Plant-based protein formulation is difficult because plant proteins carry off-flavors, lose solubility near their isoelectric point, build grainy or chalky texture, and deliver an incomplete amino acid profile relative to animal proteins. For product developers, the recurring problems are predictable: beany and bitter notes driven largely by lipid oxidation, sharp solubility loss around pH 4 to 5, sedimentation and grittiness in beverages, limiting amino acids (lysine in cereals, methionine and cysteine in legumes), and antinutrients that can lower digestibility and mineral absorption.
Most of these problems are solvable through source selection, extraction method, blending, masking, and texturization rather than through a single ingredient. Vitafoods Europe 2026 in Barcelona showed where the industry is converging: blended proteins for complete profiles, clearer and more soluble beverage systems, cleaner taste through masking, fermentation and texturization for functionality, upcycled sourcing, and AI-assisted formulation. This article covers the core formulation challenges first and then the practical lessons that we presented at the show.
Table of Contents
- What Makes Plant-Based Proteins Difficult to Formulate
- Off-Flavors: Beany, Bitter, and Earthy Notes
- Solubility, pH, and the Isoelectric Point
- Texture, Grittiness, and Mouthfeel
- Protein Quality: DIAAS, Limiting Amino Acids, and Blending
- Antinutrients and Their Effect on Digestibility
- How Source and Extraction Method Shape Functionality
- Regulatory Status: Novel Food and Allergen Labeling
- Lessons from Vitafoods Europe 2026
- Frequently Asked Questions
- Key Takeaways
- Sources
What Makes Plant-Based Proteins Difficult to Formulate
Plant-based proteins are difficult to formulate because their sensory, physicochemical, and nutritional properties were shaped by the seed, not by the product developer. Unlike whey, which is highly soluble and relatively heat and acid stable, plant proteins typically arrive with characteristic off-flavors, narrow solubility windows, variable gelation, and an amino acid profile that is rarely complete on its own [1, 6].
These limitations compound one another. The same isolation step that raises protein content can also concentrate off-flavor compounds and antinutrients, while heat treatment that improves microbial safety can denature protein and trigger aggregation, so a formulator manages trade-offs rather than a single variable. Many of these decisions begin with plant protein ingredient selection, because the chosen flour, concentrate, or isolate sets the ceiling on what later processing can achieve.
See and download our infographic on Mastering Plant-Based Protein Formulation:
Off-Flavors: Beany, Bitter, and Earthy Notes
Off-flavors are the single most cited barrier to plant-protein adoption, and they are the first problem most formulators confront. Plant proteins commonly carry beany, grassy, bitter, earthy, astringent, and green notes that originate in the source material and intensify during processing and storage [2, 3]. A large share of these notes is generated by lipoxygenase-mediated oxidation of residual lipids into hydroperoxides, which degrade into volatile aldehydes, ketones, and alcohols such as hexanal [2].
Because the compounds are partly bound to the protein, simple flavor addition rarely covers them. The literature describes three broad strategies. Removal treatments such as soaking, thermal processing, germination, enzymatic hydrolysis, and solvent extraction reduce the precursor load before formulation [3]. Binding and masking approaches trap residual volatiles: cyclodextrins are a possible, “comparatively low-cost”, and safe option for binding beany compounds. Also, fermentation of legume substrates can generate polysaccharides that bind lipid-oxidation volatiles while shifting the aroma toward sweeter notes [2, 3]. Flavor and masking systems then cover what remains.
For developers, the practical lesson is that off-flavor control begins upstream. Selecting a source with lower residual lipid, specifying low-lipoxygenase raw material, and controlling oxygen exposure during drying and storage reduce the volatile load that downstream masking has to fight. Taste work that ignores these upstream levers tends to need higher masking doses and could still underdeliver.
Solubility, pH, and the Isoelectric Point
Solubility is the property that most often decides whether a plant protein works in a given format, and it is strongly pH-dependent. Protein solubility tends to reach its minimum near the isoelectric point, where the protein carries no net charge and aggregates. Pea protein, for example, has an isoelectric point around pH 4.5, and commercial plant protein isolates commonly show solubility in the range of only 5 to 10 percent near pH 4 to 5 [6, 7].
This behavior constrains beverage design in particular. Neutral systems in the pH 6.5 to 7.5 range suit plant-based milk alternatives and protein shakes, while clear acidic beverages generally need a pH below about 3.5 to move away from the precipitation zone, with the band in between being the hardest to stabilize [7]. Heat treatment adds a second constraint: thermal processing can denature plant proteins, promoting aggregation, age gelation, and pH drift over shelf life [7]. Stabilizer systems, for example gellan gum at roughly 0.02 to 0.05 percent, are often used to suspend particles and slow sedimentation without adding unwanted viscosity [7]. Particle engineering helps too, and techniques such as spray agglomeration can improve flowability and dispersion of plant-based powders.
Texture, Grittiness, and Mouthfeel
Texture problems in plant-protein products usually trace back to insoluble material and uncontrolled aggregation rather than to the protein concentration alone. Insoluble matter carried through isolation can leave products gritty or chalky, a defect that consumers detect quickly and that masking cannot fully hide [11]. In high-protein bars, the opposite failure mode appears over time: proteins continue to interact during storage, producing hardening and a dense, dry bite.
Gelation behavior is also source-dependent and cultivar-dependent. In legumes, the ratio of legumin to vicilin storage proteins influences gel character, with higher-legumin material tending toward firmer gels and higher-vicilin material toward softer, more elastic gels [6]. Formulators can use this to their advantage by matching protein fractions to the target texture, then supporting mouthfeel with hydrocolloids, particle-size reduction, or agglomeration. Protein functionality also underpins delivery systems beyond nutrition, since plant proteins are used to build carrier particles for poorly soluble actives and as emulsifiers in nanoemulsions.
Protein Quality: DIAAS, Limiting Amino Acids, and Blending
Protein quality is where plant proteins most often fall short of animal proteins, and it is measured by how well a protein supplies digestible indispensable amino acids. The Digestible Indispensable Amino Acid Score (DIAAS) is the method recommended by the Food and Agriculture Organization (FAO), and it improves on the older Protein Digestibility Corrected Amino Acid Score (PDCAAS) by using ileal digestibility of individual amino acids and by not truncating the score [5].
Most single-source plant proteins are limited by one or two amino acids. Cereals and grains such as wheat, rice, and oats tend to be limited in lysine, while legumes such as pea, soy, and faba bean tend to be limited in the sulfur amino acids methionine and cysteine [5]. The standard formulation response is complementary blending: combining a legume protein with a cereal protein offsets each one’s limiting amino acid and raises the overall score toward a complete profile. A rice and faba bean blend is a common example used in plant-based sports nutrition, where a well-formulated blend can support muscle protein synthesis comparably to animal protein. Beyond the familiar pulses, developers are also evaluating emerging plant protein sources such as mung bean, moringa seed, and bambara nut to widen sourcing and improve resilience.
| Plant protein source | Typical limiting amino acid | Relative solubility | Notable functional strength |
|---|---|---|---|
| Soy isolate | Methionine, cysteine | Moderate to high | High water-holding and emulsifying capacity [6] |
| Pea isolate | Methionine, cysteine | Moderate (isoelectric point near pH 4.5) | Functionality close to soy; widely available [6, 7] |
| Faba bean | Methionine, cysteine | Moderate (max at pH 7 to 8) | Good foaming; globulin similar to soy [6] |
| Rice | Lysine | Lower | Hypoallergenic profile; pairs well in blends [6] |
| Wheat (gluten) | Lysine | Low in water | Strong viscoelastic texture for analogs [6] |
Table 1. Indicative functional and nutritional profile of common plant protein sources. Values vary with cultivar, extraction method, and processing; treat as directional rather than absolute.
Antinutrients and Their Effect on Digestibility
Antinutrients are naturally occurring compounds in plant material that can lower protein and mineral availability, and they are a recurring quality concern for protein isolates. The main factors include phytic acid, trypsin inhibitors, lectins, saponins, and tannins, which can reduce protein digestibility and interfere with the absorption of minerals such as iron and zinc [8, 10].
A counterintuitive point matters for formulators: antinutrient levels are not always lower in purified ingredients. Studies report that phytic acid and trypsin inhibitors can be present at higher concentrations in protein concentrates and isolates than in the raw flour, because the extraction route co-concentrates them with protein [8]. The level depends heavily on the extraction method, with traditional wet processing using alkaline solubilization followed by isoelectric precipitation behaving differently from dry fractionation [8]. The same compounds also carry documented physiological benefits at lower intakes, so the goal is generally controlled reduction rather than total elimination [10]. Specifying antinutrient limits on incoming material, and understanding how a supplier’s process affects them, is part of responsible plant-protein sourcing.
How Source and Extraction Method Shape Functionality
Functionality in plant proteins is set as much by how the protein is extracted as by which plant it comes from. The overall functionality of pea protein is generally close to that of soy, whereas rice protein tends to match poorly on solubility, foaming, and emulsification [6]. Faba bean’s major globulin fraction resembles soy globulin in molecular structure, thermal stability, solubility, emulsification, and gelling, which makes it a flexible option across formats [6].
Extraction method then modulates these baseline traits. Concentrates produced by air classification can show lower protein content but higher solubility than isolates produced by isoelectric precipitation, because harsher wet processing can partially denature protein and reduce its solubility [6]. Surface hydrophobicity and solubility together drive emulsification, both of which are typically maximized around pH 7 to 8 for legume proteins [6]. Sensory and techno-functional benchmarking of commercial plant protein powders shows wide variation between products of the same nominal type, so two isolates from the same crop can perform very differently, and functional data, not just the species name, should drive ingredient qualification [11].
| Property | Driver | Formulation consequence |
|---|---|---|
| Solubility | pH relative to isoelectric point; extraction severity | Sets feasible beverage pH and dispersion behavior [6, 7] |
| Emulsification | Solubility and surface hydrophobicity (peak near pH 7 to 8) | Stability of plant-based emulsions and dressings [6] |
| Gelation | Legumin-to-vicilin ratio; heat history | Firmness versus elasticity in gels and analogs [6] |
| Off-flavor load | Residual lipid; lipoxygenase activity; storage | Masking burden and shelf-life flavor drift [2, 3] |
Table 2. How key functional properties are driven, and what they mean for formulation.
Regulatory Status: Novel Food and Allergen Labeling
Regulatory status for plant proteins is defined primarily by novel-food classification and allergen labeling, and it varies by region. In the European Union, common pulses such as soybean, pea, chickpea, lentil, and fava bean are not classified as novel foods, so their conventional protein fractions can be used without novel-food authorization [12, 13]. However, novel sources or novel processing can trigger the Novel Food procedure under Regulation (EU) 2015/2283: examples assessed by the European Food Safety Authority (EFSA) include mung bean protein and a protein made from pea and rice fermented by shiitake mycelia [12, 13].
Allergen labeling is a separate, strict obligation. Soybean and lupin are among the allergens listed in Annex II of Regulation (EU) No 1169/2011 and require declaration when used as ingredients, and EFSA updated its allergenicity risk-assessment guidance in 2024 [13, 14]. In the United States, soy is a major food allergen under the Food Allergen Labeling and Consumer Protection Act, while pea and rice are not designated major allergens, though cross-reactivity is documented in the literature. Regulatory status changes, so confirm current classification per ingredient and market before formulating.
Lessons from Vitafoods Europe 2026
Vitafoods Europe 2026, held May 5 to 7 in Barcelona, had plant-based and blended proteins as one of its defining themes, and the show offered a clear read on how the industry is addressing the challenges above. These proteins were presented as a route to combine functionality, sustainability, and improved digestibility, with consumers now expecting an experience beyond the chalky textures and flavor compromises historically tied to protein products [15, 16]. The broader context and ingredient highlights are captured in the Vitafoods Europe 2026 recap.
Blending and Complete Profiles Went Mainstream
Blended proteins were positioned as the default answer to the amino acid completeness problem, not as a niche tactic. BENEO presented faba bean and rice protein solutions, including its BeneoPro FB faba bean protein, that pair lysine-rich faba beans with the sulfur amino acids rice supplies to build a more complete profile for sports nutrition and everyday formats [9]. More broadly, combinations of complementary plant proteins, and plant-and-dairy hybrid systems, were shown as a way to deliver a fuller amino acid profile while balancing texture and cost [15, 16]. The pairing mirrors the formulation science: combining a methionine-limited legume with a lysine-limited cereal addresses both gaps at once. The show also reflected protein moving well beyond sports nutrition into everyday bars, ready-to-drink beverages, snacks, and cereals, which widens the range of textures and pH systems a single protein must tolerate.
Download BENEO’s Plant Protein Leaflet:
Beyond Chalky Textures: Clearer, More Soluble Beverages
Beverage formats were where progress on solubility and texture was most visible. Prinova offered booth visitors a clear pea protein drink aimed at plant-based consumers seeking post-workout recovery, evidence that improved solubility and acid-stable clarity are achievable near pea protein’s troublesome isoelectric point [15]. Ingredion focused on balancing protein, fiber, and reduced sugar in bars and ready-to-drink formats while keeping familiar texture and high drinkability, pairing plant proteins with stevia-based sugar reduction so taste does not suffer [19]. The common lesson is that beverage success still depends on managing pH away from the precipitation band and on stabilizer and particle-engineering systems, not on the protein alone.
Cleaner Taste Through Targeted Masking
Taste remained a central battleground, and the emphasis shifted toward systems engineered for specific plant-protein off-notes rather than generic sweetening. Flavor houses such as Synergy Flavours showcased taste and texture systems for protein-enriched products, built to counter the beany, bitter, and earthy notes that limit adoption, on the premise that consumers now expect an experience beyond the chalky texture and flavor compromises of earlier protein products [15, 16]. At the ingredient level, Roquette, an exhibitor at the show, has brought to market in 2026 a clean-tasting pea protein isolate (NUTRALYS Pea 850F) engineered for a neutral taste profile and enhanced solubility in ready-to-mix and ready-to-drink systems, which attacks off-notes before they reach the finished product [4]. The combined message was that taste is won upstream and downstream together: lower-off-note raw materials and oxidation control reduce the load before targeted masking finishes the job.
Fermentation and Texturization as Functionality Routes
Fermentation-derived and texturized proteins featured as a way to engineer functionality that native plant isolates struggle to deliver. Angel Yeast highlighted fermentation protein aimed at mainstream food and beverage use, reflecting how microbial routes are moving from niche applications into everyday formats [20]. Biomass fermentation, which is already economically viable at industrial scale, and precision fermentation, which is still scaling, were presented as complementary routes to proteins with strong gelling, emulsifying, and foaming behavior [17, 18]. Filamentous fungal proteins in particular can mimic the textural properties of animal proteins because of their fibrous structure, and texturization methods are extending what plant and microbial proteins can do in analog and hybrid formats [18].
Sustainability and Upcycled Sourcing as Baseline
Sustainability was framed as a baseline expectation rather than a differentiator. Exhibitors highlighted clean formulations, ethically sourced ingredients, upcycled raw materials, and eco-friendly packaging as standard selling points for plant-protein products [16]. For formulators, upcycled side-stream proteins introduce additional variability in composition and off-flavor load, which raises the importance of tight incoming specifications and functional testing.
AI-Assisted Formulation
Artificial intelligence appeared as a practical tool for managing plant-protein complexity. Platforms including MeNow AI, Enbiosis, Formulaite, Centric Software, and Siftlink addressed ingredient discovery, microbiome modeling, concept-to-formula automation, compliance screening, and molecular prediction, offering ways to navigate the many interacting variables in a plant-protein formula. The role of AI formulation tools is best understood as narrowing the design space and prioritizing experiments, with bench validation still required.
Frequently Asked Questions
Why do plant proteins taste beany or bitter? Plant proteins carry beany, bitter, and earthy notes that come from the source material and from lipid oxidation. Lipoxygenase enzymes convert residual lipids into hydroperoxides, which break down into volatile compounds such as hexanal during processing and storage. Because some of these compounds bind to the protein, controlling raw-material quality and oxidation is as important as adding masking or flavor systems.
What is the hardest pH range for plant-protein beverages? The hardest range is near the isoelectric point, roughly pH 4 to 5 for many plant proteins, where solubility is lowest and the protein precipitates. Pea protein has an isoelectric point around pH 4.5. Formulators generally target a neutral pH of 6.5 to 7.5 for milk-style drinks or acidify below about pH 3.5 for clear acidic beverages, avoiding the unstable middle band.
How do formulators make plant protein a complete protein? The standard approach is complementary blending. Cereals are typically limited in lysine and legumes in methionine and cysteine, so combining a cereal protein with a legume protein offsets both limitations. A rice and faba bean blend is a common example. Blending raises the overall amino acid score and can bring a plant system closer to a complete profile.
Are antinutrients always lower in protein isolates? No. Some antinutrients, including phytic acid and trypsin inhibitors, can be present at higher concentrations in concentrates and isolates than in the raw flour, because extraction co-concentrates them with protein. The exact level depends on the extraction method. Controlled reduction, guided by incoming specifications, is generally preferred over total elimination, since some compounds also have physiological benefits.
Do plant proteins require Novel Food authorization in the EU? Common pulses such as soybean, pea, chickpea, lentil, and fava bean are not novel foods, so their conventional protein fractions do not require authorization. Novel sources or novel processing methods can trigger the Novel Food procedure under Regulation (EU) 2015/2283. Soybean and lupin are also listed allergens requiring declaration. Confirm current status per ingredient and market.
What were the main plant-protein lessons from Vitafoods Europe 2026? Vitafoods Europe 2026 emphasized blended proteins for complete profiles, clearer and more soluble beverages, targeted off-flavor masking, fermentation and texturization for functionality, upcycled and sustainable sourcing, and AI-assisted formulation. The common thread was moving plant protein beyond sports nutrition into everyday formats while removing the chalky texture and flavor compromises that limited earlier products.
Key Takeaways
Plant-protein formulation challenges cluster into five areas: off-flavor, solubility and pH, texture, protein quality, and antinutrients, and they interact rather than act independently.
Off-flavors are driven largely by lipoxygenase-mediated lipid oxidation, so control starts upstream with raw-material selection and oxidation management before masking.
Solubility is lowest near the isoelectric point (around pH 4.5 for pea protein), which sets the feasible pH window for beverages and shapes stabilizer choice.
Single-source plant proteins are usually limited in lysine (cereals) or methionine and cysteine (legumes), and complementary blending is the standard route to a complete profile.
In the European Union, common pulse proteins are not novel foods, but novel sources or processing can require Novel Food authorization, and soybean and lupin require allergen labeling.
Vitafoods Europe 2026 showed the industry converging on blending, clearer beverages, targeted masking, fermentation and texturization, sustainable sourcing, and AI-assisted formulation.
Sources
- Zhao, H., et al. “Comparison of wheat, soybean, rice, and pea protein properties for effective applications in food products.” Journal of Food Biochemistry, 44(4), 2020.
https://onlinelibrary.wiley.com/doi/abs/10.1111/jfbc.13157. - Wang, Y., et al. “Cyclodextrins mask beany off-flavors in plant-based meat analogs.” PMC, 2022.
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9165781/. - Good Food Institute India. “Approaches to address off-flavour challenges associated with plant proteins.” GFI India.
https://gfi-india.org/solutions/approaches-to-address-off-flavour-challenges-associated-with-plant-proteins/ - Roquette. “Roquette Launches a Breakthrough Clean-Tasting Pea Protein Isolate (NUTRALYS Pea 850F).” Roquette press release, 2026.
https://www.roquette.com/press-releases/clean-tasting-pea-protein-isolate - Marinangeli, C., et al. “Plant Proteins: Methods of Quality Assessment and the Human Health Benefits of Pulses.” PMC, 2023.
https://pmc.ncbi.nlm.nih.gov/articles/PMC10417564/ - Devi, S., et al. “Prediction of emulsification behaviour of pea and faba bean protein concentrates and isolates from structure-functionality analysis.” PMC, 2021.
https://pmc.ncbi.nlm.nih.gov/articles/PMC8696636/. - BevSource. “Protein Beverages: Formulation Strategies for Success.” BevSource.
https://www.bevsource.com/news/protein-beverages-formulation-strategies. - Samtiya, M., et al. “Decoding the Duality of Antinutrients: Assessing the Impact of Protein Extraction Methods on Plant-Based Protein Sources.” Journal of Agricultural and Food Chemistry, 2024.
https://pmc.ncbi.nlm.nih.gov/articles/PMC11157537/.. - BENEO. “Faba Bean Protein (BeneoPro FB) and Plant Protein Solutions.” BENEO Human Nutrition.
https://www.beneo.com/human-nutrition/human-nutrition-products/functional-proteins/faba-bean-protein. - Samtiya, M., et al. “Plant food anti-nutritional factors and their reduction strategies: an overview.” Food Production, Processing and Nutrition, 2(6), 2020.
https://fppn.biomedcentral.com/articles/10.1186/s43014-020-0020-5. - Kornet, R., et al. “Techno-Functional and Sensory Characterization of Commercial Plant Protein Powders.” PMC, 2023.
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10379337/. - EFSA NDA Panel. “Safety of mung bean protein as a novel food pursuant to Regulation (EU) 2015/2283.” EFSA Journal, 2021.
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8527371/. - EFSA NDA Panel. “Safety of pea and rice protein fermented by Shiitake (Lentinula edodes) mycelia as a Novel food pursuant to Regulation (EU) 2015/2283.” EFSA Journal, 2022.
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8985068/. - Frontiers in Toxicology. “Enhancing allergenicity risk assessment for novel foods in the EU: insights from the updated EFSA guidance.” Frontiers in Toxicology, 2025.
https://www.frontiersin.org/journals/toxicology/articles/10.3389/ftox.2025.1701391/full. - Food Ingredients First. “Vitafoods Europe 2026 preview: Five key trends shaping healthy F&B innovation.” Food Ingredients First, 2026.
https://www.foodingredientsfirst.com/news/vitafoods-europe-2026-key-trends-fb-innovation.html. - GreenPharm. “5 Insights from Vitafoods Europe 2026 Worth Paying Attention To.” GreenPharm.
https://www.greenpharm.sk/en/5-insights-from-vitafoods-europe-2026-worth-paying-attention-to/. - Teng, T.S., et al. “Precision fermentation for food proteins: ingredient innovations, bioprocess considerations, and outlook.” Current Research in Food Science / ScienceDirect, 2024.
https://www.sciencedirect.com/science/article/pii/S2214799324000729. - Good Food Institute. “Deep dive: Fermentation protein ingredients and food functionality.” GFI.
https://gfi.org/science/the-science-of-fermentation/deep-dive-fermentation-protein-ingredients-and-food-functionality/. - Food Ingredients First. “Vitafoods Europe 2026: Ingredion on the future of plant-based proteins and sugar reduction.” Food Ingredients First, 2026.
https://www.foodingredientsfirst.com/video/vitafoods-2026-ingredion-plant-proteins-texture-sugar-reduction.html. - Food Ingredients First. “Vitafoods Europe 2026: Angel Yeast highlights fermentation protein for mainstream F&B.” Food Ingredients First, 2026.
https://www.foodingredientsfirst.com/video/vitafoods-2026-angel-yeast-fermentation-protein.html.
These statements have not been evaluated by the Food and Drug Administration. This information is provided for dietary supplement industry professionals and is not intended to diagnose, treat, cure, or prevent any disease.
Read more on plant-based proteins:
Plant Proteins in Sports Nutrition
Ingredients insights. Straight to your inbox. Subscribe now.
