Fabrication of high internal phase emulsions (HIPEs) using pea protein isolate-hyaluronic acid-tannic acid complexes: Application of curcumin-loaded HIPEs as edible inks for 3D food printing.

Pea protein isolate (PPI)-hyaluronic acid (HA)-tannic acid (TA) ternary complexes were assembled using non-covalent interactions, their potential application in 3D printing and delivery of curcumin were investigated. As the HA-to-TA ratio in the complexes changed from 1:0 to 0:1, the oil-water interfacial tension first decreased and then increased, and the secondary structure of the proteins changed. The composition of the complexes (HA-to-TA ratio) was optimized to produce high internal phase emulsions (HIPEs) containing small uniform oil droplets with good storage and thermal stability. When the HA to TA ratio is 7:1 (P-H7-T1), HIPEs exhibited better viscosity, viscoelasticity, and thixotropy, which contributed to its preferable 3D printing. Moreover, curcumin-loaded HIPEs stabilized by P-H7-T1 showed a high lipid digestibility (≈101%) and curcumin bioaccessibility (≈79%). In summary, the PPI-HA-TA-stabilized HIPEs have good potential to be 3D-printable materials that could be loaded with bioactive components.

Texture improvement and in vitro digestion modulation of plant-based fish cake analogue by incorporating hydrocolloid blends.

Hydrocolloids have proven effective in improving the texture of surimi gels, yet their application in plant-based seafood analogues remains underexplored. This study aimed to develop a hydrocolloid blend comprising methylcellulose (MC), curdlan gum (CG), and high-acyl gellan gum (GG) to achieve a surimi-like texture in plant-based fish cakes (PBFC) made from brown rice and pea protein isolates. The research showcased that higher MC concentration boosted protein powder's heated oil holding capacity, while CG concentration increments lowered it. However, heated water holding capacity remained stable despite changes in MC and GG levels. Incorporating hydrocolloids elevated PBFC moisture content, decreasing expressible moisture and oil amounts with rising MC, CG and GG concentrations. PBFC hardness increased with higher hydrocolloid levels and was influenced by temperature, while springiness remained unaffected. GG helped maintain storage modulus (G') during PBFC cooling at higher concentrations, whereas the opposite effect was observed for MC. Analytically, higher MC concentrations reduced protein digestibility, while increased GG concentrations appeared to enhance it. Microstructural analysis corroborated these findings, with more protein aggregates in PBFC containing 3.8% MC and fewer in PBFCs with 6% CG and 3% GG. Consumer evaluations indicated that PBFC formulated with 1% MC, 3% CG, and 1.5% GG matched the springiness of commercial surimi-tofu fish cake, though it received slightly lower overall liking scores. In conclusion, the combined use of these three hydrocolloids demonstrated the potential to enhance the physical properties of PBFC and modify protein digestibility, offering insights into the development of innovative plant-based seafood analogues.

Novel organic-inorganic composite pea protein silica food-grade aerogel materials: Fabrication, mechanisms, high oil-holding property and curcumin delivery capacity.

The fragility of the skeleton and poor bioaccessibility limit Silica aerogel's application in the food industry. In this study, composite gels were obtained by cross-linking pea proteins isolate (PPI) with Tetraethoxysilane (TEOS)to improve the bioavailability of silica-derived aerogels. It indicated that TEOS first condensed with H+ to form secondary particles and then complexed with PPI via hydroxyl groups to form a composite aerogel. Meanwhile, the PPI-Si composite aerogel formed a dense mesoporous structure with a specific surface area of 312.5 g/cm3. This resulted in a higher oil holding percentage of 89.67 % for the PPI (10 %)-Si aerogel, which was 34.1 % higher than other studies, leading to a more stable oleogel. Finally, as a delivery system, the composite oleogel not only could significantly increase the bioaccessibility rate by 27.4 % compared with silica aerogel, but also could efficiently inhibit the premature release of curcumin in the simulated gastric fluids, while allowed sustainably release in the simulated intestinal fluids. These results provided a theoretical basis for the application of silica-derived aerogels in food and non-food applications.

High internal phase double emulsions stabilized by modified pea protein-alginate complexes: Application for co-encapsulation of riboflavin and ß-carotene.

The application of many hydrophilic and hydrophobic nutraceuticals is limited by their poor solubility, chemical stability, and/or bioaccessibility. In this study, a novel Pickering high internal phase double emulsion co-stabilized by modified pea protein isolate (PPI) and sodium alginate (SA) was developed for the co-encapsulation of model hydrophilic (riboflavin) and hydrophobic (ß-carotene) nutraceuticals. Initially, the effect of emulsifier type in the external water phase on emulsion formation and stability was examined, including commercial PPI (C-PPI), C-PPI-SA complex, homogenized and ultrasonicated PPI (HU-PPI), and HU-PPI-SA complex. The encapsulation and protective effects of these double emulsions on hydrophilic riboflavin and hydrophobic ß-carotene were then evaluated. The results demonstrated that the thermal and storage stabilities of the double emulsion formulated from HU-PPI-SA were high, which was attributed to the formation of a thick biopolymer coating around the oil droplets, as well as thickening of the aqueous phase. Encapsulation significantly improved the photostability of the two nutraceuticals. The double emulsion formulated from HU-PPI-SA significantly improved the in vitro bioaccessibility of ß-carotene, which was mainly attributed to inhibition of its chemical degradation under simulated acidic gastric conditions. The novel delivery system may therefore be used for the development of functional foods containing multiple nutraceuticals.

Exploring the effect of corn starch/pea protein blending on the physicochemical and structural properties of biopolymer films and their aging resistance.

This study investigated the potential effect of blending corn starch and pea protein isolate in various ratios (100:0, 70:30, 50:50, 30:70, and 0:100) on the aging properties of biodegradable films. Unlike previous research, the focus was on the often-overlooked aspect of film aging. Fourier-transform infrared spectroscopy and X-ray diffraction demonstrated the physical blending of corn starch and pea protein, along with chemical bonding and conformational changes. The optical and microstructural properties showed the formation of smooth, homogeneous films with good compatibility between the polymers. The water resistance, barrier, and mechanical properties corresponding to the intrinsic nature of protein polymers showed a minimized fluctuations in film properties as film ages, with a reduction of at least twice when protein is added. Remarkably, the blend with a ratio of 30:70 demonstrated the most stable properties during aging. These results demonstrated that blending the pea protein isolate was favorable for delaying the retrogradation and recrystallization of corn starch films. Understanding how these blends influence the aging characteristics of films is not only a novel contribution to the scientific community but also holds practical significance, potentially opening a potential for applications in various industries.

14C-Isotope Use to Quantify Covalent Reactions between Flavor Compounds and ß-Lactoglobulin.

A 14C-based method was developed to study the rate and extent of covalent bond formation between ß-lactoglobulin and three model flavor compounds: a ketone (2-undecanone UDO), an aldehyde (decanal DAL), an isothiocyanate (2-phenylethyl isothiocyanate PEITC), and an unreactive "methods blank" (decane DEC). Aqueous protein solutions with one of the 14C-labeled model flavor compounds were placed in water baths at 25, 45, and 65 °C for 4 weeks measuring the amount of flavor: protein reaction at 1, 3, 7, 14, 21, and 28 days. UDO showed lowest reactivity (max of 0.9% of added compound reacted), DAL (max of 16.4% reacted), and PEITC (max of 71.8% reacted). All compounds showed a rapid initial reaction rate which slowed after ca. 7 days. It appears that only PEITC (at 65 °C) saturated all potential protein-reactive sites over the storage period.

Role of pea protein isolate in modulating pea starch digestibility: insights from physicochemical and microstructural analysis.

BACKGROUND: Understanding the interactions between protein and starch is crucial in revealing the mechanisms by which protein influences starch digestibility. The present study investigated the impact of different contents of pea protein isolate (PPI) on the physicochemical properties and digestibility of pea starch (PS). RESULTS: The results demonstrated that as the content of PPI increased from 0% to 12%, and the digestion of PS decreased by 12.3%. Rheological analysis indicated that PPI primarily interacted with molecular chains of PS through hydrogen bonds. Increasing the content of PPI resulted in a 30.6% decrease in the hardness of the composite gels, accompanied by a 10% reduction in the short-ordered structure of PS. This hindered the formation of molecular aggregation and resulted in a loose and disordered gel network structure. The microstructure confirmed that the attachment of PPI to PS served as a physical barrier, impeding starch digestibility. CONCLUSION: In summary, the primary mechanism by which PPI inhibited PS digestion involved steric hindrance exerted by PPI and its interaction with PS via hydrogen bonds. These findings contribute to a better understanding of the interaction mechanisms between PS and PPI and offer insights for the optimal utilization of pea resources. © 2024 Society of Chemical Industry.

Modification of soy protein isolate and pea protein isolate by high voltage dielectric barrier discharge (DBD) atmospheric cold plasma: Comparative study on structural, rheological and techno-functional characteristics.

The modification in structural, rheological, and techno-functional characteristics of soy and pea protein isolates (SPI and PPI) due to dielectric barrier discharge cold plasma (DBD-CP) were assessed. The increased carbonyl groups in both samples with cold plasma (CP) treatment led to a reduction in free sulfhydryl groups. Moreover, protein solubility of treated proteins exhibited significant improvements, reaching up to 59.07 % and 41.4 % for SPI and PPI, respectively, at 30 kV for 8 min. Rheological analyses indicated that storage modulus (G') was greater than loss modulus (G″) for CP-treated protein gels. Furthermore, in vitro protein digestibility of SPI exhibited a remarkable improvement (4.78 %) at 30 kV for 6 min compared to PPI (3.23 %). Spectroscopic analyses, including circular dichroism and Fourier Transform-Raman, indicated partial breakdown and loss of α-helix structure in both samples, leading to the aggregation of proteins. Thus, DBD-CP induces reactive oxygen species-mediated oxidation, modifying the secondary and tertiary structures of samples.

Ultra-stable pickering emulsion stabilized by anisotropic pea protein isolate-fucoidan conjugate particles through Maillard reaction.

Bio-based emulsifiers hold significant importance in various industries, particularly in food, cosmetics, pharmaceuticals and other related fields. In this study, pea protein isolate (PPI) and fucoidan (FUD) were conjugated via the Maillard reaction, which is considered safe and widely used in the preparation of food particle. The PPI-FUD conjugated particles exhibit an anisotropic non-spherical structure, thereby possessing a high detachment energy capable of preventing emulsion coalescence and Ostwald ripening. Compared to emulsions previously prepared in other studies (< 500 mM), the Pickering emulsion stabilized by PPI-FUD conjugate particles demonstrates outstanding ionic strength resistance (up to 5000 mM). Furthermore, when encapsulating curcumin, the Pickering emulsion protects the curcumin from oxidation. Additionally, the formulated emulsions demonstrated the capability to incorporate up to 60 % (v/v) oil phase, revealing remarkable performance in terms of storage stability, pH stability, and thermal stability.

The effects of resonance acoustic mixing modulation on the structural and emulsifying properties of pea protein isolate.

The effects of resonant acoustic mixing (RAM) with different treatment times (0, 5, 10, 15, 20 and 30 min) on the structural and emulsifying properties of pea protein isolate (PPI) were investigated for the first time. Increasing the RAM treatment time from 0 to 20 min decreased the α-helix/ß-sheet ratio and particle size of the PPI samples by 37.84 % and 46.44 %, respectively, accompanied by an increase in solubility from 54.79 % to 71.80 % (P < 0.05). Consequently, the emulsifying activity index of PPI (from 10.45 m2/g to 14.2 m2/g) and the physical stability of RAM-PPI emulsions were effectively enhanced, which was confirmed by the small and uniformly distributed oil droplets in the micrographs of the emulsions. However, excessive RAM treatment (30 min) diminished the effectiveness of the aforementioned improvements. Therefore, obviously enhanced solubility and emulsifying properties of PPI can be attained through proper RAM treatment (15-20 min).

Fermentation of Texturized Pea Protein in Combination with Proteases for Aroma Development in Meat Analogues.

The potential use of texturized pea protein in meat analogues was investigated by comparing the effects of fermentation on pea and myofibrillar pork proteins in a model system including additives, microbial starters, and proteases. Model fermentation was controlled for 15 days by a pH decrease and microbial count and free amino acid increase. Besides, volatile production and sensory properties were evaluated at the end of fermentation. Protein type affected free amino acid generation and volatile profile. Models supplemented with proteases showed an increase in amino-acid-derived compounds (branched aldehydes and alcohols) and fruity odor notes. During fermentation, protease addition significantly reduced the production of linear aldehydes (pentanal, hexanal, and octanal) in vegetal models, while pyrazine compounds were not affected. This changes in the volatile profile reduced the legume beany odor but increased the perception of toasted cereal-like notes generated by the texturization process.

Konjac glucomannan-assisted fabrication of stable emulsion-based oleogels constructed with pea protein isolate and its application in surimi gels.

Konjac glucomannan (KGM) is widely used as a stabilizer for the structuring of highly unsaturated oils. This study aimed to investigate the changes in structure and functional properties of soybean oil - based oleogels (emulsion template method) prepared with different amounts of KGM-modified pea isolate protein (PPI). The findings revealed that the oleogels formed three - dimensional networks through van der Waals interactions and hydrogen bonding between the stretched PPI and KGM. As the amount of KGM increased, the oil droplets were more uniformly dispersed within the continuous PPI - KGM rigid network, especially when the ratio of PPI to KGM was 4:1. This formulation also showed the highest thixotropy (73.2 %) and the best oil binding capacity (94 %). Cryo - SEM revealed that the oleogel - prepared surimi gels successfully enclosed oil droplets in a dense matrix through a dual stabilization mechanism. Additionally, the incorporation of oleogels significantly improved the textural properties of surimi in comparison to directly adding oil.

Impact of κ-Carrageenan on the Cold-Set Pea Protein Isolate Emulsion-Filled Gels: Mechanical Property, Microstructure, and In Vitro Digestive Behavior.

More understanding of the relationship among the microstructure, mechanical property, and digestive behavior is essential for the application of emulsion gels in the food industry. In this study, heat-denatured pea protein isolate particles and κ-carrageenan were used to fabricate cold-set emulsion gels induced by CaCl2, and the effect of κ-carrageenan concentration on the gel formation mechanism, microstructure, texture, and digestive properties was investigated. Microstructure analysis obtained by confocal microscopy and scanning electron microscopy revealed that pea protein/κ-carrageenan coupled gel networks formed at the polysaccharide concentration ranged from 0.25% to 0.75%, while the higher κ-carrageenan concentration resulted in the formation of continuous and homogenous κ-carrageenan gel networks comprised of protein enriched microdomains. The hydrophobic interactions and hydrogen bonds played an important role in maintaining the gel structure. The water holding capacity and gel hardness of pea protein emulsion gels increased by 37% and 75 fold, respectively, through increasing κ-carrageenan concentration up to 1.5%. Moreover, in vitro digestion experiments based on the INFOGEST guidelines suggested that the presence of 0.25% κ-carrageenan could promote the digestion of lipids, but the increased κ-carrageenan concentration could delay the lipid and protein hydrolysis under gastrointestinal conditions. These results may provide theoretical guidance for the development of innovative pea protein isolate-based emulsion gel formulations with diverse textures and digestive properties.

Enhanced functional properties of pea protein isolate microgel particles modified with sodium alginate: Mixtures and conjugates.

Protein microgels are emerging as versatile soft particles due to their desirable interfacial activities and functional properties. In this study, pea protein isolate microgel particles (PPIMP) were prepared by heat treatment and transglutaminase crosslinking, and PPIMP were non-covalently and covalently modified with sodium alginate (SA). The effects of polymer ratio and pH on the formation of PPIMP-SA mixtures and conjugates were investigated. The optimal ratio of PPIMP and SA was found to be 20:1, with the optimal pH being 7 and 10, respectively. PPIMP-SA conjugates were prepared by Maillard reaction. It was found that ultrasound (195 W, 40 min) enhanced the degree of glycation of PPIMP, with a highest value of 37.21 ± 0.71 %. SDS-PAGE, browning intensity and FTIR data also confirmed the formation of PPIMP-SA conjugates. Compared with PPIMP and PPIMP-SA mixtures, PPIMP-SA conjugates exhibited better thermal stability, antioxidant, emulsifying and foaming properties, which opens up opportunities for protein microgel in various food applications.

Chemical acylation of pea protein isolate hydrolysate with fatty acid N-hydroxysuccinimide esters: Effect on structure and functional properties.

Applications of pea protein in the food industry have been greatly restricted by its poor functional properties. In order to solve this problem, a novel technique combining enzymatic hydrolysis and fatty acid acylation has been applied in this work to construct a pea protein-fatty acid covalent complex that aims to improve its functional properties. The processed pea protein with increased water solubility tends to decrease the chance of self-aggregation. Additionally, emulsifying and antioxidant properties have also been found after this process. On top of that, the modified pea protein has been characterized by Fourier transform infrared and circular dichroism spectroscopy. These results demonstrate that these properties were mainly caused by the acylation of the amino group from hydrolyzed pea protein and the carboxyl group from the fatty acid. The enzymatic hydrolysis/fatty acid acylation research provides insights into manufacturing high-quality functional lipoproteins from inexpensive pea protein for the food industry.

Physicochemical Quantitative Analysis of the Oil-Water Interface as Affected by the Mutual Interactions between Pea Protein Isolate and Mono- and Diglycerides.

As a commercially available ingredient, the mono- and diglycerides (MDG) were widely used in a plant protein-based emulsion to provide effective, functional, emulsifying properties. The simultaneous addition of the MDG and pea protein isolate (PPI) was investigated by the methods of interfacial rheology and quantitative protein proteomics. The physicochemical quantitative analysis of the oil-water interface revealed an interfacial stability mechanism for the protein adsorption layer. For a low MDG concentration, the interfacial quantities of vicilin and albumin were increased, which could be attributed to the adsorption rate. For a high MDG concentration, both vicilin and albumin were displaced by MDG and desorbed from the interface, while legumin was more difficult to displace due to its slow adsorption and the complex structure of protein molecules. The protein molecules with the structural rearrangement interacted with MDG, exhibiting potential effects on the interfacial film structure. Combined with some nanotechnologies, the new comprehension of protein-emulsifier interactions may promote food delivery systems. The research aims to develop an in-depth analysis of interfacial proteins, and provide more innovative and tailored functionalities for the application of the plant protein emulsion.

Effect of ultrasonic frequency on the structural and functional properties of pea protein isolation.

BACKGROUND: Pea protein, as a by-product of peas (Pisum sativum L.), is rich in a variety of essential amino acids that can meet the body's protein needs and is a valuable source of protein. Since the function of pea protein is closely related to its structure, pea protein has been subjected to different modifications in recent years to improve its application in food and to develop new products. RESULTS: The effects of sonication frequency (primary and secondary time) on pea protein isolate's (PPI's) structural and functional properties were investigated. Sodium dodecyl sulfate polyacrylamide gel electrophoresis demonstrated that different sonication frequencies at the same power (600 W) treatment had no effect on PPI's molecular weight. Fourier-transform infrared spectroscopy revealed that treatment at different sonication frequencies caused secondary structural changes in PPI. The particle size distribution, foaming, stability, surface hydrophobicity, emulsification, and oxidation resistance of PPI were improved after primary and secondary sonication, but secondary sonication was not more effective than primary sonication for an extended period of time. CONCLUSION: Overall, ultrasound is able to improve the structural and functional properties of pea proteins within a suitable range. It provides a theoretical basis for elucidating the modification of the structure and function of plant proteins by ultrasound and lays the foundation for the development of plant proteins in food applications as well as development. © 2023 Society of Chemical Industry.

pH-driven preparation of pea protein isolate-curcumin nanoparticles effectively enhances antitumor activity.

Soluble pea protein isolate-curcumin nanoparticles were successfully prepared at a novel pH combination, with encapsulation efficiency and drug loading amount of 95.69 ± 1.63 % and 32.73 ± 0.56 µg/mg, respectively, resulting in >4000-fold increase in the water solubility of curcumin. The encapsulation propensity and interaction mechanism of pea protein isolates with curcumin and colchicine were comparatively evaluated by structural characterization, molecular dynamics simulations and molecular docking. The results showed that the nanoparticles formed by curcumin and colchicine with pea protein isolates were mainly driven by hydrogen bonding and hydrophobic interactions, and the binding process did not alter the secondary structure of pea protein. In contrast, pea protein isolate-curcumin nanoparticles exhibited smaller particle size, lower RMSD value, lower binding Gibbs free energy and greater structural stability. Therefore, pea protein isolate is a suitable encapsulation material for hydrophobic compounds. Furthermore, the pea protein isolate-curcumin nanoparticles showed remarkably enhanced antitumor activity, as evidenced by a significant reduction in IC50, and the anti-tumor mechanism of it involved the ROS-induced mitochondria-mediated caspase cascade apoptosis pathway. These findings provide insights into the development of pea protein-based delivery systems and the possibility of a broader application of curcumin in antitumor activity.

pH-responsive color-indicating film of pea protein isolate cross-linked with dialdehyde carboxylated cellulose nanofibers for pork freshness monitoring.

The limited mechanical performance and responsiveness of protein-based smart packaging materials have hindered their development. To address these issues, this study prepared a pH-responsive smart film by introducing dialdehyde carboxylated cellulose nanofibers (DCCNFs) as the cross-linking agent capable of covalently reacting with proteins, and bilberry extract (BE) as a pH-responsive indicator into pea protein isolate (PPI) matrix. The results demonstrated that adding DCCNF and BE enhanced the PPI film's thermal stability, density, and UV barrier properties. Tensile tests revealed significant improvements in both tensile strength and elongation at the break for the resulting film. Furthermore, films containing DCCNF and BE exhibited lower moisture content, swelling ratio, water vapor permeability, and relative oxygen transmission compared to PPI films. Notably, the anthocyanins in BE endowed the film with visual color changes corresponding to different pH values. This feature enabled the film to monitor pork freshness; a transition from acidic to alkaline in pork samples was accompanied by a color change from brown to brownish green in the film as storage time increased. Overall, these findings highlight that this developed film possesses excellent physicochemical properties and sensitive pH response capabilities, making it a promising candidate for future smart packaging applications.

Synergistic effects of microbial transglutaminase and apple pectin on the gelation properties of pea protein isolate and its application to probiotic encapsulation.

The low gelation capacity of pea protein isolate (PPI) limits their use in food industry. Therefore, microbial transglutaminase (MTG) and apple pectin (AP) were combined to modify PPI to enhance its gelling characteristics, and the mechanism of MTG-induced PPI-AP composite gel generation was investigated. PPI (10 wt%) could not form a gel at 40 °C, while MTG-treated PPI (10 wt%) formed a self-supporting gel at 40 °C. Subsequently, the addition of AP further promoted the crosslinking of PPI and significantly improved the water holding capacity, rheology, and strength of PPI gels, which was attributed to both hydrogen and isopeptide bonds in the composite gel. Additionally, the PPI-AP composite gel showed excellent protection ability, and the survival rate of probiotics could reach over 90%, which could be used as an effective delivery system. This study verified that MTG and AP were efficient in enhancing the functional quality of PPI gels.