Bean Protein Isolate Research Articles

Fabrication of mung bean protein isolate nanofibrils and calcium ions induced hydrogels

Protein nanofibrils have excellent functional properties due to their unique fibrous structure and high aspect ratio. This article focused on the formation processes, microscopic morphology and aggregation mechanisms of mung bean isolate protein nanofibrils (MPNFs), as well as the formation of MPNFs hydrogels induced by Ca2+. Mung bean isolate protein (MPI) could self-assemble into long and curly MPNFs via a partially unfolded conformation-aggregation model when heating at pH 2.0 and 90 °C for 11 h. Hydrophobic forces, electrostatic forces and disulfide bonds drove the hydrolysis and structural rearrangement occurring simultaneously resulting in MPNFs. MPNFs could formed self-supporting hydrogels. As expected, Ca2+ could affect the network structure of the hydrogel by decreasing the electrostatic repulsion and the salt bridges between protein molecules, which can affect its water-holding capacity, texture and rheological properties. The MPNFs hydrogels formed with MPNFs of 0.050 g/mL and Ca2+ of 100 mmol/L at 90 °C for 60 min had a denser and more homogeneous gel network, with a highly cross-linked and uniform pore distribution. It is believed that this present work can give some insight into MPNFs and provide more potential applications of MPI as gelling agents in the food industry.

Effect of transglutaminase cross-linking on the structure and emulsification performance of heated black bean protein isolate.

Transglutaminase (TGase) is a heat-resistant biocatalyst with strong catalytic activity, which functions effectively under moderate temperature and pH conditions, and is used widely in protein cross-linking and recombination. Transglutaminase cross-linking is a novel and specific modification method for black bean protein isolate (BBPI). This article investigates the effect of transglutaminase cross-linking on the structure and emulsification performance of heated BBPI. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis showed that heated BBPI with TGase had a higher molecular weight than heated BBPI without TGase, and the protein bands widened with increasing enzyme activity, indicating that TGase cross-linking promoted protein molecule aggregation. A high molecular weight polymer can better stabilize the oil-water interface, preventing the emulsion from layering. Fourier transform infrared (FTIR) spectroscopy showed that the α-helix content decreased from 15.64% to 13.75%, and the β-sheet content increased from 48.13% to 54.08%. The decrease in α-helix content and increase in β-sheet content could make the structure more stable and improve the emulsifying properties of heated BBPI. When TGase was 20 U g-1, the protein emulsification activity index (EAI) reached its highest value of 1.87 m2 g-1, and the emulsification stability index (ESI) value was 0.27 min (P < 0.05); these figures were 0.19 m2 g-1, and 0.07 min higher, respectively, than in the sample without added TGase. In summary, transglutaminase cross-linking has a positive effect on the structure and emulsification performance of heated BBPI and can be used as an effective method for BBPI modification. © 2024 Society of Chemical Industry.

Effects of mono- and dual-frequency ultrasounds on structure and physicochemical properties of faba bean proteins

Faba bean proteins are currently viewed as promising animal protein alternatives. However, certain functional properties e.g. relatively low solubility compared to whey protein isolates, can limit the application of faba bean protein isolates (FPIs) in certain food products. Therefore, it may be desirable to use modification approaches such as the application of ultrasound to alter such limiting physicochemical properties. In this study, Faba Bean Protein Isolates (FPIs) were treated by ultrasound with different frequencies (20 kHz, 40 kHz and 20 + 40 kHz) prior to hydration (1 %) at different pH levels (3, 7, and 9). Then the structure and physicochemical properties (i.e. particle size, ζ-potential, surface hydrophobicity, thermal behavior, and solubility) of control and untreated FPIs were investigated. Ultrasound treatment had no obvious effect on the molecular weight of FPIs, whereas it changed the secondary structure of FPIs from a more ordered structure to a more disordered structure. The applied treatment resulted in an increase in surface hydrophobicity across all treatment levels and pHs. It also decreased the particle size of FPI at pH 3, while it increased the particle size at pH 7 and 9, compared to the untreated FPI. In addition, the solubility and thermal properties of FPI were modified through the ultrasound treatment. The higher solubility of FPI could improve its potential to be used as a functional ingredient for many food applications. Ultrasound treatment at 20 kHz and 20 + 40 kHz had more effects on the physiochemical properties of FPI compared to that at 40 kHz. Overall, ultrasound treatment with different frequencies (20 kHz, 40 kHz, and 20 + 40 kHz) modified the structure and physiochemical properties of FPI to different degrees and may be beneficial for the development of FPI for certain food applications.

Investigating the role of starch in the structuring of meat alternatives from mung bean and pea protein isolates via heat-induced gelation

IntroductionThe structuring of plant-based meat alternatives is a complex process which is highly dependent on qualitative and quantitative proportion of different ingredients. In the present study, starch, protein, and oil concentrations were optimized for the formulation of meat alternative (MA) using response surface methodology (RSM).MethodsProtein isolates of mung bean and pea protein, &amp;amp; corn starch were used along with sunflower oil to formulate meat alternatives using heat-induced gelation. The protein functionality of mungbean protein isolate (MBPI) and pea protein isolate (PPI) were analyzed. In addition, the effects of constituent composition on the physicochemical properties of meat alternatives were studied using RSM.ResultsThe protein content exhibited an elevation with increased levels of MBPI and PPI in 15:15 ratio. Moisture and hardness were chiefly influenced by oil content, as they displayed a decline with increasing oil levels. The color (L*) was principally affected by starch and oil, where the L* reduced with increasing levels of both variables. Springiness was influenced by the interaction of protein ratio (MBPI:PPI) and starch, as it showed a lowest value at the lowest level of protein and the highest level of starch. Chewiness was influenced by the interaction of hardness and springiness. The microstructure analysis showed dense protein matrix in the meat alternative.DiscussionOverall, the study shows that starch facilitated the structuring of meat alternative formulated using MBPI and PPI which could be utilized as potential materials for enhanced textural properties of the meat alternatives.

Synergistic effects of alkaline and heat treatments on structural and functional properties of mung bean protein isolate: improving physicochemical stability of plant‐based emulsions

SummaryPlant‐based meat alternatives often require fat replacers to mimic the texture of traditional products. This study aimed to develop plant‐based emulsion gels using mung bean protein isolate (MBPI) as a potential fat substitute. However, creating these gels via heat setting requires a high protein concentration, which demands modification of the MBPI structure to enhance emulsifying properties. This study investigated synergistic effects of alkaline treatment (0.3 or 3.5% Na2CO3) and heat treatments (40 or 70 °C) on the functional properties of MBPI at high protein levels, for potential application as a plant‐based emulsion. The combined treatments reduced the zeta potential of protein suspensions from −9 to −19 mV and altered the protein conformation to form smaller particles (from 426 to 166 μm) with increased β‐sheet content. These treatments improved dispersibility of 8% MBPI suspension (58 to 86%), emulsifying activity index (6.34–10.89 m2 g−1), and stability coefficient (43 to 96%). Notably, MBPI samples treated with 0.3% Na2CO3 at 40 and 70 °C exhibited excellent emulsifying properties, forming stable monolayers at the oil–water interface, likely due to the increased surface activity of MBPI. Increasing protein concentration to 11% facilitated heat‐set gel formation; however, addition of 3.5%‐Na2CO3 induced premature gelation, limiting its application in emulsions. At 0.3%‐Na2CO3, increasing the protein content from 8% to 11% and the oil content from 10% to 30% further reduced emulsion droplet size, especially for MBPI treated with 0.3% Na2CO3 at 70 °C (MB‐0.3%‐70 °C) from 5.10 to 2.61 μm, likely due to decreased coalescence. This treatment yielded superior MBPI‐stabilised emulsion gels with enhanced penetration, fluid retention, and stability by possibly reducing protein aggregation. These findings demonstrate the potential of MBPI modified by combined addition of 0.3% Na2CO3 and heat treatment, particularly MB‐0.3%‐70 °C, as a promising ingredient for producing plant‐based emulsions.

Binding mechanism and structural characteristics of alloyed protein complex for enhanced solubility of hemp seed protein isolate

Despite the numerous health benefits and high digestibility of hemp seed protein isolate (HPI), its low solubility at neutral pH limits its utilization in the food industry. Therefore, we subjected insoluble HPI and soluble mung bean protein isolate (MBPI) to pH co-shifting under extremely alkaline conditions to form an alloyed protein complex (A-HM). At a mass ratio of HPI:MBPI of 50:50, A-HM exhibited the highest solubility (95.30 ± 0.99 %), and also had high resistance to heat treatment. Native PAGE demonstrated the formation of alloyed protein complexes, and particle size analysis revealed that A-HM exhibited small particle sizes and dispersion in water without aggregation of HPI. Owing to their small size, numerous hydrophobic residues and aromatic ring of HPI were exposed on the surface. Hydrophobic interactions predominantly governed the binding force involved in the formation of A-HM. Our findings may enhance HPI applications in the food industry, particularly in plant-based beverages.

Low-moisture extruded mung bean protein isolate and wheat gluten: Structure, techno-functional characteristics and establishment of rehydration kinetics of the products

Low-moisture extruded products provide excellent shelf-life and stability, making the exploration of new formulations with various proteins highly valuable. This study prepared and compared products with different ratios of mung bean protein isolate (MPI) to wheat gluten (WG) (10:0, 9:1, 8:2, 7:3, 6:4, and 5:5). Results showed significant improvements (P < 0.05) in L∗-value and product quality with increasing WG ratios, peaking at an MPI/WG ratio of 7:3. Increased WG also enhanced protein cross-linking aggregation, as evidenced by changes in particle size, secondary structure, and fluorescence spectra. However, excessive WG (MPI/WG = 6:4) adversely affected product structure and techno-functional characteristics. Rehydration kinetics were best described by the Peleg model, with rehydrated products showing decreased hardness (291.25 N) and chewiness (227.45 N), but increased tensile resistance (P < 0.05). Eleven quadratic polynomial equations were developed to predict color and techno-functional characteristics based on WG percentage (0–50%). The findings provide a theoretical basis for expanding the application of MPI in new low-moisture extruded products.

Comparing gluten‐free eggless muffins' viscoelastic, rheological, and textural properties after combining seven plant‐based protein isolates with wheat, corn, and rice starches

SummaryThis study aimed to substitute egg albumin with eight plant‐based protein isolates and xanthan gum for the development of gluten‐free, eggless muffins. The presence of protein isolates led to reduced pasting viscosities, suggesting limited swelling capacity of the starch granules. Incorporating different protein isolates enhanced the batter's viscoelastic properties, marked by an increase in storage and loss modulus and a decrease in tan δ, indicating enhanced gel properties compared to starch‐only batters, which showed more liquid‐like characteristics. Consequently, the muffins exhibited greater specific volume, springiness, and cohesiveness. The consistency of the muffins varied depending on the protein isolates used. The inclusion of protein isolates also altered the crust's hue, shifting it towards a reddish‐brown shade, while the crumb colour varied with protein incorporated. Sensory evaluation demonstrated that overall acceptability of the muffins improved with the protein isolates, particularly for those incorporating mung bean protein isolate. Principal Component Analysis further highlighted the strong associations between specific quality attributes, underscoring the significant impact of protein isolates on the quality characteristics of gluten‐free muffins.

High moisture extrusion of pulse proteins: Texture, structure, and in vitro digestion characteristics of extrudates

Pulse proteins are promising components for plant-based food development, yet their diverse subunit compositions, influenced by source origin, result in variable extrusion properties. This study utilized high moisture extrusion (60% moisture content) to prepare extrudates from four pulse proteins: soy, pea, chickpea and mung bean protein isolates (SPI, PPI, CPI, and MPI, respectively). The texture, structure, and in vitro digestion characteristics of extrudates were examined. The results showed that SPI and PPI were mainly composed of 7S and 11S globulins, while CPI and MPI were mainly composed of 7S globulins, and 11S globulins, respectively. SPI extrudates exhibited significantly lower hardness, chewiness, and transverse and longitudinal fracture stresses, while CPI extrudates exhibited a higher anisotropy index. SPI extrudates with a higher β-sheet content (39.08%) exhibited denser structures. The gastrointestinal digestibility (86.65%) of CPI extrudates was higher than other groups. Correlation analysis showed that 7S/11S ratio was positively correlated with the melt viscosity, while negatively correlated with the anisotropy index and in vitro digestibility. This study highlights the distinct extrusion properties of pulse proteins based on their unique subunit composition. The results provide insights for selecting appropriate protein sources and developing plant-based protein products with tailored textural attributes and desirable digestibility.

Optimization of ultrasound-assisted extraction of faba bean protein isolate: Structural, functional, and thermal properties. Part 2/2

Environmental concerns linked to animal-based protein production have intensified interest in sustainable alternatives, with a focus on underutilized plant proteins. Faba beans, primarily used for animal feed, offer a high-quality protein source with promising bioactive compounds for food applications. This study explores the efficacy of ultrasound-assisted extraction under optimal conditions (123 W power, 1:15 g/mL solute/solvent ratio, 41 min sonication, 623 mL total volume) to isolate faba bean protein (U-FBPI). The ultrasound-assisted method achieved a protein extraction yield of 19.75 % and a protein content of 92.87 %, outperforming the control method’s yield of 16.41 % and protein content of 89.88 %. Electrophoretic analysis confirmed no significant changes in the primary structure of U-FBPI compared to the control. However, Fourier-transform infrared spectroscopy revealed modifications in the secondary structure due to ultrasound treatment. The U-FBPI demonstrated superior water and oil holding capacities compared to the control protein isolate, although its foaming capacity was reduced by ultrasound. Thermal analysis indicated minimal impact on the protein’s thermal properties under the applied ultrasound conditions. This research highlights the potential of ultrasound-assisted extraction for improving the functional properties of faba bean protein isolates, presenting a viable approach for advancing plant-based food production and contributing to sustainable protein consumption.

Ultrasonication assisted enzymatic hydrolysis for generation of pulses protein hydrolysate having antioxidant and ACE-inhibitory activity

The main objective of this work was to investigate the impact of ultrasonication assisted enzymatic treatment on the physicochemical and bioactive properties of broad bean (BBP), lentil bean (LBP), and mung bean (MBP) protein isolates. The protein was extracted using alkaline acid precipitation method, ultrasonicated at a frequency of 20 kHz, temperature 20–30 °C and then hydrolysed using alcalase enzyme (1 % w/w, pH 8.5, 30 min, 55 οC). The generated hydrolysates were characterized by degree of hydrolysis (DH), SDS, FTIR, surface hydrophobicity, amino acid composition, antioxidant and antihypertensive properties. Results showed that the degree of hydrolysis was found to increase in ultrasonicated protein hydrolysate (18.9 to 40.71 %) in comparison to non- ultrasonicated protein hydrolysate (11 to 16.3 %). SDS-PAGE results showed significant changes in protein molecular weight profiles (100–11kDa) in comparison to their natives. However, no substantial change was found in ultrasonicated and non-ultrasonicated protein hydrolysates. The FTIR spectrum showed structural alterations in ultrasonicated and non-ultrasonicated protein hydrolysates, suggesting modifications in secondary structure such as amide A, amide I and amide II regions. The essential amino acid content varied in the range of 60.09 mg/g to 73.77 mg/g and 28.73 to 50.26 mg/g in case of ultrasonicated and non-ultrasonicated protein hydrolysates, and non-essential content varied in the range of 49.42 to 65.93 mg/g and 43.12 to 47.12 mg/g. Both antioxidant and antihypertensive activities were found to increase significantly in ultrasonicated and non-ultrasonicated protein hydrolysates in comparison to their native counterparts, highlighting their potential as functional ingredients for management of hypertension. It was concluded that ultrasonication assisted enzymatic hydrolysis is an efficient approach for production of bioactive pulse protein hydrolysates with enhanced nutracutical properties, thus offering promising avenues for their utilization in the food industry and beyond.

Protein blend extrusion: Crafting meat analogues with varied textural structures and characteristics

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.

Technical-functional and surface properties of white common bean proteins (Phaseolus vulgaris L.): Effect of pH, protein concentration, and guar gum presence

Legumes are abundant sources of proteins, and white common bean proteins play an important role in air–water interface properties. This study aims to investigate the technical-functional properties of white common bean protein isolate (BPI) as a function of pH, protein concentration, and guar gum (GG) presence. BPI physicochemical properties were analyzed in terms of solubility, zeta potential, and mean particle diameter at pH ranging from 2 to 9, in addition to water-holding capacity (WHC), oil-holding capacity (OHC), and thermogravimetric analysis. Protein dispersions were evaluated in terms of dynamic, interfacial, and foam-forming properties. BPI showed higher solubility (>80 %) at pH 2 and above 7. Zeta potential and mean diameter ranged from 15.43 to −34.08 mV and from 129.55 to 139.90 nm, respectively. BPI exhibited WHC and OHC of 1.37 and 4.97 g/g, respectively. Thermograms indicated decomposition temperature (295.81 °C) and mass loss (64.73 %). Flow curves indicated pseudoplastic behavior, with higher η100 values observed in treatments containing guar gum. The behavior was predominantly viscous (tg δ > 1) at lower frequencies, at all pH levels, shifting to predominantly elastic at higher frequencies. Equilibrium surface tension (γeq) ranged from 43.87 to 41.95 mN.m−1 and did not decrease with increasing protein concentration under all pH conditions. All treatments exhibited ϕ < 15°, indicating predominantly elastic surface films. Foaming properties were influenced by higher protein concentration and guar gum addition, and the potential formation of protein-polysaccharide complexes favored the kinetic stability of the system.

Insight into gelation quality of low‐grade surimi as affected by fava bean protein isolate

SummaryThe effect of fava bean protein isolate (FPI) at varied concentrations (1%–4%, w/w) on gelation of sardine surimi was evaluated. Breaking force, gel strength, textural profile, and water holding capacity were improved with the addition of FPI (P &lt; 0.05). However, deformation and whiteness of gel samples decreased slightly when higher levels (3%–4%) of FPI were used (P &lt; 0.05). The improved gel properties were supported by enhanced rheological properties (G′ and G″) of gels containing FPI. Microstructure also revealed the formation of gel network with higher connectivity in samples containing 3%–4% FPI. No major changes in the myofibrillar proteins in surimi gel were observed as determined by FTIR spectra and protein patterns. Higher scores for texture and overall likeness were obtained for surimi gel containing 3%–4% FPI. Therefore, FPI is a promising plant‐based ingredient that can effectively improve the gel properties of low‐grade sardine surimi without causing beany flavour.

Whipped cream stabilized by faba bean protein isolate microgel particles substituted for sodium caseinate: Whipping performance and foam stabilization analysis

In this study, faba bean protein isolate microgel particles (FPIMPs) were used as substitutes for sodium caseinate in whipped cream ingredients, the effect of FPIMPs on properties of emulsion system before whipping and foam system after whipping was investigated, and the stabilization mechanisms of whipped cream systems stabilized by FPIMPs and sodium caseinate, respectively, were analyzed and compared. Elevated levels of FPIMPs facilitated the cross-linking and flocculation of oil droplets in the emulsions, which further promoted the formation of gel-like networks, leading to a larger average particle size and higher viscoelasticity. Meanwhile, the firmness, shaping ability, and shape retention ability of whipped creams were gradually enhanced with the increase of FPIMPs content. The quality of whipped creams with FPIMPs concentrations of 0.8% and above was comparable to that of commercial whipped cream. Tribological results showed that the coefficient of friction of whipped creams was roughly negatively correlated with the concentration of FPIMPs, and the lubricating properties of whipped creams with high FPIMPs concentrations (>0.8%) were better than those of commercial whipped cream. The oil-water interface film with high mechanical strength formed by FPIMPs made the FPIMPs-stabilized whipped creams more resistant to whipping than sodium caseinate-stabilized whipped cream, delaying the occurrence of excessive whipping phenomenon. This work has important implications for expanding the application of faba bean protein isolate in food systems, as well as provides new strategies for the development of healthier plant-based whipped creams.

The effect of heat treatment and high‐pressure homogenization on the dispersibility and interfacial behavior of faba bean protein isolate and concentrate

AbstractThe effect of hydrothermal treatments, high‐pressure homogenization (HPH) and their combined effects on faba bean protein isolate (FBI) and concentrate (FBC) dispersions was investigated. With HPH, a significant reduction in particle size was observed for FBI but not for FBC. For FBI, dispersion stability under accelerated gravitation was significantly improved by both hydrothermal and HPH. For FBC, hydrothermal treatment had a negative effect on dispersion stability unless it was combined with HPH. The protein dispersibility of FBI increased, and FBC decreased with increasing temperature. Upon HPH, the protein dispersibility of FBI dramatically improved, making it almost completely soluble. All FBI dispersions had a higher surface charge compared to FBC. SDS PAGE profile showed strong protein crosslinking in the original FBI, leading to a loss of legumin and vicilin bands, which were visible in a more native state of FBC. Physical modifications did not significantly affect the viscosities except for a significant increase in FBC heated at 75°C due to starch gelatinization. The equilibrium interfacial tension of the modified FBI was significantly lower than the FBC. Analysis of dynamic interfacial adsorption showed that FBI had a much faster initial diffusion (beyond detection limit) towards the interface than FBC. Physical modifications improved the surface hydrophobicity of the proteins, leading to faster interfacial adsorption. Overall, FBI dispersions had improved functional properties compared to FBC, and HPH had a more significant effect than hydrothermal treatments. Physically modified FBI could be a promising emulsifier in various food applications.

Mild extraction of faba bean (Vicia faba L.) proteins against conventional methods: Impact on physicochemical and thermal characteristics

Faba bean (high- and low-tannin) protein isolates were water extracted followed by dialysis or micellization in comparison to concentrates from conventional alkali extraction + acid precipitation, and salt-based extraction (1% NaCl) + dialysis. Protein fractions were characterised for secondary structure conformational changes, crystalline structure, particle size distribution in aqueous suspension and thermal properties. Mild water or salt extraction did not influence particle size distribution. Based on XRD, FTIR and CD, β-sheet structures were the most abundant secondary structures and water extraction + dialysis had minimal impact on their native conformation. DSC results showed an association between protein purity, glass transition temperature and endothermic enthalpy. High melting temperature above glass transition confirms the suitability of faba bean proteins for thermal/extrusion processing. Fractionation method was a more significant determinant of physicochemical characteristics compared to the cultivar. Further exploration of the techno-functional characteristics of faba bean proteins is essential for value-added food applications.

Effect of solid-state fermentation on the functionality, digestibility, and volatile profiles of pulse protein isolates

Fermentation, as a clean processing technique, induces structural and compositional modifications to plant proteins, improving their functionality and nutrition. However, the effect varies depending on the level of hydrolysis, the fermenting strain, and the specific substrate used. The present work examined the effect of solid-state fermentation (SSF) by Lactobacillus plantarum, Aspergillus niger and Aspergillus oryzae of several niche market pulse (chickpea, green lentil, and faba bean) protein isolates on their functional and nutritional properties. The pulse proteins were moderately hydrolyzed to different extents (degree of hydrolysis of 9%–15%) after 48 h of fermentation, enhancing surface charge and solubility while decreasing water holding capacity and emulsion stability. Protein digestibility was reduced for all pulses which was hypothesized to be due to an increase in phenolic content caused by fermentation. Among the strains, only A. niger outgrew the natural microbiota for all pulses. Variations relating to the property changes were observed among the inocula and pulses; however, no general trend could be concluded. Fermentation produced a large variety of favourable new volatile compounds in the protein isolates.

Techno-functional properties and allergenicity of mung bean (Vigna radiata) protein isolates from Imara and KPS2 varieties

Mung bean is an increasingly cultivated legume. This study compared mung bean varieties ‘KPS2’ from Thailand (Th) and ‘Imara’ from Tanzania (T) with a focus on protein composition, allergenicity, and techno-functional properties. Two rounds alkaline-acid extraction were performed to produce mung bean protein isolate (MBPI - Th1/T1 and Th2/T2), supernatant (S) and protein-poor residue (PPR). Mass spectrometric analysis revealed high abundance of 8 s-vicilin and 11 s-legumin in MBPI and S. Extraction removed considerable amounts of the seed albumin allergen but increased the relative abundance of cupins in MBPI. Higher vicilin levels were found in Th1 samples, contributed to increased protein solubility above pH 6.5. Th formed stronger gels which were more stable at higher frequencies. In contrast, T proteins were structurally more flexible, leading to its improved foaming ability. This study provides the knowledge and methods for appropriate selection of mung bean varieties for various food applications.

Effect of Dry and Wet Fractionation on Nutritional and Physicochemical Properties of Faba Bean and Yellow Pea Protein

ABSTRACTPlant‐based proteins continue to gain popularity as a sustainable alternative to animal proteins due to their nutritional, functional and health benefits. Dry and wet fractionation methods are increasingly being used for the production of value‐added pulse protein ingredients. The objective of this study was to compare the nutritional properties, protein quality, physicochemical properties and secondary structure of Australian faba bean and yellow pea protein concentrates and protein isolates obtained by dry and wet fractionation. Amino acid scores highlighted that faba bean and yellow pea protein isolates and concentrates were deficient in the sulphur‐containing amino acids, methionine and cysteine and tryptophan. Faba bean (63.7%) and yellow pea protein (63.0%) isolates had higher in vitro protein digestibility‐corrected amino acid scores compared to the protein concentrates, being 50.7% and 54.4%, respectively. Fourier‐transform infrared spectroscopy revealed different secondary structures between protein concentrates and isolates, especially for the amide I region. Faba bean and yellow pea protein concentrates had higher protein solubility (46.2% and 50.1%, respectively) and higher foaming capacity (65% and 59%, respectively) compared to the protein isolates. Water‐holding capacity was higher for faba bean and yellow pea protein isolates, being 4.3% and 4.0 g/g, respectively. These findings demonstrate that faba bean and yellow pea protein concentrates and isolates have unique functional properties that can be exploited for use in a diverse range of new and existing food applications.