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 (TE) 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%).

Fatty-acid incorporation improves hydrophobicity of pea protein based films towards better oxygen/water barrier properties and fruit protecting ability.

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.

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.

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.

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.

Formation of pea protein amyloid-like nanofibrils-derived hydrogels mediated by epigallocatechin gallate.

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.

Physicochemical Properties, Stability, and Functionality of Non-Covalent Ternary Complexes Fabricated with Pea Protein, Hyaluronic Acid and Chlorogenic Acid.

The aim of this study was to prepare and characterize stable non-covalent ternary complexes based on pea protein (PP, 0.5%), hyaluronic acid (HA, 0.125%), and chlorogenic acid (CA, 0~0.03%). The ternary complexes were comprehensively evaluated for physicochemical attributes, stability, emulsifying capacities, antioxidant properties, and antimicrobial efficacy. PP-HA binary complexes were first prepared at pH 7, and then CA was bound to the binary complexes, as verified by fluorescence quenching. Molecular docking elucidated that PP interacted with HA and CA through hydrogen bonding, hydrophobic and electrostatic interactions. The particle size of ternary complexes initially decreased, then increased with CA concentration, peaking at 0.025%. Ternary complexes demonstrated good stability against UV light and thermal treatment. Emulsifying activity of complexes initially decreased and then increased, with a turning point of 0.025%, while emulsion stability continued to increase. Complexes exhibited potent scavenging ability against free radicals and iron ions, intensifying with higher CA concentrations. Ternary complexes effectively inhibited Staphylococcus aureus and Escherichia coli, with inhibition up to 0.025%, then decreasing with CA concentration. Our study indicated that the prepared ternary complexes at pH 7 were stable and possessed good functionality, including emulsifying properties, antioxidant activity, and antibacterial properties under certain concentrations of CA. These findings may provide valuable insights for the targeted design and application of protein-polysaccharide-polyphenol complexes in beverages and dairy products.

The interplay of muscle and pea proteins in low-salt gels: An insight into in situ structure formation in hybrid meat alternatives.

The present study investigated thermal gelation of mixed sarcoplasmic (Sarc), myofibrillar (Myof), and pea proteins corresponding to partial meat replacements (0, 25, and 50%) by pea protein isolate (PPI) at reducing salt levels (0.6 â†’ 0.1 M NaCl) to understand in situ (simulated) structure-forming properties of hybrid meat analogues. The amount of soluble proteins in hybrids generally increased with salt concentrations and PPI substitution. While muscle proteins (mixed Sarc and Myof) had the strongest gelling capacity, hybrid proteins also exhibited moderate aggregation and gelling activity based on the sol→gel rheological transition and gel hardness testing. Sarc and pea 7S/11S globulins collectively compensated for the attenuated gelling capacity of mixed proteins due to diminishing Myof in the hybrids. Immobilized water within hybrid protein gels was tightly bonded (T2 from nuclear magnetic resonance), consistent with the dense and uniform microstructure observed. These findings offer a new knowledge base for developing reduced-salt hybrid meat analogues.

Encapsulation of Lactobacillus plantarum in W1/O/W2 double emulsions stabilized with the high-intensity ultrasound-treated pea protein and pectin.

This study focuses on developing a water-in-oil-in-water (W1/O/W2) double emulsion system using high-intensity ultrasound (HIU)-treated pea protein isolate (HIU-PPI) and pectin to encapsulate Lactobacillus plantarum (L. plantarum). The effects of ultrasound treatment on pea protein isolate (PPI) characteristics such as solubility, particle size, emulsification, surface hydrophobicity, and surface free sulfhydryl group were examined, determining optimal HIU processing conditions was 400 W for 10 min. The developed W1/O/W2 double emulsion system based on HIU-PPI demonstrated effective encapsulation and protection of L. plantarum, especially at the HIU-PPI concentration of 4 %, achieving an encapsulation efficiency of 52.65 %. Incorporating both HIU-PPI and pectin as emulsifiers increased the particle size and significantly enhanced the emulsion's viscosity. The highest bacterial encapsulation efficiency of the emulsion, 59.94 %, was attained at a HIU to pectin concentration ratio of 3:1. These emulsions effectively encapsulate and protect L. plantarum, with the concentration of HIU-PPI being a critical factor in enhancing probiotic survival under simulated gastrointestinal digestion. However, the concurrent utilization of pectin and HIU-PPI as emulsifiers did not provide a notable advantage compared to the exclusive use of HIU-PPI in enhancing probiotic viability during in vitro simulated digestion. This research offers valuable perspectives for the food industry on harnessing environmentally friendly, plant-based proteins as emulsifiers in probiotic delivery systems. It underscores the potential of HIU-modified pea protein and pectin in developing functional food products that promote the health benefits of probiotics.

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.

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.

Enhancing the usability of pea protein in emulsion applications through modification by various approaches: A comparative study.

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.

Thermal stability, antioxidant activity and bioavailability of pea protein-naringin Pickering emulsion for enhanced delivery applications.

After successfully addressing to mitigate bitterness of naringin through construction Pickering emulsion using pea protein (PP) and naringin (NG) in our previous study, we now probed thermal stability, antioxidant efficacy, and bioavailability. FTIR analysis and UV-vis spectroscopy indicated predominant interactions between PP and NG were hydrogen and hydrophobic bonds. TGA and DSC analyses demonstrated that PP-NG complexes exhibited superior heat-resistance compared to pure PP and NG. Thermal stability assessments indicated a significant retention of NG in the PP-NG Pickering emulsion than the control NG across varied temperatures (4 °C, 25 °C, 37 °C, and 65 °C). Moreover, the antioxidant activity of PP-NG emulsion was dependent on the concentration of NG, as evidenced by DPPH and ABTS free radicals scavenging abilities, ferric reducing power, and lipid peroxidation resistance. Additionally, PP-NG Pickering emulsion exhibited substantially high bioavailability (92.01 ± 3.91%). These results suggest a promising avenue for the application of NG with improved characteristics.

Pea protein-inulin conjugate prepared by atmospheric pressure plasma jet combined with glycosylation: structure and emulsifying properties.

Pea protein is one of plant proteins with high nutritional value, but its lower solubility and poor emulsifying properties limit its application in food industry. Based on wet-heating glycosylation of pea protein and inulin, effects of discharge power of atmospheric pressure plasma jet (APPJ) on structure, solubility, and emulsifying ability of pea protein-inulin glycosylation conjugate were explored. Results indicated that the APPJ discharge power did not affect the primary structure of pea protein. However, changes in secondary and spatial structure of pea protein were observed. When APPJ discharge power was 600 W, the solubility of glycosylation conjugate was 75.0% and the emulsifying stability index was 98.9 min, which increased by 14.85 and 21.95% than that of only glycosylation sample, respectively. These findings could provide technical support for APPJ treatment combination with glycosylation to enhance the physicochemical properties of plant-based proteins.

High-Moisture Extrusion of a Dietary Protein Blend Impairs In Vitro Digestion and Delays In Vivo Postprandial Plasma Amino Acid Availability in Humans.

BACKGROUND: Industrial processing can alter the structural complexity of dietary proteins and, potentially, their digestion and absorption upon ingestion. High-moisture extrusion (HME), a common processing method used to produce meat alternative products, affects in vitro digestion, but human data are lacking. We hypothesized that HME of a mycoprotein/pea protein blend would impair in vitro digestion and in vivo postprandial plasma amino acid availability. METHODS: In Study A, 9 healthy volunteers completed 2 experimental trials in a randomized, double-blind, crossover design. Participants consumed a beverage containing 25 g protein from a "dry" blend (CON) of mycoprotein/pea protein (39%/61%) or an HME content-matched blend (EXT). Arterialized venous blood samples were collected in the postabsorptive state and regularly over a 5-h postprandial period to assess plasma amino acid concentrations. In Study B, in vitro digestibility of the 2 beverages were assessed using bicinchoninic acid assay and optical fluorescence microscopy at baseline and during and following gastric and intestinal digestion using the INFOGEST model of digestion. RESULTS: Protein ingestion increased plasma total, essential (EAA), and branched-chain amino acid (BCAA) concentrations (time effect, P < 0.0001) but more rapidly and to a greater magnitude in the CON compared with the EXT condition (condition × time interaction, P < 0.0001). This resulted in greater plasma availability of EAA and BCAA concentrations during the early postprandial period (0-150 min). These data were corroborated by the in vitro approach, which showed greater protein availability in the CON (2150 ± 129 mg/mL) compared with the EXT (590 ± 41 mg/mL) condition during the gastric phase. Fluorescence microscopy revealed clear structural differences between the 2 conditions. CONCLUSIONS: These data demonstrate that HME delays in vivo plasma amino acid availability following ingestion of a mycoprotein/pea protein blend. This is likely due to impaired gastric phase digestion as a result of HME-induced aggregate formation in the pea protein. This trial was registered at clinicaltrials.gov as NCT05584358.

Enzymatic degradation of pea fibers changes pea protein concentrate functionality.

Pea proteins are gaining increased interest from both the food industry as well as from consumers. Pea protein isolates (PPI) excel at forming meat-like textures upon heating while pea protein concentrates (PPC) are more challenging to transform into highly sought-after foods. PPCs are richer in dietary fibers (DF) and are more sustainable to produce than PPI. In this work, degradative enzymes were used to modify the functionality of PPC-water blends with a focus on texturization upon heating. Three enzyme solutions containing ß-glucanases, hemicellulases, pectinases, xylanase, and cellulases were added to 65 wt% PPC blends. The effect of these enzymatic pretreatments was measured by monitoring the torque in a mixing reactor during blending, differential scanning calorimetry (DSC), high-pressure shear rheology (HPSR), and DF content and size analysis. Four endothermic peaks were detected in the DSC thermograms of PPC, namely at 63 °C, 77 °C, 105 °C and 123 °C. The first three peaks were attributed to phase transition and gelation temperatures of the starches and proteins constituting PPC. No endothermic peaks were measured for PPI blends. Enzyme solutions containing ß-glucanases, hemicellulases, pectinases, and xylanases increased the endothermic energy of all peaks, hinting at an effect on the gelation properties of PPC. The same enzymes decreased the resistance to flow of PPC blends and induced a shift of the weight average molecular weight (Mw) distribution of soluble dietary fibers (SDF) towards smaller values while increasing the fraction of SDF by decreasing the insoluble dietary fiber (IDF) content. The solution containing cellulases did not change the DSC results or the viscosity of the PPC mixture, nor did it affect the IDF and SDF contents. On the other hand HPSR measurements of heated PPC samples up to 125 °C showed that all tested enzyme solutions decreased the complex viscosity of PPC-water blends to values similar to PPI-water blends. We demonstrated that degradative enzymes can enhance the functionality of less refined protein-rich ingredients based on pea and other vegetal sources. Using optimized enzyme blends for targeted applications can prove to be a key changer in the development and improvement of sustainable protein-rich foods.

Effect of Heat Treatment Combined with TG Enzyme Cross-Linking on the Zein-Pea Protein Complex: Physicochemical and Gel Properties.

Plant proteins have the advantages of low cost and high yield, but they are still not comparable to animal proteins in processing due to factors such as gelation and solubility. How to enhance the processing performance of plant proteins by simple and green modification means has become a hot research topic nowadays. Based on the above problems, we studied the effect of gel induction on its properties. In this study, a pea protein-zein complex was prepared by the pH cycle method, and the effects of different induced gel methods on the gel properties of the complex protein were studied. The conclusions are as follows: All three gel induction methods can make the complex protein form a gel system, among which the gel strength of heat treatment and the TG enzyme-inducted group is the highest (372.84 g). Through the observation of the gel microstructure, the gel double network structure disappears and the structure becomes denser, which leads to a stronger water-binding state of the gel sample in the collaborative treatment group. In the simulated digestion experiment, heat treatment and enzyme-induced samples showed the best slow-release effect. This study provides a new method for the preparation of multi-vegetable protein gels and lays a theoretical foundation for their application in food processing.

Fabricating Pea Protein Micro-Gel-Stabilized Pickering Emulsion as Saturated Fat Replacement in Ice Cream.

Unsaturated fat replacement should be used to reduce the use of saturated fat and trans fatty acids in the diet. In this study, pea protein micro-gels (PPMs) with different structures were prepared by microparticulation at pH 4.0-7.0 and named as PPM (pH 4.0), PPM (pH 4.5), PPM (pH 5.0), PPM (pH 5.5), PPM (pH 6.0), PPM (pH 6.5), and PPM (pH 7.0). Pea protein was used as a control to evaluate the structure and interfacial properties of PPMs by particle size distribution, Fourier transform infrared spectroscopy (FTIR), free sulfhydryl group content, and emulsifying property. PPM (pH 7.0) was suitable for application in O/W emulsion stabilization because of its proper particle size, more flexible structure, high emulsifying activity index (EAI) and emulsifying stability index (ESI). The Pickering emulsion stabilized by PPM (pH 7.0) had a uniform oil droplet distribution and similar rheological properties to cream, so it can be used as a saturated fat replacement in the manufacture of ice cream. Saturated fat was partially replaced at different levels of 0%, 20%, 40%, 60%, 80%, and 100%, which were respectively named as PR0, PR20, PR40, PR60, PR80, and PR100. The rheological properties, physicochemical indexes, and sensory properties of low-saturated fat ice cream show that PPM (pH 7.0)-stabilized emulsion can be used to substitute 60% cream to manufacture low-saturated fat ice cream that has high structural stability and similar melting properties, overrun, and sensory properties to PR0. The article shows that it is feasible to prepare low-saturated fat ice cream with PPM (pH 7.0)-stabilized Pickering emulsion, which can not only maintain the fatty acid profile of the corn oil used, but also possess a solid-like structure. Its application is of positive significance for the development of nutritious and healthy foods and the reduction of chronic disease incidence.