Circulating Amino Acid Concentration after the Consumption of Pea or Whey Proteins in Young and Older Adults Affects Protein Synthesis in C2C12 Myotubes.

As older adults tend to reduce their intake of animal-source proteins, plant-source proteins may offer valuable resources for better protein intake. The aim of this study was to assess whether the pea proteins can be used to achieve blood amino acid levels that stimulate muscle protein synthesis. We measured variations in plasma amino acid concentrations in young and older adults given pea (NUTRALYS® S85 Plus) or whey proteins either alone or in a standardized meal. The effect of amino acid concentrations on protein synthesis in C2C12 myotubes was determined. In terms of results, plasma amino acid concentrations reflected the difference between the amino acid contents of whey and pea proteins. Blood leucine showed a greater increase of 91 to 130% with whey protein compared to pea protein, while the opposite was observed for arginine (A greater increase of 147 to 210% with pea compared to whey). Culture media prepared with plasmas from the human study induced age-dependent but not protein-type-dependent changes in myotube protein synthesis. In conclusion, pea and whey proteins have the same qualities in terms of their properties to maintain muscle protein synthesis. Pea proteins can be recommended for older people who do not consume enough animal-source proteins.

Modulation of acid-induced pea protein gels by gellan gum and glucono-δ-lactone: Rheological and microstructural insights.

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.

Effect of high pressure homogenization on in vitro digestibility and colon fermentability of pea protein-rich bread designed for elderly consumers.

Enrichment of staple foods with proteins can be a solution to tackle protein-energy malnutrition in the elderly. For instance, bread can be enriched with pea proteins that are cheap, sustainable and easily digestible. Non-conventional technologies, such as high pressure homogenization (HPH), can improve the digestibility of plant proteins. To characterize the health functionality of pea-enriched bread, a functional bread tailored to elderly consumers was developed by substituting 5% wheat flour with untreated or HPH-treated pea protein concentrate. Protein digestibility and colon fermentability were assessed by mimicking elderly in vitro gastrointestinal and gut microbiota conditions and compared with adult conditions. Bread reformulation with pea proteins affected physical and chemical properties and produced an increase in hardness, which is one of the key features for the acceptability of bread by the elderly. The highest hardness value was observed for pea protein bread, followed by HPH-treated pea protein bread and wheat bread. In vitro protein digestibility and fermentability were affected by reformulation and by physiological digestive conditions, with lower digestibility under elderly conditions compared to adult ones. The obtained results may contribute to a better understanding of food digestibility under different gastrointestinal conditions and its dependence on physiological and formulation factors, and ultimately would help to design age-tailored foods.

Pea protein hydrolysate stimulates GLP-1 secretion in NCI-H716 cells via simultaneously activating the sensing receptors CaSR and PepT1.

Glucagon-like peptide-1 (GLP-1) plays a crucial role in regulating glucose homeostasis by stimulating insulin secretion and suppressing glucagon release. Our previous study observed that pea protein hydrolysate (PPH) exhibited the function of triggering GLP-1 secretion. However, the underlying mechanisms have not been revealed. Herein, the mechanisms of PPH-stimulated GLP-1 secretion were investigated in NCI-H716 cells. The PPH-induced GLP-1 secretion was reduced (p < 0.05) after adding the sensing receptor antagonists NPS-2143 and 4-AMBA, indicating that activation of both calcium-sensing receptor (CaSR) and peptide-transporter 1 (PepT1) was involved in PPH-triggered GLP-1 release. Moreover, the intracellular Ca2+ level increased by 2.01 times during the PPH-induced GLP-1 secretion. Similarly, the cAMP content also increased by 1.43 times after stimulation by PPH. The RT-qPCR results showed that PPH increased the gene expression of prohormone convertase 1/3 (PCSK-1) by 2.79-fold, which effectively promoted the conversion of proglucagon (GCG) to GLP-1. The specific pathway of PPH-induced GLP-1 secretion may involve both CaSR and PepT1 activation-induced Ca2+ influx and cAMP generation, which effectively enhanced the enzyme activity of prohormone convertase 1/3 (PCSK-1) and ultimately promoted GLP-1 secretion.

Interfacial engineering of Pickering emulsions stabilized by pea protein-alginate microgels for encapsulation of hydrophobic bioactives.

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.

Impact of pH on the structure, interfacial and foaming properties of pea protein isolate: Investigation of the structure - Function relationship.

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.

Conformational changes induced by cellulose nanocrystals in collaboration with calcium ion improve solubility of pea protein isolate.

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.

Effect of mixed protein supplementation on golf performance and muscle function: a randomized, double-blind, placebo-controlled study.

BACKGROUND: As a relatively novel approach to enhancing skeletal muscle health, mixed protein supplementation has shown similar responses to whey protein. However, no previous studies have examined its impact on golf swing performance. This study aimed to examine the effect of mixed protein supplementation on the swing performance and muscle strength of casual golfers. METHODS: Sixty participants with a handicap of less than 20 were recruited and randomly assigned to a double-blind, placebo-controlled study design. The participants were divided into two groups: a mixed protein group (MG, n = 30), and a placebo control group (CG, n = 30). They were instructed to ingest either a supplement containing casein calcium, whey protein, and isolated pea protein, or a placebo, once daily for 8 weeks. Pre- and posttests consisted of anthropometric measurements, muscle strength (isokinetic knee and trunk strength, and handgrip strength), 2-minute push-ups, balance, and golf swing performance using a driver and 7-iron. RESULTS: After the 8-week supplementation period, ANCOVA, using baseline values as covariates, revealed significant differences for driver distance (p = .004) and driver ball speed (p < .001). MG significantly increased driver distance by 5.17 ± 12.8 m (p = .046), driver ball speed by 1.36 ± 2.87 m/s (p = .021). Additionally, significantly improvements were observed in hand grip strength (+2.12 ± 3.47 kg, p = .004), two-minute push-ups (+4.89 ± 8.14 reps, p = .004), and balance score (-0.37 ± 0.69 min, p = .009). No significant differences were observed in body composition parameters (p > .05). CONCLUSION: The intake of a mixed protein containing both animal and plant proteins had positive effects on golf performance and muscle function. Therefore, mixed proteins may represent a safe and effective approach to enhancing skeletal muscle health in golf players.

Effects of Sequential Induction Combining Thermal Treatment with Ultrasound or High Hydrostatic Pressure on the Physicochemical and Mechanical Properties of Pea Protein-Psyllium Hydrogels as Elderberry Extract Carriers.

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.

Understanding the textural enhancement of low-salt myofibrillar protein gels filled with pea protein pre-emulsions through interfacial behavior: Effects of structural modification and oil phase polarity.

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.

Development of pea protein nanoparticle/hydrolyzed rice glutelin fibril emulsion gels for encapsulation of curcumin.

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.

Pea Albumin Extracted from Pea (Pisum sativum L.) Seeds Ameliorates High-Fat-Diet-Induced Non-Alcoholic Fatty Liver Disease by Regulating Lipogenesis and Lipolysis Pathways.

Non-alcoholic fatty liver disease (NAFLD) is now recognized as the most prevalent liver disease globally. Pea albumin (PA) has demonstrated positive impacts on reducing obesity and improving glucose metabolism. In this research, a mouse model of NAFLD induced by a high-fat diet (HFD) was employed to examine the impact of PA on NAFLD and explore its potential mechanisms. The findings revealed that mice subjected to a HFD developed pronounced fatty liver alterations. The intervention with PA significantly lowered serum TC by 26.81%, TG by 43.55%, and LDL-C by 57.79%. It also elevated HDL-C levels by 1.2 fold and reduced serum ALT by 37.94% and AST by 31.21% in mice fed a HFD. These changes contributed to the reduction in hepatic steatosis and lipid accumulation. Additionally, PA improved insulin resistance and inhibited hepatic oxidative stress and inflammatory responses. Mechanistic studies revealed that PA alleviated lipid accumulation in HFD-induced NAFLD by activating the phosphorylation of AMPKα and ACC, inhibiting the expression of SREBF1 and FASN to reduce hepatic lipogenesis, and increasing the expression of ATGL, PPARα, and PPARγ to promote lipolysis and fatty acid oxidation. These results indicate that PA could serve as a dietary supplement for alleviating NAFLD, offering a theoretical foundation for the rational intake of PA in NAFLD intervention.

Screening of a Microbial Culture Collection: Empowering Selection of Starters for Enhanced Sensory Attributes of Pea-Protein-Based Beverages.

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.

Sensoproteomic Characterization of Lactobacillus Johnsonii-Fermented Pea Protein-Based Beverage: A Promising Strategy for Enhancing Umami and Kokumi Sensations while Mitigating Bitterness.

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.

Evaluation of nutritional, technological, oxidative, and sensory properties of low-sodium and phosphate-free mortadellas produced with bamboo fiber, pea protein, and mushroom powder.

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.

Creating and characteristics of a novel biomacromolecules complex of pea protein isolated-tannic acid-magnesium ion.

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.

Efficacy of Pea Protein Supplementation in Combination with a Resistance Training Program on Muscle Performance in a Sedentary Adult Population: A Randomized, Comparator-Controlled, Parallel Clinical Trial.

Animal-sourced whey protein (WPr) is the most popular protein supplement among consumers and has been shown to improve muscle mass and strength. However, due to allergies, dietary restrictions/personal choices, and growing demand, alternative protein sources are warranted. Sedentary adults were randomized to pea protein (PPr) or WPr in combination with a weekly resistance training program for 84 days. Changes in whole-body muscle strength (WBMS) including handgrip, lower body, and upper body strength, body composition, and product perception were assessed. The safety outcomes included adverse events, vital signs, clinical chemistry, and hematology. There were no significant differences in the change in WBMS, muscle mass, or product perception and likability scores between the PPr and WPr groups. The participants supplemented with PPr had a 16.1% improvement in WBMS following 84 days of supplementation (p = 0.01), while those taking WPr had an improvement of 11.1% (p = 0.06). Both study products were safe and well-tolerated in the enrolled population. Eighty-four days of PPr supplementation resulted in improvements in strength and muscle mass comparable to WPr when combined with a resistance training program in a population of healthy sedentary adults. PPr may be considered as a viable alternative to animal-sourced WPr without sacrificing muscular gains and product enjoyment.

Enhancing storage stability of pea peptides through encapsulation in maltodextrin and gum tragacanth via monitoring scavenge ability to free radicals.

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.

Embedded three-dimensional printing of thick pea-protein-enriched constructs for large, customized structured cell-based meat production.

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.

Understanding emulsifier influence on complex coacervation: Essential oils encapsulation perspective.

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%).