RESUMEN
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.
Asunto(s)
Geles , Gluconatos , Lactonas , Proteínas de Guisantes , Polisacáridos Bacterianos , Reología , Polisacáridos Bacterianos/química , Lactonas/química , Geles/química , Gluconatos/química , Proteínas de Guisantes/química , Concentración de Iones de HidrógenoRESUMEN
This study investigated the effects of pea protein pre-emulsions containing triglyceride- or diglyceride-oil on the emulsifying and gelling properties of low-salt myofibrillar protein (MP). Pea protein isolates treated with pH12-shifting (PPIpH) or ultrasonication (PPIU) demonstrated superior initial interfacial adsorption and higher final interfacial pressure than native pea protein. Within MP/PPI blends, an increased ratio of MP led to a decrease in interfacial pressure, while simultaneously enhancing film elasticity at both polar and non-polar interfaces. Polar diglyceride promoted protein adsorption and fostered interfacial interactions between modified pea proteins and MP, enhancing the cross-linking of transglutaminase (TG) in the composite emulsion gels. Combining diglyceride-type PPIU and PPIpH emulsions with TG increased gel strength to 0.58 N and 0.63 N, respectively, from an initial 0.33 N, yielding a denser protein network with uniformly dispersed oil droplets. Therefore, the utilization of diglyceride and modified PPI can serve as structural enhancers in comminuted meat products.
Asunto(s)
Emulsiones , Geles , Proteínas de Guisantes , Emulsiones/química , Geles/química , Proteínas de Guisantes/química , Miofibrillas/química , Proteínas Musculares/química , Animales , Pisum sativum/química , Productos de la Carne/análisisRESUMEN
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.
Asunto(s)
Interacciones Hidrofóbicas e Hidrofílicas , Proteínas de Guisantes , Concentración de Iones de Hidrógeno , Proteínas de Guisantes/química , Relación Estructura-Actividad , Tensión Superficial , Tamaño de la Partícula , Pisum sativum/química , Agregado de Proteínas , Electricidad EstáticaRESUMEN
This study aims to investigate the effects of interfacial layer composition and structure on the formation, physicochemical properties and stability of Pickering emulsions. Interfacial layers were formed using pea protein isolate (PPI), PPI microgel particles (PPIMP), a mixture of PPIMP and sodium alginate (PPIMP-SA), or PPIMP-SA conjugate. The encapsulation and protective effects on different hydrophobic bioactives were then evaluated within these Pickering emulsions. The results demonstrated that the PPIMP-SA conjugate formed thick and robust interfacial layers around the oil droplet surfaces, which increased the resistance of the emulsion to coalescence, creaming, and environmental stresses, including heating, light exposure, and freezing-thawing cycle. Additionally, the emulsion stabilized by the PPIMP-SA conjugate significantly improved the photothermal stability of hydrophobic bioactives, retaining a higher percentage of their original content compared to those in non-encapsulated forms. Overall, the novel protein microgels and the conjugate developed in this study have great potential for improving the physicochemical stability of emulsified foods.
Asunto(s)
Alginatos , Emulsiones , Interacciones Hidrofóbicas e Hidrofílicas , Microgeles , Proteínas de Guisantes , Alginatos/química , Emulsiones/química , Proteínas de Guisantes/química , Microgeles/química , Tamaño de la Partícula , Pisum sativum/químicaRESUMEN
Entrapping bioactive ingredients like elderberry extract in hydrogels improves their stability and functionality in food matrices. This study assessed the effect of sequential thermal treatment with ultrasound (US) or high hydrostatic pressure (HHP) and treatment duration on pea protein-psyllium hydrogels as elderberry extract carriers. Measurements included color parameters, extract entrapment efficiency, physical stability, textural properties, microrheology, FT-IR, thermal degradation (TGA), SEM images, total polyphenols content, antioxidant activity, and reducing power. The control hydrogel was obtained using only thermal induction. Both treatments impacted physical stability by affecting biopolymer aggregate structures. Thermal and US combined induction resulted in hydrogels with noticeable color changes and reduced entrapment efficiency. Conversely, thermal and HHP-combined induction, especially with extended secondary treatment (10 min), enhanced hydrogel strength, uniformity, and extract entrapment efficiency (EE = 33% for P10). FT-IR and TGA indicated no chemical structural alterations post-treatment. Sequential thermal and HHP induction preserved polyphenol content, antioxidant activity (ABTS = 5.8 mg TE/g d.m.; DPPH = 11.1 mg TE/g d.m.), and reducing power (RP = 1.08 mg TE/g d.m.) due to the dense hydrogel structure effectively enclosing the elderberry extract. Sequential thermal and HHP induction was more effective in developing pea protein-psyllium hydrogels for elderberry extract entrapment.
Asunto(s)
Antioxidantes , Hidrogeles , Presión Hidrostática , Proteínas de Guisantes , Extractos Vegetales , Hidrogeles/química , Extractos Vegetales/química , Proteínas de Guisantes/química , Antioxidantes/química , Espectroscopía Infrarroja por Transformada de Fourier , Polifenoles/química , Portadores de Fármacos/química , Ondas UltrasónicasRESUMEN
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 CaCl2 (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, ß-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.
Asunto(s)
Calcio , Celulosa , Nanopartículas , Proteínas de Guisantes , Solubilidad , Nanopartículas/química , Celulosa/química , Proteínas de Guisantes/química , Calcio/química , Pisum sativum/química , Interacciones Hidrofóbicas e Hidrofílicas , Cloruro de Calcio/química , Enlace de HidrógenoRESUMEN
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.
Asunto(s)
Curcumina , Emulsiones , Ácido Hialurónico , Proteínas de Guisantes , Impresión Tridimensional , Curcumina/química , Emulsiones/química , Proteínas de Guisantes/química , Ácido Hialurónico/química , Viscosidad , Tamaño de la Partícula , PolifenolesRESUMEN
Recent 3D-printing research showed the potential of using plant-protein-enriched inks to fabricate cultivated meat (CM) via agar-based support baths. However, for fabricating large, customized, structured, thick cellular constructs and further cultivation, improved 3D-printing capabilities and diffusion limit circumvention are warranted. The presented study harnesses advanced printing and thick tissue engineering concepts for such purpose. By improving bath composition and altering printing design and execution, large-scale, marbled, 0.5-cm-thick rib-eye shaped constructs were obtained. The constructs featured stable fibrous architectures comparable to those of structured-meat products. Customized multi-cellular constructs with distinct regions were produced as well. Furthermore, sustainable 1-cm-thick cellular constructs were carefully designed and produced, which successfully maintained cell viability and activity for 3 weeks, through the combined effects of void-incorporation and dynamic culturing. As large, geometrically complex construct fabrication suitable for long-term cellular cultivation was demonstrated, these findings hold great promise for advancing structured CM research.
Asunto(s)
Impresión Tridimensional , Animales , Andamios del Tejido/química , Proteínas de Guisantes/química , Ingeniería de Tejidos/métodos , Carne , Supervivencia Celular , Carne in VitroRESUMEN
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.
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Ácidos Grasos , Frutas , Interacciones Hidrofóbicas e Hidrofílicas , Oxígeno , Proteínas de Guisantes , Agua , Agua/química , Oxígeno/química , Ácidos Grasos/química , Frutas/química , Proteínas de Guisantes/química , Pisum sativum/química , Permeabilidad , Quitosano/química , Embalaje de Alimentos/métodos , Resistencia a la TracciónRESUMEN
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 ß-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.
Asunto(s)
Catequina , Hidrogeles , Proteínas de Guisantes , Catequina/química , Catequina/análogos & derivados , Hidrogeles/química , Proteínas de Guisantes/química , Nanofibras/química , Pisum sativum/química , Interacciones Hidrofóbicas e Hidrofílicas , Amiloide/químicaRESUMEN
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 ß-sheet and ß-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.
Asunto(s)
Magnesio , Proteínas de Guisantes , Polifenoles , Antioxidantes/química , Sustancias Macromoleculares/química , Magnesio/química , Proteínas de Guisantes/química , Proteínas de Guisantes/aislamiento & purificación , Pisum sativum/química , Polifenoles/químicaRESUMEN
Pea peptides can lead to degradation through oxidation, deamidation, hydrolysis, or cyclization during production, processing, and storage, which in turn limit their broader application. To stabilize pea peptides, this study employed spray drying technology to create a pea peptide micro-encapsule using maltodextrin, gum tragacanth, and pea peptides. Four key factors, including polysaccharide ratio, glycopeptide ratio, solid-liquid ratio, and inlet temperature, were optimized to enhance the antioxidant properties of the pea peptide micro-encapsule. The results indicated that the utilization of maltodextrin and gum tragacanth significantly improves the storage stability and antioxidant activity of pea peptides. Moreover, optimal storage stability for pea peptides was achieved with a polysaccharide ratio of 9:1, a glycopeptide ratio of 10:1, a solid-liquid ratio of 4:40, and an inlet temperature of 180 °C. After 60 days of storage, the encapsulated pea peptides maintained 70.22 %, 25.19 %, and 40.32 % for scavenging abilities to hydroxyl radical, superoxide anion, and ABTS radical, respectively. In contrast, the unencapsulated pea peptides showed a decline to 47.02 %, 0 %, and 24.46 % in the same antioxidant activities after storage. These findings underscore the potential of spray drying technology to enhance the functional properties of pea peptides for various applications.
Asunto(s)
Depuradores de Radicales Libres , Proteínas de Guisantes , Polisacáridos , Tragacanto , Depuradores de Radicales Libres/química , Polisacáridos/química , Tragacanto/química , Proteínas de Guisantes/química , Péptidos/química , Antioxidantes/química , Pisum sativum/química , Temperatura , Radicales Libres/química , Estabilidad de MedicamentosRESUMEN
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'/ Gâ³ 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.
Asunto(s)
Curcumina , Emulsiones , Geles , Glútenes , Nanopartículas , Oryza , Proteínas de Guisantes , Curcumina/química , Curcumina/farmacología , Emulsiones/química , Nanopartículas/química , Proteínas de Guisantes/química , Oryza/química , Glútenes/química , Geles/química , Hidrólisis , Tamaño de la Partícula , Reología , Composición de MedicamentosRESUMEN
From a physicochemical perspective, foods like vegan cheese and meat analogues are complex multicomponent gels. The aim of this study was to investigate the effect of processing conditions and composition on the textural properties of multicomponent gels containing starch, pea protein isolate (PPI) and emulsion droplets. Mechanical properties were measured, and structural analysis was carried with CLSM and SEM. In the case of particle gels prepared with maize starch (MS), a higher shearing speed decreased Young's modulus, fracture stress and fracture strain due to break up of the starch granules. In polymer gels prepared with potato starch (PS), structure and mechanical properties were not much affected by processing conditions. The addition of emulsion droplets increased the Young's modulus of MS gels and decreased that of PS gels. In PS gels, the fracture stress decreased further for smaller oil droplets. The addition of emulsion droplets was also found to decrease adhesiveness, cohesiveness and chewiness, regardless of the matrix structure. With protein addition into PS gels, an increase in Young's modulus and a decrease in fracture strain were observed. These results show that processing conditions and composition can be used to modulate the physical properties of complex food systems.
Asunto(s)
Emulsiones , Geles , Proteínas de Guisantes , Solanum tuberosum , Almidón , Emulsiones/química , Geles/química , Almidón/química , Proteínas de Guisantes/química , Solanum tuberosum/química , Módulo de Elasticidad , Pisum sativum/químicaRESUMEN
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.
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Agaricales , Fibras de la Dieta , Productos de la Carne , Valor Nutritivo , Proteínas de Guisantes , Gusto , Proteínas de Guisantes/química , Animales , Productos de la Carne/análisis , Fibras de la Dieta/análisis , Agaricales/química , Humanos , Antioxidantes , Polvos , Manipulación de Alimentos/métodos , Masculino , Fosfatos , Color , Oxidación-Reducción , Porcinos , Sustancias Reactivas al Ácido Tiobarbitúrico/análisis , Femenino , Sasa/químicaRESUMEN
The objective of this research was to explore the viability of pea protein as a substitute for gelatin in the complex coacervation process, with a specific focus on understanding the impact of incorporating an emulsifier into this process. The study involved the preparation of samples with varying polymer mixing ratios (1:1, 1:2, and 2:1) and emulsifier content. As core substances, black pepper and juniper essential oils were utilized, dissolved beforehand in grape seed oil or soybean oil, to minimize the loss of volatile compounds. In total, 24 distinct samples were created, subjected to freeze-drying to produce powder, and then assessed for their physicochemical properties. Results revealed the significant impact of emulsifier addition on microcapsule parameters. Powders lacking emulsifiers exhibited higher water solubility (57.10%-81.41%) compared to those with emulsifiers (24.64%-40.13%). Moreover, the emulsifier significantly decreased thermal stability (e.g., without emulsifier, Ton = 137.21°C; with emulsifier, Ton = 41.55°C) and adversely impacted encapsulation efficiency (highest efficiency achieved: 67%; with emulsifier: 21%).
Asunto(s)
Emulsionantes , Aceites Volátiles , Emulsionantes/química , Aceites Volátiles/química , Proteínas de Guisantes/química , Solubilidad , Tamaño de la Partícula , Liofilización , Gelatina/química , Cápsulas , Aceite de Soja/químicaRESUMEN
Pea-protein-based ingredients are gaining attention in the food industry due to their nutritional benefits and versatility, but their bitter, astringent, green, and beany off-flavors pose challenges. This study applied fermentation using microbial cultures to enhance the sensory qualities of pea-protein-based beverages. Using UHPLC-TOF-MS analyses along with sensory profile comparisons, microbial species such as Limosilactobacillus fermentum, Lactococcus lactis, Lactobacillus johnsonii, Lacticaseibacillus rhamnosus, and Bifidobacterium longum were preselected from an entire culture collection and found to be effective in improving the overall flavor impression by reducing bitter off-notes and enhancing aroma profiles. Notably, L. johnsonii NCC533 and L. fermentum NCC660 exhibited controlled proteolytic activities after 48 h of fermentation, enriching the matrix with taste-active amino acids, nucleotides, and peptides and improving umami and salty flavors while mitigating bitterness. This study has extended traditional volatile analyses, including nonvolatile metabolomic, proteomic, and sensory analyses and offering a detailed view of fermentation-induced biotransformations in pea-protein-based food. The results highlight the importance of combining comprehensive screening approaches and sensoproteomic techniques in developing tastier and more palatable plant-based protein products.
Asunto(s)
Fermentación , Aromatizantes , Proteínas de Guisantes , Pisum sativum , Gusto , Humanos , Proteínas de Guisantes/metabolismo , Proteínas de Guisantes/química , Pisum sativum/química , Pisum sativum/metabolismo , Pisum sativum/microbiología , Aromatizantes/metabolismo , Aromatizantes/química , Femenino , Masculino , Adulto , Bebidas/análisis , Bebidas/microbiologíaRESUMEN
This study investigated the mechanism underlying the flavor improvement observed during fermentation of a pea protein-based beverage using Lactobacillus johnsonii NCC533. A combination of sensomics and sensoproteomics approach revealed that the fermentation process enriched or generated well-known basic taste ingredients, such as amino acids, nucleotides, organic acids, and dipeptides, besides six new taste-active peptide sequences that enhance kokumi and umami notes. The six new umami and kokumi enhancing peptides, with human recognition thresholds ranging from 0.046 to 0.555 mM, are produced through the degradation of Pisum sativum's storage protein. Our findings suggest that compounds derived from fermentation enhance umami and kokumi sensations and reduce bitterness, thus improving the overall flavor perception of pea proteins. In addition, the analysis of intraspecific variations in the proteolytic activity of L. johnsonii and the genome-peptidome correlation analysis performed in this study point at cell-wall-bound proteinases such as PrtP and PrtM as the key genes necessary to initiate the flavor improving proteolytic cascade. This study provides valuable insights into the molecular mechanisms underlying the flavor improvement of pea protein during fermentation and identifies potential future research directions. The results highlight the importance of combining fermentation and senso(proteo)mics techniques in developing tastier and more palatable plant-based protein products.
Asunto(s)
Fermentación , Aromatizantes , Lactobacillus , Proteínas de Guisantes , Pisum sativum , Gusto , Humanos , Proteínas de Guisantes/metabolismo , Proteínas de Guisantes/química , Lactobacillus/metabolismo , Lactobacillus/genética , Pisum sativum/química , Pisum sativum/metabolismo , Aromatizantes/metabolismo , Aromatizantes/química , Proteómica , Adulto , Masculino , Femenino , Adulto Joven , Bebidas/análisis , Bebidas/microbiologíaRESUMEN
In this work, dispersions were prepared with commercial pea protein isolate (PPI) and subjected to different (i) high pressure homogenization (HPH) intensities (0 - 200 MPa) (room temperature, pH 7) or (ii) environmental conditions (60 °C, pH 7 or pH 12) to generate dispersions with distinct protein molecular and microstructural characteristics, impacting protein solubility. Besides, protein digestion was analyzed following the static INFOGEST in vitro digestion protocol. Generally, increasing pressure of the homogenization treatment was linked with decreasing particle sizes and enhanced protein digestion. More specifically, the dispersion that did not undergo HPH (0 MPa) as well as the dispersion treated at 60 °C, pH 7, had highly similar microstructures, consisting of large irregular particles (10 - 500 µm) with shell-like structures, and exhibited low solubility (around 15 % and 28 %, respectively), which resulted in limited proteolysis (35 % and 42 %, respectively). In contrast, the dispersion subjected to HPH at 100 MPa and the dispersion treated at 60 °C, pH 12 also had similar microstructures with small and homogeneous particles (<1 µm), and exhibited relatively good solubility (54 % and 31 %, respectively), which led to enhanced protein digestion levels (87 % and 74 %, respectively). This study highlights the potential of food processing on macronutrient (micro)structure and further gastrointestinal stability and functionality.
Asunto(s)
Digestión , Manipulación de Alimentos , Tamaño de la Partícula , Proteínas de Guisantes , Presión , Solubilidad , Proteínas de Guisantes/química , Concentración de Iones de Hidrógeno , Manipulación de Alimentos/métodos , Proteolisis , Pisum sativum/química , TemperaturaRESUMEN
The extensive utilization in food industry of pea protein is often impeded by its low water solubility, resulting in poor functional properties. Various methods, including pH-shifting (PS), ultrasonication (US), high-pressure micro-fluidization (MF), pH-shifting combined with ultrasonication (PS-US), and pH-shifting with micro-fluidization (PS-MF), were utilized to modify pea protein isolate (PPI) in order to enhance its functionality in emulsion formulation. The physicochemical properties and structural changes of the protein were investigated by assessing solubility, particle size, surface charge, protein profile, surface hydrophobicity, free sulfhydryl groups, and secondary structure content. The extent of modification induced by each treatment method on PPI-stabilized emulsions was compared based on parameters such as adsorbed interfacial protein concentration, particle size, zeta potential, and microstructure of the prepared emulsions. All modification increased the solubility of pea protein in the sequence of PS (4-fold) < MF (7-fold) < US (11-fold) < PS-US (13-fold) < PS-MF (14-fold). For single treatments, proteins dissolved more readily under US, resulting in the most uniform emulsions with small particle. The combined processes of PS-US and PS-MF further improved solubility, decreased emulsions particle size, promoted uniformity of emulsions. PS-US-stabilized emulsions displayed more smaller droplet size, narrower size distribution, and slightly higher stability than those prepared by PS-MF. The relatively higher emulsifying capacity of PPI treated by PS-US than those by PS-MF may be attributed to its higher surface hydrophobicity.