Pea protein ingredients vary widely in composition and functional properties depending on their processing history, which strongly affects their behavior during high-moisture extrusion. This study compared pea protein isolate (PPI, 81% protein), pea protein concentrate (PPC, 52% protein), and a 1:1 blend (PPC-PPI, 67% protein) to elucidate how raw material properties influence protein aggregation and the resulting texture of meat analogues processed at high moisture contents (50-60%). PPI exhibited low solubility, high water-holding capacity (WHC), and a partially denatured protein state, whereas PPC contained higher levels of carbohydrates and fiber, showed greater solubility, and retained a more native protein structure. These differences resulted in distinct rheological responses: PPI dispersions formed dense, elastic networks at ambient temperature, while PPC showed limited initial structure but pronounced heat-induced gelation; the blend exhibited comparatively low viscosity and elasticity. During extrusion, PPI formed predominantly disulfide-stabilized networks, resulting in high hardness and anisotropy at low moisture (50%). In contrast, PPC aggregated mainly via non-disulfide covalent bonds, producing stiff but brittle structures. The PPC-PPI blend showed moisture-dependent behavior: at high moisture (60%), enhanced non-covalent interactions promoted molecular mobility and alignment, whereas at low moisture increased non-disulfide covalent cross-linking strengthened the network but constrained anisotropy. Correlation analysis confirmed that aggregation pathway, rather than protein content alone, governs extrudate texture. Overall, controlling the balance between disulfide, non-disulfide, and non-covalent interactions is critical for optimizing strength and alignment during high-moisture extrusion of pea proteins, highlighting blending as a practical strategy to tailor texture while leveraging the sustainability advantages of dry-fractionated proteins.

Pea protein isolate (PPI) is widely used to produce plant-based meat analogues via high-moisture extrusion. Key parameters during extrusion processing such as temperature and shear play critical roles in the structural changes that determine the final product's texture and mechanical properties. However, achieving a fibrous meat-like texture remains challenging. Consequently, this study aims to systematically investigate the effects of cooling die temperature and shear rate during the cooling phase of high-moisture extrusion on the rheological and textural properties of PPI-based meat analogues. A rotating cooling die system was employed to independently control shear rates (0-9.03 s-1) and cooling temperatures (70-90 degrees C). Texture and rheological analysis were conducted to assess hardness, anisotropy, and viscoelastic characteristics. The findings indicate that higher cooling die temperatures (up to 80 degrees C) resulted in harder extrudates with higher anisotropy, enhancing fibrous structure formation. Increased shear rates during cooling did not significantly influence the hardness and the anisotropy decreased. Hardness, anisotropy, and elastic modulus increased primarily due to enhanced aggregation via disulfide bonds, while aggregation through non-covalent bonds had a comparatively smaller impact on the mechanical properties. Thermomechanical treatment of PPI at higher moisture contents in a rheometer corroborated these results, with both shear rate and cooling temperature significantly affecting the elasticity. This indicated that predictive insights into the texturization potential of plant-based proteins can be gained under extrusion-like conditions by assessing their rheological properties.

Pulsed electric field (PEF) technology has gained interest for its potential to enhance the functional properties of food proteins. This study examined how PEF treatment, used to inactivate microorganisms, additionally affects the structure and functionality of mildly extracted pea proteins, and compared it to conventional heat pasteurization. PEF treatments (Eel = 24 kV/cm, f = 50 Hz, tau = 20 mu s, tt = 126 mu s) combined with different product inlet temperatures (25, 30, 35 and 40 degrees C) were selected based on previously studied Pseudomonas trivalis and Erwinia gerundensis reductions, which ranged from 2.0 to 4.2 logs. Thermal treatments (TTs) of 51, 54, 57 and 60 degrees C for 27 s, leading to comparable microbial inactivation (from 0.1 up to 4.2 log reduction), were taken as reference and selected for comparison of protein modifications. Fluorescence and circular dichroism spectroscopy were performed on IEX-isolated pea albumins and globulins and revealed inverse impact on the structure for both proteins. While PEF-treatment led to protein unfolding (red shift of the Tryptophan (Trp) emission maxima), protein aggregation (blue shift) was observed for TT samples. Additionally, the impact of the treatments on the functionality of the extract was evaluated. While the gelling properties of pea extract were enhanced following PEF treatments (+35%), regardless of inlet temperature, the opposite was observed for the TTs, with a reduction of 60% compared to PEF-treated ingredients. The findings validated the advantage of PEF treatments over TTs for effective microbial reduction in pea protein extract while simultaneously enhancing the gelling properties.

Innovative extraction methods involving dry fractionation and aqueous phase separation have been recently developed to obtain plant-based protein ingredients with high texturing functionality. Such a process was applied to yellow peas, and the microbial quality of the extract was assessed. Pseudomonas trivalis and Erwinia gerundensis were identified as critical microbial contaminants due to their high growth capacities (at 10 degrees C). As a preservation strategy, pulsed electric field (PEF) treatment (24 kV/cm, 50 Hz, 126 mu s) was employed, combined with different product inlet temperatures (25-45 degrees C). Ohmic heating (Delta T = 20 degrees C) was measured. At 25-30 degrees C, the microbial reduction reached 3 logs, attributed solely to electrical effects. At 40 degrees C, the reduction exceeded 4 logs, where thermal effects dominated. Further increase to 45 degrees C resulted in thermal modification of pea proteins, potentially compromising its gelling capacity. Additionally, the growth of PEF-treated contaminants at 5 and 10 degrees C were monitored, revealing rapid cell adaptation and proliferation. Finally, the extracts native microbiota showed an extension of the lag phase (4 days at 5 degrees C) after PEF treatment, accompanied by a pH stability of 10 days. The findings indicate improved microbial stability of the pea extract following PEF treatment.

The addition of pectin to soy protein isolate (SPI) is a route to create fibrous products using shear cell technology. In this study, we investigated pectins derived from soybean, sugar beets, and citrus (two variants) that vary in sugar composition, degree of methylation and acetylation. The objective was to examine how these different pectins impact the functional properties of the SPI dispersions. The SPI-pectin blends were shear structured and their visual appearance, microstructural, rheological, and mechanical properties were analyzed. The addition of pectins from citrus (the highly methyl-esterified form) and soybean resulted in fibrous products when mixed with SPI. The addition of the low methyl-esterified pectin derived from citrus led to less pronounced fibrous product, and pectin from sugar beet did not lead to fibrous products. To explain the effect, several properties of the blends and products were tested. It was found that the fibrous products contained more air (i.e. higher void fraction) than products that were not fibrous, and that air bubbles were deformed in the shear direction. The rheological measurements of the blends revealed that the pectins lowered the yield and flow point of SPI, and the flow transition index. The blend with the highest elasticity after heating also had the highest deformation of air bubbles. Based on all results it was concluded that pectin influenced the structure formation in two ways: 1) affecting the ability to facilitate air inclusion and 2) influencing the storage modulus and elasticity of the matrix.

The Bacillus cereus group represents a serious risk in powdered and amylaceous foodstuffs. Cold plasma (the fourth state of matter) is emerging as an alternative effective nonthermal technology for pasteurizing a wide range of matrices in solid, liquid, and powder form. The present study aims to evaluate the mechanisms involved in Bacillus cereus inactivation via cold plasma, focusing on (i) the technology’s ability to generate damage in cells (at the morphological and molecular levels) and (ii) studying the effectiveness of cold plasma in biofilm mitigation through the direct effect and inhibition of the biofilm-forming capacity of sublethally damaged cells post-treatment. Dielectric barrier discharge cold plasma (DBD-CP) technology was used to inactivate B. cereus, B. thuringiensis, and B. mycoides under plasma power settings of 100, 200, and 300 W and treatment times ranging from 1 to 10 min. Inactivation levels were achieved in 2–7 log10 cycles under the studied conditions. Percentages of sublethally damaged cells were observed in a range of 45–98%, specifically at treatment times below 7 min. The sublethally damaged cells showed poration, erosion, and loss of integrity at the superficial level. At the molecular level, proteins and DNA leakage were also observed for B. cereus but were minimal for B. mycoides. Biofilms formed by B. cereus were progressively disintegrated under the DBD-CP treatment. The greater the CP treatment intensity, the greater the tearing of the bacteria’s biofilm network. Additionally, cells sublethally damaged by DBD-CP were evaluated in terms of their biofilm-forming capacity. Significant losses in the damaged cells’ biofilm network density and aggregation capacity were observed when B. cereus was recovered after inactivation at 300 W for 7.5 min, compared with the untreated cells. These results provide new insights into the future of tailored DBD-CP design conditions for both the inactivation and biofilm reduction capacity of B. cereus sensu lato species, demonstrating the effectiveness of cold plasma and the risks associated with sublethal damage generation.

Pulsed electric field (PEF) processing has emerged as an alternative to thermal pasteurization for the shelf-life extension of heat-sensitive liquids at industrial scale. It offers the advantage of minimal alteration in physicochemical characteristics and functional properties. In this study, a pilot-scale continuous PEF processing (Toutlet < 55 °C) was applied to microalgae Chlorella vulgaris (Cv) suspensions (pH = 6.5), which was proposed as a functional ingredient for plant-based foods. Cv suspensions were inoculated with three distinct food spoilage microorganisms (Pseudomonas guariconensis, Enterobacter soli and Lactococcus lactis), isolated from the Cv biomass. PEF treatments were applied with varying electric field strength Eel of 16 to 28 kV/cm, pulse repetition rate f of 100 to 140 Hz, with a pulse width τ of 20 μs and an inlet product temperature Tin of 30 °C. The aim was to evaluate the PEF-induced microbial reduction and monitor the microbial outgrowth during a 10-day cold storage period (10 °C). Maximum inactivation of 4.1, 3.7 and 3.6 logs was achieved (28 kV/cm and 120 Hz) for the investigated isolates, respectively. Under these conditions, the critical electric field strengths Ecrit, above which inactivation was observed, ranged from 22.6 to 24.6 kV/cm. Moreover, repeated PEF treatment resulted in similar inactivation efficiency, indicating its potential to enhance shelf-life further.

Powdered Arthrospira platensis (Spirulina) is one of the most valuable nutraceutical products in terms of functionality and food-fortification due to its recognized prebiotic, antioxidant, and immunomodulatory potential. The present study aims to assess the quality of this matrix as a prebiotic after Cold Atmospheric Pressure Plasma (CAPP) processing. CAPP-treated Spirulina samples (1 mg/mL), at effective discharge power of 1.1, 1.7, 2.2 and 3.3 W for 5 min, were used to promote the growth of the probiotics Limosilactobacillus reuteri and Lacticaseibacillus rhamnosus GG. Chicory inulin was used as reference prebiotic material (1 mg/mL). - Microorganisms were inoculated in the different prepared media, and incubated 48 h, at 30 degrees C, under anaerobic conditions. The probiotics' growth rate on Spirulina (CAPP treated and untreated) dispersions, protein stability and their secondary metabolites production were evaluated. The bacterial growth (>7.0 +/- 0.2 log(10) cycles) and prebiotic indices of treated Spirulina samples (compared to untreated Spirulina) confirm the prebiotic functionality before and after CAPP processing. The proteomic and metabolomic profiles of the hydrolyzed matrix post-fermentation revealed significant differences in the nutritional values of the final fermented product, depending on the applied CAPP intensity. The present study provides first-time insight into CAPP optimization for increased bioavailability of Spirulina compounds and quality proofed nutraceutical development.

Research regarding meat analogues is mostly based on formulation and process development. Information concerning their safety, shelf life, and long-term nutritional and health effects is limited. This article reviews the existing literature and analyzes potential hazards introduced or modified throughout the processing chain of plant-based meat analogues via extrusion processing, encompassing nutritional, microbiological, chemical, and allergen aspects. It was found that the nutritional value of plant-based raw materials and proteins extracted thereof increases along the processing chain. However, the nutritional value of plant-based meat analogues is lower than that of e.g., animal-based products. Consequently, higher quantities of these products might be needed to achieve a nutritional profile similar to e.g., meat. This could lead to an increased ingestion of undigestible proteins and dietary fiber. Although dietary fibers are known to have many positive health benefits, they present a hazard since their consumption at high concentrations might lead to gastrointestinal reactions. Even though there is plenty of ongoing research on this topic, it is still not clear how the sole absorption of metabolites derived from plant-based products compared with animal-based products ultimately affects human health. Allergens were identified as a hazard since plant-based proteins can induce an allergic reaction, are known to have cross-reactivities with other allergens and cannot be eliminated during the processing of meat analogues. Microbiological hazards, especially the occurrence of spore- and non-spore-forming bacteria, do not represent a particular case if requirements and regulations are met. Lastly, it was concluded that there are still many unknown variables and open questions regarding potential hazards possibly present in meat analogues, including processing-related compounds such as n-nitrosamines, acrylamide, and heterocyclic aromatic amino acids.

Microalgae attract increasing interest in enhancing the nutritional values of plant-based foods. However, alterations in the final product's color (by green algae) and mushy texture can be induced. In this study, we incorporated yellow Chlorella vulgaris (Cv) in pea protein-based meat substitutes and aimed to minimize properties alteration by using wet and disrupted Cv biomass. The cell wall disruption, done by high-pressure homogenization (HPH) at 150 MPa and initial biomass temperature below 10 degrees C, significantly increased the gelation capacity. The effect was confirmed by (i) a 10x increase in the apparent viscosity of 14% (w/w) Cv suspensions, and (ii) a 2x increase in the storage modulus (G') of 9:1 (w/w) pea protein isolate - Cv gels. Furthermore, the HPH-treated Cv was successfully incorporated (10% (w/w)) into pea protein-based meat substitutes produced with high-moisture extrusion cooking without altering their visual appearance, hardness, or anisotropy index. Finally, spray drying or fractionation steps of the HPH-treated Cv did not improve protein gels, or meat substitutes produced thereof. This study demonstrated that disrupted Cv is a promising nutritious and sustainable ingredient for meat substitutes.

High-moisture extrusion (HME) is an effective process to make fibrous products that can be used as meat analogues. In this study, the effect of extrusion of already extruded products (i.e., re-extrusion) was tested with the aim to explore the potential of rework in HME. The rework of material is important because it is a route to reduce waste, which is always produced, for example during the start or at the end of a production run. Pea and soy protein isolates (PPI and SPI) were first extruded, then freeze-dried and ground, and extruded again. The visual and textural properties of the fibrous products were evaluated. Also, the rheological properties, solubility, and water-holding capacity (WHC) of the ingredients and the products after the first and second extrusion were quantified. The obtained freeze-dried powders after the first HME cycle had a reduction in solubility of 15% for PPI and 74% for SPI. Furthermore, WHC was reduced by 65% and 17% for PPI and SPI, respectively. After the second HME cycle, the reduction in solubility and WHC was augmented to 22% and 90% for PPI, and 79% and 63% for SPI. No effect on stock and loss moduli after heating and cooling were found, even after two HME cycles. SPI fibrous products did not differ in cutting strength, anisotropy index, or visual appearance after re-extrusion. Only, a decrease in hardness was detected, from 62.0 N to 51.1 N. For PPI, re-extrusion did reduce the cutting force and hardness but not the anisotropy index. It was concluded that even though HME induces a loss of solubility and WHC, this did not affect the fibrous texture formation of the protein. This means that the texture formed during HME does not depend on the process history and that rework is thus possible for fibrous products.

Aldehydes are important flavor molecules to consider in plant-based products. Here, the flavor retention of a series of saturated aldehydes and mono-unsaturated aldehydes (2-alkenals) with different chain lengths (C4, C6, C8, and C10) in dispersions with protein isolates of pea, soy, fava bean, chickpea, and whey (as reference) was analyzed with APCI-TOF-MS. The headspace concentrations of alkenals were lower than aldehydes, meaning alkenals were retained more than saturated aldehydes. The retention was modeled by assuming hydrophobic interactions and covalent interactions. The ratio between the hydrophobic interaction parameter and the covalent parameter showed that covalent interactions are mainly important for butanal and butenal (C4). For the other aldehydes, hydrophobic interactions became increasingly important. Correlations were found between the chemical interaction parameters and the cysteine and methionine content of the different proteins. The obtained model parameters for each set of proteins and flavors allow the prediction of flavor retention when developing a flavored product with high protein content.

Novel pulsed electric field (PEF) applications to modify the techno-functionality of biomacromolecules have recently emerged. Insights into the involved interplay of factor domains (electrical, flow, concentration, temperature) with respect to the treatment chamber locations, and into the scalability are lacking. Therefore, a parallel plate batch (0.8 mL) and a scaled up parallel plate continuous (50 mL, 0.83 mL s-1) setup were built and simulated to investigate these domains and resulting gradient interactions using liquid whey protein solutions (0.5% w/w). In both setups, protein agglomerations and aggregations were observed below 60 degrees C at the electrode boundary layers for pulses in the range of 2-2.5 kV cm-1, 10 mu s, 40-350 Hz. The boundary layer is characterized by higher protein concentrations due to temperature- and pH-dependent migration trajectories, increased electrochemical reactivity (e.g., pH), and increased residence times due to the laminar flow or no flow conditions. Characterizing the domain interconnectivity led to effective scaling-up approaches of protein aggregations and insights into involved mechanisms.

The interaction between flavors and proteins results in a reduced headspace concentration of the flavor, affecting flavor perception. We analyzed the retention of a series of esters and ketones with different chain lengths (C4, C6, C8, and C10) by protein isolates of yellow pea, soy, fava bean, and chickpea, with whey as a reference. An increase in protein concentration led to a decrease in flavor compound in the headspace as measured with atmospheric pressure chemical ionization time-of-flight mass spectroscopy (APCI-TOF-MS). Flavor retention was described with a flavor-partitioning model. It was found that flavor retention could be well predicted with the octanol-water partitioning coefficient and by fitting the hydrophobic interaction parameter. Hydrophobic interactions were highest for chickpea, followed by pea, fava bean, whey, and soy. However, the obtained predictive model was less appropriate for methyl decanoate, possibly due to its solubility. The obtained models and fitted parameters are relevant when designing flavored products with high protein concentrations.

Pea protein isolates (PPI) mainly contain globulin proteins responsible for forming fragile gels affecting the texture properties of plant-based foods like extruded meat analogs. This study aims to extract a soluble protein fraction (SPF) from air-classified pea protein concentrate (PPC) containing globulins and albumins and use it directly in its liquid form to enhance the elasticity of PPI gels and extrudates produced by high moisture extrusion (HME). Two commercially available PPIs and one PPC were characterized by protein solubility, differential scanning calorimetry, and heat-induced gelation capacity by rotational rheology. Gel characterization was done by small amplitude oscillation rheology. Protein extraction at concentrations between 5% and 10% w/w and mildly alkaline pH was the most efficient way to produce functional SPF with high protein yield (> 67%). The SPF had a positive effect on the yield strain of PPI gels. However, the effect on the elastic modulus (G') depended on the degree of protein isolate purification. Moreover, adding SPF directly as wet feed in HME reduced the brittleness of PPI extrudates. This research highlights the texture formation potential of minimally pre-processed pea protein ingredients in plant-based foods (e.g., meat analogs) manufactured with HME.

The market has observed a rapid increase in the demand for plant-based foods as an alternative to animal meat products. Technologies such as high-moisture extrusion (HME) have the potential to develop anisotropic structures using alternative protein ingredients. This article discusses the different possible mechanisms responsible for structure formation and the effect of extrusion process parameters and outlines the recent advances in the long cooling dies (LCDs) used for meat alternative development. The role of different protein ingredients and the impact of combining them with other biopolymers were also evaluated. The underlying mechanism behind anisotropic structure formation during HME is a synergistic effect, with substantial dependence on the source of ingredients and their processing background. Formulation including proteins derived from plants, insects, animals, and microalgae with other biopolymers could pave the way to develop structured meat alternatives and fill nutritional interstices. Dynamic or rotating annular gap cooling dies operating at freely controllable shear and static annular gap dies are recent developments and assist to produce layered or fibrous structures. The complex chemical sites created during the HME of plant protein favour flavour and colour retention. This paper summarises the recent information published in the scientific literature and patents, which could further help researchers to fill the present knowledge gaps.

We have developed a new methodology for measuring aroma release by coupling together two high performance instruments, a proton-transfer-reaction mass spectrometer and closed-cell pressure-controlled rheometer. In this article we report the aroma release from aqueous solutions as a function of different agitation levels, in connection with the theoretical model of mass transfer across interfaces. Two aspects are described in more detail: (1) the use of model parameters to fit the aroma release curves, and (2) the underlying theoretical model in terms of the separate mass transfer coefficients for the liquid phase and the gas phase, including the dependency of these mass transfer coefficients on agitation. As expected from classical theories, the mass transfer coefficient for the liquid phase was found to correlate with agitation of the liquid phase following a power law relation. The overall aroma release was found to be related to a combination of factors: the thermodynamic equilibrium partition coefficient, as well as the mass transfer coefficient for the liquid phase (at low agitation levels) and the mass transfer coefficient for the gas phase (at high agitation levels). Industrial relevance: The use of modelling based on the dynamics and mechanistic aspects of aroma release enables a better understanding of the aroma release in real life, and therefore a shorter development cycle for new products. Currently, many experimental studies on aroma release underexpose the need for understanding the dynamics and mechanistic aspects of mass transfer. The new methodology with more accurate measurements and more robust fitting is essential for obtaining experimental data that can be fitted with details of mass transfer models. Furthermore, the experimental system and approach can be used directly in an empiric way for the optimization of the aroma impact and profile of new food products.

Whey proteins are being integrated as high-value food product ingredients due to their versatile and tunable techno-functionality. To meet high food quality and clean label expectations by consumers, electric field (EF) technologies have been proposed to open new frontiers in this field. Despite a variety of studies, it remains ambiguous which EF parameters are crucial to achieving targeted whey protein modifications. Reconstituted liquid whey protein concentrate (WPCL) and filtered, non-heat-treated liquid whey (WPL_filt) at low protein dry weight concentrations (0.4% wt/wt) were exposed to microsecond pulsed electric field (μsPEF) treatments at EF intensities between 1.25 and 12.5 kV/cm, pulse repetition frequencies between 0.38 and 85 Hz, and pulse lengths set to 10 or 100 μs. Protein aggregations were quantified spectroscopically. We report here that aggregates formed at lower temperatures for μsPEF compared with purely thermal treatments in identical treatment geometries at similar time-temperature profiles. We suggest that the observed increase in absorbance is linked to protein migration, the isoelectric point, local deprotonation phenomena of thiol groups, and cation precipitation. The μsPEF treatment time, which is dependent on the pulse repetition frequency, pulse length, and time of process, is the main driver of the increase in absorbance. High EF intensities balanced with shorter pulse repetition frequencies to ensure similar energy inputs resulted in no aggregate formation. For WPL_filt, 12.5 kV/cm, 10 μs, 0.38 Hz (620 ± 96 kJ/kg; ± standard deviation) did not result in an increase in absorbance, whereas 1.25 kV/cm, 10 μs, 50 Hz (634 ± 57 kJ/kg) with similar time-temperature profiles increased the absorbance at a wavelength of 380 nm by a factor of 8.2 ± 1.7 compared with untreated WPL_filt. In conclusion, the treatment time seems to dominate over high EF intensities at similar energy inputs for aggregate formation and increase in absorbance.

Flaxseeds are typically consumed either as whole flaxseed, ground flaxseed, flaxseed oil, partially defatted flaxseed meal, or as a milk alternative. They are considered a rich source of vitamins, minerals, proteins and peptides, lipids, carbohydrates, lignans, and dietary fiber, which have shown hypolipidemic, antiatherogenic, anticholesterolemic, and anti-inflammatory property activity. Here, an in vitro batch culture model was used to investigate the influence of whole milled flaxseed and partially defatted milled flaxseed press cake on the gut microbiota and the liberation of flaxseed bioactives. Microbial communities were profiled using 16S rRNA gene-based highthroughput sequencing with targeted mass spectrometry measuring lignan, cyclolinopeptide, and bile acid content and HPLC for short-chain fatty acid profiles. Flaxseed supplementation decreased gut microbiota richness with Firmicutes, Proteobacteria, and Bacteroidetes becoming the predominant phyla. Secoisolariciresinol, enterodiol, and enterolactone were rapidly produced with acetic acid, butyric acid, and propionic acid being the predominant acids after 24 h of fermentation. The flaxseed press cake and whole flaxseed were equivalent in microbiota changes and functionality. However, press cake may be superior as a functional additive in a variety of foods in terms of consumer acceptance as it would be more resistant to oxidative changes.

The present study challenges the in vivo assessment of cold atmospheric pressure plasma (CAPP) technology on the bioactive activity (antioxidant/antiaging and antimicrobial potential) of Spirulina powder, using Caenorhabditis elegans as an animal model. Surface microdischarge cold atmospheric pressure plasma (SMD-CAPP) treatment was 3.3 W discharge power for 7 min. C. elegans lifespan and egg laying were used as indicators of antioxidant/antiaging potential of Spirulina (1 mg/mL), when grown with Spirulina CP-treated [E_SCP] and untreated [E_S], compared with a control [E_0] (non-supplemented with Spirulina). According to our results, under both Spirulina supplemented media [E_SCP and E_S] and for the first 17 days, nematodes experienced an increase in lifespan but without significant differences (p > 0.05) between control and Spirulina CP-treated. Regarding the in vivo assay of the antimicrobial potential of Spirulina against Salmonella enterica serovar Typhimurium (infected worms), no significant differences (p > 0.05) were found between the three exposure scenarios (control [S_0]; Spirulina supplemented media [S_S]; CP-treated Spirulina supplemented media [S_SCP]). According to present results, CAPP-treatment do not influence negatively the lifespan of C. elegans but a reduction in the Spirulina antiaging potential was found. No in vivo modifications in antimicrobial activity seem to be linked to CAPP-processed Spirulina.