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Practical Application This study aimed to improve lentil proteins’ (LPs) functionality and nutritional value, specifically addressing their lower water solubility and digestibility. A unique combination of LP‐disaccharide interactions was employed. Spectroscopic technologies, which include fluorescence spectra, ultraviolet spectra, and Fourier‐transform infrared, investigated the structure of LPs at various concentrations of trehalose. The results indicate that the LP structures and conformation were considerably modified (p < 0.05) following trehalose conjugation. The surface charge and hydrophobicity of the trehalose‐conjugated LPs (T‐LPs) were significantly altered (p < 0.05), from −22.7 to −31.4 and 753 and 543 a.u., respectively. Furthermore, the digestibility and solubility of T‐LPs increased from 75% to 81.8% and 60% to 66%, respectively. In conclusion, this study showed that combining LPs and trehalose conjugation could improve the quality of conjugates LPs, which could expand their use in manufacturing as the acceptance of plant‐based diets increases.Currently, lentil proteins (LPs) are used in plant‐based protein powders and supplements. Though less popular than soy or pea proteins, LPs are valued for their high protein content and good amino acid profile. LPs are utilized in meat alternatives and high‐protein snack products. The application of these products is mainly due to their nutritional benefits rather than functional properties due to their poor water solubility. Increasing the water solubility of LPs could significantly expand their application in various food industries, making LPs a more competitive and functional plant‐based protein source. Trehalose‐conjugated LPs with better water solubility allow LPs to be used in other food products, such as plant‐based protein beverages. Better solubility would enhance the clarity and smoothness of these products, making them more appealing to consumers. [ABSTRACT FROM AUTHOR]

The overall goal of this research was to develop plant protein-based lipid composite films by examining the effect of shear (mechanical shear; MS vs. high pressure shear; HPS) and type of legume protein isolates (pea, lentil, soy, and faba bean). Compared to MS, HPS emulsions had smaller droplet size, and HPS emulsions from pea and lentil were more viscous than soy and faba bean. The HPS films were lighter and more green and yellow in colour compared to MS films. HPS also improved the mechanical properties of the films resulting in higher tensile and puncture strength for pea and soy and higher tensile elongation and puncture deformation for most of the legumes. There was an inverse relationship between legumes where overall stronger and less flexible films were prepared from pea and soy, and vice versa from lentil and faba bean. HPS resulted in pea and soy films with less swelling ability and higher water vapour permeability (WVP), indicative of a poorer moisture barrier when homogenized this way. The MS films had similar WVP regardless of legume type, while under HPS it was the lowest for faba bean and highest for soy, despite the high swelling ability for both legumes. In short, pea, lentil, and faba bean protein isolates prepared emulsion films with good mechanical properties and water resistance, suggesting the potential to replace soy as edible packaging materials. HSP films had better mechanical attributes but poorer vapor barrier properties then those produced using MS. [ABSTRACT FROM AUTHOR]

Citrus reticulata 'Chachiensis' is a citrus cultivar in the Rutaceae family, and its peel is commonly utilized as a raw material for Guangchenpi. This study used flavonoid extract from the peel of immature Citrus reticulata 'Chachiensis' (CCE) as the raw material to investigate the encapsulation ability of different wall materials (plant-based proteins, including soybean protein isolation (SPI), pea protein (PP), and zein; carbohydrates, including maltodextrin (MD), Momordica charantia polysaccharide (MCP), and gum acacia (GA); and composite wall materials of both types) on CCE. The wall material with the highest encapsulation rate was selected for the preparation of CCE microcapsules. Furthermore, the physicochemical characteristics, antioxidant capacity, bioavailability, and storage stability of the CCE microcapsules were explored. The results indicated that among all wall materials, the composite wall material PPMD had the highest encapsulation rate, which was 84.44 ± 0.34%. After encapsulation, the microcapsules tended to have a yellow color and exhibited characteristics such as system stability, low moisture content, and low hygroscopicity. In vitro antioxidant assays revealed that the encapsulation of CCE significantly increased the scavenging rates of DPPH and ABTS free radicals. In vitro gastrointestinal digestion experiments indicated that the release rate of PPMD-CCE in intestinal fluid was significantly greater than that of free CCE, ultimately reaching 85.89 ± 1.53%. Storage experiments demonstrated that after 45 days under various temperature and light conditions, the retention rate of CCE in the microcapsules was significantly greater than that of free CCE. The above findings provide new possibilities for the application of PP and plant proteins and lay a foundation for the future industrial application of CCE. [ABSTRACT FROM AUTHOR]

This study aimed to develop a product that closely replicates the texture and appearance of tripe. The effect of three different proteins (soy protein isolate (SPI), pea protein isolate (PPI), and whey protein isolate (WPI)) at different protein levels and processing conditions (heating (90 °C, 1 h) followed by cooling (4 °C, 12 h) and heating (90 °C, 1h) followed by freezing (−18 °C, 12 h)) of konjac glucomannan (KGM) was analyzed. The optimal formulations for simulating tripe were screened by examining their similarity to real tripe in terms of texture, color, and sensory experience. The screened formulations were also subjected to a preliminary mechanistic investigation. The results show that all three proteins improved the gel's textural properties to varying degrees. At the same concentration, the hardness and chewiness of the KGM/WPI composite gel were significantly higher than those of the other two KGM/protein composite gels, among which the composite gel obtained by adding 8% WPI and 5% KGM heating-frozen (FWK4) had the greatest hardness and chewiness of 4338.07 g and 2313.76, respectively, and the springiness differences in all of the composite gels were small. In addition, the addition of protein increased the whiteness of the hybrid gels, with WPI having the most significant effect on the whiteness of the composite gels (whiteness increased from 30.25 to 62.80 as the concentration of WPI increased from 0 to 10%). Freezing increased composite gel hardness and chewiness, but reduced gel springiness and whiteness. Cluster analysis showed that the composite gel obtained by heating–cooling 8% WPI and 5% KGM (WK4) was very similar to the real tripe in terms of chewiness and whiteness, and WK4 had the highest sensory scores for color, tissue morphology, tactile sensation, taste, and odor. The acceptability score in terms of tissue morphology reached 4.3. Meanwhile, the characterization results of WK4 indicate the presence of large junction areas in the gel network. Fourier transform infrared spectroscopy (FTIR) analysis, X-ray diffraction, and intermolecular force contributions indicated that the incorporation of WPI promoted integral interactions, and that hydrophobic interactions and disulfide bonding played a key role in the WK4 composite gel system. Moreover, scanning electron microscopy (SEM) also showed that the combination of WPI and konjac glucan resulted in a more compact gel structure. This study is informative for the development of the field of bionic tripe processing. [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]

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]

Reducing meat consumption reduces carbon emissions and other environmental harms. Unfortunately, commercial plant-based meat substitutes have not seen widespread adoption. In order to enable more flexible processing methods, this paper analyzes the characteristics of commercially available spirulina, soy, pea, and brown rice protein isolates to provide data for nonmeat protein processing that can lead to cost reductions. The thermal and rheological properties, as well as viscosity, density, and particle size distribution, were analyzed for further study into alternative protein-based food processing. The differential scanning calorimetry analysis produced dry amorphous-shaped curves and paste curves with a more distinct endothermic peak. The extracted linear temperature ranges for processing within food production were 70–90 °C for spirulina, 87–116 °C for soy protein, 67–77 °C for pea protein, and 87–97 °C for brown rice protein. The viscosity analysis determined that each protein material was shear-thinning and that viscosity increased with decreased water concentration, with rice being an exception to the latter trend. The obtained viscosity range for spirulina was 15,100–78,000 cP, 3200–80,000 cP for soy protein, 1400–32,700 cP for pea protein, and 600–3500 cP for brown rice protein. The results indicate that extrusion is a viable method for the further processing of protein isolates, as this technique has a large temperature operating range and variable screw speed. The data provided here can be used to make single or multi-component protein substitutes. [ABSTRACT FROM AUTHOR]

The continuous development and increasing demand of the fast-growing market for meat alternatives will offer abundant opportunities for food scientists and entrepreneurs to innovate new technologies. Product development and applied research primarily focus on the sensory qualities related to the texture of meat analogues. The preference for sustainable plant-based meat over animal meat worldwide is primarily driven by the growing concerns regarding the environment and health. In this study, various plant-based composites were investigated to create plant-based meat alternatives with distinctive texture profiles using an innovative freeze-structuring technique. Statistical ANOVA was utilized to optimize the composite consisting of pea proteins isolate (PPI) and soy protein isolate (ISP). The physicochemical, textural, and sensory properties of the analogs were thoroughly examined. The findings indicated that the analog with a ratio of 40:60 (PPI:ISP) was the most favored compared to other formulations. The incorporation of soy protein seemed to have an impact on the textural properties. The optimized composition level (40:60) exhibited a hardness of 842.87g, chewiness of 721.35 N/cm, and the highest sensory properties on an 8.3 hedonic scale. Additionally, the water activity was measured to be 0.553, classifying the product as an intermediate moisture food. The nutritional analysis shows that optimized meat substitutes have 16 % increased protein levels when compared to conventional chicken meat. This study improved the comprehension of the impacts of composites on the structure and physicochemical characteristics of plant-based meat substitutes. It highlighted the potential of utilizing plant protein composites in the development of satisfactory meat analogues. [ABSTRACT FROM AUTHOR]

Different protein sources create distinct textures in plant‐based meat due to differences in their hydration properties when exposed to different time, temperature, and shear regimes, which in turn depend upon their solubility, protein structure, and specific amino acids. This research aimed to identify these differences and manipulate them to reach a desired texture utilizing simple and reproducible analytical methods to characterize protein properties as either cold or heat swelling. Protein functionality was determined through least gelation concentration (LGC), water absorption index (WAI), and rapid visco analysis (RVA). Cold swelling or CS proteins (pea protein isolate, soy protein isolate, Arcon S soy protein concentrate) were characterized by an LGC < 14% and/ or WAI > 4.0 g/g, while LGC > 16% and/ or WAI < 4.0 g/g indicates proteins with heat swelling or HS properties (Arcon F soy protein concentrate, wheat gluten, and fava protein concentrate). An RVA peak time of around or less than 3 min (<75°C peak temperature) indicated CS properties while greater than 3.5 min (>80°C peak temperature) was considered HS. Protein mixes or treatments comprising mainly of different combinations and ratios of CS proteins were hypothesized to create a softer textured vegetable protein product or texturized vegetable protein (TVP) and those based on HS proteins a firmer TVP. Bulk density was higher for HS treatments (274–287 g/L) than for CS treatments (160–223 g/L). CS treatments exhibited a microstructure that was porous, while HS showed a dense, laminar microstructure. Texture profile analysis showed that CS treatments seemed to show a lower hardness (1154–1595 g) than the HS treatments (1893–2231 g). Practical Application: Controlling texture can be a valuable tool when producing a plant‐based meat product. Different applications have various texture requirements. For example, a plant‐based fish stick would require a softer texture than a hamburger or chicken nugget. By increasing the knowledge of how protein functionality affects meat analogue texture, the time needed to produce new products with novel textures can be reduced. Money could also be saved by being able to quickly replace ingredients with a more affordable or accessible protein with similar swelling abilities to preserve product quality. [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]

Developing carriers capable of efficiently transporting both hydrophilic and lipophilic payloads is a captivating focus within the pharmaceutical and drug delivery research domain. Antibubbles, constituting an innovative encapsulation system designed for drug delivery purposes, have garnered scientific interest thanks to their distinctive water-in-air-in-water (W1/A/W2) structure. However, in contrast to their precursor, i.e., nanoparticle-stabilized W1/O/W2 double emulsion, traditional antibubbles lack the ability to accommodate a lipophilic payload, as the intermediary (volatile) oil layer of the emulsion is replaced by air during the antibubble fabrication process. Therefore, here, we report the fabrication of triple-emulsion-based antibubbles (O1/W1/A/W2), in which the inner aqueous phase was loaded with a nanoemulsion stabilized by various proteins, including whey, soy, or pea protein isolates. As model drugs, we employed the dyes Nile red in the oil phase and methylene blue in the aqueous phase. The produced antibubbles were characterized regarding their size distribution, entrapment efficiency, and stability. The produced antibubbles demonstrated substantial entrapment efficiencies for both lipophilic (ranging from 80% to 90%) and hydrophilic (ranging from 70% to 82%) components while also exhibiting an appreciable degree of stability during an extended rehydration period of two weeks. The observed variations among different antibubble variants were primarily attributed to differences in protein concentration rather than the type of protein used. [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]

High-moisture extrusion (HME) is an effective process to make fibrous products that can be used as meat analogues. In this study, the effect of extrusion of already extruded products (i.e., re-extrusion) was tested with the aim to explore the potential of rework in HME. The rework of material is important because it is a route to reduce waste, which is always produced, for example during the start or at the end of a production run. Pea and soy protein isolates (PPI and SPI) were first extruded, then freeze-dried and ground, and extruded again. The visual and textural properties of the fibrous products were evaluated. Also, the rheological properties, solubility, and water-holding capacity (WHC) of the ingredients and the products after the first and second extrusion were quantified. The obtained freeze-dried powders after the first HME cycle had a reduction in solubility of 15% for PPI and 74% for SPI. Furthermore, WHC was reduced by 65% and 17% for PPI and SPI, respectively. After the second HME cycle, the reduction in solubility and WHC was augmented to 22% and 90% for PPI, and 79% and 63% for SPI. No effect on stock and loss moduli after heating and cooling were found, even after two HME cycles. SPI fibrous products did not differ in cutting strength, anisotropy index, or visual appearance after re-extrusion. Only, a decrease in hardness was detected, from 62.0 N to 51.1 N. For PPI, re-extrusion did reduce the cutting force and hardness but not the anisotropy index. It was concluded that even though HME induces a loss of solubility and WHC, this did not affect the fibrous texture formation of the protein. This means that the texture formed during HME does not depend on the process history and that rework is thus possible for fibrous products. [ABSTRACT FROM AUTHOR]

Biomimetic foods are expected to have potential health benefits for the management and prevention of chronic diseases, such as diabetes and cardiovascular disease. In the current research, two commercially available and affordable plant proteins (soy protein isolate—SPI and pea protein isolate—PPI) at two levels (5%, 10%) were added to the Yangyu jiaotuan with the objective of developing a product with reduced glycaemic properties and high protein content while maintaining its original taste and texture. The results showed that several important textural properties such as hardness and chewiness did not change significantly during the refrigerated storage. The storage modulus G′ increased with refrigerated storage time for different samples, but there were significant differences among the five samples (with and without protein addition) with respect to frequency dependence during rheological measurements. The in vitro starch digestion experiments showed that the starch hydrolysis of Yangyu jiaotuan decreased considerably (by up to 42.08%) with the increase in PPI content and during refrigerated storage due to starch retrogradation. Protein has protected the microstructure and there was less damage when compared to samples without protein. The bimodal peaks of the particle size distribution curves showed that the newly developed Yangyu jiaotuan contains two different sizes of particles; the smaller particles (~30 μm) corresponded to PPI and starch granules, while the larger particles corresponded to the fragments of the gel network of the starch matrix. Based on the above results, Yangyu jiaotuan mixed with pea protein is a convenient potato staple food product, which complies with the biomimetic potato food very well. [ABSTRACT FROM AUTHOR]

Copyright of Food Research & Development is the property of Food Research & Development Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Successfully replacing meat with plant-based options will require not only replicating the texture of muscular fibres, but also imitating the taste, aroma, and juiciness of meat as closely and realistically as possible. This study examines the impact of rapeseed oil on the textural properties of meat analogues. Pea protein and soy protein are chosen as model systems to assess the effect of rapeseed oil. Optical, mechanical, and rheological characterisation tests are conducted to investigate the oil droplet distribution, the gel strength, Young's modulus, and the length of the LVE region. The hypothesis is that oil droplets will act as active fillers in the protein matrix, and thus, diminish the strength of the protein gel network. The results of this study show that rapeseed oil droplets act as inactive fillers, as they are not bound to both examined protein matrices. Soy protein extrudates display minimal changes, while pea protein extrudates are significantly affected by the addition of oil. For example, oil addition decreased the G′ in the LVE region of pea protein meat analogues by 50%, while soy protein samples showed no significant changes. Despite the similar interfacial activities of the investigated proteins, the decreased encapsulation efficiency of pea protein was confirmed by the higher amount of extracted oil from the respective extrudates. [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]

During the last decades, there has been a huge consumer concern about animal proteins that has led to their replacement with plant proteins. Most of those proteins exhibit emulsifying properties; thus, the food industry begins their extensive use in various food matrices. In the present study, pea and soy protein isolates (PPI and SPI) were tested as potential candidates for stabilizing food emulsions to encapsulate α-tocopherol and squalene. More specifically, PPI and SPI particles were formulated using the pH modification method. Following, emulsions were prepared using high-shear homogenization and were observed at both a microscopic and macroscopic level. Furthermore, the adsorption of the proteins was measured using the bicinchoninic acid protein assay. The emulsions' droplet size as well as their antioxidant capacity were also evaluated. It was found that the droplet diameter of the SPI-based emulsions was 60.0 μm, while the PPI ones had a relatively smaller diameter of approximately 57.9 μm. In the presence of the bioactives, both emulsions showed scavenging activity of the 2,20-Azinobis-(3-ethylbenzothiazoline-6-sulphonate) radical cation (ABTS·+) and 2,2-diphenyl-1-picrylhydrazyl (DPPH) radicals, with the ones loaded with α-tocopherol having the greatest antioxidant capacity. Overall, the proposed systems are very good candidates in different food matrices, with applications ranging from vegan milks and soups to meat alternative products. [ABSTRACT FROM AUTHOR]

This study focused on predicting high-moisture texturization of plant-based proteins (soy protein concentrate (SPC), soy protein isolate (SPI), pea protein isolate (PPI)) at different water contents (57.5%, 60%, 65%, 70%, and 72.5% (w/w db)) to optimize and guarantee the production of high-moisture meat analogs (HMMA). Therefore, high-moisture extrusion (HME) experiments were performed, and the texture of the obtained high-moisture extruded samples (HMES) was sensory evaluated and categorized into poorly-textured, textured, or well-textured. In parallel, data on heat capacity (cp) and phase transition behavior of the plant-based proteins were determined using differential scanning calorimetry (DSC). Based on the DSC data, a model for predicting cp of hydrated, but not extruded, plant-based proteins was developed. Furthermore, based on the aforementioned model for predicting cp and DSC data on phase transition behavior of the plant-based proteins in combination with conducted HME trials and the mentioned model for predicting cp, a texturization indicator was developed, which could be used to calculate the minimum threshold temperature required to texturize plant-based proteins during HME. The outcome of this study could help to minimize the resources of expensive extrusion trials in the industry to produce HMMA with defined textures. [ABSTRACT FROM AUTHOR]

Copyright of Food Research & Development is the property of Food Research & Development Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Double emulsions (W1/O/W2) have long been used in the food and pharmaceutical industries to encapsulate hydrophobic and hydrophilic drugs and bioactive compounds. This study investigated the effect of different types of emulsifiers (plant- vs. animal-based proteins) on the encapsulation properties of Mentha piperita leaf extract (MLE) prepared using the double emulsion method. Using response surface methodology, the effect of ultrasound-assisted extraction conditions (amplitude 20–50%; time 10–30 min; ethanol concentration 70–90%) on the total phenolic content (TPC) and antioxidant activity (percent inhibition) of the MLE was studied. MLE under optimized conditions (ethanol concentration 76%; amplitude 39%; time 30 min) had a TPC of 62.83 mg GA equivalents/g and an antioxidant activity of 23.49%. The optimized MLE was encapsulated using soy, pea, and whey protein isolates in two emulsifying conditions: 4065× g/min and 4065× g/30 s. The droplet size, optical images, rheology, and encapsulation efficiency (EE%) of the different encapsulated MLEs were compared. The W1/O/W2 produced at 4065× g/min exhibited a smaller droplet size and higher EE% and viscosity than that prepared at 4065× g/30 s. The higher EE% of soy and pea protein isolates indicated their potential as an effective alternative for bioactive compound encapsulation. [ABSTRACT FROM AUTHOR]

The demand for pulse proteins as alternatives to soy protein has been steeply increasing over the past decade. However, the relatively inferior functionality compared to soy protein is hindering the expanded use of pulse proteins, namely pea and chickpea protein, in various applications. Harsh extraction and processing conditions adversely impact the functional performance of pea and chickpea protein. Therefore, a mild protein extraction method involving salt extraction coupled with ultrafiltration (SE-UF) was evaluated for the production of chickpea protein isolate (ChPI). The produced ChPI was compared to pea protein isolate (PPI) produced following the same extraction method in terms of functionality and feasibility of scaling. Scaled-up (SU) ChPI and PPI were produced under industrially relevant settings and evaluated in comparison to commercial pea, soy, and chickpea protein ingredients. Controlled scaled-up production of the isolates resulted in mild changes in protein structural characteristics and comparable or improved functional properties. Partial denaturation, modest polymerization, and increased surface hydrophobicity were observed in SU ChPI and PPI compared to the benchtop counterparts. The unique structural characteristics of SU ChPI, including its ratio of surface hydrophobicity and charge, contributed to superior solubility at both a neutral and acidic pH compared to both commercial soy protein and pea protein isolates (cSPI and cPPI) and significantly outperformed cPPI in terms of gel strength. These findings demonstrated both the promising scalability of SE-UF and the potential of ChPI as a functional plant protein ingredient. [ABSTRACT FROM AUTHOR]

Four commercial pea protein isolates were analyzed for their physico-chemical properties including water absorption capacity (WAC), least gelation concentration (LGC), rapid visco analyzer (RVA) pasting, differential scanning calorimetry (DSC)-based heat-induced denaturation and phase transition (PTA) flow temperature. The proteins were also extruded using pilot-scale twin-screw extrusion with relatively low process moisture to create texturized plant-based meat analog products. Wheat-gluten- and soy-protein-based formulations were similarly analyzed, with the intent to study difference between protein types (pea, wheat and soy). Proteins with a high WAC also had cold-swelling properties, high LGC, low PTA flow temperature and were most soluble in non-reducing SDS-PAGE. These proteins had the highest cross-linking potential, required the least specific mechanical energy during extrusion and led to a porous and less layered texturized internal structure. The formulation containing soy protein isolate and most pea proteins were in this category, although there were notable differences within the latter depending on the commercial source. On the other hand, soy-protein-concentrate- and wheat-gluten-based formulations had almost contrary functional properties and extrusion characteristics, with a dense, layered extrudate structure due to their heat-swelling and/or low cold-swelling characteristics. The textural properties (hardness, chewiness and springiness) of the hydrated ground product and patties also varied depending on protein functionality. With a plethora of plant protein options for texturization, understanding and relating the differences in raw material properties to the corresponding extruded product quality can help tailor formulations and accelerate the development and design of plant-based meat with the desired textural qualities. [ABSTRACT FROM AUTHOR]

The object of research is pea (Pisum sativum var. arvense) and pea protein isolate. The chemical composition of pea (Pisum sativum var. arvense) was studied to determine its potential as a new raw material for obtaining protein isolate by pH-shifting treatment. The obtained results confirm the effectiveness of using peas to obtain protein isolate for use in the food industry instead of soy protein isolate. Peas are low in lipids (1.61 % on dry matter), high in crude protein (19.21 % on dry matter), ash (3.41 % on dry matter) and minerals (Se, Fe, Zn, Mn, Cu, Mg, P). The ratio of essential amino acids to replaceable amino acids (0.78), which is higher than the amount recommended by the World Health Organization. Vegetable protein is an alternative to animal protein in the food industry. Protein isolate from peas was obtained by pH-shifting treatment and its chemical composition and functional properties were determined. After pH-shifting treatment, the chemical composition of protein and mineral substances did not show significant changes. The protein content of pea protein isolate was 82.2 %, and the yield of pea protein isolate was 5.6 %. To confirm the functional properties of pea protein isolate, the indicators of moisture-holding capacity (1.05 ml/g) and fat-holding capacity (0.82 ml/g) were investigated. Peas and protein isolate from it showed high functional properties and high-quality chemical composition of proteins and minerals for use in the technology of sausage products, which should be the focus of further research. [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]

The use of vegetable proteins has been the focus of research efforts to develop new products and/or to replace other sources of protein. Ergo, there is a need to assess the effects of new processing technologies on this type of protein. This work evaluated the influence of high-pressure processing (HPP) (pressure: 200, 400 and 600 MPa; holding time: 5, 10 and 15 min) on selected properties of pea (PPI) and soy (SPI) protein isolates at three pH values (6, 7 and 8). SPI presented a higher percentage of soluble proteins than PPI, still, HPP increased protein solubility of both isolates. This effect was more pronounced on SPI, particularly at pH 7 and 8, where the percentage of soluble proteins almost tripled under some HPP conditions. Similarly, the surface hydrophobicity also increased with HPP for proteins from both sources, increasing, in general, with increasing pressure and holding time. On the contrary, the content of free sulfhydryl groups generally decreased with HPP for proteins from both sources, suggesting a complex balance between protein unfolding and further aggregation under certain conditions. The effects of HPP on the emulsifying properties of the protein isolates were dependent on pH, pressure, holding time and whether the soluble or total fraction of the protein isolates were used. [ABSTRACT FROM AUTHOR]

BACKGROUND: Auricularia auricula (A. auricula) is one of the most abundant sources of plant protein in edible fungi. Problems of low protein yield exist in traditional methods of protein extraction such as alkali extraction and ultrasonic-assisted alkali after pretreatment with enzymes. Thus, the protein extraction process was investigated and optimized using a definitive screening design from A. auricula to improve the protein yield under practical operating conditions of temperature, the concentration of NaCl, meal/water ratio, extraction time and pH. RESULTS: The yield of protein isolates of the isoelectric-ammonium sulfate precipitation (9.34% w/w) was obtained almost three times and the protein content (55.23% w/w) was approximately 1.6 times that of the traditional extraction method of isoelectric precipitation. Next, the optimized method was successfully applied to the analysis of the functional properties of the protein. A. auricula protein isolate (AAPI) had better solubility, emulsification and foaming capacity than soy protein isolate (SPI) and pea protein isolate (PPI), and the oil holding capacity of AAPI exhibited extremely well, which was approximately five times that of SPI and six times that of PPI. The texture properties of AAPI gel were similar to those of PPI gels. CONCLUSION: AAPI extracted by the optimized method had a satisfactory yield and had the potential to substitute plant-originated proteins in food processing. [ABSTRACT FROM AUTHOR]

Patients with dysphagia diseases require food with acceptable textural characteristics. Additionally, due to the consumption of smaller portions, these patients receive insufficient amounts of nutrients. Therefore, this study aimed to develop plant-based purée as a meal for an oro-pharyngeal dysphagia (OD) diet, enriched with proteins, fiber and antioxidant vitamins. The suitability of three protein sources—soy protein isolate, whey protein isolate and brown pea protein concentrate—was tested through evaluation of their effect on the rheological properties of protein-enriched plant-based purées for OD diets. Based on the rheological analysis, whey protein was selected for incorporation into the new product formulations. Two prototypes of soups and two prototypes of desserts produced in this study demonstrated acceptable textural properties and high nutritional value. [ABSTRACT FROM AUTHOR]

Introduction: Patients who form kidney stones are typically advised to limit intake of nondairy animal protein. Plant-based meat products may be a processed substitute protein source for these patients and have recently gained popularity because of health concerns, increased retail availability, decreased environmental impact, and meat supply shortages during the COVID-19 pandemic. Despite these perceived benefits and tangential association with whole food plant-based diets, the potential lithogenic risks associated with these products are not well characterized. Methods: The U.S. Department of Agriculture database was queried with a sample of plant-based meat products widely available to U.S. consumers. Nutrient profile data were compiled and compared with animal protein data using standardized serving sizes. Primary protein sources were identified using verified ingredient lists. Oxalate content was extrapolated based on dietary data sources. Results: A total 47 plant-based meat products (16 beef, 11 pork, 10 chicken, and 10 seafood) were analyzed. Compared with their respective animal protein, most products contained on average fewer calories (plant-based beef 77%, pork 94%, chicken 86%, and seafood 83%) and less protein (plant-based beef 68%, pork 96%, chicken 53%, and seafood 54%). Most products used soy protein as the primary protein source (55%). Soy-based beef contained the highest average oxalate content (18 mg per serving), whereas soy-based seafood contained the lowest (7 mg). The most common non-soy protein source was pea protein (30%), containing trace amounts of oxalate. Sodium content was higher in most plant-based products overall (72%) and in each category (plant-based beef 109%, pork 128%, chicken 100%, and seafood 148%). Calcium content was higher (plant-based beef 317%, pork 144%, chicken 291%, and seafood 295%) compared with animal protein. Conclusions: Most plant-based meat products consist of protein sources that are, relative to animal protein sources, higher in oxalate, sodium, and calcium. Stone-forming patients should be counseled about the potential lithogenic risk of these processed products. [ABSTRACT FROM AUTHOR]

Demand for plant-based meat is increasing as the flexitarian diet becomes popular. Many meat analog products in the market are made from soy and wheat proteins, but other protein sources can be used. Alternate legume proteins can be an economically and functionally viable option. This review discusses qualities of traditional meat analog proteins (soy and wheat gluten), pea protein, and emerging pulse proteins (chickpea, faba bean, lentil, mung bean). Raw traits of protein are important for texturization via extrusion. This review focuses specifically on protein sedimentation coefficients, amino acid composition, least gelation concentration, denaturation temperature, water and oil absorption capacity, viscosity and flow temperature. Product qualities (protein solubility, water holding capacity, amino acid composition, digestibility and texture) of meat analogs based on various protein sources are also discussed. Physicochemical properties of each protein should be considered before extrusion, as their functionality can vary even when from the same botanical source. The analysis and methods used for transitioning from soy and wheat gluten to pea can be useful in the utilization of additional pulse proteins. The quality of pea based textured vegetable protein is heavily dependent on processing parameters such as specific mechanical energy, moisture, and temperature. However in general, pea protein based texturized products have a lower cutting strength, and less chewiness than soy or gluten based products due to differences in protein sub-units and also cold and hot water swelling (or gelling) properties that can be potentially manipulated by using functionality modifiers. • Peas are fast emerging as a plant protein source for texturization via extrusion. • Characteristics of pea and other new legumes must be considered versus traditional wheat and soy proteins for extrusion. • Established analysis techniques can be used to make advancements in use of legume proteins. • Due to differences in their physico-chemistry, texturization of pea protein will need process and formulation adjustments. [ABSTRACT FROM AUTHOR]

Dried porous materials based on plant proteins are attracting large attention thanks to their potential use as sustainable food ingredients. Nevertheless, plant proteins present lower gelling properties than animal ones. Plant protein gelling could be improved by optimising gelation conditions by acting on protein concentration, pH, and ionic strength. This work aimed to systematically study the effect of these factors on the gelation behaviour of soy and pea protein isolates. Protein suspensions having different concentrations (10, 15, and 20% w/w), pH (3.0, 4.5, 7.0), and ionic strength (IS, 0.0, 0.6, 1.5 M) were heat-treated (95 °C for 15 min) and characterised for rheological properties and physical stability. Strong hydrogels having an elastic modulus (G′) higher than 103 Pa and able to retain more than 90% water were only obtained from suspensions containing at least 15% soy protein, far from the isoelectric point and at an IS above 0.6 M. By contrast, pea protein gelation was achieved only at a high concentration (20%), and always resulted in weak gels, which showed increasing G′ with the increase in pH and IS. Results were rationalised into a map identifying the gelation conditions to modulate the rheological properties of soy and pea protein hydrogels, for their subsequent conversion into xerogels, cryogels, and aerogels. [ABSTRACT FROM AUTHOR]

Over the past few decades, there has been a noticeable surge in the market of plant-based meat analogs (PBMA). Such popularity stems from their environmentally friendly production procedures as well as their positive health effects. In order to meet the market demand, it is necessary to look for plant protein processing techniques that can help them match the quality of conventional meat protein from the aspects of sensory, quality and functionality. Bean proteins are ideal options for PBMA with their easy accessibility, high nutrient-density and reasonable price. However, the high polyunsaturated lipids content of beans inevitably leads to the unpleasant beany flavor of soy protein products, which severely affects the promotion of soy protein-based PBMA. In order to solve this issue, various methods including bleaching, enzyme and fermentation etc. are developed. Among these, fermentation is widely investigated due to its high efficiency, less harm to the protein matrix, targeted performance and low budget. In addition, proper utilization of microbiome during the fermentation process not only reduces the unpleasant beany flavors, but also enhances the aroma profile of the final product. In this review, we provide a thorough and succinct overview of the mechanism underlying the formation and elimination of beany flavor with associated fermentation process. The pros and cons of typical fermentation technologies for removing beany flavors are discussed in alongside with their application scenarios. Additionally, the variations among different methods are compared in terms of the strains, fermentation condition, target functionality, matrix for application, sensory perception etc. [ABSTRACT FROM AUTHOR]

Enzyme cross-linking is a pivotal method for enhancing the functionality of plant proteins, offering improvements in texture, stability, and nutritional value, which are essential for food applications. Pea protein is increasingly used as it is not identified as allergenic and has fewer other negative health concerns. However, the lower gelling capacity compared with soybean protein has limited its application in plant-based meat or protein-based products. Thus, this study focused on investigating the effects of transglutaminase (TG) and laccase (LAC) and their concentrations on pea protein isolate (PPI) gelation, towards comparison with that of soybean protein isolate (SPI). Results showed that TG and LAC both contribute to the formation of PPI gels while exhibiting different action ways. As the TG content increased, the particle size of PPI significantly increased from 97.27 ± 4.61 μm to 146.67 ± 9.87 μm at 0.8% TG concentration, whereas the particle size remained constant with increasing LAC content. Both TG and LAC significantly enhanced the PPI gel properties, with 0.4% TG addition resulting in gel strength comparable to SPI and 0.8% TG content increasing PPI gel strength by approximately 4.2 times compared to the control, surpassing SPI. Moreover, PPI with TG treated demonstrated superior effects compared to LAC-treated gels at the same concentration. Water retention of gels increased from 89.37 ± 1.97% to 94.90 ± 3.86% with TG concentration increasing, while it decreased with LAC increasing. SDS-PAGE results revealed that TG promoted the formation of larger aggregates in PPI, indicating that legumin and vicilin were the main target sites for TG, while LAC was inapparent on molecular weight. The viscosity of PPI increased from 36.91 ± 2.32 Pa·s to 70.57 ± 1.00 Pa·s with 0.8% TG, while 0.8% LAC increased viscosity to 61.79 ± 1.32 Pa·s. Hydrogen bonds and disulfide bonds play a crucial role in the gel formation process facilitated by TG and LAC. Besides, TG is also expected to contribute through the formation of isopeptide bonds. These findings validated the potential of TG and LAC in improving the quality of PPI gels and provided insights for the application and development of cross-linking enzymes in the protein processing industry. A good pea protein gel property induced by TG/LAC and its mechanism. [Display omitted] • 0.4% transglutaminase or 0.8% laccase improved gelation of PPI, making it comparable to SPI. • Transglutaminase promoted to larger aggregates of PPI gel. • Thin-chain mesh gel of PPI was formed induced by laccase. [ABSTRACT FROM AUTHOR]

The advent of direct-ink-writing 3D printing in food processing highlights potential for innovation but underscores challenges with food-grade inks, notably their inadequate self-supporting properties post-extrusion that impede maintaining structural integrity and crating complex 3D forms. This challenge is particularly pronounced with starch—a key food ingredient. This study aims to bolster the printability of normal corn starch (NCS) through integration with pregelatinized (PG) high-amylose starch (G50 and G70, with 55% and 68% amylose contents, respectively) and proteins (soy, wheat, pea protein isolates, and whey protein). The PG starch was prepared by disorganizing the high-amylose starches in 33% CaCl 2 solution and then precipitating them with ethanol. The formulation featuring an NCS/PG-G70/soy protein isolate ratio of 5:5:3 emerged superior, yielding enhanced formability, precise line printing, and robust self-support. This adapted starch-based gel facilitated the 3D printing of sophisticated structures, such as hollow and overhanging architectural forms, without necessitating chemical modification or a support bath. In vitro enzymatic hydrolysis tests on the printed constructs manifested approximately 50% resistant starch and 15% slowly digestible starch. These results suggest that the composite biopolymer ink developed in this study showcases not only superior printability but also boasts improved digestion-resistance. Thus, the findings from this research provide a foundation for developing food-grade inks capable of crafting customizable, intricately structured food products while conferring health advantages. [Display omitted] • 3D printing models with sophisticated structures can be printed by starch-based gel. • Addition of PG-G70 improves the support capabilities of starch-based gel. • After rehydration, pre-gelatinized high-amylose starch (PG-G70) forms micro-domains. • The 3D printing models manifest 50% resistant starch and 15% slowly digestible starch. • Soy protein isolate can adjust in vitro enzymatic hydrolysis properties of starch-based gel. [ABSTRACT FROM AUTHOR]

Despite ecological and nutritional benefits, food ingredients derived from microalgae remain a niche market. A contributing factor to this is the lack of knowledge to exploit their techno-functional properties. This research investigated the structurability of Auxenochlorella protothecoides microalgal biomass during high moisture extrusion cooking for meat analogues. The fibrous extrudate structure weakened with increasing A. protothecoides content in the recipe. To scrutinise reasons for this phenomenon, a thorough compositional comparison of microalgal biomass and conventional raw materials from soy and pea was performed. The identified macrocompositional differences were shown to exert only a minor impact on fibrous structure formation. Thus, structurability appears to be predominately influenced by protein composition, protein properties and electrolyte environment. The proteins of the analysed microalgal biomass were 20 % smaller in molecular weight, had 18–68 % higher solubility and contained 15–50 % less hydrophobic sidechains, all of which may impede protein interaction potential and thereby network formation. Additionally, the pH of microalgae suspensions was lower, which has a negative impact on disulfide bridge formation. Moreover, the analysed microalgal biomass contained considerable amounts of kosmotropic ions that stabilise individual proteins. Denaturation, pH shift, addition of cysteine, transglutaminase and polyvalent cations were proposed as measures to improve structurability of the microalgae A. protothecoides. [Display omitted] • Heterotrophic A. protothecoides biomass contains close to 50% proteins per dry mass. • A. protothecoides biomass shows limited structurability in high-moisture extrusion. • Lower structurability is not caused by intact cells, low protein or high fat content. • Smaller, less hydrophobic proteins, lower pH and present ions may limit structuring. • Denaturation, pH increase or addition of polyvalent cations are proposed measures. [ABSTRACT FROM AUTHOR]

Interactions between pea protein isolate (PPI, 1%) and soy lecithin (SL, 0.1%–2%) in bulk phase and the impacts on the emulsifying properties of PPI were investigated. Fluorescence spectra, molecular docking, and infrared spectroscopy verified that PPI and SL formed complexes in aqueous phase via hydrophobic interactions, hydrogen bonds, and electrostatic interactions. CMC of SL was increased to 1% in presence of PPI (1%). Increased particle size, surface charge, and surface hydrophobicity of PPI-SL complexes with increasing SL concentrations were observed. Addition of SL transformed the composition of oil/water interface from pure PPI into a mixture of PPI and SL, which decreased the surface tension and resulted in smaller droplet size of emulsions. The inclusion of all PPI-SL complexes enhanced emulsion stability during storage. Incorporating SL below 1% also showed similar protective effects for curcumin against UV irradiation compared to pure PPI. The study may provide a theoretical basis for the rational non-covalent combination of pea protein and lecithin as complex emulsifiers. [Display omitted] • PPI primarily interacts with SL through hydrophobic interactions. • In the presence of 1% PPI, the CMC of SL was increased to 1%. • Incorporation of SL (0.1%–2%) improved the physical stability of PPI-based emulsions during storage. • Addition of SL reduced the partitioning of CUR in the oil phase. • Beyond the CMC, SL adversely affected the photostability of CUR. [ABSTRACT FROM AUTHOR]

Quantitative data on powder swelling kinetics is essential to understand phenomena occurring during rehydration, e.g. lump formation. In this study, swelling kinetics of food powders (gelatin powder, soy protein isolate, pea protein concentrate) were quantified by Nuclear Magnetic Resonance (NMR) relaxometry. Using gelatin plates as a model system, it was successfully demonstrated that NMR relaxometry is an efficient, non-destructive method to study swelling kinetics of non-dissolving systems with moderate swelling speeds. For plant-based proteins, high swelling speeds were observed. The obtained maximum water uptake due to swelling was 5.10 ± 0.80 g/g for soy protein isolate and 3.93 ± 0.16 g/g for pea protein isolate, which is in the expected range. Measurement speed was too low to resolve early swelling kinetics (below 84 s), evaluation was more elaborate and results less unambiguous. [Display omitted] • Successful investigation of NMR relaxometry as method to quantify powder swelling. • Water uptake of gelatin quantified with high accuracy using NMR. • Plant-based protein powders swell significantly faster than gelatin powder. • Quantification of water uptake possible for plant-based proteins but more complex. • Method recommended especially for slow and strongly swelling material. [ABSTRACT FROM AUTHOR]

Different sources of proteins have various ways for facilitating the gelation process of surimi matrices, leading to the diverse combined effects with transglutaminase (TG). In this study, the effects of two plant proteins, soy protein isolate (SPI) and pea protein isolate (PPI), and two animal non-muscle proteins, egg white protein (EWP) and whey protein isolate (WPI), with TG addition on the gel properties of clam Meretrix meretrix (MM) surimi gels were investigated, and the mechanisms were explored. In the presence of TG, the exogenous protein addition significantly improved (p < 0.05) the gelation process of the MM surimi. The best improvements were obtained with the combination of EWP, where the gel strength, cooking loss, and water holding capacity were enhanced by 113.08%, 67.89%, and 26.30%, respectively. The addition of SPI showed a relatively weak enhancement compared to EWP incorporation, followed by the addition of PPI and WPI. The results of optical microscopy, differential scanning calorimetry, and chemical forces demonstrated that TG preferentially promoted plant proteins to form self-aggregation in the surimi system, and SPI generated more polymers than PPI. In contrast, the interpenetration of animal proteins and MM myofibrillar proteins was improved by TG. EWP formed a double cross-linking network within the MM protein network, while WPI acted as a binder to promote protein-protein interactions. This research could provide novel insights for developing MM resources and establish a theoretical foundation for the use of composite exogenous protein additives to enhance the gel properties of MM surimi products. • Plant/animal proteins could improve the gelation of TG-added MM surimi. • TG generated more polymers between plant proteins within MM gel network. • SPI generated more self-aggregates than PPI in the presence of TG. • The interpenetration of animal proteins with MM surimi was promoted by TG. • TG induced a double cross-linking network between EWP and MM protein. [ABSTRACT FROM AUTHOR]

Mixing surimi/plant proteins to reduce animal proteins is considered as an effective way to improve the sustainable production of surimi-based products. The effect of partial substitution (10%∼50%, plant proteins/surimi proteins ratio) of surimi proteins by plant proteins (wheat protein, soybean protein, rice protein, and pea protein) on the properties of the composite gels were investigated. The replacement caused the reductions in gel strength and whiteness. There was a slight increase in water holding capacity (WHC) of mixed gels made from soy or pea protein, but decrease in the cereal protein group. E-nose investigations revealed that the reactions to the W5S and W1W sensors caused the scent profiles to shift dramatically as the replacement amount increased. Organoleptic inspection revealed the substitution ratios of wheat protein, soy protein, rice protein, and pea protein to achieve the sensorial rejection were 30%, 40%, 30%, and 40%, respectively. LF-NMR and MRI showed the cereal proteins increased the T 22 relaxation time, while the legume proteins caused a reduction. The mixed gels contained all the essential amino acid, and the digestibility in the wheat protein groups was the highest. These results proved an elaborate formulation can achieve balanced sensory and nutritional attributes in surimi gelled foods. [Display omitted] • Meat-reduced surimi gel was prepared by partial substitution of myofibrillar proteins. • The replacement by plant proteins decreased the strength and whiteness of gels. • Alternative substitution ratios that meet sensory requirements of gels were found. • Proteins in the mixed surimi gels contained enough essential amino acids. • An elaborate formulation can achieve balanced sensory and nutritional attributes. [ABSTRACT FROM AUTHOR]

Nowadays, a growing offering of plant-based meat alternatives is available in the food market. Technologically, these products are produced through high-moisture shear technology. Process settings and material composition have a significant impact on the physicochemical characteristics of the final products. Throughout the process, the unfolded protein chains may be reduced, or associate in larger structures, creating rearrangement and cross-linking during the cooling stage. Generally, soy and pea proteins are the most used ingredients in plant-based meat analogues. Nevertheless, these proteins have shown poorer results with respect to the typical fibrousness and juiciness found in real meat. To address this limitation, wheat gluten is often incorporated into the formulations. This literature review highlights the key role of wheat gluten in creating products with higher anisotropy. The generation of new disulfide bonds after the addition of wheat gluten is critical to achieve the sought-after fibrous texture, whereas its incompatibility with the other protein phase present in the system is critical for the structuring process. However, allergenicity problems related to wheat gluten require alternatives, hence an evaluation of underutilized plant-based proteins has been carried out to identify those that potentially can imitate wheat gluten behavior during high-moisture shear processing. [ABSTRACT FROM AUTHOR]

The focus of the global cheese industry on accessing new markets for cheese is currently driving a greater need for innovation in cheese products. Research to date suggests that, for example, East Asian consumers prefer cheeses that have a soft texture, with mild and milky flavors. Strategies for achieving such cheese characteristics are reviewed in this article. For example, incorporation of polysaccharides into cheese results in cheese with higher moisture levels and softer textures; this also results in modification of other properties such as adhesiveness, meltability and flavor release. Hydrated polysaccharides may be considered as filler particles within cheese matrices, and therefore filled gel models with suitable filler particles can be used to establish the effect of filler volume, size and surface properties on the fractural and rheological properties of cheese matrices, thus guiding the use of polysaccharides. Addition of plant proteins such as soy and pea protein can also result in cheeses with softer texture. Furthermore, it has been suggested that heat-induced gelation of soy or pea protein with casein results in a gel structure consisting of two independent protein gels, thus facilitating the design of bespoke structures by adjusting the ratio of the two proteins. Finally, it is proposed that incorporation of ingredients with sensory properties familiar to East and Southeast Asian consumers and with the capacity to achieve bespoke textures offer potential for the development of cheese products for consumers in these markets. [ABSTRACT FROM AUTHOR]

Plant proteins, especially legume proteins, are among the most versatile, nutritious, and sustainable protein sources compared to animal-derived counterparts. Moreover, legume proteins have recently attracted interest of the scientific community owing to their wall-forming, gelling, and emulsifying properties in microencapsulation delivery systems. However, many industries have limited the use of legume proteins due to their poor solubility, lower functionality, presence of saponins and phenols leading to beany favor, and susceptibility to environmental stress. Modification of legume protein functional properties through emerging high-pressure and ultrasound technologies have therefore attracted considerable research interests to prepare legume proteins with desirable functional properties as wall material. This article reviews recent studies on the application of emerging technologies to modify legume protein functional properties for the improvement in encapsulation properties. The application of legume protein-based microcapsules in the design of novel foods and their bioavailability is thoroughly discussed with an emphasis on the current scientific knowledge and future perspective. The review highlighted the growing interest on legume proteins due to consumer shift towards healthy diet choices that also have a better ecological footprint. The legume protein-based market has gained momentum among the consumer market with USD 267.53 million over 2019 to 2023, which is ultimately due to growing preference for sustainable and healthier foods. Application of non-thermal technologies, such as high-pressure and ultrasound technologies to legume proteins significantly improved their structure, functionality, and other encapsulation properties to better encapsulate the bioactive core materials. The designed novel foods using microencapsulated bioactive compounds with legume proteins showed the increased bioavailability of active components along with controlled release, improved nutritional values, sensory attributes, and other health-promoting effects. [Display omitted] • Legume proteins are clean-green sources for microencapsulation applications. • High-pressure and ultrasound improve the legume protein functional properties. • Legume proteins can be applied in microencapsulation as wall materials. • Legume protein market continues to skyrocket in global plant-based protein market. • Pea and soy proteins are among the prominent sources in the legume protein market. [ABSTRACT FROM AUTHOR]

Pea protein (PP) was moderately hydrolyzed using four proteolytic enzymes including flavourzyme, neutrase, alcalase, and trypsin to investigate the influence of the degree of hydrolysis (DH) with 2%, 4%, 6%, and 8% on the structural and functional properties of PP. Enzymatic modification treatment distinctly boosted the solubility of PP. The solubility of PP treated by trypsin was increased from 10.23% to 58.14% at the 8% DH. The results of SDS-PAGE indicated the protease broke disulfide bonds, degraded protein into small molecular peptides, and transformed insoluble protein into soluble fractions with the increased DH. After enzymatic treatment, a bathochromic shift and increased intrinsic fluorescence were observed for PP. Furthermore, the total sulfhydryl group contents and surface hydrophobicity were reduced, suggesting that the unfolding of PP occurred. Meanwhile, the foaming and emulsification of PP were improved after enzymatic treatment, and the most remarkable effect was observed under 6% DH. Moreover, under the same DH, the influence on the structure and functional properties of PP from large to small are trypsin, alcalase, neutrase and flavourzyme. This result will facilitate the formulation and production of natural plant-protein-based products using PP. [ABSTRACT FROM AUTHOR]

Fischer et al. [[1]] studied the impact of ageing on pea protein volatile compounds and the correlation with pea protein odour. Since 1975, the Weurman Flavour Research Symposium has been held every three years in different European countries, and has been finally established as an international event that offers unique opportunities for distinguished scientists from academia and industry, from different disciplines, and from all over the world, to discuss trends and new paradigms in the field of flavour research. Key aroma compounds were elucidated by GC-MS-O to be dihydroactinidiolide, isovaleraldehyde and coumarin, which were also confirmed by a recombination study. [Extracted from the article]

Legume proteins are appealing in the food industry for their nutrition and sustainability, but their low solubility due to the compact structure makes their applications in food industry limited. In this study, three commonly used legume proteins in food industry were selected as samples to be tested: soy protein (SP), pea protein (PP), and chickpea protein (CP). This study aims to improve the structural properties of these three proteins, so that it could promote effective grafting with epigallocatechin gallate (EGCG) through a combined hot alkaline and pH-shift treatments. Legume protein solutions were adjusted to pH 12 and heated at 80 °C for 30 min, resulting to a 13%–19% increase in free thiol content and a 59%–610% increase in surface hydrophobicity. This kind of change in structure leads to a 19%–46% increase in EGCG grafting degree. Treated protein-EGCG conjugates exhibited smaller and more uniform particle sizes, improved emulsification activity by 27%–218%, and additionally enhanced solubility, thermal stability, and antioxidant activity. Among all the tested proteins, pre-treated SP-EGCG conjugates showed the best solubility, emulsification, and thermal stability due to their highest surface hydrophobicity, highest EGCG grafting degree, and loose structure. These results indicate that combined hot alkaline and pH-shift treatment enhances the functional properties of legume proteins, expanding their potential applications as functional ingredients in the food industry. [Display omitted] • Hot alkaline and pH-shifting induced protein hydrolysis, exposing reactive groups. • The combined treatment facilitated grafting of EGCG to legume proteins. • Treated protein-EGCG conjugates showed improved emulsification and solubility. • Soy protein exhibited the best functional properties of the three legume proteins tested. [ABSTRACT FROM AUTHOR]

With an increasing emphasis on health and environmental consciousness, there is a growing inclination toward plant protein-based meat substitutes as viable alternatives to animal meat. In the pursuit of creating diverse and functional plant protein-based substitutes, innovative plant proteins have been introduced in conjunction with soy protein isolate (SPI), encompassing pea protein isolate (PPI), rice bran protein (RBP), fava bean protein isolate (FPI), and spirulina protein isolate (SPPI). Notably, SPI-WG extrudates and SPI-PPI extrudates exhibited superior fiber structures (fiber degrees were 1.72 and 1.88, respectively), with coarse fibers in SPI-WG extrudates and fine, dense fibers in SPI-PPI extrudates. The addition of RBP, FPI and SPPI had minimal effect on fiber structure. Fresh SPI-FPI displayed the slowest rate of water loss, losing about 7.11% of their total weight in 5 h. Different plant proteins can be selected for the preparation of plant protein-based meat substitutes according to practical needs. • Chemical bonding differences emerge across extrusion phases. • The SPI-WG and SPI-PPI blends demonstrate exceptional fiber degrees. • SPI-FPI, SPI-RBP and SPI-SPPI display distinctive hardness, network structure, significant toughness. • Proteins' structural transitions from α-helix to β-sheet structures occur during processing. [ABSTRACT FROM AUTHOR]

Although protein-based biomimetic fibers are available, green and inexpensive protein-based fibers remain a challenge to develop. Herein, a microfluidic chip was designed to prepare protein-based fibers using cellulose nanofibers and various plant-derived proteins, including wheat gluten, zein, soy protein, pea protein, and rice bran protein. Furthermore, a comprehensive elucidation of the plant protein fiber formation mechanism was conducted. The results showed that plant protein fibers prepared by microfluidic spinning had smooth surfaces, strong mechanical properties, high thermal stability and antioxidative activity, good digestibility, and low sensitization. Additionally, the strong hydrodynamic shear force produced during microfluidic spinning changed the secondary structure of the protein, which promoted the binding of protein molecules to cellulose nanofibers, thus enhancing the molecular orientation of both protein and nanofiber. Consequently, this study may facilitate the development of natural, environmentally friendly, and functional protein-based fibers. [Display omitted] • Plant protein can be used as raw material to prepare microfluidic spinning biofiber. • The mechanism of plant protein fiber prepared by microfluidic spinning was revealed. • Plant protein fibers showed high mechanical property and thermal stability. • Plant protein fibers indicated higher antioxidant activity and hypoallergenicity. • Plant protein fiber obtained by microfluidic spinning has good application prospect. [ABSTRACT FROM AUTHOR]

[Display omitted] • Protein carbonyl content increased after Cold Plasma (CP) treatment in both the isolates. • Functional and emulsification properties of both isolates improved after CP treatment. • Circular Dichroism (CD) and Fourier Transform (FT) Raman Spectroscopy confirmed the reduction of α-helix content in isolates. • CP-treated Pea Protein Isolate (PPI) showed better rheological properties and creep recovery than Soy Protein Isolate (SPI). • CP treatment at 30 kV and 6 min gave optimum results for modifying isolates among all the treatments. The modification in structural, rheological, and techno-functional characteristics of soy and pea protein isolates (SPI and PPI) due to dielectric barrier discharge cold plasma (DBD-CP) were assessed. The increased carbonyl groups in both samples with cold plasma (CP) treatment led to a reduction in free sulfhydryl groups. Moreover, protein solubility of treated proteins exhibited significant improvements, reaching up to 59.07 % and 41.4 % for SPI and PPI, respectively, at 30 kV for 8 min. Rheological analyses indicated that storage modulus (G′) was greater than loss modulus (G″) for CP-treated protein gels. Furthermore, in vitro protein digestibility of SPI exhibited a remarkable improvement (4.78 %) at 30 kV for 6 min compared to PPI (3.23 %). Spectroscopic analyses, including circular dichroism and Fourier Transform-Raman, indicated partial breakdown and loss of α-helix structure in both samples, leading to the aggregation of proteins. Thus, DBD-CP induces reactive oxygen species-mediated oxidation, modifying the secondary and tertiary structures of samples. [ABSTRACT FROM AUTHOR]