Pea Protein Isolate Research Articles

Characterization of Plant-Based Raw Materials Used in Meat Analog Manufacture

The purpose of this research was to investigate the characteristics of different plant-based sources rich in protein, chickpea flour (CPF), hazelnut oil cake (HOC), soy protein isolate (SPI) and concentrate (SPC), and pea protein isolate (PPI) for their subsequent use in the manufacture of meat analogs. The protein sources were analyzed for dry matter, ash, protein, fat, starch, dietary fiber, water holding capacity, granulosity, color parameters (L*, a*, b*, C*, YI), antioxidant activity before and after gastrointestinal in vitro digestion, and amino acid and mineral compositions. The highest dry matter content was determined in hazelnut oil cake and pea protein isolate. For the protein content, maximum values were obtained for the protein isolate and concentrate samples, from 52.80% to 80.50%, followed by hazelnut oil cake and chickpea flour. The water-holding capacity of all plant sources was directly influenced by the values of protein content, dietary fiber, and granulosity. The results obtained after gastrointestinal digestion also showed quite significant antioxidant activity, which is due to the process of hydrolysis and denaturation of plant-based protein sources in the gastrointestinal tract. Major amino acids identified in the analyzed samples were glutamic acid, leucine, arginine, phenylalanine, serine, valine, alanine, and tyrosine from minerals P, Na, Mg, and Ca. Principal component analysis (PCA) was used to illustrate the relationship between physicochemical characteristics, amino acid composition, mineral composition, and antioxidant activity determined in the plant-based materials.

Sulfonated cellulose nanocrystalline- and pea protein isolate-mixture stabilizes the citral nanoemulsion to maintain its functional activity for effectively preserving fruits.

The instability of citral greatly limits its application in food field. This study aimed to develop a safe and green emulsifier-stabilized nanoemulsion (NE) to encapsulate citral for exerting its activities. A series of NEs were prepared using varying proportions (1:2 and 1:3) of sulfonated cellulose nanocrystalline- (CNC-C) and pea protein isolate- (PPI) mixture as emulsifier to encapsulate citral with different content (1%, 2%, and 3%), and their stability, antioxidant and antibacterial activities were evaluated to identify the optimal system. When CNC-C and PPI proportion was 1:3 and citral content was 2% (CC1-P3-C2), the obtained CC1-P3-C2 incorporated into pectin achieved the excellent preservation effect on kiwifruits and blueberries. It was attributed to the stability and functional activities of CC1-P3-C2. On the one hand, after storage (25 d) or at pH11 or 100mM NaCl, its size and polydispersity index were still within acceptance level (<300nm and 0.3). On the other hand, it showed good antioxidant and antibacterial activities against Escherichia coli, Staphylococcus aureus, Botrytis cinerea, and Botryosphaeria dothidea, which was due to its high encapsulation efficiency (96.78%). Therefore, CC1-P3-C2 showed a great application potential in fruit preservation, which also provided a feasible strategy to design stable citral NEs.

Mechanical stretching technology for plant-based meat analogs with enhanced texture utilizing wheat gluten and pea protein isolate

Mechanical stretching technology for plant-based meat analogs with enhanced texture utilizing wheat gluten and pea protein isolate

PH-dependent emulsifying properties of pea protein isolate: Investigation of the structure - Function relationship.

This study investigated the relationship between pea protein isolates (PPI) emulsifying properties and their structural, interfacial, and physicochemical characteristics at various pH values (native pH, 7, 5, and 3). Emulsion characteristics including emulsifying activity and stability, droplet size, flocculation index (FI) and coalescence index (CI) were examined. Additionally, physicochemical properties such as solubility, zeta potential, surface hydrophobicity, interfacial protein adsorption and protein conformation were analyzed. Results revealed significant pH-dependent variations in emulsifying performance. The poorest emulsifying performance was observed at pH5, with the largest droplet size (28.84μm) and highest CI (38.94%). Optimal emulsifying properties were noticed at native pH, with the smallest droplet size (7.73μm) and lowest CI (4.69). At pH3, good emulsifying ability with the highest physical stability (5.43) were observed, associated with increased surface hydrophobicity and the presence of some aggregates contributing to the formation of cohesive interfacial film. Structural elements, particularly β-sheets and random coils, were positively correlated with emulsifying activity and stability, while β-turns had a negative impact. These findings provide insights into the pH-dependent emulsifying behavior of PPI, highlighting the complex relationship between protein structure and functionality, enabling the optimization of the use of PPI as an emulsifier in food applications.

Effect of resonance acoustic mixing treatment on the gelation properties of pea protein isolate and the gel in vitro digestibility.

This study aimed to investigate the effect of different durations (0, 5, 10, 15, 20, and 30 min) of resonance acoustic mixing (RAM) treatment on the gel properties and digestibility of pea protein isolate (PPI). Results indicated that RAM treatment enhanced the water holding capacity (WHC) of PPI gels, with the highest WHC of 94.79 % achieved after RAM treatment for 20 min. A 15-20 min RAM treatment altered the secondary structure of proteins in PPI gels, reducing α-helix content while increasing β-sheet content. This treatment also refined the microstructure of PPI gels, changing the surfaces from rough to smooth and the pores from large to small. RAM treatment for 5-20 min decreased the shear viscosity and gel strength of heat-induced PPI gels, although these properties slightly recovered when the treatment was extended to 30 min. Additionally, RAM treatment improved the in vitro digestibility of PPI gels. In conclusion, RAM treatment significantly influenced the structural, mechanical and digestive properties of PPI gels, and this effect can be regulated by adjusting the treatment duration, making it suitable for various practical applications.

ИЗУЧЕНИЕ ВОЗМОЖНОСТИ ПРИМЕНЕНИЯ ИЗОЛЯТА ГОРОХОВОГО БЕЛКА В ТЕХНОЛОГИИ ПРОИЗВОДСТВА МЯСО-РАСТИТЕЛЬНОГО КУЛИНАРНОГО ИЗДЕЛИЯ

The purpose of research is to study the possibility of using pea protein isolate in the production technology of a meat and vegetable culinary product of a functional orientation. Tasks: to study the physicochemical and biochemical parameters of pea protein isolate; to develop the technology of a meat and vegetable culinary product with the addition of pea protein isolate; to determine the quality indicators of the finished product and develop a production control program. Objects: commercially produced pea protein isolate, a laboratory sample of a meat and vegetable product prepared according to a standard recipe and technological scheme (control), prototype soufflé samples with the addition of 5 %, 10 and 15 % pea protein isolate to the mass of poultry meat. At the first stage of the research, the physicochemical parameters and biochemical composition of the pea protein isolate were determined. It has been established that the test sample contains an easily soluble and easily digestible protein base (60.6±0.02 %) and special easily soluble carbohydrates (30.1±0.02 %), gluten, lactose and anti-food components are absent. The study of biochemical parameters allows us to conclude that the pea protein isolate contains 7 essential amino acids, as well as polyunsaturated fatty acids, the content of which is 2 times higher than the total content of saturated and monounsaturated fatty acids and is 66.5 and 33.4 %, respectively. The data obtained allow us to conclude that it is possible to use pea protein isolate in the technology for the production of functional foods. The technology of a meat and vegetable culinary product with the addition of pea protein isolate in the amount of 5% by weight of poultry meat has been developed and the quality indicators of the finished product have been determined. The results of the organoleptic evaluation indicate high quality indicators of the prototype. Physical and chemical indicators have the following values: humidity – 70.52 % (at a rate of 70.5 ± 2 %), the minimum allowable amount of soluble solids per 100 g – 17.92 %, pH is 6.9. Microbiological indicators are within acceptable limits. The determination of nutritional value indicators indicates an increase in the amount of protein compared to the control by 23.7 % and a decrease in fats and carbohydrates by 12.2 and 9.1 %. At the final stage of research, a production control program has been developed.

Impact of Autoclaving on Functional Properties of Pigeon Pea Protein Isolates

Pigeon pea (Cajanus cajan) is a protein-rich legume crop widely cultivated in tropical and subtropical regions, serving as a vital dietary protein source, particularly where protein malnutrition is a concern. The protein fractions in pigeon pea seeds are primarily composed of albumin, globulin, glutelin, and prolamin, with globulins accounting for nearly 60% of the total protein. Despite its nutritional value, pigeon pea protein remains underutilized in plant protein market. This study investigated the impact of autoclaving treatment on the functional properties of protein isolates obtained from two pigeon pea genotypes, Pusa Arhar 2018-4 and ICP 1452. Key functional properties, including protein solubility, surface hydrophobicity, water holding capacity (WHC), oil holding capacity (OHC), emulsifying properties, and foaming properties, were analysed. Autoclaving significantly reduced protein solubility across all pH levels in the range of 35.85-75.28% due to thermal denaturation and aggregation. Surface hydrophobicity increased by 10.68% and 16.18% for Pusa Arhar 2018-4 and ICP 1452, respectively. WHC decreased to 210.28% for Pusa Arhar 2018-4 and 209.8% for ICP 1452, while OHC increased to 186.44% for Pusa Arhar 2018-4 and 189.25% for ICP 1452. Emulsifying activity index (EAI) and stability index (ESI) decreased after autoclaving, EAI decreasing to 16.39 m2/g for Pusa Arhar 2018-4 and 16.34 m2/g for ICP 1452 and ESI decreasing to 29 min for Pusa Arhar 2018-4 and 30.33 min for ICP 1452. Conversely, autoclaving significantly improved foaming capacity by 22.90% and 34.31% for Pusa Arhar 2018-4 and ICP 1452, respectively, with greater foaming stability, at 60 minutes, it increased to 15.92% for Pusa Arhar 2018-4 and 16.91% for ICP 1452. These findings highlight the potential of autoclaving to modulate the functional properties of pigeon pea protein isolates, enhancing their suitability for diverse food applications like inclusion in development of protein rich functional foods.

High-throughput precision assessment of pea-derived protein products using near infrared hyperspectral imaging.

This study aims to develop rapid and non-invasive methods based on near-infrared hyperspectral imaging and chemometrics for quantitative prediction of chemical compositions of pea-derived products. Hyperspectral imaging was used to acquire images from pea processing streams, namely pea flour, pea protein concentrate, and pea protein isolate. The PLS algorithm was used to develop quantitative prediction models based on the relationship between the hyperspectral image data and the chemical compositions of the pea products, including moisture, protein, ash, insoluble fiber, and total starch. Prediction results in terms of coefficient of determination (R2) and root mean square errors in the prediction (RMSEP) datasets show accurate results for moisture (R2=0.844, RMSEP = 0.407%), protein (R2=0.99, RMSEP = 2.074%), ash (R2=0.778, RMSEP = 0.474%), and total starch (R2=0.991, RMSEP = 2.316%) contents. Low prediction accuracy was obtained for insoluble fiber (R2=0.597, RMSEP 2.474%) content. The accurate prediction achieved by hyperspectral imaging highlights its suitability for high throughput multi-parameter assessment of pea-derived products, which is particularly important given their increasing market demand.

Impact of soy/pea protein isolate-oil interactions on the physicochemical and structural properties of high-moisture texturized proteins under different oil concentrations.

This study investigated the effects of oil addition on the physical and chemical properties of high-moisture texturized proteins (HMTPs), focusing on soy protein isolate (SPI) and pea protein isolate (PPI). Rheological analysis revealed contrasting behaviors: SPI exhibited decreased rheological parameters at low oil concentrations (1, 3 %), followed by a significant increase at higher concentrations (5, 10 %), whereas PPI showed a consistent decline across all oil concentrations. The superior emulsifying and gelling abilities of SPI resulted in stronger protein-protein interactions and greater hardness at higher oil concentrations. In contrast, PPI exhibited minimal protein-oil interactions, reducing hardness and weakening textural properties. Further analysis showed that SPI-based and PPI-based HMTP exhibited structural changes upon oil addition, with contrasting directional shifts due to differing degrees of protein-oil interactions. These results emphasize the critical role of protein selection in optimizing oil-containing HMTP formulations, with SPI demonstrating clear advantages in achieving desirable texture due to its superior functional properties. This study provides valuable insights for developing sustainable plant-based meat analogs, particularly those requiring oil incorporation to replicate the textural and structural characteristics of traditional meat products.

Impacts of solid-state fermentation on functional properties of pea protein isolate

Impacts of solid-state fermentation on functional properties of pea protein isolate

Insight Into the Film‐Forming Properties of Pea Protein Isolate Improved by Cellulose Nanocrystals From the Perspective of Water Phase Stabilization

ABSTRACTThis study is dedicated to explore the effect of cellulose nanocrystal (CNC) on the film formability of pea protein isolate (PPI) and propose the regulation mechanism from the perspective of water phase stabilization. Compared with PPI film, the CNC‐PPI composite films showed the improvement in mechanical properties and barrier properties of water/air. CNC reduced the proportion of free water in the PPI film and induced its conversion to immobilized water. From the microscopic observation of the films, it could be found that 0.25%–0.75% CNC made the dispersion of PPI more uniform, and formed more compact film structure. Meanwhile, the exposure of tyrosine and tryptophan in PPI molecules and the increase in the content of β‐sheet resulted in the improvement of film‐forming properties of PPI. The enhanced stability of water phase induced by CNC restrained the formation of water channels, thus improving the structural integrity of gel network and the film‐forming properties of PPI. This work provided a theoretical reference for regulation of the film‐forming properties of PPI with CNC, which was expected to improve the product performance of PPI films and enrich the application scenarios of PPI.

Proteomic and peptidomic profiling of spirulina-fortified probiotic powder formulations during in vitro digestion.

This study reports on the influence of lactic acid fermentation on the proteomic and peptidomic profiles of spirulina protein isolate (SPI)-fortified, freeze-dried powders containing living Lacticaseibacillus rhamnosus GG (LGG) cells during in vitro digestion. For comparison, powders fortified with whey protein isolate (WPI) and pea protein isolate (PPI) were also evaluated. Prior to freeze-drying, the powder precursors were either non-treated or fermented. Capillary SDS-PAGE electropherograms revealed a mild proteolytic effect due to fermentation. C-phycocyanin (SPI) and β-lactoglobulin (WPI) showed the highest resistance to pepsinolysis. All samples were responsive to pancreases, with fermented WPI showing the lowest responsiveness. Fermentation enhanced the degree of hydrolysis (DH) in gastric chymes, whereas in intestinal chymes, DH followed the order SPI > PPI > WPI, with fermentation showing no significant impact. A total of 6, 11, and 52 potential bioactive peptide sequences, associated with various beneficial activities, were identified in the SPI, PPI, and WPI digesta, respectively. The highest amino acid bioaccessibilities were observed for cysteine and methionine in SPI, isoleucine and arginine in PPI, and glycine in WPI. In conclusion, fortifying probiotic formulations with protein isolates offers secondary health benefits, stemming from the release of bioactive peptides and bioaccessible essential amino acids.

Controlling pea starch gelatinization behavior and rheological properties by modulating granule structure change with pea protein isolate

Controlling pea starch gelatinization behavior and rheological properties by modulating granule structure change with pea protein isolate

Thermogelation of nanoemulsions stabilized by a commercial pea protein isolate: high-pressure homogenization defines gel strength.

The impact of animal-based food production on climate change drives the development of plant-based alternatives. We demonstrate the use of colloidal thermogelation on a real nanoemulsion system to create structured gels that could be of interest for thermo-mechanical processing of next-generation plant-based food applications. We use a commercial pea protein isolate (PPI) without further purification to stabilize a 20 vol% peanut oil-in-water nanoemulsion at pH = 7 by high-pressure homogenization (HPH) and demonstrate the temperature induced gelation behavior of the nanoemulsion as a function of the HPH processing parameters. Bright-field and laser scanning confocal fluorescence microscopy reveals a diverse microstructure of the aqueous PPI dispersions, with a large amount of insoluble protein particles, cell-wall debris particles, and lipid inclusions. Sedimentation of particulates is prevented by HPH treatment and leads to a loss of the dispersion's thermogelation properties. The non-gelling PPI dispersion stabilizes nanoemulsions and the insoluble components of the PPI dispersions persist throughout the HPH processing. We perform a systematic rheological investigation of the effect of HPH processing on thermogelation and demonstrate that the number of HPH passes n and HPH pressure P control the average nanoemulsion droplet size measured by DLS at a 90° scattering angle. We show that the droplet size defines the final gel strength with a strong inverse dependence of the elastic modulus on droplet size. Furthermore, processing can lead to heterogeneously structured gels that yield over a large strain amplitude range.

Construction of W/O/W microcapsules based on the combination of polyglycerol polyricinoleate/protein for the co-encapsulation of crocin and quercetin: Physical properties, stability and in vitro digestion.

Due to health reasons of polyglycerol polyricinoleate (PGPR), there has been a growing interest in reducing it. To address this, this study developed the PGPR/Protein (whey, pea, and chickpea protein isolates) emulsifier combinations. The effects of these combinations on the preparation, structure, physicochemical and in vitro digestive properties of W/O/W microcapsules were evaluated. The FTIR and XRD analyses revealed hydrogen bonding interactions between the protein and PGPR (or bioactive compounds), which may contribute to the enhanced encapsulation efficiency (EE) and stability of microcapsules. PGPR/pea protein isolate (PP) microcapsules exhibited more uniform size, better rehydration, and higher EE than other microcapsules. PP combinations prolonged shelf-life of microcapsules by 1.35 to 1.73-fold, as predicted by oxidation kinetic models. Furthermore, PP microcapsules improved the bioavailability of crocin (≥ 11.08%) and quercetin (≥ 8.47%). Overall, this study hoped to provide a promising strategy for preparing W/O/W microcapsules with low PGPR content.

Identification and comparison of N-glycome profiles from common dietary protein sources

The N-glycomes of bovine whey, egg white, pea, and soy protein isolates are described here. Glycoproteins from four protein isolates were analyzed by HILIC high performance liquid chromatography and quadrupole time-of-flight tandem mass spectrometry (HILIC-FLD-QTOF-MS/MS). A total of 33 N-glycans were identified from bovine whey and egg white, and 10 structures from soy and pea glycoproteins. The type of N-glycans per glycoprotein source were attributable to differences in biosynthetic glycosylation pathways. Animal glycoprotein sources favored a combination of complex and hybrid glycan configurations, while the plant proteins were dominated by oligomannosidic N-glycans. Bovine whey glycoprotein isolate contained the most diverse N-glycans by monosaccharide composition as well as structure, while plant sources such as pea and soy glycoprotein isolates contained an overlap of oligomannosidic N-glycans. The results suggest N-glycan structure and composition is dependent on the host organism which are driven by the differences in N-glycan biosynthetic pathways.

The structural and physiochemical properties of conjugated form of pea protein isolate with inulin and its influences on encapsulation of ferulic acid

The structural and physiochemical properties of conjugated form of pea protein isolate with inulin and its influences on encapsulation of ferulic acid

Oleogel-based Pickering emulsions stabilized by pea protein isolate aggregates with different morphologies: Curcumin protection and microencapsulation.

In this study, the effect of pea protein isolate aggregate morphologies on the basic properties and potential applications of oleogel-based Pickering emulsions was investigated. The results showed that pea protein fibrils exhibited a three-phase contact angle of 81.3° and a more effective reduction of oil-water interfacial tension, which suggested better emulsification properties. Meanwhile, microscopic analysis revealed that pea protein fibrils were effectively adsorbed on the oil-water interface, forming a spatial hindrance that prevented droplet coalescence. The oleogel-based Pickering emulsion stabilized by pea protein fibril exhibited higher stability, stronger gel strength, and improved the bioavailability of curcumin. Additionally, the microcapsules generated from oleogel-based Pickering emulsions stabilized by pea protein fibrils maintained better physical integrity during the spray drying process. This work could provide valuable insights into the effects of pea protein aggregate morphologies on the stabilization of oleogel-based Pickering emulsions and their potential applications in the food industry.

Effects of transglutaminase on the gelation properties and digestibility of pea protein isolate with resonance acoustic mixing pretreatment.

Our previous research confirmed that resonance acoustic mixing (RAM) pretreatment effectively improved the emulsification and water retention of commercial pea protein isolate (PPI), but significantly reduced its gel performance. This study aimed to investigate the effect of transglutaminase (TGase, 0.1%, 0.2%, 0.3%, 0.4%, and 0.5%) on the gel properties and digestibility of PPI with RAM pretreatment (RAM-PPI). Results showed that moderate TGase (0.1-0.3%) significantly increased the α-helix/β-sheet ratio, surface hydrophobicity and covalent crosslinking of protein molecules, enhancing the texture and digestibility of RAM-PPI gels. The SEM imaging demonstrated a fine, uniform and dense network structure with many pores in these RAM-PPI gels. However, excessive TGase (0.5%) reduced the water holding capacity and intestinal digestibility of the RAM-PPI gels, mainly due to the excessive protein cross-linking and re-aggregation. These findings suggest that the combined treatment of moderate TGase with RAM can be a promising approach for the modification of plant-based proteins.

Optimizing Protein Bars With Whey Protein Isolate, Pea Protein Isolate, and Blue Whiting (Micromesistius poutassou) Fish Protein Hydrolysate: A Simplex-Centroid Mixture Design Study.

The aim of this study was to use blue whiting fish protein hydrolysate (BWFPH) as a novel dietary amino acid supplement in whey protein isolate (WPI) and pea protein isolate (PPI)-based protein bars. The findings indicate that incorporating BWFPH significantly influenced the nutritional profile of the protein bars, leading to a ~93% reduction in hardness compared to bars without the hydrolysate. Additionally, BWFPH effectively delayed the hardening process during storage. However, sensory evaluation revealed that the inclusion of BWFPH adversely affected the sensory characteristics, indicating a need for optimization. Using a simplex centroid mixture design, we identified an optimized protein blend compromising 76.02% WPI, 6.72% PPI, and 17.26% BWPFH, which achieved a balance of improved texture and sensory appeal. These results suggest that high-protein bars can be enhanced by integrating novel protein sources through careful formulation and optimization.