Pea Protein Isolate Research Articles

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 → 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.

Rheology of plant protein–polysaccharide gel inks for 3D food printing: Modeling and structure–property relations

Plant protein–polysaccharide composite hydrogels and emulsion gels are attractive materials for production of edible inks for 3D food printing. Their ability to satisfy the printability requirements is conventionally evaluated in small- and large-amplitude oscillatory shear tests. A model is derived that describes experimental data in linear and nonlinear rheological tests on protein gels in a unified manner. The model is based on the population-balance approach and involves a reasonably small number of adjustable parameters. Fitting observations on soy protein isolate–xanthan gum, peanut protein–gellan gum, peanut protein–carrageenan, pea protein–carrageenan and pea protein isolate–flaxseed gum gels demonstrates that material parameters evolve consistently with composition of the gels. The governing equations describe adequately the effects of pH and ionic strength of aqueous solutions on the mechanical properties of the gels and predict the stress–strain Lissajous curves and the crossover amplitudes for transition from the solid-like to fluid-like response. Based on the analysis of observations in large-amplitude oscillatory tests with various frequencies, a mechanism is proposed for transition from the type-I (strain thinning) to type-III (weak strain overshoot) response of protein–polysaccharide gels.

Chemical stability of β-carotene composite or bilayer emulsions coated with pea protein isolate and γ-polyglutamic acid compared to monolayer emulsion

Abstract The integration of β-carotene into functional foods is limited due to its limited hydrophilicity and chemical stability. To address this issue, emulsion was encouraged to be utilized. Monolayer, composite, and bilayer emulsions were prepared using pea protein isolate (PPI) alone or in combination with poly-γ-glutamic acid (γ-PGA). Our findings indicate that the bilayer emulsion utilizing γ-PGA as an external emulsifier exhibited the smallest droplet size (737.61 nm) and highest zeta potential (−35.23 mV). Under various environmental stresses, the chemical stability of the composite emulsion surpassed that of the monolayer emulsion but was inferior to that of the bilayer emulsion. Moreover, following simulated gastrointestinal digestion, the β-carotene bioaccessibility in the composite emulsion (12.76 %) exceeded that in the monolayer emulsion (6.57 %) but was less than that in the bilayer emulsion (20.01 %). Therefore, the emulsion preparation method or the sequence of γ-PGA addition significantly affects emulsion stability. Among the studied emulsions, the bilayer emulsion demonstrated the most stable structure, enhancing the stability of β-carotene within the oil droplets.

Development of plant‐based burger patties with pea protein isolate and barnyard millet flour and its storage stability in aerobic and vacuum packaging

AbstractThere is an increasing demand for plant‐based burger patties owing to the health and sustainability issues raised from the consumption of meat. This study aimed to develop plant‐based burger patties from pea protein isolates (PPIs) and barnyard millet flour (BMF) through high‐moisture extrusion cooking. The extrudates for plant‐based burger patties were developed with a blend ratio of 90:10 PPIs:BMF with different screw speeds ranging from 40 to 120 rpm. The extrudates produced with different screw speeds were analyzed, followed by the analysis of the plant‐based burger patties. Commercial plant‐based burger patties were used as a control. The optimized plant‐based burger patties were then stored in aerobic or vacuum packaging for 12 days under refrigerated condition and analyzed. The optimized extrudates produced using screw speed of 80 rpm displayed moderate water absorption index (3.33%), high hardness (4143–4390 g), and high adhesion (0.47 mJ). The plant‐based burger patties produced using the optimized extrudates had 2006–2608‐g hardness, 0.17 cohesiveness, and 6.70% cooking loss. In comparison to aerobic packaging, the plant‐based burger patties stored in vacuum packaging demonstrated lower cooking loss (8.46%), moisture content (18.03%), total color difference (3.02), and total plate count (8.65 log10 cfu/g) after 12 days of refrigerated storage. The protein content of plant‐based burger patties was not affected throughout the refrigerated storage. This shows the potential of PPIs and BMF mixtures as meat analogue ingredients and the suitability of vacuum packaging for the storage of plant‐based meat.

High internal phase double emulsions stabilized by modified pea protein-alginate complexes: Application for co-encapsulation of riboflavin and β-carotene

The application of many hydrophilic and hydrophobic nutraceuticals is limited by their poor solubility, chemical stability, and/or bioaccessibility. In this study, a novel Pickering high internal phase double emulsion co-stabilized by modified pea protein isolate (PPI) and sodium alginate (SA) was developed for the co-encapsulation of model hydrophilic (riboflavin) and hydrophobic (β-carotene) nutraceuticals. Initially, the effect of emulsifier type in the external water phase on emulsion formation and stability was examined, including commercial PPI (C-PPI), C-PPI-SA complex, homogenized and ultrasonicated PPI (HU-PPI), and HU-PPI-SA complex. The encapsulation and protective effects of these double emulsions on hydrophilic riboflavin and hydrophobic β-carotene were then evaluated. The results demonstrated that the thermal and storage stabilities of the double emulsion formulated from HU-PPI-SA were high, which was attributed to the formation of a thick biopolymer coating around the oil droplets, as well as thickening of the aqueous phase. Encapsulation significantly improved the photostability of the two nutraceuticals. The double emulsion formulated from HU-PPI-SA significantly improved the in vitro bioaccessibility of β-carotene, which was mainly attributed to inhibition of its chemical degradation under simulated acidic gastric conditions. The novel delivery system may therefore be used for the development of functional foods containing multiple nutraceuticals.

Solubility, (micro)structure, and in vitro digestion of pea protein dispersions as affected by high pressure homogenization and environmental conditions

In this work, dispersions were prepared with commercial pea protein isolate (PPI) and subjected to different (i) high pressure homogenization (HPH) intensities (0 – 200 MPa) (room temperature, pH 7) or (ii) environmental conditions (60 °C, pH 7 or pH 12) to generate dispersions with distinct protein molecular and microstructural characteristics, impacting protein solubility. Besides, protein digestion was analyzed following the static INFOGEST in vitro digestion protocol. Generally, increasing pressure of the homogenization treatment was linked with decreasing particle sizes and enhanced protein digestion. More specifically, the dispersion that did not undergo HPH (0 MPa) as well as the dispersion treated at 60 °C, pH 7, had highly similar microstructures, consisting of large irregular particles (10 – 500 µm) with shell-like structures, and exhibited low solubility (around 15 % and 28 %, respectively), which resulted in limited proteolysis (35 % and 42 %, respectively). In contrast, the dispersion subjected to HPH at 100 MPa and the dispersion treated at 60 °C, pH 12 also had similar microstructures with small and homogeneous particles (<1 µm), and exhibited relatively good solubility (54 % and 31 %, respectively), which led to enhanced protein digestion levels (87 % and 74 %, respectively). This study highlights the potential of food processing on macronutrient (micro)structure and further gastrointestinal stability and functionality.

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.

Sensory and Physical Properties of Fibrous Meat Analogs Made from Faba Bean, Pea, and Oat Using High-Moisture Extrusion.

Faba bean is a promising source of ingredients for the production of meat analogs. However, sensory properties of faba bean, especially the bitter taste of the protein concentrate, restrict its use. Our aim was to assess the feasibility of two types of faba bean ingredients-flour (from germinated, gently heat-treated beans) and groat (from non-germinated, roasted beans)-in combination with pea protein isolate and oat fiber concentrate for producing meat analogs using high-moisture extrusion. We produced six samples using varying recipes, while maintaining constant process parameters. An untrained panel (55 participants) evaluated the samples for key sensory attributes (check-all-that-apply) and rated their pleasantness. The water absorption capacity and mechanical properties of the samples were assessed using instrumental measurements. The samples were frequently described as 'beany' and 'tasteless', but very rarely as 'bitter'. The most frequently cited attributes for mouthfeel varied between the samples containing 30% ('tough', 'gummy') and 50% ('crumbly', 'floury') of faba bean flour/groat and were associated with corresponding mechanical properties. On average, the sample containing a blend of faba bean groat and pea protein isolate (50% each) appeared to be the most pleasant. Our results suggest that faba bean groat with pea protein isolate enables the production of fibrous meat analogs with acceptable taste and texture, without the bitter off-taste.

Swelling of food powders: Kinetics measurement and quantification using NMR relaxometry

Quantitative data on powder swelling kinetics is essential to understand phenomena occurring during rehydration, e.g. lump formation. In this study, swelling kinetics of food powders (gelatin powder, soy protein isolate, pea protein concentrate) were quantified by Nuclear Magnetic Resonance (NMR) relaxometry. Using gelatin plates as a model system, it was successfully demonstrated that NMR relaxometry is an efficient, non-destructive method to study swelling kinetics of non-dissolving systems with moderate swelling speeds. For plant-based proteins, high swelling speeds were observed. The obtained maximum water uptake due to swelling was 5.10 ± 0.80 g/g for soy protein isolate and 3.93 ± 0.16 g/g for pea protein isolate, which is in the expected range. Measurement speed was too low to resolve early swelling kinetics (below 84 s), evaluation was more elaborate and results less unambiguous.

Exploring the effect of corn starch/pea protein blending on the physicochemical and structural properties of biopolymer films and their aging resistance

This study investigated the potential effect of blending corn starch and pea protein isolate in various ratios (100:0, 70:30, 50:50, 30:70, and 0:100) on the aging properties of biodegradable films. Unlike previous research, the focus was on the often-overlooked aspect of film aging. Fourier-transform infrared spectroscopy and X-ray diffraction demonstrated the physical blending of corn starch and pea protein, along with chemical bonding and conformational changes. The optical and microstructural properties showed the formation of smooth, homogeneous films with good compatibility between the polymers. The water resistance, barrier, and mechanical properties corresponding to the intrinsic nature of protein polymers showed a minimized fluctuations in film properties as film ages, with a reduction of at least twice when protein is added. Remarkably, the blend with a ratio of 30:70 demonstrated the most stable properties during aging. These results demonstrated that blending the pea protein isolate was favorable for delaying the retrogradation and recrystallization of corn starch films. Understanding how these blends influence the aging characteristics of films is not only a novel contribution to the scientific community but also holds practical significance, potentially opening a potential for applications in various industries.

Interactions with soy lecithin regulate the emulsification capacity of pea protein: Effects of soy lecithin concentration

Interactions between pea protein isolate (PPI, 1%) and soy lecithin (SL, 0.1%–2%) in bulk phase and the impacts on the emulsifying properties of PPI were investigated. Fluorescence spectra, molecular docking, and infrared spectroscopy verified that PPI and SL formed complexes in aqueous phase via hydrophobic interactions, hydrogen bonds, and electrostatic interactions. CMC of SL was increased to 1% in presence of PPI (1%). Increased particle size, surface charge, and surface hydrophobicity of PPI-SL complexes with increasing SL concentrations were observed. Addition of SL transformed the composition of oil/water interface from pure PPI into a mixture of PPI and SL, which decreased the surface tension and resulted in smaller droplet size of emulsions. The inclusion of all PPI-SL complexes enhanced emulsion stability during storage. Incorporating SL below 1% also showed similar protective effects for curcumin against UV irradiation compared to pure PPI. The study may provide a theoretical basis for the rational non-covalent combination of pea protein and lecithin as complex emulsifiers.

Transglutaminase-crosslinked cold-set pea protein isolate gels modified by pH shifting: Properties, structure and formation mechanisms

The poor gelation properties of pea protein isolate (PPI) limit their use in food industries. In the present study, PPI was modified by pH-shifting combined with heat treatment, followed by cold-set gelation of PPI gels induced by transglutaminase. Both pH 2–3 and pH 10–12 promoted the unfolding of PPI molecules and the transformation of secondary structures from ordered to disordered. In particular, PPI molecules with pH 12-shifting tended to expand and unfold, which resulted in the exposure of internal active groups and improvement in surface hydrophobicity. Accordingly, after the addition of 50 U/g transglutaminase, PPI gels with pH 12-shifting and heating treatment exhibited homogeneous and dense gel network with high cross-linking degree (88.12 ± 1.80%) and water holding capacity (92.13 ± 2.40%), since pH 12-shifting and heating treatment promoted the conversion of random coils and β-turns to β-folds and α-helices in PPI gels. However, with pH 10 and 11-shifting, the PPI molecules was partially unfolded and the PPI gels had a high non-network protein content, resulting in low-strength gel networks of PPI gels with rough and loose microstructures and a low WHC. These results showed that TGase-crosslinked cold-set PPI gels after pH 12-shifting and heat treatment could promote the formation of homogeneous and dense gel network structure, so that improved the PPI gelation properties, which had great potential to be used as gelling agents or nutraceutical delivery systems for thermal sensitive bioactive compounds in food and non-food fields.

Pea protein isolate-soluble soybean polysaccharides electrostatic assembly: effect of pH, biopolymer mass ratio and heat treatment.

In past years, thousands of protein-polysaccharide complexes have been investigated to modify protein characteristics and functionality in food systems. However, the interaction between pea protein isolate (PPI) and soluble soybean polysaccharide (SSPS) has not been thoroughly characterized yet. In the present study, the phase behavior of PPI and SSPS mixtures was analyzed as a function of PPI:SSPS mixing ratio (1:1 to 1:0.10) and pH (7.0 to 2.0), showing that these biopolymers could be electrostatically assembled at 1:1 to 1:0.25 mixing ratios and 4.0 to 3.0 pH values. Then, the characteristics of the PPI-SSPS complexes were studied before and after heating (90 °C and 30 min) by ζ-potential, surface hydrophobicity, protein solubility, particle size distribution and physical stability for 56 days. By lowering the pH and PPI:SSPS mixing ratio, the complexes showed increased solubility, changed 𝜁-potential and higher physical stability. By heating, the complexes presented increased hydrophobicity and physical stability. Overall, PPI-SSPS complexes increased the protein solubility, reduced the particle size, and changed both the ζ-potential and the surface hydrophobicity with respect to PPI control, allowing stabilization of the colloidal system and broadening the possible applications of these high-quality proteins in acidic food systems. © 2024 Society of Chemical Industry.

Comparative studies on enhancing pea protein extraction recovery rates and structural integrity using ultrasonic and hydrodynamic cavitation technologies

This study explored the efficacy of various cavitation technologies, including ultrasonic bath (USB), ultrasonic plate (US-plate), ultrasonic probe (US-probe), and hydrodynamic cavitation (HDC), in extracting proteins from peas. US-probe showed the highest protein recovery rate (52.53 g/hg protein in pea powder) among all lab-scale cavitation equipment while HDC demonstrated significant potential for scaling up, notably improving both the purity (80.35 g/hg dried precipitate) and recovery rate (56.85 g/hg) of pea protein isolate (PPI) compared to conventional extraction (CE). SDS-PAGE, LC-MS/MS, FTIR and Fluorescence analysis were used to analyse the impact of these cavitation technologies on the structures of pea protein. The results confirmed that cavitation preserved PPI's primary structure while altering its secondary and tertiary structures, particularly under US-probe treatment, which significantly unfolded proteins. The SEM results revealed a marked reduction in protein bodies adhering to starch granules in residues from US-probe and HDC treatments compared to CE, correlating with their higher protein recovery rates.

Antioxidant polypeptides derived from pigeon pea (Cajanus cajan (L) Mill sp.) by enzymatic hydrolysis

Pigeon pea (Cajanus cajan (L) Mill sp.) seeds are rich sources of protein in the legume family and their consumption has been associated with the prevention of noncommunicated diseases, which is attributable to their content of bioactive components. Antioxidant protein hydrolysates were produced from pigeon pea protein isolate (PPI) by enzymatic hydrolysis using pancreatin and flavourzyme. The hydrolysates were analyzed for their physicochemical, molecular weight, amino acid composition, and in vitro antioxidant activities. The molecular weights of polypeptides in the hydrolysates were 8, 20, 25 and 48 kDa, which were determined after pancreatin or flavourzyme hydrolysis of the protein isolate for 4 h. Pancreatin-hydrolyzed pigeon pea protein (PPHP) contained high hydrophobic amino acids, especially isoleucine, leucine and valine, which were related to the high content of aromatic amino acids. The hydrolysates obtained from flavourzyme hydrolysis of pigeon pea proteins (PPHF) presented significantly higher capacities to scavenge ABTS˙+ and reduce Fe3 + better than that of PPI, while the PPI exhibited strong DPPH scavenging (98.4 mg trolox equivalent antioxidant capacity). The results indicated that the partial hydrolysis for PPI provided medium to high molecular weight of peptides. Therefore, PPHF could be a promising source of bioactive peptides and a potential ingredient for the formulation of functional foods against oxidative stress

Influence of emulsifier on lipid oxidation in spray-dried microencapsulated O/W emulsions

Lipid oxidation limits the shelf-life of dried microencapsulated oils (DMOs), such as infant formula. However, it is poorly understood how lipid oxidation is affected by different types of emulsifiers. To improve our understanding, we prepared DMOs with different emulsifiers (whey protein isolate (WPI), pea protein isolate (PPI), and non-proteinaceous CITREM) and studied lipid oxidation in both the free and encapsulated fat. Only a small difference in oxidation rate was observed between these fat fractions for all formulations. We ascribed this to a non-discrete distribution of the fractions and the subsequent low fractionation selectivity as shown by Raman microscopy. The DMO with PPI showed hardly any oxidation during a 7-week incubation at 40 °C, whereas the DMOs with WPI and CITREM both reached significantly higher contents of oxidation products (lipid hydroperoxides, aldehydes, and epoxides). The enhanced stability of DMO-PPI could not be ascribed to the presence of phytic acid. In conclusion, we demonstrate the potential of using PPI to produce oxidatively stable DMOs.

High moisture extrusion of pea protein isolate to mimic chicken texture: Instrumental and sensory insights

High moisture extrusion processing (HMEP) is gaining attention in the plant-based food industry to obtain meat-like textures from different vegetal protein sources. The aim of this study was to evaluate the impact of extrusion process parameters (water feeding rate, barrel temperature and screw speed) on the texture and moisture content of high moisture extrudates (HME) from pea protein isolate using response surface methodology. Sensory textural profile of selected HME was compared with those of cooked chicken breast and a commercial extruded meat analogue sample. Extrusion process parameters had a significant effect on the characteristics of the final product. Barrel temperatures between 145 °C and 165 °C and a water feed rate between 53% and 57% produced HME with an instrumental texture similar to cooked chicken breast, 165 °C and 55% water feed being the conditions that produced the HME with the highest meat-like appearance and sensory fibrousness.

Digital Image Analysis to Evaluate Sensory Attributes of Protein-Enriched Whole-Wheat Bread

New food products or reformulated food products require intensive sensory assessment using a group of panelists before launching in the market. Sometimes, the sensory results obtained by the panelists are inconclusive due to their subjective scores. An indirect and accurate method to evaluate the sensory attributes using images is highly beneficial to conduct preliminary screening during product development stages. Therefore, the objective of this study was to determine the potential of red-green-blue (RGB) color images to evaluate the sensory qualities of whole wheat bread reformulated with pea and soy protein isolates as model food. In this study, reformulated whole wheat (WW) bread was used as model food to determine the potential of digital color images in assessing the selected sensory attributes. Seven types of WW bread was evaluated by ten untrained panelists. Four features (edge detection, pore numbers, pore area and Hu-moment similarity) were extracted from the images of the bread slices and compared with measured sensory scores. In general, the polynomial regression models yielded higher R2 values than linear regression models. The R2 values in polynomial regression models ranged 0.82-0.97, 0.60-0.92, 0.55-0.96, 0.77-0.99, 0.67-0.97, and 0.50-0.87 for chewiness, graininess, moistness, taste, desired aroma and overall acceptability, respectively. Hu-moment similarity provided the highest R2 values for the sensory attributes in polynomial regression models. In conclusion, although image-based sensory assessment may not substitute the current human sensory, it can provide valuable information to supplement the decision making process.

Improving functional merit of commercially available pea protein isolate by employing a combination of physical, chemical, and enzymatic modification

Pea protein-based diets have garnered global attention as a viable alternative to meat or primary protein sources. Nevertheless, the utilization of pea protein is hindered by issues such as solubility, and emulsifying properties. This research presents a combined set of techniques employed to commercially available Pea Protein Isolate (PPI) to effectively address major setbacks associated with the usage of pea protein in diverse industrial sectors, especially meat. The set integrates pH at 10.0, sonication at three different magnitudes (1,2 and 4 W/mL), heat at 60 °C, and enzyme hydrolysis through Flavourzyme at three different enzyme-to-substrate ratios (0.25%, 0.5%, and 1.0%). Among the twelve treatments, PPI11, PPI12, and PPI13 showed promising outcomes for artificial meat. The treatments exhibited favorable solubility, gelling, emulsifying, and foaming properties while containing the optimum and desirable protein size after undergoing partial hydrolysis comprehended in the gel electrophoresis results. Solubility (for PPI11, PPI12, PPI13) had seen significant (p < 0.05) improvement from 31.03% ± 2.11% (Control) to 64.43% ± 2.09%, 66.23% ± 2.11%, and 69.87% ± 1.57%, accompanied by changes in protein morphology in scanning electron microscopy. Furthermore, treated PPIs were applied to stabilize sunflower oil-in-water emulsion, showing a significant escalation in emulsion capacity (38.46%, 39.42% and 66.61% increase for PPI11, PPI12, PPI13), foaming capacity (46.88%, 51.20%, and 69.60% increase for PPI11, PPI12, PPI13), and foaming stability (30 min) (23.97%, 28.70%, and 30.22% increase for PPI11, PPI12, PPI13). Gelling properties were decisive in this study (2.512 ± 0.1 N, 2.604 ± 0.1 N, and 2.168 ± 0.3 N, for PPI11, PPI12, and PPI13), predominantly in plant-based meat analog perspective. So the mechanism proposed through this research will enable pea protein treated with this set of operations, combining physical, chemical and enzymatic treatments, to further its journey towards considerably improved meat analogs.

Improvement in 3D printability, rheological and mechanical properties of pea protein gels prepared by plasma activated microbubble water

Three-dimensional (3D) food printing is one of the emerging processing technologies that enables the construction of complex food structures and customization. Although various food ingredients have been explored for their 3D printability, pea protein is among the plant proteins that have not been studied extensively on its 3D printability, owing to its native inability to hold shape and structure following extrusion. This study investigated the effect of plasma activated microbubble (PAMB) treatment on the thermal gelation and 3D printability of pea protein isolate (PPI). PAMB treatments with different combinations of discharge gases (80% argon and 20% air, 90% argon and 10% air, 100% argon, and 100% air) were applied to prepare PPI suspensions. These suspensions were then heated at 85 °C for 30 and 60 min, followed by immediate cooling to prepare PPI gels. The viscoelastic measurements and mechanical properties of PPI gels indicated that this combined application was suitable for 3D printing, with a notable increase in storage modulus (G '), loss modulus (G '') and compressive stress in PPI-PAMB gels. The 3D printed PPI gels prepared using PAMB treatment exhibited better structure retention, resistance to deformation, and stability during storage. The treatment using PAMB prepared by the combination of argon and air, i.e., 80% argon and 20% air and 90% argon and 10% air, resulted in PPI gels with better rheological properties, mechanical stability, and 3D printability. Freeze drying was investigated as a possible post-3D printing processing operation to enhance the shelf life and storage stability of 3D printed PPI gels. The moisture content, water activity, and textural properties of the freeze-dried 3D printed PPI were investigated.