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Background: Osteoarthritis (OA) can cause disability and reduce quality of life (QoL). Objectives: This study aimed to determine whether GreenShell mussel (GSM) powder (PERNAULTRA) consumption was more effective than placebo at improving physical performance and subjective measures of symptoms and function in adults with early signs of knee OA. Methods: The Researching Osteoarthritis and GSM study was a 6-mo randomized, double-blind, placebo-controlled trial in adults aged 55-80 y, screened for signs of OA (n = 120, 65.9 ± 6.43 y, 63% female). Participants consumed either 3 g of powdered whole GSM or placebo (pea protein) daily. Baseline and end data collection included 30-s chair stand, stair test, 40-m fast-paced walk test, Knee Injury and Osteoarthritis Outcome Score (KOOS) questionnaire categorized into 5 subscales [pain (P), symptoms except pain (S), function in activities of daily living (ADL), function in sports/recreation (SP), and QoL], a measure of Intermittent and Constant Osteoarthritis Pain, and visual analog scale of pain and symptoms. Results: Visual analog scale symptoms showed a significantly greater reduction in percentage change for GSM than that for placebo [-28.1 (-59.2, 43.2) compared with 0.00 (-28.6, 100); P = 0.03]. Further, a trend for improvement in percentage change for GSM compared with placebo was seen in 40m fast-paced walk [2.51 (-3.55, 8.12) compared with 0.20 (-6.58, 4.92); P = 0.09], KOOS-SP [11.4 (-4.48, 27.0) compared with 0.00 (-11.1, 17.7); P = 0.09], and Intermittent and Constant Osteoarthritis Pain intermittent pain scale [-27.7 (-77.3, 0.00) compared with -14.6 (-50.0, 36.4); P = 0.08]. In those with body mass index (BMI; in kg/m²) <25, GSM consumption significantly improved KOOS-S compared with placebo [6.35 (3.49, 12.7) compared with 0.00 (-4.65, 4.49); P = 0.03] and showed a trend for improvement in KOOS-ADL [3.29 (1.01, 8.79) compared with 1.01 (-5.75, 4.30); P = 0.07]. Those with BMI of >25, consuming GSM showed a trend for improvement in KOOS-SP [13.6 (-4.76, 33.3) compared with 0.00 (-12.5, 20.0); P = 0.07]. Conclusions: This research suggests consumption of GSM has potential to alleviate symptoms and improve functionality in OA. [ABSTRACT FROM AUTHOR]

Three modifications (pH shift, ultrasound, combined pH shift and ultrasound) induced alterations in pure whey protein isolate (WPI), pea protein isolate (PPI), and mixed whey and pea protein (WPI-PPI) were investigated. The processing effect was related to the protein type and technique used. Solubility of WPI remained unchanged by various treatments. Particle size was enlarged by pH shift while reduced by ultrasound and combined approach. All methods exposed more surface hydrophobic groups on WPI, while pH shift and joint processing was detrimental to its emulsifying activity. The PPI and mixture exhibited similar responses toward the modifications. Solubility of PPI and the blend enhanced in the sequence of pH shift and ultrasound > ultrasound > pH shift. Individual approach expanded while co-handling diminished the particle diameter. Treatments also caused more disclosure of hydrophobic regions in PPI and WPI-PPI and emulsifying activity was ameliorated in the order of pH shift and ultrasound > ultrasound > pH shift. [Display omitted] [ABSTRACT FROM AUTHOR]

This study investigates the effects of treating pea protein concentrate (PPC) with hydro-alcoholic solutions on off-flavour removal. Increasing ethanol concentration in the hy-droalcoholic solutions from 15 to 75% (v/v) enhanced the removal of volatile compounds contributing to off-flavours such as 1-hexanol, 1-octanol, 3-hexen-l-ol, 1-nonanol and trans-2-hexenal. Differential scanning calorimetry and protein solubility studies showed that higher ethanol concentration induced more protein denaturation as evidenced by the lower enthalpy change and protein solubility of the treated PPC samples. Insoluble protein aggregates formed were hypothesized to be linked by hydrogen bonding. Hydroalcoholic washing of PPC also increased its water holding capacity but reduced oil holding capacity. Ethanol concentrations deployed in the hydroalcoholic solutions influenced gelling behaviour, where increase in PPC gel strength was observed in PPC treated with lower concentrations of ethanol, i.e., 15 and 25% (v/v). However, higher ethanol concentrations, i.e., 50 and 75% (v/v) induced higher extent of insoluble aggregates which weakened the gel network and reduced gel strength. In conclusion, PPC treated with high ethanol concentrations reduced majority of volatile compounds contributing to off-flavour, but significant protein structural changes which could influence product development performance were also observed. [ABSTRACT FROM AUTHOR]

Improving the functionality of commercial plant proteins is essential for food application. Here an alternative strategy is provided to modify the structure of pea protein by microbial transglutaminase-induced cross-linking with whey protein for enhancing emulsifying and encapsulation properties. The protein structures and the physicochemical stability of 0-carotene-loaded emulsions were investigated subject to protein ratio and cross-linking. Formation of disulphide and isopeptide bonds between heteroproteins according to crosslinking changed protein structures by exposing the hydrophobic sites of proteins with stiffer network. The cross-linked pea/whey protein complexes at protein ratio of 2:1 formed a stable emulsion with a droplet size of 0.10 _m, showing no phase separation for 30 days of storage and high encapsulation efficiency of 92%. These findings provided a novel strategy to design plant/dairy protein networks to protect lipophilic bioactive compounds by replacing half or more dair-y protein with plant protein, leading to gradual change towards plant-based diets. [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]

Cold-set interpenetrating polymer network gels as riboflavin (RF) delivery vehicles based on wheat bran arabinoxylans (AX) and pea protein isolate (PPI) were developed via enzymatic-crosslinking. The impact of AX concentrations on the physicochemical property, in vitro digestion property and microstructure of IPN gels was explored. Increased concentrations of AX enhanced the viscoelasticity of IPN gels and resulted in a more compact microstructure. However, at a concentration of 5.0 % (w / v), the faster and stronger crosslinking of AX molecules caused separate network gel between PPI and AX. The IPN gel improved the encapsulation efficiency and release property of embedded RF as compared to PPI gel. SEM results showed that IPN gel maintained a complete network structure after gastric digestion. Particularly, the IPN gel with 1.0 % AX exhibited a homogeneous and complete network structure even after intestinal digestion, which explained the reason for the highest encapsulation efficiency and lowest release ratios of RF. [Display omitted] • IPN gels based on arabinoxylans and pea protein isolate were prepared via enzymatic crosslinking. • The IPN structure improved the rheological properties and water mobility of gel samples. • AX could protect PPI gel from faster degradation during in vitro digestion. • IPN gel prepared with 1.0 wt% AX showed huge potential as delivery vehicles for riboflavin. [ABSTRACT FROM AUTHOR]

This study investigated the interaction between pea protein amyloid-like nanofibril and epigallocatechin gallate, constructed and characterized the novel pea protein nanofibrils-derived hydrogel mediated by epigallocatechin gallate, and researched the functionalities of the hydrogel. Epigallocatechin gallate remodeled the structure of pea protein nanofibrils, and a stable and strong hydrogel was formed at a relatively low protein concentration (4.5%). Additionally, the hydrogels exhibited various surface structures and hydrogel properties dependent on the mass ratio. Strongest gel strength (51 g) was attained at 0.25 epigallocatechin gallate/pea protein nanofibrils mass ratio. Whereas, the hydrogels exhibited the highest water holding capacity (87%) at 0.05 mass ratio. The primary driving forces in the formation and maintaining of the hydrogels were hydrophobic interactions and ionic bonds. Progressive rise of β-sheet content of pea protein nanofibrils occurred increasing epigallocatechin gallate concentration. This hydrogel holds great potential for applications in food processing, targeted delivery of nutraceuticals and biomedicine. [Display omitted] • A stable hydrogel was formed at 4.5% (w / v) pea protein nanofibrils with EGCG. • Viscoelasticity and gel strength of pea protein nanofibrils hydrogels enhanced with EGCG. • Thermal stability of pea protein nanofibrils hydrogels improved with EGCG. • Hydrophobic interactions and ionic bonds mainly drove the formation hydrogels. • EGCG rise led to the progressive raise of β-sheet content of pea protein nanofibrils. [ABSTRACT FROM AUTHOR]

This study examines the effects of protein glutaminase modification on the interfacial properties and emulsion stability of pea protein isolates (PPI). Emulsions were prepared using native (NPPI) and deamidated PPI (DPPI) at concentrations from 0.5 wt% to 3.6 wt%. The stability of these emulsions was evaluated by examining droplet size distribution, flocculation index, ζ-potential, and CLSM. DPPI demonstrated superior emulsifying ability and stability, requiring only 2.0 wt% to prevent flocculation compared to NPPI's 3.6 wt%. Interfacial properties, such as protein coverage, composition, thickness, tension, and rheology, were characterized. Large Amplitude Oscillatory Dilatation analysis showed minimal differences between NPPI and DPPI-stabilized interfaces at 1 wt%. However, at 3.6 wt%, NPPI interfaces demonstrated abrupt intra-cycle yielding and viscous behavior, whereas DPPI interfaces exhibited gradual softening and a higher maximum linear strain. Additionally, DPPI showed higher interfacial protein coverage and lower interfacial tension. NPPI formed dense, brittle films prone to rupture under dynamic deformation, leading to poor stability. Deamidation of PPI unfolded the protein structure, exposing hydrophobic groups and increasing carboxyl groups, which reduced aggregation. This resulted in a uniform, extensible, and elastic interfacial film resistant to large deformations. Thus, DPPI-stabilized emulsions demonstrated superior stability, showcasing their potential for industrial applications. • Deamidation obviously enhances emulsifying properties of pea protein isolate (PPI). • DPPI requires 2.0 wt% to prevent flocculation, vs. 3.6 wt% for native PPI. • DPPI shows higher interfacial coverage and lower tension than NPPI. • Deamidation reduces aggregation, forming uniform, elastic interfacial films. • DPPI-stabilized emulsions exhibit superior stability under large deformations. [ABSTRACT FROM AUTHOR]

Industry-scale microfluidizer system (ISMS) was applied to superfine-grinding green peas at 30, 60, 90, 120 MPa for one pass, and 120 MPa for two passes to prepare whole component peas. The particle size distribution of whole component pea and the influence on starch, protein, and fiber in whole component peas was investigated. Particle size parameters including D [4,3] , D [50] and D [90] of whole component peas were reduced from 123.7, 119.0 and 269.0 μm to 33.9, 27.7 and 70.7 μm, respectively. Damaged starch content was greatly increased, and severe destruction of starch granules was observed by SEM morphology. The decrease in protein content and nitrogen element in the precipitate of ISMS-ground pea determined by Kjeldahl method and energy-dispersive X-ray spectroscopy indicated that more pea proteins were converted into soluble form. Confocal laser scanning microscope analysis found that fluorescence of pea fibers became bright, and its dimensions were enlarged, which indicated that dense fibers were separated to structurally loose form. Comparison with modifying pea macromolecules by ISM, there were difference in the degree of starch damage, increase in protein solubility, and fiber destruction in ISMS-ground pea. These phenomena implied that the superfine grinding effect of ISMS on green pea was mainly achieved by changing macromolecule components. • Whole component pea was prepared by superfine grinding using ISMS. • An increase in damaged starch degree and collapse of starch granules were found. • Decrease of nitrogen element in the precipitate of ISMS-ground peas was found. • Dense fibers in whole component pea were torn to be structurally loose state. • Macromolecules change degree in ISMS-ground peas was different from modifying by ISM. [ABSTRACT FROM AUTHOR]

[Display omitted] • GC–MS analysis identified 54 volatile compounds in common vetch protein. • Glutaminase-mediated deamidation effectively mitigated beany flavor in common vetch protein. • Protein structural modifications reduced interactions between common vetch protein and beany volatile compounds. Common vetch protein, similar to pea protein, offers valuable qualities like being non-GMO, hypoallergenic, and nutritious. However, its strong beany flavor hinders consumer acceptance. This study explores enzymatic deamidation using glutaminase to address this issue. GC–MS analysis identified 54 volatile compounds in the raw material protein, with 2-pentylfuran, hexanal, and several nonenals contributing the most to the undesirable aroma. Principal component analysis (PCA) confirmed the effectiveness of glutaminase deamidation in removing these off-flavors. The study further reveals that deamidation alters the protein's secondary structure, with an increase in α – helix structure and a decrease in β – sheet structure. The surface hydrophobicity increased from 587.33 ± 2.63 to 1855.63 ± 3.91 exposing hydrophobic clusters that bind flavor compounds. This disruption weakens the interactions that trap these undesirable flavors, ultimately leading to their release and a more pleasant aroma. These findings provide valuable insights for enzymatic deodorization of not only common vetch protein but also pea protein. [ABSTRACT FROM AUTHOR]

[Display omitted] • GG improved the viscoelastic behavior and gel strength of PPI gel. • GG transformed PPI gels from particles to a chain-like structure. • At high GG concentrations, GDL increased PPI gel strength and water holding capacity. • High GDL content facilitated electrostatic interaction between PPI and GG molecules. This study investigated the effect of gellan gum (GG) and glucono-δ-lactone (GDL) on the acid-induced gel properties of pea protein isolate (PPI) pretreated with media milling. The inclusion of GG substantially enhanced the gel hardness of PPI gel from 18.69 g to 792.47 g though slightly reduced its water holding capacity (WHC). Rheological analysis showed that GG increased storage modulus (G') and decreased damping factor of gels in the small amplitude oscillatory shear region and transformed its strain thinning behavior into weak strain overshoot behavior in the large amplitude oscillatory shear region. SEM revealed that GG transformed the microstructure of gel from a uniform particle aggregate structure to a chain-like architecture composed of filaments with small protein particles attached. Turbidity and zeta potential analysis showed that GG promoted the transformation of PPI from a soluble polymer system to an insoluble coagulant during acidification. When GG content was relatively high (0.2 %-0.3 %), high GDL content increased the electrostatic interaction between PPI and GG molecules, causing their rapid aggregation into a dense irregular aggregate structure, further enhancing gel strength and WHC. Overall, GG and GDL can offer the opportunity to modulate the microstructure and gel properties of acid-induced PPI gels, presenting potential for diversifying food gel design strategies through PPI-GG hybrid systems. [ABSTRACT FROM AUTHOR]

The study investigated the impact of pea protein isolate (PPI) on the short-term and long-term retrogradation behavior of pea starch (PS). Dynamic time scanning and water migration analysis revealed that the presence of PPI enhanced water mobility within the PS gel during short-term storage (4 °C, 8 h) and impeded amylose gelation, effectively suppressing the short-term retrogradation of amylose. Over long-term storage (4 °C, 14 d), PPI reduced the retrogradation enthalpy and the ordered structure of starch molecules. The relative crystallinity and retrogradation degree reduced by 40.6% and 29.9%, respectively, as the PPI content increased from 0 to 12%. Textural profile analysis showed PPI decreased the gel hardness and induced the formation of a weak gel of PS, thereby delaying the long-term retrogradation of amylopectin. Scanning electron microscopy analysis further confirmed that the PS-PPI mixed gel exhibited a more disordered and loose structure compared to the PS gel, which resulted from PPI inhibiting the rearrangement and aggregation of amylose and amylopectin molecules. These findings suggested that PPI exhibited the potential to inhibit the short-term and long-term retrogradation of PS, thus providing valuable theoretical evidence for enhancing the development and research of pea-based products. [Display omitted] • The storage modulus of pea starch (PS) was reduced by pea protein isolate (PPI). • PPI enhanced water mobility within the PS gel. • PPI disrupted the ordered structure of PS and hindered its recrystallization. • PPI effectively mitigated both short-term and long-term retrogradation of PS. [ABSTRACT FROM AUTHOR]

In this study, the mixture of pea protein isolate (PPI) and oat protein isolate (OPI) (1:1, w/w), curdlan, and soybean oil were used as the main ingredients to prepare flourless plant-based eggs. Meanwhile, the effects of different protein/curdlan ratios (8:2, 6:4, 5:5, 4:6, 2:8) on the properties of the thermal behavior and foamability of samples were investigated. All formulas formed stable, uniform, and flowing plant-based eggs. Compared to commercial plant-based eggs, the thermal behavior of flourless plant eggs with protein/curdlan ratios greater than 8:2 exhibited thermal behavior closer to real eggs and can be adapted to environments such as water bath heating (simulating the formation of steamed egg custard) or frying (simulating omelettes), demonstrating promising culinary potential. As curdlan content increased, the gel structure, primarily governed by hydrophobic interactions and hydrogen bonds, became denser, leading to higher gel strength and water-holding capacity. However, the plant-based eggs remained suboptimal in foaming properties. Proteins established a relatively stable interface, while oil droplets formed a more fluid-like film at the gas-liquid interface throughout the foaming process. As drainage progressed, oil droplets flowed out from the interface, liquid film, and plateau borders, diminishing their capacity to sustain bubble stability. Curdlan can only affect foam properties by increasing viscosity and blocking channels. In conclusion, this study provided a reference for constructing flourless plant-based eggs with good thermal gelling properties and foaming capabilities. [Display omitted] • Flourless plant-based eggs were primarily made with proteins, curdlan, and oil. • The plant-based eggs had irreversible heat-set gelling properties like real eggs. • The cooking adaptability of plant-based eggs is better than commercial products. • Plant-based eggs still need improvement in foaming properties. [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]

The roles of increasing concentration of konjac glucomannan polysaccharide (KGM) in modifying the thermal, textural, and rheological properties of heat-induced pea protein isolate (PPI) hydrogels at neutral pH and low ionic strength were investigated in this study. Differential scanning calorimetry was first applied to investigate the effect of KGM addition on the thermal properties of pea proteins, finding that an addition of 0.5 % w/v increased the glass transition temperature of pea proteins (from 150 to 154 °C) while on the contrary, higher concentrations of 1.0–1.5 % w/v reduced glass transition temperatures (from 150 °C to ∼ 144 °C). Water holding capacity highlighted that KGM addition significantly increased water retention, reaching values up to 90 % for KGM concentration ≥ 1.0 % w/v. Confocal laser scanning microscopy showed the presence of a phase separation system with increasing concentrations of KGM. Molecular interactions and Fourier transform infrared spectroscopy analysis highlighted that the hydrogels were mainly stabilized by non-covalent intermolecular interactions. Texture analysis confirmed that KGM significantly influenced texture of the hydrogels, in which 1.5 % w/v KGM presented the highest hardness value of 1.34 N. Lastly, small amplitude rotational and oscillatory rheology was employed to evaluate the hydrogels viscosity and viscoelastic properties, which both were significantly increased with increasing KGM concentrations. [Display omitted] • KGM modified thermal glass transition of pea protein isolates. • KGM improved water holding capacity of pea protein isolate hydrogels. • Increasing KGM concentrations led to a segregative phase separation. • Composite hydrogels are mainly stabilized through non-covalent intermolecular interactions. • Viscoelastic properties of the hydrogels were significantly influenced by KGM. [ABSTRACT FROM AUTHOR]

The application of the commercial pea protein isolate (CPPI) and polyphenols are often limited by their poor solubility. To address it, a time-saving pH-ultrasonic-shifting method was skillfully developed by combining the pH-shifting and ultrasonic methods to efficiently encapsulate polyphenols, and this final obtained nanoparticles was named CPPI-NAR-4. CPPI-NAR-4 has shown higher encapsulation efficiency (EE, 93.81 ± 0.56%) and loading capacity (LC, 8.58 ± 0.05%) for NAR, smaller particle size (126.40 ± 3.84 nm) and lower zeta potential (−18.50 ± 0.98 mV) as compared to nanoparticles prepared by other three known methods. This high EE and LC of CPPI-NAR-4 were attributed by both CPPI-NAR-4 and CPPI-4 having the higher surface hydrophobicity, the higher fluorescence intensity, and more protein expansion in their comparison. Multi-spectra evaluations indicated that the pH-ultrasonic-shifting process might produce more hydrogen bonding in the combination of CPPI and NAR. As to the interaction mechanisms between CPPI and NAR in CPPI-NAR nanoparticles, molecular docking results showed that hydrogen bonds, van der Waals forces, and hydrophobic interactions were dominant in the binding of NAR and CPPI; further molecular dynamics simulations revealed that NAR and CPPI had more interactions at pH 12 than at pH 7. Based on these experimental and simulative results, it could be suggested that the effects of ultrasonic on the binding between CPPI and NAR might be better at pH 12 than at pH 7. In conclusion, this pH-ultrasonic-shifting method was expected to be further developed for industrial fabricating protein-polyphenol nanoparticles such as CPPI-NAR. [Display omitted] • A pH-ultrasonic-shifting method was designed for encapsulating polyphenols. • CPPI-NAR was fabricated by pH-ultrasonic-shifting method and other known methods. • Different processes exhibited different interaction mechanisms of CPPI and NAR. • Molecular dynamics predicted ultrasonic effects on CPPI-NAR binding at different pH. [ABSTRACT FROM AUTHOR]

Recently, plant-based meat analogues (MAs) have received increased attention as a sustainable diet. In this study, MAs were prepared from pea protein isolate (PPI) and wheat gluten (WG) via high-moisture extrusion. The effects of different WG contents (0%, 10%, 30%, 50% and 70%) on the product characteristics of MAs were investigated. Results revealed that the addition of WG significantly reduced the hardness and chewiness of MAs, but significantly improved their springiness, brightness and whiteness. MAs containing 30% WG and 50% WG both exhibited a distinct fibrous structure in terms of microstructure, with MAs containing 30% WG having the highest fibrous degree in terms of texture properties. After the addition of WG, there was a tendency for water molecules in MAs to shift from bound water and free water to immobilized water. In addition, the results of protein solubility analysis indicated that hydrogen bonds and disulfide bonds played a major role in forming and maintaining structures within MAs. With the increase of WG content, the ordered structure content, apparent viscosity, storage modulus, loss modulus and protein molecular weight of MAs increased significantly. Finally, the addition of 30% and 50% content of WG resulted in decreased in vitro protein digestibility and essential amino acid content of MAs, but significantly improved their flavor and sensory scores. This study provides useful information for improving the quality of PPI-based MAs to meet consumer needs. [Display omitted] • Pea protein-wheat gluten meat analogues (MAs) are made by high-moisture extrusion. • Wheat gluten (WG) makes MAs brighter and whiter. • MAs with a WG content of 30% have the highest fibrous degree. • The addition of WG reduces the hardness and increases the springiness of MAs. • MAs with a WG content of 30% have the highest sensory score. [ABSTRACT FROM AUTHOR]

Using a combination of pea protein isolates (PPI) and β-lactoglobulin (βlg) presents an interesting approach to improve the gelling properties of PPI compared to the use of PPI alone. While controlling the 7S/11S ratio has proven effective in improving the gelling properties of PPI, more complex models need to be studied. Specifically, the effects of diverse 7S/11S ratios and the inclusion of βlg and 2S albumin on gel formation remain unexplored. Therefore, this study aimed to 1) determine the optimal 7S/11S ratios and 2) identify the interactions involved in the formation of model βlg—pea protein gels generated from globulin and albumin-enriched fractions. Results revealed that pea protein gels with a 7S/11S ratio of ∼ 1.89 achieved the highest firmness (131 Pa). Gelation was primarily driven by hydrophobic interactions (∼ 41%) involving 7S vicilin and 2S albumin, while most of the 11S legumin did not contribute to the protein gel. Conversely, a 7S/11S ratio of ≤ 1 facilitated the formation of the firmest gels (300–657 Pa) in the presence of βlg. These gels were primarily formed via disulfide bonds (36–65%) with βlg, 11S legumin, and 2S albumin as the main proteins involved, while 7S vicilin gelled independently through hydrophobic interactions. Based on these results, we propose a mechanism illustrating the interactions in mixed βlg—pea protein gels. This study provides new insights into how 7S/11S ratios, gel firmness, and protein interactions interplay during the gelation of mixed βlg–pea protein systems, paving the way for innovation in developing a new food category. [Display omitted] • Without βlg, gel firmness peaks at a 7S/11S ratio of 1.89 • Without βlg, hydrophobic interactions dominate pea protein gel formation. • Gel firmness peaks at a 7S/11S ratio ≤1 with βlg present. • With βlg, 7S independently gels through hydrophobic interactions. • With βlg, βlg, 11S, and 2S gel via disulfide bonds. [ABSTRACT FROM AUTHOR]

The low solubility of pea protein isolate (PPI) greatly limits its functional properties and its wide application in food field. Thus, this study investigated the effects and mechanisms of cellulose nanocrystals (CNC) (0.1–0.4 %) and CaCl 2 (0.4–1.6 mM) on the solubility of PPI. The results showed that the synergistic effect of CNC (0.3 %) and Ca2+ (1.2 mM) increased the solubility of PPI by 242.31 %. CNC and Ca2+ changed the molecular conformation of PPI, enhanced intermolecular forces, and thus induced changes in the molecular morphology of PPI. Meanwhile, the turbidity of PPI decreased, while surface hydrophobicity, the absolute zeta potential value, viscoelasticity, β-sheet ratio, and thermal properties increased. CNC bound to PPI molecules through van der Waals force and hydrogen bond. Ca2+ could strengthen the crosslinking between CNC and PPI. In summary, it is proposed a valuable combination method to improve the solubility of PPI, and it is believed that this research is of great significance for expanding the application fields of PPI and modifying plant proteins. [Display omitted] [ABSTRACT FROM AUTHOR]

Plant protein–polysaccharide composite hydrogels and emulsion gels are attractive materials for production of edible inks for 3D food printing. Their ability to satisfy the printability requirements is conventionally evaluated in small- and large-amplitude oscillatory shear tests. A model is derived that describes experimental data in linear and nonlinear rheological tests on protein gels in a unified manner. The model is based on the population-balance approach and involves a reasonably small number of adjustable parameters. Fitting observations on soy protein isolate–xanthan gum, peanut protein–gellan gum, peanut protein–carrageenan, pea protein–carrageenan and pea protein isolate–flaxseed gum gels demonstrates that material parameters evolve consistently with composition of the gels. The governing equations describe adequately the effects of pH and ionic strength of aqueous solutions on the mechanical properties of the gels and predict the stress–strain Lissajous curves and the crossover amplitudes for transition from the solid-like to fluid-like response. Based on the analysis of observations in large-amplitude oscillatory tests with various frequencies, a mechanism is proposed for transition from the type-I (strain thinning) to type-III (weak strain overshoot) response of protein–polysaccharide gels. • A model is derived for the response of protein gels in small- and large-amplitude oscillatory tests. • The model correctly describes experimental data on plant protein-polysaccharide gels. • Material parameters evolve consistently with composition and preparation conditions. • The model predicts adequately the stress–strain Lissajous curves. • A mechanism is proposed for transition from type-III to type-I responses in oscillatory tests. [ABSTRACT FROM AUTHOR]

The phytochemical composition and physicochemical attributes of polyphenol-enriched protein particle ingredients produced with pulse proteins (e.g. chickpea protein, pea protein, and a chickpea-pea protein blend) and polyphenols recovered from wild blueberry pomace were investigated for colloidal and interfacial properties. Anthocyanins were the major polyphenol fraction (27.74–36.47 mg C3G/g) of these polyphenol-rich particles (44.95–62.08 mg GAE/g). Dispersions of pea protein-polyphenol particles showed a superior phase stability before and after heat treatment compared to the chickpea pea protein-polyphenol system. This observation was independent of the added amount of NaCl in the dispersion. In general, at quasi equilibrium state, pulse protein-polyphenol particles and parental pulse protein ingredients showed similar oil-water interfacial tension. However, pea protein-polyphenol particles demonstrated a reduced diffusion-driven oil-water interfacial adsorption rate constant compared to the parental pea protein ingredient. Overall, the obtained results suggest application potential of pea protein-polyphenol particles as a functional food/beverage ingredient. [Display omitted] • Spray dried microparticles were produced with pulse proteins and blueberry pomace polyphenols. • Anthocyanins were the major polyphenol fraction of polyphenol-rich particles. • Protein-polyphenol interaction may reduce particle size in protein dispersion systems. • Pulse protein composition determines the colloid stability of protein-polyphenol particles. • Pea protein-polyphenol particles have superior colloid stability compared to chickpea particles. [ABSTRACT FROM AUTHOR]

The use of nanotechnology in food production (in particular protein base nanoemulsion) is a solution that is gaining popularity, which allows to design of smart food with targeted health-promoting properties. This study aimed to assess the impact of the dose of the phytochemical extract (1%; 3%; 5% w /w) comprising isolated lipophilic compounds from Calendula officinalis L. on selected physicochemical properties of the emulsion, antioxidant, antidiabetic and antiaging effects, and its impact on carotenoids content and their in vitro bioavailability. The results showed that the use of a 3% extract dosage appears to be optimal for obtaining a nanoemulsion. This variant was characterized by the highest antidiabetic activity and there was no overloading of the nanostructure. Additionally, the use of a pea protein - lipophilic compounds - sunflower/hemp oil matrix to create nanoforms seems to be a promising solution in the context of pro-health properties and bioavailability of bioactive compounds. • Nanoemulsions can be successfully used to protect and deliver carotenoid compounds. • Nanoemulsion with pea protein after vacuum drying shows high biological activity. • Nanoemulsions can increase the bioavailability of carotenoid compounds. • The matrix of lipophilic compounds of marigold in nano form is a 'smart food'. [ABSTRACT FROM AUTHOR]

This study explored the relationship between pea protein foaming properties and their structure and physicochemical properties under neutral and acidic pH. Results showed that pH modified the zeta potential, particle size and surface tension due to electrostatic changes. FT-MIR and fluorescence spectra revealed pH-induced conformational changes, exposing hydrophobic groups and increasing sulfhydryl content, promoting protein aggregation. At pH 3, the highest foaming capacity (1.273) and lowest foam expansion (6.967) were observed, associated with increased surface hydrophobicity and net charges, ideal for creating light foams with high liquid incorporation for acidic beverages or fruit-based mousses. Pea protein isolate generated stable foams with foam volume stability between 86.662 % and 94.255 %. Although neutral pH conditions showed the highest foam volume stability, their air bubbles increased in size and transitioned from spherical to polyhedral shape, suitable for visual-centric applications, like cappuccino foam and beer-head retention. Foams at pH 5 exhibited the smallest bubbles and maintained their spherical shape, enhancing drainage resistance, beneficial for whipped toppings. Strong correlations (Pearson correlation coefficient higher than 0.600) were noted between the structure, surface and foaming properties, providing crucial insights into optimizing pea protein functionality across various pH conditions, enabling the development of plant-based foamed products with tailored properties. [Display omitted] • pH altered secondary and tertiary structure, and surface properties of PPI. • Significant impact is noticed on β-sheet, β-turn, A1, A2 and SS bonds contents. • Decreasing pH from neutral to acidic increased surface hydrophobicity. • Neutral pH had highest foam stability; pH 5 produced smaller, more uniform bubbles. • Correlations showed links between structural changes and foaming properties. [ABSTRACT FROM AUTHOR]

• Polyvinyl alcohol (PVA) and pea protein isolate (PPI) were used to prepare nanofibers. • Fast-dissolving PVA/PPI nanofibers were successfully produced. • Lion's Mane (LM) extract was encapsulated within PVA/PPI nanofibers. • LM extract loaded-PVA/PPI nanofibers exhibited fast dissolution in phosphate solution. This research aimed to produce "fast-dissolving nanofibers" from polyvinyl alcohol (PVA) and pea protein isolate (PPI) by electrospinning using a green approach. Lion's Mane (LM) mushroom extract was added to the optimized PVA/PPI solution (PVA:PPI 50:50 by weight ratio added with 1 % v/v Tween20) to increase solubility of LM extract. LM extract can be encapsulated within PVA/PPI nanofibers and fast-dissolved in a phosphate solution. Results exhibited high potential use of electrospinning for encapsulation of bioactive compounds through fast-dissolving nanofiber forms. [ABSTRACT FROM AUTHOR]

The present study investigated thermal gelation of mixed sarcoplasmic (Sarc), myofibrillar (Myof), and pea proteins corresponding to partial meat replacements (0, 25, and 50%) by pea protein isolate (PPI) at reducing salt levels (0.6 → 0.1 M NaCl) to understand in situ (simulated) structure-forming properties of hybrid meat analogues. The amount of soluble proteins in hybrids generally increased with salt concentrations and PPI substitution. While muscle proteins (mixed Sarc and Myof) had the strongest gelling capacity, hybrid proteins also exhibited moderate aggregation and gelling activity based on the sol→gel rheological transition and gel hardness testing. Sarc and pea 7S/11S globulins collectively compensated for the attenuated gelling capacity of mixed proteins due to diminishing Myof in the hybrids. Immobilized water within hybrid protein gels was tightly bonded (T 2 from nuclear magnetic resonance), consistent with the dense and uniform microstructure observed. These findings offer a new knowledge base for developing reduced-salt hybrid meat analogues. [Display omitted] • Sarcoplasmic (Sarc), myofibrillar (Myof), and pea protein formed hybrid gels. • The ratio of soluble Myof/Sarc/pea proteins is specific to the salt content. • Sarc and pea 7S/11S compensate for the attenuated gelling capacity of hybrids. • Hybrid muscle/pea protein gels display dense and uniform structure. • Immobilized water is strongly bonded in low- or reduced-salt meat hybrids. [ABSTRACT FROM AUTHOR]

The emulsification potential of plant-based emulsifiers, that is, pea (PPI) and lentil (LPI) proteins (4%), corn arabinoxylans (CAX, 1%), and legume protein-arabinoxylan mixtures (4% proteins + 0.15 or 0.9% CAX), was evaluated by assessing: the surface tension and potential of emulsifiers, emulsifier antinutritional contents, emulsion droplet size, emulsion physical stability, and vitamin E bioaccessibility from 10% oil-in-water emulsions. Tween 80 (2%) was used as a control. All emulsions presented small droplet sizes, both fresh and upon storage, except 4% LPI + 0.9% CAX emulsion that exhibited bigger droplet sizes (d(4,3) of approximately 18.76 μm vs 0.59 μm for the control) because of droplet bridging. Vitamin E bioaccessibility from emulsions stabilized with the combination of 4% PPI and either 0.15% or 0.9% CAX (28 ± 4.48% and 28.42 ± 3.87%, respectively) was not significantly different from that of emulsions stabilized with Tween 80 (43.56 ± 3.71%), whereas vitamin E bioaccessibility from emulsions stabilized with individual emulsifiers was significantly lower. • Legume proteins and/or arabinoxylans present good emulsifying capacities. • All tested emulsions present a very good stability over time (21 days). • Pea protein and arabinoxylans as emulsifiers promote vitamin E bioaccessibility. • Legume proteins and arabinoxylans can be an alternative to Tween 80 as emulsifiers. [ABSTRACT FROM AUTHOR]

[Display omitted] • An oral reversible UGTs&SULTs dual-target-mild-inhibition strategy was designed. • The self-assembly binding between R-Q@P-D was the non-covalent bonds. • The in-silicon simulation and experimental results investigated their interactions. • The tremendous oral safety and simple fabrication benefited its medical translation. • A promising strategy for improving the bioavailability and efficacy of polyphenols. The low bioavailability of polyphenols, such as resveratrol (RES), is typically caused by the poor solubility and first-pass effect. To improve bioavailability and reduce adverse effects, an oral reversible UDP-glucuronosyltransferases (UGTs) and sulfotransferases (SULTs) dual-target-mild-inhibition strategy was designed, and a proof-of-concept was studied. This R-Q@P-D nanoparticle for the codelivery of RES and quercetin (QUE) was constructed using pea protein isolate and dipotassium glycyrrhizinate (DG) as nanocarriers. These nanoparticle ingredients were all plant extracts approved by the FDA, and the fabrication process was a simple but novel pH-ultrasonic-shifting method in water conditions. R-Q@P-D exhibited high encapsulation efficiency of RES (97.25 ± 1.13 %) and QUE (94.21 ± 0.62 %), with a uniform nanosize (147.73 ± 1.85 nm). Characterizations implied that RES and QUE could be successfully encapsulated in nanoparticles in amorphous states, and the self-assembly binding between them was non-covalent bonds. Moreover, the in-silicon simulation and experimental results verified interactions between RES and DG, while there was no interaction between QUE and DG. In vivo evaluations showed that R-Q@P-D increased the bioavailability of RES by mildly and reversibly inhibiting intestinal UGTs and SULTs, but without inhibiting hepatic UGTs and SULTs. Moreover, molecular simulations showed that QUE and RES are competitively bound to SULTs but not UGTs. R-Q@P-D had significant therapeutic efficacy and excellent safety performance for its oral application. The tremendous safety and simple fabrication benefited the clinical translation. Together, R-Q@P-D based on reversible UGTs and SULTs dual-target-mild-inhibition strategy might be a promising nano-platform for improving the bioavailability and efficacy of hydrophobic polyphenols. [ABSTRACT FROM AUTHOR]

Plant-based fish analogues have been proposed as a sustainable solution to address the inefficiencies and environmental challenges of traditional aquaculture. In this study, structurally stable salmon fillet simulants were constructed using three-dimensional (3D) printing technology coupled with transglutaminase (TGase) post-treatment. The myomere bioinks containing corn starch, flaxseed oil, and pea protein were optimised for the construction of structurally stable simulants. The flaxseed oil and pea protein myosepta bioinks were then injected into the 3D printed myomere analogues according to the macronutrients of real salmon fillets. The rheological properties of the myomere and myosepta bioinks, as well as the microstructure and chemical composition of the myomere and myosepta analogues, were systematically characterized. TGase was added to both myomere and myosepta simulants for paste-solid transformation. The printed raw salmon fillet simulants were microwaved to obtain cooked salmon fillet simulants. Moreover, the textural properties of the raw and cooked salmon fillet simulants were investigated. The prepared salmon fillet simulants exhibited fish muscle-like fibre structures in myomere analogues and good similarity to real salmon meat, demonstrating the great potential in simulating better fish meat texture. [Display omitted] • Plant-based salmon fillet simulants were prepared with myomere and myosepta analogues. • Myomere bioinks matched printing utilized pea protein, corn starch, and flaxseed oil. • The myomere and myosepta analogues were solidified with transglutaminase. • The prepared myomere analogues exhibited fish muscle-like fibre structures. • The salmon fillet simulants achieved good textural similarity with real salmon fillets. [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]

This study examined the effects of replacing alkaline phosphate (AP) with bamboo fiber (BF), isolated pea protein (PP), and mushroom powder (MP) on the nutritional, technological, oxidative, and sensory characteristics of low-sodium mortadellas. Results indicated that this reformulation maintained the nutritional quality of the products. Natural substitutes were more effective than AP in reducing water and fat exudation. This led to decreased texture profile analysis (TPA) values such as hardness, cohesiveness, gumminess, and chewiness. The reformulation reduced the L* values and increased the b* values, leading to color modifications rated from noticeable to appreciable according to the National Bureau of Standards (NBS) index. Despite minor changes in oxidative stability indicated by increased values in TBARS (from 0.19 to 0.33 mg MDA/kg), carbonyls (from 2.1 to 4.4 nmol carbonyl/mg protein), and the volatile compound profile, the sensory profile revealed a beneficial increase in salty taste, especially due to the inclusion of MP, which was enhanced by the synergy with BF and PP. In summary, the results confirmed the potential of natural alternatives to replace chemical additives in meat products. Incorporating natural antioxidants into future formulations could address the minor oxidation issues observed and enhance the applicability of this reformulation strategy. • Emulsion stability was improved in reformulated samples. • BF and PP enhanced MP's salty taste effect. • Reformulation led to a slight decrease in oxidative stability. • BF, PP, and MP are a promising combination to reduce phosphate in mortadellas. [ABSTRACT FROM AUTHOR]

Ulcerative colitis (UC) is a chronic, incurable disease that causes great suffering to patients. High internal phase emulsions (HIPEs) are promising carriers of curcumin (Cur), which has a beneficial effect on UC. The retention rate of Cur encapsulated in HIPEs prepared by pea protein isolated nanoparticles/octenyl succinic anhydride-modified linear dextrin composite particles (PPINs/OSA-LD) or PPINs reached 84.85% and 85.98%, respectively, which was significantly higher than that of Cur dissolved in corn oil (73.84%) due to the superior protection of the emulsion interfacial structure. The HIPEs showed higher bioaccessibility of Cur (31.16%) due to the higher degree of free fatty acid release. After emulsion treatment, the symptoms of UC were ameliorated, mainly manifested by the recovery of body weight, growth of the colon, down-regulation of pro-inflammatory factors, up-regulation of anti-inflammatory factors, and balance of gut microbiota composition. The Cur-loaded HIPEs show an outstanding improvement in UC. [Display omitted] • The stability and bioaccessibility of curcumin are improved based on the HIPE structure. • HIPEs, as a carrier of curcumin, can alleviate the ulcerative colitis. • OSA-LD, as a resistant starch, can regulate the composition of gut microbiota. [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]

More recently, the concepts of cell-free supernatants (CFS, so-called postbiotics) and whole-cell postbiotics (WCP) of probiotics have gained increasing attention for the development of bio-based films. However, reports on CFS and WCP of Lactobacillus gasseri remain scarce. In this study, pea protein isolate/psyllium mucilage was incorporated with CFS and WCP of L. gasseri to produce bio-based edible films. pH, total soluble solid content, antioxidant activity, total phenolic content, antimicrobial activity, and structural analyses were conducted to characterize the CFS and WCP of L. gasseri. Furthermore, the effects of CFS (10% and 20%, v/v) and WCP (10% and 20%, v/v) on the physicochemical, mechanical, barrier, optical, microstructural, and antimicrobial properties of the bio-based films were investigated. The results showed that CFS and WCP exhibited antioxidant and antibacterial activities and were significant sources of phenolic compounds. The incorporation of 20% WCP caused a significant increase in the thickness and water vapor permeability of films, while a significant increase in moisture content was observed with 10% WCP. The control and 10% WCP films had the highest tensile strength values. Furthermore, the addition of 10% WCP resulted in a significant increase in elasticity. Films incorporating CFS and WCP exhibited lower opacity values and darker, yellow, and red color intensities. The addition of CFS and WCP caused a rough texture and cracked structure on the surface of the film. In conclusion, pea protein/psyllium mucilage-based films containing CFS and WCP of L. gasseri can be considered as a new alternative for environmentally friendly bio-based films. • Films containing cell-free supernatant (CFS) and whole-cell supernatant (WCP) were developed. • CFS and WCP were effective on the physicochemical properties of the films. • Films containing CFS and WCP exhibited cracks on their surfaces. • The addition of CFS and WCP weakened the tensile strength of the films. • Films containing CFS and WCP may be an alternative to alternative biobased films. [ABSTRACT FROM AUTHOR]

In light of the diversity and complexity of pea flavor, the odor profile of pea protein isolate (PPI) has not been comprehensively characterized. This study aims to explore the odor profile of PPI by SPME and SAFE coupled with multidimensional flavor analytical approaches, including GC-O-MS, GC × GC-O-TOF-MS and GC-IMS analyses. A total of 148 volatile compounds were detected by all three analytical techniques, with over 80% being identified by GC × GC-O-TOF-MS. Furthermore, 42 odor-active compounds were identified by GC-O/GC × GC-O analyses, among which 2, 3-octanedion, butyl acetate and ethyl acetate showed odor activity in PPI for the first time. Subsequently, these 21 odorants with flavor dilution (FD) factors ranging from 9 to 243 were quantified by external standard curves and their odor activity values (OAVs) were calculated. Notably, (E, E)-2,4-decadienal exhibited the highest OAV, followed by hexanal and nonanal, which all contributing the typical fatty and grassy odors to PPI. Finally, the contribution of 20 key odor-active compounds with OAV >1 to the odor profile of PPI was further validated through a reconstitution experiment. These findings provide basis for the flavor analysis and sensory improvement of pea-derived products. [Display omitted] • SPME was more effective in volatile compounds extraction of PPI compared to SAFE. • The odor profile of PPI was characterized by GC-O-MS, GC × GC-O-TOF-MS, and GC-IMS. • More than 80% of volatile compounds were identified by GC × GC-O-TOF-MS. • Three odor-active compounds were identified in PPI for the first time. • Reconstitution experiment validated the contribution of volatiles (OAV >1). [ABSTRACT FROM AUTHOR]

The current study was undertaken to synthesize pea protein based films containing fatty acids with various chain lengths. Films namely PFAF1, PFAF2, and PFAF3 were fabricated in the presence of pelargonic acid, margaric acid, and pentacosanoic acid, respectively. Also, negative (PF: film formulated using protein alone) and positive control (PCF: film formulated using mixture of protein and chitosan) control were prepared. Interactions occurring within films were clarified by FTIR. Moreover, morphology and thermal behavior of samples were evaluated by SEM and TGA. Variations in thickness (PF: 0.03 mm, PFAF1: 0.03 mm, PFAF2: 0.04 mm, PFAF3: 0.04 mm, PCF: 0.06 mm) and water content (PF: 28.85 %, PFAF1: 16.20 %, PFAF2: 14.51 %, PFAF3: 12.04 %, PCF: 13.83) were obvious. Superior opacity was identified in PCF, followed by PFAF3, PFAF2, PFAF1, and PF. PFAF3 together with PCF were more successful than others in reducing/protecting oxygen and water permeation. Adding fatty acid or chitosan to protein films led to the decline in tensile strength (TS) and increment in elongation at break (E). As for preservation performances, maximum limitations against shifts in weight and color of bananas during 7-day storage were provided by PFAF3. Also, except for PF, all coatings (especially PFAF3) postponed the rotting of fruits. • A versatile approach to food wrapping field. • Designing eco-friendly innovative natural plant protein based films. • A strategy for enhancing the film forming ability of plant proteins. • Positive correlation between fatty acid chain length and barrier behavior of films. • Packaging for maintaining postharvest quality of fruit over prolonged storage. [ABSTRACT FROM AUTHOR]

Pea protein isolate (PPI) was used as a carrier matrix to load tannic acid (TA) due to its multiple cavity structures and reaction sites, after that, magnesium ion (M) was further added to form more stable carrier structures. PPI was covalently bound with TA to form TA-PPI complexes in alkaline conditions, then M induced the aggregation of TA-PPI to produce M-TA-PPI complexes. TA mainly interacted with free amino groups and sulfhydryl groups of PPI, thereby decreasing their content in complexes. TA further decreased the α-helix content and increased the β-sheet and β-turn content in TA-PPI complexes correspondingly, nevertheless the M would decline these changes in M-TA-PPI complexes. As a result of binding, TA and M jointly increased the average molecular size of complexes. The higher TA addition amount (10–20 mg/g PPI) was conducive to the stronger intramolecular interactions (more hydrophobic interactions and disulfide bonds), gel structure (higher hardness value) and storage modulus in M-TA-PPI gels. Compared with TA-PPI complexes, M-TA-PPI complexes showed higher stability in gastric digestion and higher TA releasement and antioxidant capacity of its digesta in intestinal digestion. This kind of metal-phenolics-protein complexes may have potentials to be a stable and efficient carrier for loading gastric sensitive polyphenols. [Display omitted] • Tannic acid (TA) covalently binding with pea protein (PPI) to form TA-PPI complexes. • Magnesium ion (M) induces TA-PPI to aggregate as tighter M-TA-PPI complexes. • M-TA-PPI complexes reserve more bioactive TA after gastric digestion. • M-TA-PPI complexes release more bioactive TA during intestinal digestion. • M-TA-PPI is a potential carrier for delivering gastric sensitive compounds. [ABSTRACT FROM AUTHOR]

The potential of using emulsion gels stabilized by binary plant protein nanoparticle mixtures for the encapsulation and delivery of lipophilic nutraceuticals was evaluated. The particle characteristics, physical stability, water diffusivity, microrheology, large amplitude oscillating shear (LAOS) properties, and in vitro digestion of emulsion gels prepared by different ratios of hydrolyzed rice glutelin fibrils (HRGFs) and pea protein nanoparticle (PNP) were characterized. The emulsion gel with P/H = 2:1 (0.84 μm) exhibited the best storage stability and freeze-thaw stability, as seen by the smaller oil droplet size (1.02 and 1.42 μm, respectively). Low-field pulsed NMR indicated that the majority of water in samples was highly mobile. All the samples were predominantly elastic-like materials. The P/H 2:1 emulsion gel had the lowest FI value (6.21 × 10−4 Hz), the highest MVI value (5.57 s/nm2), G′/ G″ values and enclosed area, showing that it had denser 3D network structures, higher stiffness values, and a high sensitivity to changes in strain. Additionally, P/H 2:1 emulsion gel had a relatively high lipid digestibility (96.1 %), curcumin bioaccessibility (58.9 %), and curcumin stability (94.2 %). This study showed that emulsion gels stabilized by binary protein nanoparticle mixtures (PNP/HRGF) have potential as edible delivery systems for lipophilic nutraceuticals. [Display omitted] • The binary protein nanoparticle-based emulsion gels were fabricated by HRGF and PNP. • PNP/HRGF 2:1 emulsion gel had superior storage and freeze-thaw stability. • PNP/HRGF 2:1 emulsion gel had denser network structure and more elastic behavior. • PNP/HRGF 2:1 emulsion gel had high curcumin bioaccessibility and stability. [ABSTRACT FROM AUTHOR]

Cuticular proteins, in conjunction with chitin, compose the insect exoskeleton, and play a key role in the growth, development, and molting of insects. However, the specific functions of most cuticular protein genes in the growth, development, and reproductive processes of the pea aphid (Acyrthosiphon pisum) remain unclear. In this study, we have identified six cuticular protein genes in the pea aphid, namely ApCP7 , ApCP10 , ApCP19 , ApCP19.8-like , ApCP35 and ApCP62. We found that the expression levels of six genes were highly expressed during the adult stage, and except for ApCP10 , which is highly expressed in the pea aphid cuticle, other genes were highly expressed in the ovaries. Subsequently, we observed that the survival rate and fecundity of pea aphid were significantly lower than those of the control group after silencing ApCP7 and ApCP62 through RNA interference. Furthermore, when ApCP7 transcript levels were reduced, aphid encountered difficulties in molting, were smaller in body size, and exhibited a darker body color. These results indicate that ApCP7 and ApCP62 are involved in the development and reproduction of pea aphid, and could be used as RNAi targets for controlling pea aphid. [Display omitted] [ABSTRACT FROM AUTHOR]

The poor gelation properties of pea protein isolate (PPI) limit their use in food industries. In the present study, PPI was modified by pH-shifting combined with heat treatment, followed by cold-set gelation of PPI gels induced by transglutaminase. Both pH 2–3 and pH 10–12 promoted the unfolding of PPI molecules and the transformation of secondary structures from ordered to disordered. In particular, PPI molecules with pH 12-shifting tended to expand and unfold, which resulted in the exposure of internal active groups and improvement in surface hydrophobicity. Accordingly, after the addition of 50 U/g transglutaminase, PPI gels with pH 12-shifting and heating treatment exhibited homogeneous and dense gel network with high cross-linking degree (88.12 ± 1.80%) and water holding capacity (92.13 ± 2.40%), since pH 12-shifting and heating treatment promoted the conversion of random coils and β-turns to β-folds and α-helices in PPI gels. However, with pH 10 and 11-shifting, the PPI molecules was partially unfolded and the PPI gels had a high non-network protein content, resulting in low-strength gel networks of PPI gels with rough and loose microstructures and a low WHC. These results showed that TGase-crosslinked cold-set PPI gels after pH 12-shifting and heat treatment could promote the formation of homogeneous and dense gel network structure, so that improved the PPI gelation properties, which had great potential to be used as gelling agents or nutraceutical delivery systems for thermal sensitive bioactive compounds in food and non-food fields. [Display omitted] • TGase-crosslinked PPI cold-set gels were prepared by pH shifting and heat treatment. • pH 12-shifting promoted the formation of Gln-Lys covalent and disulfide bonds in PPI gels. • TGase-crosslinked PPI after pH 12-shifting and heat treatment assisted in the formation of a dense gel network. • Highly strengthened network exhibited high gel strength and water holding capacity. • TGase-crosslinked PPI after pH10 and 11-shifting resulted in rough and loose structures. [ABSTRACT FROM AUTHOR]

High moisture extrusion processing (HMEP) is gaining attention in the plant-based food industry to obtain meat-like textures from different vegetal protein sources. The aim of this study was to evaluate the impact of extrusion process parameters (water feeding rate, barrel temperature and screw speed) on the texture and moisture content of high moisture extrudates (HME) from pea protein isolate using response surface methodology. Sensory textural profile of selected HME was compared with those of cooked chicken breast and a commercial extruded meat analogue sample. Extrusion process parameters had a significant effect on the characteristics of the final product. Barrel temperatures between 145 °C and 165 °C and a water feed rate between 53% and 57% produced HME with an instrumental texture similar to cooked chicken breast, 165 °C and 55% water feed being the conditions that produced the HME with the highest meat-like appearance and sensory fibrousness. [Display omitted] • Obtainment of meat-like textures from plant-based protein sources is a challenge. • Pea protein isolate extrusion is optimised with response surface methodology. • Temperature and water feed rate influence extrudate texture. • Pea protein extruded with 55% water at 165 °C shows texture most similar to chicken. • Gumminess and moisture mouthfeel of extrudates needs to be improved. [ABSTRACT FROM AUTHOR]

The use of pea protein in dense food is limited because of the low gel strength. Commercial pea proteins were modified with phenolics under alkaline conditions (pH 9, 24 h) that favour covalent bonding. Three phenolic compounds that differ in molecular size but contain similar structural units were selected (gallic acid, 0.17 kDa; epigallocatechin gallate, 0.458 kDa; tannic acid, 1.71 kDa) to better understand the role of molecular weight and added hydroxyl and aromatic groups on the gelling properties. The effect of the dose on gelling properties was studied by varying the phenolic concentrations (0–4 mM). The maximum changes were observed for conjugates prepared with tannic acid: colour, Δ E 38; decreased concentration of binding sites, 43%; solubility, 31%. The maximum increase in gel strength was 16-fold from 3.0 to 48 kPa. The result was positively correlated with the mass concentration of the added phenolic compounds, molecular weight and the approximate number of hydroxyl groups. Modification of pea proteins with phenolics can be as effective as adding thickening agents to increase the gel strength. To increase the elasticity of pea protein gel, the phenolic concentration added should not exceed 1.36 g/L, which is equal to 3.8 wt% of the protein mass. We demonstrated that pea protein modification with phenolics makes a useful tool to tailor gel strength and elasticity based on the molecular weight and the dose of phenolic compounds added. [Display omitted] • Conjugation of pea proteins with phenolic compounds decreased protein solubility. • Gel strength increased after pea protein modification with phenolics. • Gel strength scaled with concentration and molecular weight of added phenolic. • Elasticity decreased after surpassing a critical modification level. • Moderate modification is promising to tailor the properties of pea proteins. [ABSTRACT FROM AUTHOR]

Oral delivery systems for nutrients and nutraceuticals are required for personalized nutrition applications. In some applications, these delivery systems need to encapsulate both hydrophilic and hydrophobic bioactive agents. In this study, bigel beads (2 mm) were prepared using pea protein (PP) and sodium alginate (SA) to form the hydrogel phase, and glyceryl monostearate and soybean oil to form the oleogel phase. The hydrogel phase was crosslinked by using Ca2+ ions to form electrostatic bridges between the alginate molecules. The bigel beads had an oil-in-water type structure consisting of an oleogel dispersed phase within a hydrogel continuous phase. These beads were used to encapsulate and control the release of model hydrophobic (curcumin) and hydrophilic (epigallocatechin gallate) nutraceuticals. The textural and microstructural characteristics of the bigel beads were evaluated by dynamic shear rheology, textural profile analysis, cryo-electron microscopy, and fluorescence confocal microscopy. As the concentration of SA increasing from 0.2 to 1.0%, the hardness of bigel beads increased from 306.75 g to 792.40 g. In vitro digestion experiments showed that most of the nutraceuticals were released in the small intestine, rather than the stomach. Nutraceutical release could be controlled by manipulating bead composition, with the extent of nutraceutical release decreasing with increasing alginate concentration. The bigel beads developed in this study could be used as easy-to-swallow carriers for the controlled release of hydrophilic and hydrophobic bioactive ingredients. These kinds of products may be especially useful for people with dysphagia. [Display omitted] • Core-shell bigel beads (2 mm) were prepared from food grade biopolymers. • The hydrogel part consisted of Ca2+-crosslinked pea protein and alginate. • The oleogel part consisted of glyceryl monostearate and soybean oil. • Bigel beads could encapsulate hydrophilic and hydrophobic active ingredients. • The release characteristics could be manipulated by altering alginate level. [ABSTRACT FROM AUTHOR]

O/W/O double emulsions are an advanced oil-structuring approach that has been attracting considerable interest in recent years. However, their structural characteristics remain unsolved compared to conventional W/O emulsions. To clarify the differences from a multi-scale perspective, we prepared W/O emulsions and O/W/O double emulsions with the same components. For the stabilization of the O/W interface, modified pea protein isolate (MPPI) was utilized. A combination of polyglycerol polyricinoleate (PGPR) and beeswax (BW) was used for the stabilization of the W/O emulsions. Then, texture and oil binding capacity (OBC), rheological properties, and microstructure of emulsions were recorded to compare the differences samples. Results showed that all the emulsions kept excellent storage stability and similar crystallization and melting profiles over two weeks of storage. Interestingly, texture exhibited significant variations, with oleogelled O/W/O double emulsions possessing an improved firmness and OBC compared to W/O emulsions. This was probably caused by a larger fraction of the dispersed phase and a higher wax concentration in the outer oil phase. Further, the stabilization mechanism of the emulsions was illustrated. BW, in synergy with PGPR, could stabilize the oil-water interface as Pickering particles, providing a physical barrier to improve the emulsion stability. Also, BW acted as the gelator of the bulk phase, forming a viscoelastic network to support the structural function of the emulsions. Additionally, the droplet-droplet interaction caused by the dispersed phase could promote the formation of the gelling network. Altogether, this research provides a multi-scale fundamental understanding on the structural comparison between W/O and O/W/O double emulsions, and indicates that O/W/O double emulsions with less wax or gelator content can achieve the same structural functionality as W/O emulsions, thus presenting superior industrial potential. • W/O and O/W/O beeswax-based emulsions were successfully formulated. • The differences in structural characteristics of different emulsions were initially compared. • O/W/O double emulsions possessed a stronger network than W/O emulsions. • The stabilization mechanism of BW-based emulsions was comprehensively illustrated. [ABSTRACT FROM AUTHOR]

This study aimed to assess the antioxidant activity of golden chlorella (GoC) and grape pomace (GrP) extracts both in vitro and in pea protein-based extrudates. We hypothesized that GoC/GrP would limit oxidation of proteins in the extrudates compared with commercial antioxidants. The results showed that GoC extract was effective in metal chelation and GrP extract possessed excellent radical scavenging activity and reducing power. Protein oxidation inevitably occurred after low-moisture extrusion in terms of elevated level of protein carbonyls and the gradual loss of thiols. LC-MS/MS revealed that the monoxidation and 4-hydroxynonenal adduction were the major oxidative modifications, and legumin was the most susceptible globulin for oxidation. The GoC/GrP extracts effectively retarded the oxidation progress in extrudates by lower intensity of oxidized peptides, whereas protein electrophoretic profiles remained unaffected. This study highlighted the great potential of GoC/GrP as natural antioxidants in plant-based foods. • Low-moisture extrusion induced site-specific protein oxidation. • Monoxidation and lipoxidation were the major oxidative modifications of extrudates. • Golden chlorella and grape pomace extract inhibited protein oxidation in extrudates. [ABSTRACT FROM AUTHOR]

The present study investigated the effects of low protein diets with different starch sources and starch to protein ratio on growth, digestibility, intestinal health, caecal short chain fatty acids (SCFAs), serum cholesterol and triglycerides in broiler chickens. Eight hundred one-day-old male broiler chicks (Ross 308) were randomly allotted to one of 4 dietary treatments with 10 repeats and 20 birds in each repeat. The dietary treatments included 1) a standard protein corn-SBM based diet (SP), 2) a low protein corn-SBM based diet (LPI) without reduced starch: protein ratio, 3) a low protein corn-SBM based diet (LPII) with reduced starch: protein ratio, and 4) a low protein corn-SBM-peas based diet (LPP) and reduced starch: protein ratio. Soy hulls were added in the LPII and LPP diets to reduce starch: protein ratio. During the experiment period from 11 to 24 d, FI was not affected by the dietary treatments (P > 0.05). The BWG was significantly reduced in the LPI diet compared to the SP diet (P < 0.05). Likewise, FCR deteriorated in LPI and LPII but was better in the SP diet followed by the LPP diet (P < 0.05). The apparent total tract digestibility (ATTD) of dry matter (DM) varied significantly among the dietary treatments (P < 0.01). While ATTD of starch was similar for all the diets except the LPP diet wherein the ATTD of starch was significantly lower (P < 0.001). Ether extract digestibility was also significantly different between the SP and LPII dietary treatments (P < 0.01). The AME and AME n values were significantly lower in the LPP diet compared with other dietary treatments (P < 0.001). Nitrogen retention (%) was increased in all the LP diets compared with the SP diet (P < 0.001), but it was significantly better in both LPII and LPP diets compared to the LPI diet. The data showed that cecal SCFAs production was increased in the LPII and LPP compared to the SP and LPI diets (P < 0.001). Further, the production of acetic, butyric, and propionic acids was substantially higher in the LPP diet (P < 0.001). There was no significant difference in gene expression of Claudin-1 and ZO-1 (P > 0.05). However, MUC-2 and GLUT-1 gene expression were significantly downregulated in the LPI diet (P < 0.05). The concentration of cholesterol and triglycerides was significantly increased in the LPI diet (P < 0.001). In conclusion, the addition of peas as a slowly digestible starch source combined with soy hulls in low protein diet helped to partly recover the growth performance and improved cecal SCFAs production compared to other low protein diets with and without reduced starch: protein ratio in broiler chickens. [ABSTRACT FROM AUTHOR]

Pea flour and a blend of pea starch and protein isolate with a starch-to-protein ratio close to 2/1 were processed using co-rotating twin-screw extruders. Different extruder scales operated at a moisture content of 18-35% and a screw speed of 120-700 rpm resulted in large intervals of melt temperature T (95-165 °C) and specific mechanical energy SME (150-2000 ki/kg). With increasing T and SME, starch solubility in water increased due to starch melting and depolymerisation, and protein solubility in SDS decreased due to formation of protein aggregates linked by disulphide bonds. Extruded foods' morphology was studied by CLSM. Protein cross-linking increased the median size of protein aggregates; starch destructuration increased the area of the starch phase to the detriment of the protein one. Melt shear viscosity was determined using a pre-shearing capillary rheometer. The melts exhibited shear-thinning behaviour according to a power-law model, with values close to those of model parameters observed for pea flour and SP 2/1 blend. The rheological model was implemented in a lD global extrusion model to simulate pea ingredient extrusion. Satisfactory correlations between predicted extrusion variables (T, SME) and biopolymer transformation suggested that products with target structure can be obtained using simulation to tune extrusion conditions. [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]