Search Results (159)

The broader application of gluten in both the food and non-food industries is limited by its lack of functional properties, such as solubility, foaming ability, and rheological characteristics. This study aimed to evaluate the physicochemical properties of proteins in various gluten products and to investigate the effects of enzymatic hydrolysis and ultrasound (US) treatment on wheat flour gluten yield, gliadin–glutenin complex structure, and gelation properties. The gelation properties of wheat gluten (GL)/pea protein (PP) treated with US and transglutaminase (TG) were studied. The results demonstrated that the ratio of low- to high-molecular-weight components in gliadins and glutenins significantly influenced the quality of commercial gluten products. A 90 min treatment of wheat flour with 24 TGU/100 g increased the yield of high-quality gluten by 32% while reducing the gliadin content by up to 6-fold. Additionally, a 30 min US treatment of 18–20% pure gluten suspensions yielded a sufficiently strong gel. The addition of PP isolate (80% protein) improved the texture of gluten gels, with the best results observed at a GL:PP ratio of 1:2. The application of TG increased the hardness, consistency, and viscosity of GL-PP gels by an average of 5.7 times while reducing stickiness. The combined TG and US treatments, along with the addition of PP, notably increased the levels of lysine, isoleucine, and tryptophan, thereby enhancing both the nutritional quality and amino acid balance of the final product. Full article

Microbeads of raspberry extract were produced using encapsulation matrices alginate + pea protein isolate + psyllium mucilage, alginate + pea protein isolate + psyllium mucilage + okra, and alginate + pea protein isolate + psyllium mucilage + Aloe ferox gel + gallic acid using freeze-drying method. The microbeads were characterised and assessed for their effectiveness on the release, bioaccessibility, of anthocyanin components and antioxidant activities during in vitro digestion. Alginate + pea protein isolate + psyllium mucilage + Aloe ferox gel + gallic acid matrix showed the highest encapsulation efficiency of 91.60% while the lowest encapsulation efficiency was observed in alginate + pea protein isolate + psyllium mucilage + okra (69.94%). Scanning electron microscope images revealed spherical shapes and varying surface morphologies for different encapsulation matrices. Despite the differences observed in Fourier transform infrared spectra, microbeads showed similar thermal degradation patterns. X-ray diffractograms showed amorphous structures for different encapsulation matrices. Comparatively, alginate+ pea protein isolate + psyllium mucilage + Aloe ferox gel + gallic acid microbeads exhibited the highest bioaccessibility for total phenols (93.14%), cyanidin-3-O-sophoroside (54.61%), and cyanidin-3-O-glucoside (55.30%). The encapsulation matrices of different biopolymer combinations (alginate+ pea protein isolate+ psyllium mucilage, alginate + pea protein isolate + psyllium mucilage + okra, and alginate + pea protein isolate + psyllium mucilage + Aloe ferox gel + gallic acid) enhanced anthocyanin stability and protected it against in vitro degradation of bioactive compounds. Full article

The EGCG/PPN composite, prepared by combining pea protein nanofibrils (PPNs) with epigallocatechin gallate (EGCG), could be used as a multifunctional nanocarrier. Compared to pea protein isolate (PPI), EGCG/PPN composites exhibited remarkably higher turbidity and zeta potential, along with similar UV spectra. Intrinsic fluorescence spectroscopy, ThT fluorescence spectroscopy, and surface hydrophobicity analysis suggested that the interactions between EGCG and PPN were primarily driven by hydrophobic forces. UV spectra indicated that the microenvironment of amino acid residues in the tertiary structure of the protein changes upon complexation, and circular dichroism (CD) revealed that the incorporation of EGCG increases the β-sheet content in the protein’s secondary structure. Analyses of DPPH and ABTS radical scavenging activity, as well as reducing power, demonstrated that the synergistic effect between EGCG and PPN did not hinder the inherent antioxidant properties of EGCG but rather enhanced them significantly. Transmission electron microscopy (TEM) images showed that the addition of EGCG reconstructed the fibril morphology, thereby affecting the properties of PPNs. Overall, the composite fabricated through the interaction between PPN and EGCG shows great potential as a nanocarrier in the processing of functional foods. Full article

Anthocyanins (ACNs), characterized by their polyhydroxy structures, exhibit high susceptibility to external environmental factors, which significantly limits their application in the food and industrial sectors. To enhance the stability of anthocyanins, anthocyanin nanoliposomes (ACN-NLs) were developed, with encapsulation efficiency, particle size and zeta potential serving as key evaluation parameters. Furthermore, through layer-by-layer self-assembly and electrostatic interactions, ACN-NLs were modified using synanthrin (SY) and pea protein isolate (PPI). Consequently, PPI-modified ACN-NLs (PPI-ACN-NLs) and SY-PPI-modified ACN-NLs (SY-PPI-ACN-NLs) were successfully synthesized. In this study, the structural characteristics of liposomes were investigated using X-ray diffraction (XRD), their in vitro digestibility was evaluated, and their stability under different temperatures, light conditions, and simulated food system conditions was assessed. The results demonstrated that when the mass ratio of soybean lecithin to cholesterol, soybean lecithin to anhydrous ethanol, and drug-to-lipid ratio were set at 5:1, 3:100, and 3:10, respectively, with an ACN concentration of 4 mg/mL, a pea protein solution with pH 3.0, a PPI concentration of 10 mg/mL, and an SY concentration of 8 mg/mL, the prepared ACN-NLs, PPI-ACN-NLs, and SY-PPI-ACN-NLs exhibited optimal performance. Their respective encapsulation efficiencies were 52.59 ± 0.24%, 83.80 ± 0.43%, and 90.38 ± 0.24%; average particle sizes were 134.60 ± 0.76 nm, 213.20 ± 0.41 nm, and 246.60 ± 0.24 nm zeta potentials were −32.4 ± 0.75 mV, −27.46 ± 0.69 mV, and −16.93 ± 0.31 mV. The changes in peak shape observed via X-ray diffraction (XRD), in vitro digestion profiles, and alterations in anthocyanin release rates under different conditions collectively indicated that the modification of ACN-NLs using SY and PPI enhanced the protective effect on the ACNs, improving their biological activity, and providing a robust foundation for the practical application of ACNs. Full article

Background/Objectives: In recent years, increasing attention has been paid to the stabilization of natural biologically active compounds in order to expand their application in the food, pharmaceutical, and cosmetic industries. Such compounds, such as polyphenols, essential fatty acids, or vitamins, are extremely sensitive to environmental factors. This study aims to review the spray-drying-based microencapsulation technology and its application for stabilizing sensitive biologically active substances. Methods: This article systematically analyzes the main steps of the spray-drying microencapsulation process and discusses traditional and innovative wall materials, including natural polymers (polysaccharides and proteins), as well as new raw material sources (e.g., yeast cells, canola and pea protein isolates, and hemicelluloses). It also examines the potential of these systems for the stimulated release of active ingredients. Results: This review provides a comprehensive overview of the main stages of the spray-drying process and critically examines both conventional (e.g., maltodextrin and gum Arabic) and innovative wall materials (e.g., plant-based proteins and food industry by-products). Studies show that using different wall materials can achieve high encapsulation efficiency, improve the stability of biologically active substances, and control their release. Various compounds have been successfully microencapsulated—polyphenols, essential oils, carotenoids, fatty acids, and vitamins—protecting them from oxidation, light, and temperature. The review identifies key factors that can enhance product quality, increase encapsulation yield, and reduce processing costs and energy input—offering meaningful insights for optimizing the microencapsulation process. Conclusions: Spray-drying-based microencapsulation is an advanced technology that effectively protects sensitive active ingredients and allows for wider industrial food, pharmaceutical, and cosmetic applications. In the future, more attention is expected to be paid to personalized formulations, stimulated release systems, and sustainable wall materials from by-products. Full article

Hydrogels (Hy) were obtained with a ternary system of proteins (pea (P) or soy isolate (S) 2%), guar (0.5%), and xanthan gums (0.5%) and were subjected to thermal treatment (70 °C/20 min or 85 °C/15 min, or not) prior to structure formation. The FTIR spectra of the hydrogels and the turbidity test (spectrophotometrically red at 600 nm) were used for studying protein–polysaccharide interactions. Amplitude sweeps (0.01–100%) and flow behavior tests (0.1–100 s⁻¹) were conducted for structure analysis. Emulgels were obtained by emulsification of the Hy with 40% or 60% sunflower oil. The centrifugal stability and texture (TPA test) of the emulgels were assessed and SND_40% exhibited the highest hardness (5.30 ± 0.23 N). Based on the results, SND_40%, PND_40%, SD70_40%, and PD_70% were chosen as fat-replacing systems in biscuit formulation. The textural, color, and stability attributes of the reformulated samples were compared with a reference containing margarine. Increased hardness and fracturability were determined for the emulgel-based biscuits, while the color parameters were statistically similar to the reference. Thermal treatments applied to enhance protein–polysaccharide interactions increased the structural performances of some emulgels, while their application as fat-replacing systems should be further evaluated since no statistical differences were recorded in the sensory evaluation of the reference and reformulated biscuits. Emulgels with tuned technological properties have the potential to replace saturated fats in foods. Full article

The covalent interactions of polysaccharides and protein can improve the emulsification and stability of Pickering emulsions, which are promising systems for the delivery of active substances. Okra flowers, which commonly represent agricultural waste, have high-viscosity polysaccharides that can be used for the development of protein–polysaccharide-based emulsifiers. In this study, the Maillard reaction was performed under optimized conditions (70 °C, pH 10, and 12 h) with a 1:1 mass ratio to generate pea protein isolate (PPI)–okra flower polysaccharide (OP) conjugate with the highest grafting degree of 22.80 ± 0.26%. The covalent binding of OP facilitated variations in the secondary and tertiary structures of PPI, decreasing its particle size (from 535.70 to 212.05 nm) and zeta-potential (from −30.37 to −44.39 mV). The emulsifying stability of the emulsion stabilized by OP-PPI conjugates was significantly improved due to the formation of a stable interfacial layer, showing an 80.39% increase compared to that of free PPI. Simultaneously, the emulsions prepared with the conjugates demonstrated excellent stability across diverse environmental conditions by enhancing the interaction between the lipid and protein. Moreover, the conjugate-stabilized emulsion not only exhibited a higher encapsulation efficiency of 91.52 ± 0.75% and superior protective efficacy but also controlled the release of apigenin (API) during gastrointestinal digestion, achieving the highest API bioaccessibility (74.58 ± 1.19%). Furthermore, it also contributed to the absorption and transmembrane transport efficiency of API in Caco-2 cells, improving its bioavailability. These results confirmed that covalent conjugation with OP is a valuable strategy for enhancing the emulsifying features of PPI. The PPI–OP emulsion delivery system holds great potential for nutrient delivery. Full article

Respiratory syncytial virus (RSV) is the leading cause of respiratory infections in children. Extracellular vesicles (EVs), released by airway epithelial cells, contain proteins and different families of non-coding RNAs (EV cargo) that can modulate the responses of target cells to viral infection. Nasal mucosa is a primary site of viral entry and the source of EVs present in the upper airway secretions. In this study we characterized proteins, including inflammatory mediators and cytokines, and the piwi-interacting RNA (piRNAs) cargo of EVs isolated from pediatric human nose organoids (HNO) and nasopharyngeal secretions (NPS) positive for RSV. Using Proximity Extension Assay (PEA) and Luminex multi-target arrays, we found significant enrichment in several chemokines and other mediators/biomarkers, including CCL2, CCL20, CXCL5, CX3CL1, CXCL6, MMP-1, MMP-10, uPA, Flt3L, ARNT and CD40 in EVs secreted by RSV-infected HNO compared to control mock HNO. Analysis of NPS samples from RSV infected children revealed that CCL3, CCL20, CXCL8, uPA, VEGFA, were concentrated in the NPS-EV fraction. LC-MS/MS and Gene Ontology indicated that RSV positive NPS-EVs originate from different cellular sources, with the most abundant proteins from neutrophils and epithelial cells. A total of 490 piRNAs were detected by NGS sequencing of small RNA libraries obtained from NPS-EVs, which has not been reported prior to this study. Identification of inflammatory mediators and small non-coding RNAs which are compartmentalized in EVs contributes to understanding mechanisms of virus-mediated pathogenesis in RSV infections. Full article

This study investigated the extraction and colloidal properties of pea protein isolates (PPIs) from four pea cultivars produced in a southern region in Italy. The control PPIs (C-PPIs) were obtained via an alkaline extraction and isoelectric precipitation method and then subjected to ultrasound treatment (US) to yield US-PPIs. The effects of cultivars and sonication on the physicochemical characteristics and emulsifying property of the PPIs were studied. Fourier-transform infrared (FTIR) spectroscopy, colorimetric measurement, dynamic light scattering (DLS), and confocal laser scanning microscopy (CLSM) were applied to characterize the samples. DLS results showed that C-PPIs displayed smaller particle sizes (8.86–15.9 µm) in comparison to US-PPIs (15.8–66.5 µm). DSC data showed that US-PPIs had improved thermal stability compared to control PPIs. FTIR analysis detected differences in the protein secondary structure of the various cultivars and between the native and US-PPIs. Emulsion stability studies indicated that emulsions stabilized with C-PPIs exhibited lower droplet sizes, implying improved stability in comparison to emulsions stabilized with US-PPIs. In conclusion, PPIs can be successfully extracted from different cultivars and applied as a natural emulsifier. Full article

This study explores the potential of some commercially available plant proteins to increase the protein content of gluten free cookies produced from green lentil flour. Isolates from hemp seed, brown rice, yellow pea, and pumpkin seed were investigated. Cookies were additionally enriched with inulin and matcha tea. Products were characterized in terms of physicochemical parameters (e.g., crude protein content, total phenolics and flavonoids, antioxidant activity, and color). Additionally, technological properties including geometry, baking loss, and texture profile were determined, and a sensory profile test was conducted. The replacement of a quarter of lentil flour with plant proteins increased the protein content (control: 12.4% vs. 15.1–20.4%), but suppressed the polyphenol content, resulting in reduced antioxidant capacity (3.13 vs. 2.14–2.69 mmol TE/100 g). The geometry, texture properties, and color of the cookies were affected by all the proteins investigated. The biggest difference was shown in the case of using yellow pea (YP) protein, which showed the highest browning index (YP: 66.36 vs. 42.63–63.45) and spread ratio (8.38 vs. 5.63–6.39) among the samples tested. The sensory attributes of the cookies, such as tea notes, surface homogeneity, crunchiness, and crumbliness, proved to be negatively affected by the plant proteins, which may be a limitation for consumer acceptance. Full article

While protein-stabilized emulsions have demonstrated potential for various applications in food, their poor lipid oxidation remains a major challenge. The relationship between the architecture of polyphenolic compounds and their capacity to suppress lipid oxidation has not received extensive scrutiny. In this research, pea protein isolate (PPI)–polyphenol complexes were synthesized to examine their capability of maintaining emulsion stability and suppressing lipid oxidation. The collective evidence from fluorescence spectroscopy and molecular dynamics simulations pointed towards non-covalent and self-initiated interactions between the polyphenols and PPI. The presence of additional hydroxyl groups on the polyphenols could significantly boost the extent of these interactions. Specific clusters in PPI and polyphenols which might have formed hydrogen bonds and hydrophobic interactions. Polyphenols also reduced the interfacial tension and increased the surface hydrophobicity of the complex, thus driving more proteins to adsorb at the oil–water interface. The PPI-rosmarinic acid (RA)-stabilized emulsion had a smaller droplet size and higher electrostatic repulsion, enabling it to resist droplet aggregation. This emulsion stood out as having the most robust stability amongst all PPI-polyphenol emulsions and proved highly efficient in preventing lipid oxidation. This study bolsters the viability of employing polyphenol and pea protein-stabilized emulsions in developing new food products. Full article

Mixed extrusion of animal and plant proteins has great potential in meat substitution studies. In this study, we analyzed the mechanism of change in the reorganization of animal and plant proteins during extrusion by exploring the changes in physicochemical properties with different percentages of silkworm chrysalis protein (SCP) additions (3%, 6%, 9%, 12%, 15%) mixed with pea protein isolate (PPI). The results showed that the moderate addition of SCP (12%) reduced the stiffness and denseness of the protein structure of the extrudates, and increased the total amino acid content of the extrudates, up to 74.83. Meanwhile, the addition of SCP changed the rearrangement of the proteins to form new chemical cross-linking bonds with higher bonding energies. Enthalpy of the sample up to 252.6 J/g, enhancing the denaturation energy requirement of the sample. Notably, the addition of SCP weakened the textural properties of the product, resulting in a minimum fibrous degree of 0.88, and improved the overall color of the sample, resulting in an L* value of up to 114.61. Such a change makes the product more suitable for further processing. Scanning electron microscopy (SEM) revealed that the addition of SCP changed the microstructure of the product, resulting in a looser, more porous sample overall. These results systematically elucidate the microscopic mechanisms of SCP and PPI restructuring during high-moisture extrusion. Full article

This study aims to explore the feasibility of using pea protein isolate (PPI)/sodium alginate (SA) complex as a sugar substitute to develop low sugar plant fat cream. Firstly, this study analyzed the influence of SA on the structure and physicochemical properties of PPI and evaluated the types of interaction forces between PPI and SA. The addition of SA effectively induces the unfolding and structural rearrangement of PPI, causing structural changes and subunit dissociation of PPI, resulting in the exposure of internal-SH groups. In addition, the addition of SA increased the content of β-folding in PPI, making the structure of PPI more flexible and reducing interfacial tension. The ITC results indicate that the binding between PPI and SA exhibits characteristics of rapid binding and slow dissociation, which is spontaneous and accompanied by heat release. Next, the effect of PPI/SA ratio on the whipping performance and quality of low sugar plant fat creams was studied by using PPI/SA complex instead of 20% sugar in the cream. When using a PPI/SA complex with a mass ratio of 1:0.3 instead of sugar, the stirring performance, texture, and stability of plant fat cream reach their optimum. Finally, the relevant analysis results indicate that the flexibility and interface characteristics of PPI are key factors affecting the quality of cream. This study can provide theoretical support for finding suitable sugar substitute products and developing low sugar plant fat cream. Full article

The substitution of animal proteins with plant-based ones to fit environmental and economic demands is a challenge in gel applications. This study examined the thermal elation of mixtures of pea protein isolate (PPI) and egg white proteins (EWPs) at different PPI/EWP weight ratios (100/0, 75/25, 50/50, 25/75, 0/100) at pH 7.5 and 9.0. Viscoelastic and texture properties of the composite gels, along with the microstructure and molecular interactions involved in the gel network, were investigated. Except for PPI-EWP 100/0 at pH 9.0, all systems gelled with increasing gel hardness, springiness, and cohesiveness when EWP content increased. This was explained by the microstructure of the gels, wherein the presence of PPI enhanced the formation of aggregates embedded in the EWP network, thus loosening it. The rheological properties of the mixed gels were primarily influenced by the EWP network, involving disulfide bonds. However, upon the addition of PPI, hydrogen bonds and hydrophobic interactions predominated and the structure of the gel became more sensitive to pH as electrostatic repulsions interfered. Adjusting the ratio of PPI/EWP allows the production of gels with varying textures, and suggests the possibility of partially substituting egg white with pea proteins in food gel formulation. Full article

The objective was to determine the digestible indispensable amino acid score (DIAAS) of food sources using the pig model and in vitro procedures. The standardized ileal digestibility (SID) of amino acids (AA) in white rice, wheat, pea protein concentrate (PPC), soy protein isolate (SPI), and skim milk powder (SMP) were determined in pigs. Twelve barrows with an initial body weight of 28.4 kg (standard deviation = 4.0) equipped with a T-cannula at the distal ileum were allotted to a replicated 6 × 5 incomplete Latin square design with six diets and five periods. Five experimental diets contained each ingredient as the only source of AA. Additionally, a nitrogen-free diet was prepared to measure the basal endogenous losses of AA for the calculation of the SID of AA. The in vitro ileal disappearance (IVID) of crude protein (CP) in the five food sources was also determined using the conventional flask procedure and the multi-sample simultaneous in vitro procedure employing the Daisy^II incubator. The DIAAS values for white rice were 42, 50, and 60 for infants, children, and adults, respectively. For wheat, the DIAAS values were 46, 56, and 66, respectively. The DIAAS values for PPC were 47, 58, and 69 for infants, children, and adults, respectively. For SPI, the values were 61, 74, and 87, respectively. The DIAAS for SMP were 82, 112, and 131 for infants, children, and adults respectively. The IVID of CP in SMP was greater (p < 0.05) than that in other sources. The DIAAS calculated based on IVID of CP were similar to those determined based on the SID of AA in pigs. In conclusion, white rice, wheat, pea protein concentrate, and soy protein isolate were observed to have DIAAS values less than 100, indicating that these ingredients need to be combined with other protein sources to meet the indispensable AA requirements. Skim milk powder had a DIAAS greater than 100 for children and adults. Full article