Pea Protein Research Articles

Pea protein-p-coumaric acid conjugate-based antioxidant film: The relationship between protein structure and film properties after covalent bonding

In this study, pea protein isolates (PPI) have been used to make conjugates by covalent binding with p-coumaric acid (p-CA), and the effect of conjugation on PPI structural characteristics and the structural, optical, mechanical, and physicochemical properties of conjugate-based films were investigated. The conjugation with p-CA unfolds the tertiary structure of PPI and significantly reduces the surface charge. A tendency of aggregation with increasing p-CA addition was proposed. The conjugate-based films show stronger tensile strength (TS) and better water barrier properties than PPI-based films. However, no significant improvement of the elongation at break (EAB) and thermal stability was found for conjugate-based films. FTIR spectroscopic and zeta-potential analyses indicated that such improved film properties could be attributed to the enhancement of hydrogen bonds and weakening of electrostatic repulsion between conjugate-conjugate. Additionally, the conjugates impart the antioxidant activity to the films as confirmed by DPPH scavenging capacity. This study demonstrates the potential of using pea protein-phenolic acid conjugate to make PPI-based films with improved mechanical properties, water barrier properties, and antioxidant activity.

Effect of mixed protein supplementation on golf performance and muscle function: a randomized, double-blind, placebo-controlled study.

As a relatively novel approach to enhancing skeletal muscle health, mixed protein supplementation has shown similar responses to whey protein. However, no previous studies have examined its impact on golf swing performance. This study aimed to examine the effect of mixed protein supplementation on the swing performance and muscle strength of casual golfers. Sixty participants with a handicap of less than 20 were recruited and randomly assigned to a double-blind, placebo-controlled study design. The participants were divided into two groups: a mixed protein group (MG, n = 30), and a placebo control group (CG, n = 30). They were instructed to ingest either a supplement containing casein calcium, whey protein, and isolated pea protein, or a placebo, once daily for 8 weeks. Pre- and posttests consisted of anthropometric measurements, muscle strength (isokinetic knee and trunk strength, and handgrip strength), 2-minute push-ups, balance, and golf swing performance using a driver and 7-iron. After the 8-week supplementation period, ANCOVA, using baseline values as covariates, revealed significant differences for driver distance (p = .004) and driver ball speed (p < .001). MG significantly increased driver distance by 5.17 ± 12.8 m (p = .046), driver ball speed by 1.36 ± 2.87 m/s (p = .021). Additionally, significantly improvements were observed in hand grip strength (+2.12 ± 3.47 kg, p = .004), two-minute push-ups (+4.89 ± 8.14 reps, p = .004), and balance score (-0.37 ± 0.69 min, p = .009). No significant differences were observed in body composition parameters (p > .05). The intake of a mixed protein containing both animal and plant proteins had positive effects on golf performance and muscle function. Therefore, mixed proteins may represent a safe and effective approach to enhancing skeletal muscle health in golf players.

A Novel Nutraceutical Gummy for Hair Regrowth in Women: A Case Series

Introduction:Hair loss is a common concern among women, with female pattern hair loss (FPHL) and telogen effluvium (TE) being the most prevalent types. At least 50% of women experience hair loss by age 50 [1]. Many patients turn to nutritional supplements, with one hair loss clinic reporting that up to 81% of their patients use supplements [2]. While various nutraceuticals have demonstrated clinical efficacy in hair regrowth [2], none have been evaluated in gummy form. This case series aims to assess the efficacy of a novel nutraceutical gummy containing a proprietary blend of NAD, pumpkin seed extract, taurine, pea protein, ashwagandha, saw palmetto, and other anti-inflammatory ingredients in promoting hair regrowth in women with FPHL and TE. Procedure:Three women, aged 43, 52,64, with diagnoses of FPHL and TE, were included in this series. Each participant consumed two nutraceutical gummies daily for 2 or 3 months. One participant experiencing TE, also took oral minoxidil 1.25 mg daily. Baseline assessments included patient-reported outcomes related to hair shedding and photographic comparisons. Follow-up assessments were performed at 2 or 3 months. Results:All three women demonstrated noticeable improvements in hair density and a reduction in hair shedding by the 3-month mark. Participants also reported subjective improvements in hair quality, volume, and overall satisfaction with the product. No adverse effects were observed during the study period. Conclusion:This case series suggests that the novel nutraceutical gummy may be an effective, well-tolerated option for promoting hair regrowth in women with FPHL and TE. This nutraceutical can be efficacious as a sole treatment and in conjunction with traditional hair loss medical therapy. These findings highlight the potential for a gummy formulation to provide an accessible, evidence-based treatment for hair loss. Further studies with larger sample sizes are ongoing to validate these results.

Biochemical and proteomic approaches to investigating effects of IAA-aspartate in pea (Pisum sativum L.) seedlings during osmotic shock.

Osmotic shock is the first step of high salt or drought action that involves biochemical and molecular changes during plant response to these unfavorable conditions. Indole-3-acetyl-aspartate (IAA-aspartate, IAA-Asp) is the main amide conjugate of auxin in pea (Pisum sativum L.) tissues. Although the exact molecular mechanism of the IAA-Asp action is unknown, this conjugate's indole-3-acetic acid (IAA)-independent biological activity has been observed during physiological and stress conditions. In this work, we investigated the effect of IAA-Asp alone, as well as in combination with NaCl or polyethylene glycol (PEG) (osmotic shock) on reduced/oxidized glutathione (GSH/GSSG) ratio, activities of enzymes modulating glutathione concentration, protein S-glutathionylation, and IAA homeostasis. We did not observe the hydrolysis of IAA-Asp to IAA in pea seedlings, which, together with other results, suggests that IAA-Asp modulates plant response to abiotic stimuli independently of IAA. Moreover, despite the effect of IAA-Asp on the enzymes responsible for IAA conjugation, no changes in this phytohormone level were visible. Furthermore, 3h plant treatment with IAA-Asp increased the activity of glutathione reductase (GR), which correlates with an elevated GSH/GSSG ratio. On the contrary, more extended (48h) incubation with IAA-Asp diminished the GSH/GSSG ratio and increased the activity of glutathione peroxidase (GPX). IAA-Asp reduced GR activity during salt treatment but did not affect the GSH/GSSG ratio. Similarly, under plant incubation with PEG, IAA-Asp did not change the GSH/GSSG ratio but increased glutathione S-transferase (GST) activity. We also analyzed the effect of IAA-Asp on pea protein S-glutathionylation. Increased S-glutathionylation of heat shock 70 kDa protein (HSP70) was observed after plant treatment with IAA-Asp, PEG, or IAA-Asp combined with PEG. The proteomic analysis also revealed that IAA-Asp diminished S-glutathionylation of lipoxygenase during plant incubation with PEG. Thus, we suggest that IAA-Asp modulates redox status in pea during oxidative stress and under normal physiological conditions.

Effect of Microwave–Vacuum Drying and Pea Protein Fortification on Pasta Characteristics

The widespread popularity of pasta has driven innovations in formulations and production technologies to enhance its versatility. Techniques such as alternative drying methods and fortification of wheat pasta seek to improve the nutritional value and functional properties of pasta products, thereby increasing their attractiveness to consumers. This study aimed to evaluate the effects of microwave–vacuum drying versus conventional drying on the characteristics of durum wheat semolina pasta, including moisture content, water activity, microstructure, colour, texture, weight gain factor, and cooking loss. Three types of pea protein concentrates (80, 84, and 88% dry matter) were used at levels of 3, 6, and 9% (g/100 g flour). Results indicated that microwave–vacuum drying had a significant impact on the physical properties and cooking quality of pasta. Microwave–vacuum drying caused material puffing, resulting in microstructure with high open porosity (64.1%) and minimal closed porosity (0.1%). This has likely contributed to the short rehydration time (2 min in boiling water) of produced pasta, effectively transforming it into an instant food product. All pasta samples had low water content (&lt;9%) and water activity (&lt;0.4), which ensure food safety. The microwave–vacuum-dried pasta weight gain factor (2.2) was lower than in the conventionally dried pasta (2.8). The firmness of microwave–vacuum-dried pasta was significantly higher (135 g) than that of conventional pasta (16 g). Fortification with pea protein enhanced porosity but did not affect pasta’s culinary parameters, such as weight gain or cooking loss, although it resulted in darker pasta (p = 0.001), especially notable with a 9% pea protein addition.

Effect of pH shifting and temperature on the functional properties of a commercial pea protein isolate

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

Preparation, Characterization, Stability and In Vitro Release of a Pea Protein Fibril-Based Iron Fortificant via Self-Assembly

Preparation, Characterization, Stability and In Vitro Release of a Pea Protein Fibril-Based Iron Fortificant via Self-Assembly

Maillard reaction-based conjugation of pea protein and prebiotic (polydextrose): optimization, characterization, and functional properties enhancement

There is a growing demand for plant-based protein ingredients with improved functionality for use in diverse food and nutraceutical applications. In line with this, the current study aimed to investigate the effect of plant protein-prebiotic (polydextrose) conjugation on the techno-functional properties (emulsification, solubility, fat absorption and foaming) of pea proteins through wet heating Maillard reaction. Pea protein (PeP) was conjugated with polydextrose by incubating the mixture at various process conditions (pea protein: polydextrose mass ratios, temperature, and time). Response surface methodology coupled with Box–Behnken design was used to optimize multiple responses, including conjugation efficiency (CE), emulsifying activity (EAI), and foaming capacity (FC). The pea protein conjugate (optimized value) showed improved solubility throughout a wide pH (2–10) range and higher emulsification activity than pea protein alone. The development of conjugates (PeC) was validated through ultraviolet–visible spectroscopy, FTIR, and o-Phthaldialdehyde (OPA) assay. Browning index, FT-IR spectra, thermal properties, and scanning electron microscopy (SEM) micrographs were analyzed for the conjugate (PeC) obtained at optimized values. The FTIR spectra of the conjugates showed new peaks at 3100–3480 cm−1 and 1,000–1,166 cm−1 indicating conjugation. The Maillard conjugation increased the proportion of β-turn, random coil, accompanied by a decrease in α-helix, and β-sheet. These conformational changes were associated to the improved techno-functional properties of the pea protein upon conjugation, offering potential applications in the formulation of plant-based foods and beverages.

Beyond soybean meal: investigating the effects of dietary protein alternatives on gut health, liver function and microbiota in traditional slow-growing chicken breeds

The use of soybean meal in animal feed is crucial for nutrition but has a significant environmental impact, especially related to deforestation and biodiversity loss. With the increasing demand for sustainable agricultural practices, it becomes essential to explore alternatives to soybean meal. This study evaluated the effect of a soy-free diet, replaced with fava beans and pea protein, on an Italian slow-growing chicken breed: the Bianca di Saluzzo. The results indicate that the experimental diet did not compromise the growth, final weight or intestinal health of the animals, demonstrating a good tolerance and adaptability of the breed to these alternative ingredients. Furthermore, the analysis of the intestinal microbiota showed a positive impact, with an increase in organic acids such as succinic and citric, which could improve intestinal health and metabolic efficiency. Some changes in liver enzyme levels were observed, such as the increase in glutamate-oxaloacetate transaminase, an enzyme involved in amino acid metabolism. This increase could indicate a higher efficiency in protein metabolism, suggesting that the diet based on alternative ingredients could support an improvement in liver metabolism. Although this aspect deserves further investigation, it could represent a positive effect of the diet on liver function and overall health of the animals. Further studies are needed to fully understand the long-term implications of these dietary modifications, particularly in relation to the gut microbiota and metabolism.

Wavelength selection enables robust quantification of oil content with near-infrared spectroscopy in pea protein gels produced under varying heating conditions

Thermal processing influences the near-infrared (NIR) spectra of food products, causing inaccuracy when quantifying the composition of the product. In this study, the effect of thermal processing on NIR measurements of the oil content in pea protein isolate (PPI) gels was investigated. Analysis of variance showed that the heating temperature (30°C–120 °C) during the production of PPI gels influenced large parts of the NIR spectra and time (2.5–15 min) only had a limited effect. Stepwise multiple linear regression was used to select a combination of 5 wavelengths that was suitable to create a robust model for the prediction of oil content (Q2 = 0.9928 ± 0.002, root mean standard error of prediction = 0.2806 ± 0.0423 wt%). This combination of wavelengths was shown to reduce the effect of the history of thermal processing on the measurement, improving the accuracy of oil content quantification. This approach can be applied for in-line quantification of the oil content of food products subjected to varying heating conditions using specialized sensors.

A comprehensive review on composition to application of pea protein and its components

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

Assessing the impact of bacterial blends, crosslinking enzyme and storage times on volatile and non-volatile compound production in fermented pea protein emulsion gels

Pea protein is a promising ingredient for plant-based cheese production but has poor consumer acceptance due to intrinsic beany flavors. Fermentation could potentially decrease these off-flavors while also producing desirable cheese-like aromas. Pea protein emulsion gels were fermented using four different bacterial blends for 16 weeks with and without the crosslinking enzyme transglutaminase. The volatile organic compound (VOC) profiles were assessed by GC–MS and the peptide profile was measured by LC-MS/MS during storage. VOC production was mainly affected by the composition of the bacterial blends, followed by storage time. Crosslinking of the protein gel structure had minimal impact on VOC production. The peptide-level profiling revealed that crosslinking can reduce peptide size and the production of bitterness-like peptides in some blends. This study provides insights into the effect of bacterial blends, storage time, and enzymatic crosslinking on the production of volatile components and peptides related to aroma and peptide profiles for pea protein.

Ultrasound treatment on commercial pea protein isolates systems: Effect on structure, rheology and gelling properties

Pea protein has attracted great attention due to its capability to meet the growing requirements from consumers for desired nutrition and texture from plant protein. Hence, the current study aimed to investigate the effects of different ultrasonic treatment parameters (power and duration) on the gelling characteristics of commercial pea protein isolates (PPIc). The findings demonstrated that by manipulating the ultrasonic power and treatment duration, great enhancement of the solubility, adhesiveness and formation strength of PPIc gel can be realized. The reduction in particle size was positively correlated with higher power and longer treatment durations. Interestingly, no direct correlation between average particle size, solubility, turbidity, and ζ-potential was observed. Additionally, the ultrasound-modified PPIc in this study exhibited comparable characteristics to laboratory-prepared pea protein isolates, in terms of solubility, water-holding capacity, and gel strength. Overall, manipulating ultrasonic parameters presents a feasible method to customize the texture of pea-protein-based substitute.

Fabrication and characterization of novel electrospun nanofibers based on grass pea (Lathyrus sativus L.) protein isolate loaded with sumac (Rhus coriaria L.) extract

In this study, sumac extract was utilized as an active ingredient and combined with grass pea protein isolate and polyvinyl alcohol to produce novel active nanofiber mats using an electrospinning technique. First, nanofiber mats were fabricated by different ratios (100:0, 90:10, 70:30, 50:50, 30:70, 10:90, 0:100) of grass pea protein isolate and polyvinyl alcohol. The characterization of nanofiber mats revealed that the nanofibers with a polymer ratio of 50:50 had appropriate mechanical properties and presented a fibrous and uniform morphology. Therefore, the 50:50 polymer solution ratio was selected to produce active nanofibers by adding different amounts (0%, 2%, and 4% (w/v)) of sumac extract. The average diameters of nanofibers decreased from 150 ± 31 to 122 ± 25, and 105 ± 19 nm, by increasing the concentration of sumac extract. Based on the SEM results, the electrospun nanofibers exhibited a bead-free and smooth surface. The FTIR and XRD analyses indicated the presence of intermolecular hydrogen bonds between the components. The antioxidant activity of the nanofibers was confirmed by DPPH analysis and ranged between 3.33% and 68.75%. Additionally, the antimicrobial test results indicated that the nanofibers with the highest sumac concentration (4%) displayed inhibitory activity against Staphylococcus aureus, resulting in an inhibition zone of 10 mm. The optimal treatment of this study was grass pea protein isolate: polyvinyl alcohol ratio of 50:50 containing 4% sumac extract which can be used as a natural antimicrobial and antioxidant agent.

Towards hybrid protein foods: Heat- and acid-induced hybrid gels formed from micellar casein and pea protein

Towards hybrid protein foods: Heat- and acid-induced hybrid gels formed from micellar casein and pea protein

A multiscale investigation on protein addition toward steering agglomeration and yield in spray drying

The positive effect of protein drying aids that reduce the stickiness of sugar-rich products on the spray drying yield is known. However, as agglomeration also depends on stickiness, one can expect an effect of these drying aids on interparticle collisions. Therefore, the effect of protein addition to maltodextrin systems on agglomeration and yield in spray drying was investigated using single droplet drying and pilot-scale spray drying experiments. Single droplet drying was used to compare the sticking regimes of whey and pea proteins at different concentrations. Adding protein increased the chance of creating agglomerates upon forced collisions between a drying droplet and a glass bead. This was reflected in an increased fraction of agglomerated particles in pilot-scale experiments with injection of fines. Pea protein decreased the fraction of non-agglomerated primary particles from 38% to 22% when the protein content in the liquid feed was 50 g/kg dry basis. In pilot-scale spray drying, protein addition improved the yield. Industrially, these results can be used to steer formulations regarding agglomeration and yield.

Enhanced characterization and utilization of cowpea protein isolate: rheological and textural properties of heat-induced gels for plant-based egg omelet formulation

This study aimed to evaluate the potential of cowpea isolate (CPI) as an effective plant-based egg substitute by comparing its composition and physicochemical properties with those of commercial isolates, including mung bean, soy, and pea proteins. Sodium dodecyl sulfate–polyacrylamide gel electrophoresis identified a distinctive vicilin-like globulin in CPI that is critical for the unique functional properties of CPI. CPI has a smaller particle size, resulting in superior gelation capacity and water retention, which are essential for egg substitute applications. Thermal analysis revealed the high stability of CPI, which is advantageous for food processing. Notably, the unique heat-induced gelation behavior of CPI, characterized by a smooth transition from solid- to liquid-like states, provided a strength not observed in its commercial counterparts. Microstructural analysis showed that the CPI gel closely resembled the egg gel, underscoring the potential of CPI to mimic the texture of eggs, particularly in omelets.

Pea and rice proteins with gellan gum and monovalent salts for the development of plant-based gels for food applications

Pea and rice proteins with gellan gum and monovalent salts for the development of plant-based gels for food applications

Relationship between rheological parameters and structure formation in high moisture extrusion of plant protein biopolymers

High moisture extrusion (HME) is widely employed to texturize plant-derived protein ingredients, but its development is still much based on trial and error. In this project, it was hypothesized that the rheological properties of plant-based mixtures analyzed when in the molten state and during their cooling can aid in understanding their structure formation. To test this hypothesis, biopolymer formulations containing pea protein isolate (PPI) were examined at different moisture and starch contents, and their rheological properties were analyzed using a closed cavity rheometer (CCR) at temperatures relevant to those applied during HME processing. The results obtained with the CCR were then contrasted with the mechanical properties of HME obtained using a lab scale extruder, measured using oscillatory rheology, large deformation, and dynamic mechanical analysis. Low moisture (55 %) HMEs were stiff and brittle, while high moisture (65 %) HMEs formed more flexible and anisotropic structures. Addition of starch created softer structures. The viscoelastic properties of the biopolymer mixes measured with the CCR were correlated with the mechanical parameters of the final extrudates. Strong correlations were found between small deformation rheological parameters measured in the CCR and the hardness values, while non-linear viscoelastic parameters were correlated with anisotropy indexes. Results demonstrated that the material properties measured at the early cooling stages strongly influence the structural heterogeneity in HMEs. This study highlights the potential to use the viscoelastic properties of the biopolymer mix measured with the CCR to predict their structural features when processed by extrusion.

Biodegradable genipin cross-linked chitosan/pea protein isolate sponges for effective adsorption of methyl blue: Batch experiments and quantum chemical analysis

This study successfully prepared double crosslinked chitosan (CS) and pea protein isolate (PPI) composite sponges using genipin as a crosslinking agent and investigated their effectiveness as an adsorbent for methyl blue (MEB) in aqueous solutions. The composite sponges were characterized using scanning electron microscopy, Fourier transform infrared spectroscopy, Brunauer-Emmett-Teller measurement, swelling tests, gel fraction measurement, zeta potential, and X-ray diffraction. Additionally, the effects of genipin content, pea protein isolate content, sponge dosage, initial pH of the solution, adsorption time, dye concentration, and adsorption temperature on dye removal ability were studied. The results showed that at pH 3.0 and a dye concentration of 100 mg/L, the adsorption capacity of the sponge for methyl blue was found to be 351.6 mg/g. At 298 K and after 720 min, with a dye concentration of 700 mg/L, the maximum adsorption capacity of the sponge for methyl blue reached 959.3 mg/g. The adsorption process follows a pseudo-second-order kinetic model and a Langmuir isotherm. Theoretical analysis using density functional theory suggests that the adsorption of methyl blue by the composite sponge is attributed to the anionic sulfonic acid group of the dye. The composite sponge degraded 76.1 % after being buried in soil for 21 days. This study reveals the enormous potential of biodegradable chitosan-protein-based sponges in effectively removing methyl blue dye pollutants from wastewater.