and lays the foundation for the development of plant proteins in food applications as well as development. © 2023 Society of Chemical Industry. [ABSTRACT FROM AUTHOR]

BACKGROUND: Tomato is an indispensable ingredient of the Mediterranean diet. Reformulation of traditional Mediterranean products to increase the adherence of consumers is becoming popular. In this study, a tomato snack bar enriched with olive powder and pea protein was developed by using microwave‐vacuum drying. Formulations also included tomato powder (TP) and low‐methoxylated pectin (LMP) as a structuring agent. RESULTS: The moisture content of microwave‐vacuum‐dried samples varied in the range 13.6–19.8% and water activity (aw) values were ~0.6. LMP and TP concentrations affected the color of microwave‐vacuum‐dried samples. However, the color mainly changed in conventionally dried samples due to browning. In microwave‐vacuum‐dried samples, lycopene content decreased with increasing LMP, but increased with increasing TP. Textural properties of microwave‐vacuum‐dried snack bars increased with increasing LMP and TP. CONCLUSION: Both texture and Fourier transform infrared spectroscopy results indicated that there was a network formation due to the contribution of protein and pectin; however, the type of interaction was highly dependent on the drying mechanism. Nuclear magnetic resonance relaxometry data showed that microwave‐vacuum‐dried samples had a more uniform water distribution. Besides its time and energy efficiency, microwave‐vacuum drying improved the color and textural properties of tomato snack bars compared to conventionally dried ones. © 2023 The Authors. Journal of The Science of Food and Agriculture published by John Wiley & Sons Ltd on behalf of Society of Chemical Industry. [ABSTRACT FROM AUTHOR]

Summary: Pea protein concentrate and isolate were blended to obtain protein blend formulas (PBFs) with three levels of protein content and investigated for their potential for developing texturised vegetable proteins (TVPs). PBFs were extruded at three screw speeds and two feed moisture contents to obtain TVPs. Nitrogen solubility index (NSI) and techno‐functional properties, i.e. water holding capacity, oil absorbance capacity, emulsion capacity and emulsion stability, of the raw materials and the TVPs were examined. Raising the protein content through PBF decreased NSI for both the raw formulas and the TVPs. Regardless of the PBF, extrusion processing substantially decreased NSI, but increased oil absorption capacity. Extrusion's impact on water holding capacity, emulsion capacity and stability was complex and might have been impacted by the protein content and source. Overall, PBF's impact on the techno‐functionality of TVPs was more pronounced than that of extrusion conditions. At higher PBF, the NSI, emulsion capacity and stability values of TVPs were negatively impacted, implying that high protein content does not equate to better TVP quality. Future, TVP techno‐functionality research should focus on a wider range of extrusion screw speed and feed moisture content or the effects of protein content and source. [ABSTRACT FROM AUTHOR]

Finding new protein sources and processes comprising targeted functional properties is crucial for the increasing global food demand. In the current paper, a new protein isolate is introduced with potential benefits based on the seeds of Persian everlasting pea (Lathyrus rotundifolius L.). Conventional aqueous extraction for the preparation of protein isolates (CPEP) was compared with pre‐ultrasonic (PUPEP) and ultrasound‐assisted (UAPEP) extractions, and the physicochemical and functional properties of the proteins were investigated. By the implication of ultrasound trials, protein recovery was increased from 49.88% for CPEP to 55.02% and 56.11%, for PUPEP and UAPEP, respectively. According to gel electrophoresis, no major distinction in molecular weight between protein fractions of different samples was perceived and sonication practice did not convert the primary structures of proteins. FTIR results uncovered changes in different extraction modes, implying that ultrasound could transform the secondary structures of the protein. Thermal properties and surface tension were decreased during sonication due to the conformational changes. The results of this study indicated that Persian everlasting pea protein isolate could be considered as a novel source of valuable protein and functional ingredient in the food industry. Practical applications: The utilization of plant‐based protein products as sustainable alternatives to animal proteins has been increasing recently. However, compared with animal proteins, plant‐based proteins reveal relatively weak functional properties such as water‐holding capacity and gelation. Therefore, they need to be modified before being incorporated into food products. Ultrasonic treatment is an emerging technology that has many applications in food science and technology, such as increasing the extraction efficiency and improving the physicochemical and functional properties of food ingredients. Lathyrus rotundifolius seeds contain high amounts of protein and can be used as a source of plant‐based protein. The effect of ultrasonic treatment in the study was investigated and confirmed to improve the extraction efficiency and functional properties of Persian everlasting pea protein, which can be used in the food industry. [ABSTRACT FROM AUTHOR]

The growing emphasis on dietary health has facilitated the development of plant-based foods. Plant proteins have excellent functional attributes and healthenhancing effects and are also environmentally conscientious and animalfriendly protein sources on a global scale. The addition of plant proteins (including soy protein, pea protein, zein, nut protein, and gluten protein) to diverse cheese varieties and cheese analogs holds the promise of manufacturing symbiotic products that not only have reduced fat content but also exhibit improved protein diversity and overall quality. In this review, we summarized the utilization and importance of various plant proteins in the production of hybrid cheeses and cheese analogs. Meanwhile, classification and processing methods related to these cheese products were reviewed. Furthermore, the impact of different plant proteins on the microstructure, textural properties, physicochemical attributes, rheological behavior, functional aspects, microbiological aspects, and sensory characteristics of both hybrid cheeses and cheese analogswere discussed and compared. Our study explores the potential for the development of cheeses made from full/semi-plant protein ingredients with greater sustainability and health benefits. Additionally, it further emphasizes the substantial chances for scholars and developers to investigate the optimal processing methods and applications of plant proteins in cheeses, thereby improving the market penetration of plant protein hybrid cheeses and cheese analogs. [ABSTRACT FROM AUTHOR]

Pea pod (PP) is an agricultural by‐product with 10%–13% protein content which has a potential to be converted to value‐added ingredients. In this study, different protein extraction strategies including three different solvents (water, salt, and alkaline) and two different pretreatments (ultrasound [US] and enzyme such as pectinase and Viscozyme®) before conventional alkaline extraction were employed to maximize the extraction yield. The US‐pretreated alkaline extraction achieved the highest yield (21.1%) in protein extracts under optimum conditions (30% amplitude for 5 min). PP protein concentrates showed significant differences in solubility, sodium dodecyl sulfate–polyacrylamide gel electrophoresis protein patterns, scanning electron microscopy images, and color depending on the applied extraction method. All PP residues after extraction still remained protein (5.2–8.0 g/100 g) regardless of the extraction techniques, representing the challenges in protein extraction from agricultural by‐products with a lignocellulosic matrix. The combined use of US and enzyme treatments should be further investigated for higher extraction yields. Practical Applications: Agricultural wastes and by‐products could be potential protein sources; however, their lignocellulosic structure could be challenging for protein extraction. In the current study, different extraction strategies including ultrasound (US) and enzyme pretreatments were performed for the extraction of proteins from pea pods which is an agro‐industrial by‐product. Results suggest that US pretreatment may have promising applications for the extraction of valuable compounds from agricultural and industrial by‐products, contributing to sustainable food processing strategies. [ABSTRACT FROM AUTHOR]

BACKGROUND: Rapeseed protein isolate is used in the food industry, and heating is often used during rapeseed processing. However, the digestible indispensable amino acid score (DIAAS) for heat‐treated rapeseed protein isolate is unknown. The present study aimed to test the hypothesis that heating rapeseed protein isolate improves protein quality resulting in DIAAS that is greater than for pea and rice protein concentrates, and comparable to that of soy and whey protein isolates. RESULTS: Standardized ileal digestibility (SID) of amino acids (AA), except leucine and methionine, was not different between heat‐treated rapeseed protein isolate and soy protein isolate, but SID of most AA was greater (P < 0.001) for heat‐treated rapeseed protein isolate than for brown rice protein concentrate, pea protein concentrate, rapeseed protein isolate and soy protein isolate, but not whey protein isolate. Non‐heated rapeseed protein isolate had a reduced (P < 0.001) DIAAS for 6‐month‐old to 3‐year‐old children compared with soy protein isolate, but this was greater (P < 0.001) than for pea and brown rice protein concentrates. The DIAAS for heat‐treated rapeseed protein isolate was greater (P < 0.001) than for non‐heated rapeseed protein isolate for all age groups. Heat‐treated rapeseed protein isolate and whey protein isolate had a DIAAS > 100 for individuals older than 3 years. CONCLUSION: Rapeseed protein isolate had a DIAAS comparable to soy protein isolate, but heat‐treated rapeseed protein isolate and whey protein isolate had DIAAS ≥ 100, qualifying these proteins as 'excellent'. Rice and pea protein concentrates had DIAAS < 75. © 2023 Society of Chemical Industry. [ABSTRACT FROM AUTHOR]

In this study, the effects of konjac glucomannan (KGM) at different concentrations on the physiochemical and sensory properties of soy protein isolate (SPI), pea protein isolate (PPI), or peanut protein isolate (PNPI) compound gels were investigated. The results revealed that when the ratio of PNPI to KGM was 90:10, the denaturation temperature of PNPI could be significantly enhanced to 119.32°C by KGM modification. Concerning the textural and microstructural features, the amount of KGM addition had positive correlation with the hardness and chewiness of each compound gel, however, too much KGM addition will cause the unstable internal structure of the PNPI/KGM compound gels (70:30 and 60:40). Furthermore, sensory results indicated that PNPI/KGM (80:20), PPI/KGM (80:20), SPI/KGM (80:20) had great potential to be considered as prototypes for novel plant‐based products, which generated the highest acceptance scores of 5.04, 5.94, and 5.36 in each group, respectively. [ABSTRACT FROM AUTHOR]

Concerns have been raised about the potential health risks associated with elevated sugar levels in food products of osmotic dehydration (OD). To address this issue, a new strategy was proposed and validated in this study. Pea protein isolate (PPI) and inulin were introduced into osmotic solutions to reduce sucrose uptake in apple slices. Apple samples were subjected to OD (40%wt sucrose) at 40°C with different concentrations of PPI or inulin. Three parameters, including performance ratio (Pr), dehydration efficiency index (DEI), and sucrose gain rate were used to evaluate the effect of PPI and inulin addition on reducing sucrose uptake. The result showed that sucrose content in apple tissues after OD for 4 h was 51.79 mg/100 mg dry basis when treated by a sucrose solution alone, but was reduced to 43.43 mg/100 mg dry basis and 46.12 mg/100 mg dry basis when 1.5%wt inulin and 3% wt PPI was added, respectively. Practical applications: The use of low‐temperature and phase‐change‐free osmotic dehydration methods for the preservation of fruits is advantageous due to low energy consumption, better quality retention, and ease of operation. It has been used to produce intermediate moisture foods or as a pretreatment for other drying methods. However, the most widely used osmotic agents often contain high calories because carbohydrates have become the most popular osmotic agents. This has promoted the exploration of natural methods to reduce sugar uptake while maintaining the drying characteristic of osmotic dehydration. This study was undertaken to investigate the use of two biomacromolecules, that is, pea protein isolate and inulin as a simple yet effective means for achieving sugar reduction. The finding of this work has demonstrated that both methods can significantly reduce sucrose content in dried apple slices, thus confirming the potential for practical applications. [ABSTRACT FROM AUTHOR]

Summary: This study investigated the effects of pea and whey proteins on the bio‐accessibility and antioxidant activity of blueberry polyphenolic compounds during digestion using an in vitro gastrointestinal model (TIM‐1). The research objective was understanding how different protein sources affect blueberry polyphenols' bio‐accessibility and antioxidant activity. The study found that pea proteins resulted in higher bio‐accessibility and anthocyanin content compared to whey proteins. Additionally, interactions between blueberry polyphenols and proteins decreased the antioxidant activity. However, forming a non‐covalent and reversible complex between pea proteins and blueberry polyphenols may improve polyphenol stability and bio‐accessibility during digestion. The novel aspects of this research provide valuable insights into the effects of protein sources on the bio‐accessibility and antioxidant activity of blueberry polyphenols and may have important implications for developing functional foods and dietary supplements. The most important impact of the research is that pea proteins resulted in higher bio‐accessibility and anthocyanin content compared to whey proteins, which suggests that pea proteins may be a better protein source for combining with blueberries to maximise their health benefits. Additionally, forming a non‐covalent and reversible complex between pea proteins and blueberry polyphenols may improve polyphenol stability and bio‐accessibility during digestion, which has implications for the food industry in developing new products. [ABSTRACT FROM AUTHOR]

Summary: Naringin has various biological activities with an unacceptable bitter taste. In this work, pea protein–naringin complexes (PP–NG complexes) were constructed to stabilise the Pickering emulsion and reduce the bitterness of naringin. Sensory evaluation results showed that the bitterness and after‐bitterness of the PP–NG complexes were reduced by 77.78% and 75.99% compared with 1 mm naringin respectively. For the PP–NG complexes, the fluorescence spectra results showed that the endogenous fluorescence intensity of pea protein decreased with the naringin concentration increased (0–2 mm), and each pea protein molecule bound to one naringin molecule. Results obtained via thermodynamic analysis molecular docking demonstrated that naringin had an excellent binding affinity (−7.4 kcal mol−1) with pea protein and could form five hydrophobic bonds and four hydrogen bonds with pea protein. These findings would provide a new idea for the masking of bitterness and the evolution of Pickering emulsions stabilised by the protein–polyphenol nanoparticles. [ABSTRACT FROM AUTHOR]

In this study, we investigated the effects of proteins on the properties of soy protein concentrate‐based meat analogs under high‐moisture extrusion conditions. The rheological properties of soy protein concentration‐sodium alginate (SPC‐SA) and soy protein isolate‐SPC‐SA (SPI‐SPC‐SA), pea protein isolate‐SPC‐SA (PPI‐SPC‐SA), and zein‐SPC‐SA were evaluated, and the texture properties, microstructure, water absorption, and cooking properties of the resulting protein–meat analogs were characterized after addition of the protein raw materials. Results obtained indicated that the raw material containing 30% SPI had the best viscoelasticity, and the hardness and chewiness of resulting meat analog analogs were the highest when 30% SPI was added, along with the largest volume and best water absorption after cooking. The degree of texturization and toughness of meat analogs were the highest when PPI and zein were 30 and 50%, respectively. Results from this study showed that the texture properties of soy protein concentrate‐based meat analogs were improved by adding proteins to raw material, thus providing a theoretical basis for further development of soy protein concentrate‐based meat analogs. [ABSTRACT FROM AUTHOR]

BACKGROUND: Binders in plant‐based meat analogues allow different components, such as extrudate and fat particles, to stick together. Typically, binders then are solidified to transform the mass into a non‐sticky, solid product. As an option for a clean‐label binder possessing such properties, the solidification behavior of pea protein–pectin mixtures (250 g kg−1, r = 2:1, pH 6) was investigated upon heating, and upon addition of calcium, transglutaminase, and laccase, or by combinations thereof. RESULTS: Mixtures of (homogenized) pea protein and apple pectin had higher elastic moduli and consistency coefficients and lower frequency dependencies upon calcium addition. This indicated that calcium physically cross‐linked pectin chains that formed the continuous phase in the biopolymer matrix. The highest degree of solidification was obtained with a mixture of pea protein and sugar beet pectin upon addition of laccase that covalently cross‐linked both biopolymers involved. All solidified mixtures lost their stickiness. A mixture of soluble pea protein and apple pectin solidified only slightly through calcium and transglutaminase, probably due to differences in the microstructural arrangement of the biopolymers. CONCLUSION: The chemical makeup of the biopolymers and their spatial distribution determines solidification behavior in concentrated biopolymer mixtures. In general, pea protein–pectin mixtures can solidify and therefore have the potential to act as binders in meat analogues. © 2023 The Authors. Journal of The Science of Food and Agriculture published by John Wiley & Sons Ltd on behalf of Society of Chemical Industry. [ABSTRACT FROM AUTHOR]

BACKGROUND: This research was aimed at the fabrication of jujube extract (JE)‐loaded beads by extrusion, using whey protein isolate (WPI), chickpea protein concentrate (PPC) and a combination of two types of hydrocolloid insoluble fraction of Persian gum (IFPG) and sodium alginate (Al). RESULTS: JE‐loaded beads with the highest encapsulation efficiency (10.87%) and polyphenol content (120.8 mg L−1 gallic acid) were obtained using Al‐IFPG/PPC at 4 °C. The Al‐IFPG, Al‐IFPG/WPI and Al‐IFPG/PPC beads revealed 5.66, 6.85 and 5.76 mm bead size, respectively, and almost all of them demonstrated a homogeneous and spherical structure. Fourier transform infrared spectroscopy data proved that the stable structure of the Al‐IFPG beads was due to hydrogen bonding and electrostatic interactions. The thermostability of beads loaded with JE based on Al‐IFPG/WPI was significantly enhanced compared to pure Al‐IFPG. Texture evaluation of JE‐loaded beads based on Al‐IFPG incorporation with WPI revealed an increment in the hardness of beads. CONCLUSION: This study confirmed the potential of Al‐IFPG complex beads for the effective delivery of jujube extract via incorporation into pea and whey proteins and for the expansion of its use in products. © 2023 Society of Chemical Industry. [ABSTRACT FROM AUTHOR]

BACKGROUND: Hybrid batters constitute the base for the processing of cooked and dry meat analogues. The use of texturized plant proteins in their formulation is a key strategy to reduce the consumption of animal proteins, although off‐flavors present in these plant proteins often cause sensory rejection. The aim was to study the effect of a deodorization process of pea protein, for their use in hybrid meat batters at different percentages of substitution. RESULTS: Hybrid patties with higher percentages of pea protein showed higher values of yellowness, pH, and water activity, whereas hardness was reduced. Soaking treatment with ethanol for deodorization of the texturized pea protein increased humidity and pH in all patties but reduced the textural properties (hardness, springiness, cohesiveness, and chewiness). The addition of oat flour improved the patty texture at higher percentages of pea protein, but in soaked deodorized patty formulations it affected volatile retention. Volatile compounds related to off‐flavors (aldehydes, alcohols, acid compounds, ketones, and pyrazines) appeared significantly increased as the pea percentage increased, although these were efficiently removed by the soaking deodorizing process applied. CONCLUSION: Soaking of the texturized pea protein with ethanol is an effective strategy to reduce off‐flavors in hybrid meat patties. However, it produces changes in the textural characteristics by the solubilization of the proteins of the texturized pea, reducing the availability to form a network and affecting volatile retention. The formulation of hybrid batter should be controlled in all sensory aspects for the processing of cooked and dry cured meat product analogues. © 2023 The Authors. Journal of The Science of Food and Agriculture published by John Wiley & Sons Ltd on behalf of Society of Chemical Industry. [ABSTRACT FROM AUTHOR]

Background: Surimi products occupy a large market in the food industry, and the gel performance is an important index to evaluate them. Thus, it is of great significance and practical value to find better food ingredients to regulate the structure and gel performance of surimi products. In this study, we used pea protein (PP) to restructure fish myofibrillar proteins (MPs) to achieve regulation of protein gel performance. Results: PP could enhance MP gel performance in terms of compressive strength, water‐holding capacity, and some texture parameters. This may be the result of an increasing β‐sheet content and a decreasing trend in the α‐helix content, along with enhancements in hydrophobic interactions, nonspecific associations, and ionic bonds in a mixed PP–MP gel. The compressive strength, texture, and water‐holding capacity of MP gel were positively correlated with surface hydrophobicity, active sulfhydryl, turbidity, and β‐sheet of the mixed PP–MP system. Conclusion: The findings suggest that PP can regulate the gel performance by remodeling the structure of MP. The regulation and correlation analysis between gel performance, structure, and physicochemical properties were explored and established to provide a theoretical basis for improving the quality of surimi products. This study will broaden the application of PP in the field of food processing and provide theoretical guidance for the manufacture of new surimi products. © 2023 Society of Chemical Industry. [ABSTRACT FROM AUTHOR]

BACKGROUND: The poor gelling and emulsification properties of pea protein (PeaP) limit its application in gel‐based products. In this study, a strong hydrogel and a high internal phase emulsion (HPLE) gel of PeaP were constructed by covalent cross‐linking of transglutaminase (TGase) assisted by high‐intensity ultrasound. RESULTS: Ultrasound promoted the catalytic efficiency of TGase, with the gel‐point temperature dropping from 44 °C to 28 °C after 10 min of ultrasound. As the ultrasound time increased from 1 min to 10 min, the microstructure of the hydrogel also changed from an irregular macropore structure to a relatively homogeneous honeycomb structure. This was accompanied by an improvement in gel strength, water holding capacity, and ultimate stress. Ultrasound enhanced the binding of water to PeaP, but had little effect on the water‐locking ability of the network structure. Ultrasonication improved the self‐supporting ability of the HPIE gels. The oil droplets within the HPIE gels were closely aligned to form a hexagonal structure. The PeaP layer was further cross‐linked by TGase, strengthening the network structure. High internal phase emulsion gel displayed a higher gel strength, viscosity, and good self‐healing ability under 1 min ultrasound. Meanwhile, HPIE gel at 1 min of ultrasound could be printed with the highest clarity. CONCLUSION: This work provided some insights into improving the functional properties of PeaP, which is helpful for the design and development of PeaP‐based gel products. © 2022 Society of Chemical Industry. [ABSTRACT FROM AUTHOR]

Summary: The physicochemical properties and heat‐induced gel properties of pumpkin seed protein isolates (PSPI) were explored and compared with soybean protein isolate (SPI) and pea protein isolates (PPI). These plant proteins were subjected to ultrasound, acid or alkaline treatment (pH 3 or 11). The content of amino acids and subunit composition were different in PSPI compared with SPI and PPI. Rheological and textural experiments showed that native PSPI had the highest gel strength among the three proteins. This was due to the high hydrophobicity of PSPI and the filling effect of insoluble particles in the protein solution. PSPI had a more pronounced improvement in gel properties after ultrasound or alkaline treatment compared with SPI and PPI, which was due to the increased surface hydrophobicity, increased solubility and reduced particle size of the proteins. The acid treatment induced insoluble aggregates increased the protein particle size, and decreased the protein solubility, resulting in a negative effect on the PSPI protein gel. Therefore, it can be concluded that PSPI has better heat‐induced gelation than SPI and PPI and can be used as a substitute for SPI and PPI in the food industry. [ABSTRACT FROM AUTHOR]

We conducted a combined sensory and discrete choice experiment study with a 100% beef burger, a plant‐based burger using pea protein, a plant‐based burger using animal‐like protein, and a blended burger with 70% beef and 30% mushroom involving US consumers. Respondents were either assigned to a blind or an informed tasting condition with information about the ingredients before tasting the burgers. Results reveal that (i) beef burgers are preferred over alternatives, (ii) consumers favor blended burgers over alternatives in the blind condition but demand decreases in the informed condition; (iii) consumers prefer the plant‐based burger with animal‐like protein over the one with pea protein. Related Content: Meet the meatless: Demand for new generation plant‐based meat alternatives [ABSTRACT FROM AUTHOR]

Summary: The present study compared the effect of various modification methods on emulsifying properties and emulsion stabilising properties of the pea protein isolate (PPI) and investigated the possible mechanism of emulsion stability from the perspectives of interfacial and rheological properties. The PPI was modified by physical extrusion (EPPI), chemical phosphorylation (PPPI), and synergistic extrusion and phosphorylation (EPPPI); natural PPI was used as a control. The results revealed that the adsorption energy of modified PPI at the O/W interface was reduced, and the viscoelasticity of the interfacial film of modified PPI was increased, suggesting that modified PPI could have better adsorption at the O/W interface. The emulsions by modified PPI had higher electrostatic repulsion, smaller particle size, and more uniform particle size distribution. Moreover, the emulsions by modified PPI promoted the formation of the spatial network structure by increasing the viscosity and extending the linear viscoelastic zone. These results showed that EPPI, PPPI, and EPPPI could improve PPI's emulsifying and emulsion‐stabilising properties. [ABSTRACT FROM AUTHOR]