Functional Properties of Insect Proteins in Food Formulation

Solubility, Water and Oil Binding, Emulsification, Foaming, Gelation and Rheology

By TasteLab Scientific Editorial Board

Article: 007
Category: Insect Proteins · Food Technology · Product Development
Scientific Level: Technical / Professional

Keywords: insect protein, functional properties, edible insects, protein solubility, water holding capacity, oil holding capacity, emulsification, foaming, gelation, rheology, Acheta domesticus, Tenebrio molitor, food formulation

Abstract

A protein ingredient is valuable to a food manufacturer for two fundamentally different reasons.

The first is nutritional: how much digestible protein and indispensable amino acids it delivers.

The second is technological: what that protein actually does inside a food matrix.

Can it dissolve?

Can it retain water?

Can it bind oil?

Can it stabilize an emulsion?

Can it produce or stabilize foam?

Can it form a gel?

Can it modify viscosity and structure?

For insect-derived ingredients, these questions are particularly important because functional behavior changes substantially according to species, lipid content, protein extraction method, pH, ionic strength, heat treatment and other processing operations. Studies with Acheta domesticus, Tenebrio molitor, grasshopper and other edible insects have demonstrated measurable water- and oil-binding, emulsifying, foaming and gel-forming properties, but no single set of values can be considered universal for “insect protein.”

This article examines the major techno-functional properties of insect proteins from the perspective of professional food formulation and explains how they can be used—or modified—to create better products.

The central principle is:

Protein percentage tells us how much protein is present. Functional properties tell us what that protein can do.

Key Takeaways

• Insect proteins can exhibit solubility, water binding, oil binding, emulsification, foaming and gelation, but performance depends strongly on species and processing.

• Whole insect powder, defatted flour and extracted protein fractions should not be treated as equivalent ingredients.

• pH and salt concentration can substantially change protein solubility, interfacial behavior and gel formation.

• Mealworm protein has demonstrated the ability to stabilize oil-in-water emulsions, although stability decreases under certain heat and pH conditions.

• Extraction technology can produce insect-protein fractions with dramatically different functionality even when they originate from the same species.

• Functional performance must be evaluated inside the intended food matrix, not only in a laboratory protein solution. Bread and pasta research demonstrates that insect ingredients modify rheology, structure and processing behavior of the complete formulation.

1. From Nutrient to Functional Ingredient

ARTICLE 006 examined insect protein primarily as a nutritional resource.

For an R&D department, however, nutrition represents only one part of ingredient selection.

Consider a hypothetical ingredient specification:

Protein: 70%

That value tells us almost nothing about whether the ingredient can successfully formulate a beverage, gelato, protein bar or meat analogue.

Two 70% protein ingredients could behave completely differently.

One may disperse easily in water.

Another may sediment.

One may stabilize an emulsion.

Another may aggregate.

One may produce a firm heat-set gel.

Another may remain weak and particulate.

This occurs because techno-functionality depends on protein structure, surface charge, molecular interactions, lipid content, particle size and the processing history used to manufacture the ingredient. Research comparing insect flours, defatted flours and protein preparations has demonstrated precisely this type of variation.

For this reason, TasteLab recommends viewing insect ingredients as functional systems, not simply alternative sources of protein.

2. The Six Functional Properties That Matter Most

For most food-development applications, six parameters deserve particular attention:

1. Protein solubility

2. Water-holding or water-absorption capacity

3. Oil-holding or oil-absorption capacity

4. Emulsifying properties

5. Foaming properties

6. Gelation and rheological behavior

These properties are interconnected.

A protein must often become sufficiently dispersed before it can migrate effectively toward an oil-water or air-water interface.

Likewise, thermal unfolding may reduce solubility while simultaneously increasing the ability of proteins to interact with one another and form a gel.

The formulation challenge is therefore not to maximize every functional property.

It is to optimize the correct property for the intended product.

3. Protein Solubility

Solubility is one of the most important variables governing protein functionality.

It becomes especially relevant in:

• beverages;

• liquid nutrition;

• protein drinks;

• sauces;

• emulsions;

• frozen desserts;

• dairy-alternative systems.

If proteins remain strongly aggregated or precipitate from the continuous phase, their ability to contribute predictable texture and interfacial functionality can be reduced.

pH matters

Protein solubility is strongly dependent on pH.

Near the isoelectric region, net protein charge is reduced and protein-protein attraction becomes more favorable. Aggregation and precipitation can therefore increase.

Away from this region, higher electrostatic repulsion can improve dispersion.

Research on mealworm protein preparations demonstrates how dramatically processing route can change this parameter. Gkinali and colleagues produced multiple protein preparations from defatted Tenebrio molitor. A salt-soluble preparation reached approximately 88% solubility at acidic pH, while other fractions behaved differently.

This immediately suggests an important R&D rule:

Do not ask whether “mealworm protein is soluble.” Ask whether the specific commercial mealworm protein is soluble at the pH of your product.

A protein beverage at pH 3.5 and a neutral savory sauce at pH 6.5 represent completely different environments.

4. Water-Holding Capacity

Water-holding capacity describes the ability of an ingredient to retain or associate with water under defined testing conditions.

This property can influence:

• dough hydration;

• batter viscosity;

• product yield;

• juiciness;

• syneresis;

• softness;

• storage stability;

• texture.

A 2022 study involving Acheta domesticus cricket powder measured approximately 175.2% water absorption capacity under the conditions used by the authors.

This does not mean that every cricket powder absorbs exactly 1.752 times its mass in water.

The value is ingredient- and methodology-specific.

But it illustrates an important phenomenon: incorporating cricket powder may materially alter the water balance of a formulation.

This becomes particularly relevant in bakery.

Research from the USDA examining cricket protein powders in bread systems found that different cricket powders affected dough development and mixing behavior differently, emphasizing that water management must be adjusted according to the ingredient rather than simply maintaining the original formulation.

5. Why Water Binding Matters in Product Development

Imagine replacing 10% wheat flour with cricket powder.

The formulation does not simply gain protein.

At the same time:

• starch concentration decreases;

• protein concentration increases;

• chitin-containing material may increase;

• lipid concentration may change;

• water competition changes.

The original water level may no longer be optimal.

That can influence:

• dough consistency;

• expansion;

• final volume;

• hardness;

• moisture perception.

This explains why alternative-protein reformulation should rarely be carried out by simple one-for-one replacement.

The ingredient changes the water architecture of the food.

6. Oil-Holding Capacity

Oil-holding capacity measures the ability of an ingredient to associate with or retain lipids.

This can influence:

• flavor retention;

• mouthfeel;

• fat distribution;

• filling systems;

• meat analogues;

• snack formulations;

• sauces.

The same cricket-powder study that reported high water absorption measured approximately 140.4% oil absorption capacity for the Acheta domesticus powder used in the experiment.

Protein extraction can change this characteristic substantially.

For example, different mealworm protein preparations produced by Gkinali and colleagues showed very different water- and oil-binding behavior according to whether alkaline extraction, isoelectric precipitation or salt treatment was used.

Again:

Species alone does not define functionality. Species + process define functionality.

7. Emulsification

An emulsion contains two normally immiscible phases—typically oil and water.

Proteins can act at the interface between these phases.

When appropriately structured, they can adsorb to newly created oil droplets during homogenization and help prevent droplets from recombining.

This is important in products such as:

• sauces;

• mayonnaise-type systems;

• dressings;

• meat emulsions;

• beverages;

• frozen desserts;

• cream-style products.

8. Mealworm Protein as an Emulsifier

Gould and Wolf investigated mealworm protein at an oil-water interface and demonstrated strong interfacial activity.

In their experimental system, mealworm-protein-stabilized oil-in-water emulsions could remain without significant droplet coalescence for an extended storage period.

However, stability was affected near the protein's isoelectric region and after heating to approximately 90°C, illustrating how environmental conditions can modify emulsion performance.

This is a critical lesson.

A protein may produce an excellent emulsion during laboratory homogenization but fail after:

• pasteurization;

• acidification;

• salt addition;

• freezing;

• storage.

Therefore, professional emulsifier evaluation should include the complete process conditions of the final food.

9. Cricket Powder and Emulsion Capacity

Aleman and colleagues measured an emulsion capacity of approximately 77.7% for the Acheta domesticus powder used in their cookie-development study.

The result demonstrates that whole cricket powder contains components capable of interacting within oil-water systems.

However, whole powder contains considerably more than protein.

It also contains:

• lipid;

• chitin-associated material;

• minerals;

• pigments;

• other structural components.

Consequently, functional behavior of whole powder cannot automatically be attributed exclusively to isolated protein.

This distinction becomes increasingly important as the industry moves toward purified protein concentrates and isolates.

10. Protein Extraction Can Increase Emulsifying Performance

Protein fractionation creates new possibilities.

Gkinali and colleagues compared several Tenebrio molitor preparations.

Their salt-soluble fraction produced emulsifying activity around 86 m²/g under the reported conditions, while the different extraction routes produced distinctly different interfacial behavior.

The implication is commercially significant.

Instead of treating mealworm powder as one commodity ingredient, manufacturers could potentially develop:

• high-solubility fractions;

• high-emulsification fractions;

• water-binding fractions;

• gel-forming fractions.

This is the same direction in which established protein industries have evolved.

11. Foaming Properties

Foams consist of gas bubbles dispersed in a liquid or semi-solid continuous phase.

Proteins can help create and stabilize these air-water interfaces.

Foaming functionality is relevant in:

• whipped systems;

• bakery;

• mousses;

• aerated desserts;

• specialty beverages;

• certain snack structures.

A protein that migrates rapidly to the air-water interface can help form a film around incorporated air.

But two different properties must be distinguished.

Foam Capacity

How much foam can initially be produced?

Foam Stability

How well does that foam remain over time?

They are not the same parameter.

12. A Useful Example: Cricket Powder

In the Acheta domesticus powder tested by Aleman and colleagues, foam capacity was approximately 15.9%, while measured foam stability was approximately 80.5% under their test conditions.

This illustrates why a single word such as “good foaming properties” can be misleading.

An ingredient can demonstrate:

• relatively limited initial foam generation;

• but strong persistence of the foam that is created.

Another protein could show exactly the opposite behavior.

Professional ingredient specifications should therefore report foam capacity and foam stability separately.

13. Species Differences

Not all insects produce proteins with identical foaming behavior.

Kim and colleagues compared water-soluble and salt-soluble proteins extracted from several edible insects and found significant species-dependent differences.

A salt-soluble protein fraction obtained from Protaetia brevitarsis demonstrated particularly strong foaming and emulsifying properties relative to the other materials examined.

Mishyna and colleagues similarly found that extracted protein-rich fractions from grasshopper and honeybee brood could improve foam stability relative to less-refined materials.

These findings reinforce a recurring theme throughout the TasteLab insect-protein series:

There is no single technological profile called “insect protein.”

14. Gelation

Gelation may become one of the most commercially important functional properties of insect proteins.

Protein gelation occurs when protein molecules interact strongly enough to form a three-dimensional network capable of immobilizing water and creating a structured material.

Applications can include:

• meat alternatives;

• hybrid meats;

• fillings;

• structured protein products;

• emulsion gels;

• high-protein snacks;

• specialized desserts.

Gel formation depends on variables including:

• protein concentration;

• temperature;

• pH;

• ionic strength;

• molecular structure;

• other formulation components.

15. Salt as a Gel-Design Tool

A 2025 study by Lanza and colleagues investigated the gelation of Acheta domesticus protein extracts under different NaCl concentrations.

Increasing ionic strength strongly altered the rheological response.

The storage modulus G′ increased from approximately 150 Pa without added salt to more than 1300 Pa at 0.5 M NaCl, demonstrating substantial reinforcement of the protein network.

Interestingly, other functional properties did not simply increase continuously with salt.

Protein solubility peaked at approximately 79.5% at 0.1 M NaCl, while emulsifying activity reached a maximum around 59.1 m²/g at 0.3 M before declining at higher ionic strength.

This is an excellent demonstration of protein engineering through formulation.

The same ingredient can perform differently simply because the ionic environment changes.

16. Rheology: From Ingredient to Texture

Rheology examines how materials deform and flow.

For protein systems, commonly evaluated parameters include:

• viscosity;

• storage modulus G′;

• loss modulus G″;

• yield behavior;

• flow properties.

These measurements can help predict whether an insect-protein system behaves more like:

• a liquid;

• a weak viscoelastic structure;

• a strong gel.

For developers of meat analogues and structured protein foods, this information can be considerably more useful than protein percentage alone.

The 2025 Acheta domesticus gelation study demonstrates that ionic strength can transform protein-network elasticity dramatically, making formulation conditions a powerful texture-design variable.

17. Defatting Changes Functionality

Insects naturally contain varying amounts of lipid.

Removing fat changes more than nutritional composition.

Defatting can alter:

• protein concentration;

• surface hydrophobicity;

• aggregation;

• oil binding;

• foaming;

• emulsification.

Jeong and colleagues examined protein concentrates produced from Gryllus bimaculatus after different defatting treatments and found that solvent choice materially affected techno-functional characteristics.

Other experiments with insect proteins have similarly demonstrated that defatting treatment changes solubility, foam and emulsification behavior.

Therefore, specifying:

“cricket protein concentrate”

is still insufficient.

The manufacturer should understand how that concentrate was produced.

18. Extraction Technology Is Functional Engineering

ARTICLE 005 discussed alkaline extraction, isoelectric precipitation and salt-assisted processing primarily as manufacturing technologies.

ARTICLE 007 reveals their second purpose.

They are also tools for functional engineering.

Gkinali and colleagues created three different protein-rich preparations from the same Tenebrio molitor raw material.

The resulting fractions differed in:

• protein concentration;

• water binding;

• oil binding;

• solubility;

• emulsifying activity;

• emulsion stability.

This opens an important future direction for insect ingredient suppliers.

Rather than offering one generic protein concentrate, suppliers may eventually offer:

TM-S — High-solubility mealworm protein

TM-E — Emulsifying mealworm protein

TM-G — Gel-forming mealworm protein

The same way established hydrocolloid and dairy-protein industries supply ingredients according to functional performance.

19. Heat Is Not Simply “Good” or “Bad”

Heat modifies protein structure.

Depending on conditions, this can:

• expose previously buried molecular groups;

• increase protein-protein interaction;

• improve gel formation;

• cause aggregation;

• decrease solubility;

• destabilize emulsions.

The effect is therefore application-dependent.

Mealworm emulsions studied by Gould and Wolf experienced flocculation after exposure to 90°C under their test conditions.

Conversely, protein network formation may require thermal unfolding in applications where a gel structure is desirable.

The correct question is not:

“Does heating damage insect protein?”

It is:

“Does the heat treatment produce the molecular structure required for this application?”

20. Food Matrix Effects: Bread

A protein does not behave inside bread exactly as it behaves in water.

Perez-Fajardo, Bean and Dogan examined two commercial cricket protein powders in wheat-bread formulations.

The powders differed in their functional characteristics and consequently interacted differently with the gluten-starch system.

The study demonstrated that successful incorporation is possible at appropriate levels, but the ingredient affects dough mixing and bread characteristics rather than functioning as an inert protein addition.

This is a powerful lesson for R&D teams.

Ingredient-level functionality must always be followed by matrix-level validation.

21. Food Matrix Effects: Pasta

Insect proteins can also modify pasta structure.

Research involving Acheta domesticus and Tenebrio molitor ingredients in pasta systems reported changes in firmness, cooking loss and color compared with conventional durum-wheat pasta.

Again, the insect protein is not merely increasing nutritional value.

It is modifying the structural system.

In traditional pasta, gluten and starch interact to control:

• hydration;

• cooking;

• firmness;

• starch loss.

Replacing part of that matrix with insect material changes the balance.

The formulation must therefore be redesigned rather than simply fortified.

22. Implications for Protein Gelato

This topic is particularly relevant to the TasteLab Gelato Science program.

A high-protein frozen dessert requires proteins to function simultaneously within a complex system containing:

• water;

• fat;

• sugars;

• minerals;

• stabilizers;

• air;

• ice crystals.

An insect protein selected for gelato development should therefore be evaluated for:

Solubility

Poor dispersion could create sediment or sandy texture.

Water Binding

Excessive hydration can increase viscosity; insufficient hydration can reduce body.

Emulsification

Protein can contribute to the fat-water interface.

Foaming

Air incorporation and stability affect overrun and structure.

Heat Stability

Pasteurization may modify the protein.

Flavor

Functional performance is irrelevant if sensory quality becomes unacceptable.

Insect proteins should therefore not be incorporated into gelato based solely on protein content.

A complete functional profile is required.

23. Implications for Snacks

For snack development, priorities may be different.

An extruded or baked snack may require:

• water absorption;

• controlled oil interaction;

• extrusion tolerance;

• expansion;

• crispness;

• flavor compatibility.

The ideal protein for a beverage is therefore not automatically the ideal protein for an extruded snack.

This is why protein ingredients should be selected backwards from the finished product.

24. The TasteLab Functional Selection Matrix

Application

Priority Properties

Protein Beverage

Solubility · sedimentation stability

Sauce / Dressing

Emulsification · viscosity

Gelato

Solubility · emulsification · hydration · foaming

Protein Bar

Water binding · oil binding · texture

Bakery

Hydration · dough interaction · heat behavior

Pasta

Hydration · structural interaction · cooking stability

Meat Analogue

Gelation · water holding · oil holding · rheology

Aerated Dessert

Foaming capacity · foam stability

Extruded Snack

Hydration · thermal behavior · structure formation

This matrix should be considered a development framework rather than a universal ranking.

Different formulations within the same category can require different functionality.

25. What Should Be Included in a Professional Specification?

TasteLab recommends that advanced insect-protein suppliers progressively move beyond standard proximate analysis.

A functional ingredient specification should ideally include:

Protein Characteristics

• protein concentration;

• extraction method;

• particle size;

• solubility vs pH.

Hydration

• water-holding capacity;

• water-absorption capacity.

Lipid Interaction

• oil-holding capacity.

Interface Performance

• emulsifying activity;

• emulsion stability;

• foaming capacity;

• foam stability.

Structural Performance

• minimum gelation concentration;

• rheological profile;

• heat stability.

Application Conditions

• pH range;

• salt tolerance;

• heat tolerance.

Without these parameters, the R&D department must perform much of the ingredient characterization itself.

26. The Future: Tailored Insect Protein Ingredients

The next stage of the edible-insect industry is unlikely to be dominated exclusively by generic insect powder.

More sophisticated ingredient systems are technically possible.

Processing research already demonstrates that:

• extraction changes solubility and emulsification;

• saline extraction can alter functional performance;

• defatting changes protein behavior;

• ionic strength can tune gelation;

• protein fractions can stabilize emulsions.

This points toward a future in which insect proteins are sold according to performance specification, not just species.

That would transform them from novel foods into serious industrial ingredients.

27. TasteLab R&D Framework

Before selecting an insect protein, define the technical problem.

STEP 1 — Define the Food Matrix

Beverage?

Gelato?

Snack?

Bakery?

Meat analogue?

STEP 2 — Define the Required Function

Solubility?

Emulsification?

Hydration?

Foam?

Gel?

STEP 3 — Select the Ingredient Format

Whole powder?

Defatted flour?

Protein concentrate?

Protein isolate?

Hydrolysate?

STEP 4 — Define Processing Conditions

pH?

Salt?

Temperature?

Shear?

Freezing?

STEP 5 — Validate in the Final Product

Because laboratory functionality does not guarantee identical performance in a complex food matrix.

Conclusion

Insect proteins should not be evaluated only as nutritional replacements for conventional proteins.

They can also function as technological ingredients.

Research demonstrates that insect-derived proteins can provide:

• water binding;

• oil binding;

• emulsification;

• foaming;

• gelation;

• rheological structure.

However, these properties vary significantly according to species, processing, extraction method and formulation environment.

The commercial opportunity is therefore larger than simply producing “cricket flour” or “mealworm powder.”

The future opportunity is the development of purpose-designed insect protein ingredients engineered for specific food applications.

Instead of asking:

“How much protein does this ingredient contain?”

R&D teams should increasingly ask:

“What technological function does this protein perform in my product?”

That distinction will determine whether insect protein remains a niche nutritional novelty or develops into a genuine industrial ingredient platform.

Frequently Asked Questions

Are insect proteins good emulsifiers?

Some insect protein preparations have demonstrated strong emulsifying properties, including mealworm protein fractions and selected cricket powders. Performance varies strongly with extraction process, pH, heat and ionic environment.

Can insect proteins form gels?

Yes. Recent experiments with Acheta domesticus protein extracts demonstrated substantial gel-network formation, with ionic strength strongly influencing elasticity.

Is whole cricket powder equivalent to cricket protein isolate?

No. Whole powder contains lipid, chitin-associated material and other components, while extraction and defatting alter composition and protein functionality.

Does pH influence insect protein functionality?

Yes. Protein charge and aggregation vary with pH, affecting solubility and interfacial behavior. Experimental mealworm preparations have demonstrated markedly different solubility and emulsion performance according to pH and extraction method.

Can insect protein be used in bread?

Yes, but incorporation changes dough behavior. Research with commercial cricket protein powders showed that different powders interacted differently with dough and affected bread-processing characteristics.

Could insect protein work in gelato?

Potentially, but it must be evaluated for solubility, hydration, emulsification, foaming, heat stability and sensory impact in the actual frozen-dessert formulation. Existing studies establish that insect proteins can possess several of these technological functions, but performance is ingredient-specific.

Selected Scientific References

1. Zielińska E. Evaluating the Functional Characteristics of Certain Insect Flours (Non-Defatted/Defatted Flour) and Their Protein Preparations. Molecules. 2022;27:6339.

2. Gkinali AA, Matsakidou A, Paraskevopoulou A. Characterization of Tenebrio molitor Larvae Protein Preparations Obtained by Different Extraction Approaches. Foods. 2022;11:3852.

3. Gould J, Wolf B. Interfacial and emulsifying properties of mealworm protein at the oil/water interface. Food Hydrocolloids. 2018;77:57–65. DOI: 10.1016/j.foodhyd.2017.09.018.

4. Kim TK, Yong HI, Jeong CH, et al. Technical Functional Properties of Water- and Salt-soluble Proteins Extracted from Edible Insects. Food Science of Animal Resources. 2019;39:643–654.

5. Mishyna M, Martinez JJI, Chen J, Benjamin O. Extraction, characterization and functional properties of soluble proteins from edible grasshopper and honey bee. Food Research International. 2019;116:697–706.

6. Aleman RS, Marcia J, Pournaki SK, et al. Formulation of Protein-Rich Chocolate Chip Cookies Using Cricket (Acheta domesticus) Powder. Foods. 2022;11:3275. DOI: 10.3390/foods11203275.

7. Jeong MS, et al. Effect of Three Defatting Solvents on the Techno-Functional Properties of an Edible Insect Protein. 2021.

8. Perez-Fajardo M, Bean SR, Dogan H. Effect of cricket protein powders on dough functionality and bread quality. Cereal Chemistry. 2023;100:587–600. DOI: 10.1002/cche.10652.

9. Pasini G, et al. Potentiality of protein fractions from house cricket and mealworm for pasta formulation. LWT. 2022.

10. Lanza RF, Muccio E, Malvano F, et al. Tuning Gelation of Insect Proteins: Effect of Ionic Strength on Acheta domesticus Protein Extracts. Gels. 2025;11:937.