How is Gluten Created? The Science Behind the Chewy Protein

January 4, 2026 •

4 min read

Over 40 million Americans report having some form of gluten sensitivity, making its composition a topic of great interest. The common misconception is that gluten exists as a complete substance in flour, but it is actually a composite protein network created through the reaction of two distinct proteins: glutenin and gliadin.

Quick Summary

Gluten is formed when water is added to the wheat proteins glutenin and gliadin, which then bond and organize into a stretchy network through mixing and kneading. The strength and elasticity of the resulting gluten depend on the flour type and handling techniques.

Key Points

Two Primary Proteins: Gluten is formed by the reaction of two distinct proteins in flour, glutenin and gliadin, not already present as a single compound.
Hydration is Key: The process begins when liquid, such as water, is added to the flour, which hydrates and activates the dormant glutenin and gliadin proteins.
Mixing Activates Bonding: Mechanical action like kneading or mixing is required to encourage the hydrated protein molecules to bond and form the interconnected gluten network.
Glutenin and Gliadin Roles: Glutenin provides elasticity and strength, while gliadin contributes to the dough's extensibility and stretchiness.
Flour Protein Content Matters: Higher protein flours lead to stronger gluten, while lower protein flours result in weaker gluten, influencing the final texture of baked goods.
Factors Affecting Strength: Ingredient additions like salt (strengthens), fats and sugars (weaken), water hardness, and pH levels can all affect the final strength of the gluten network.
Elasticity and Extensibility: The balance of elasticity and extensibility, known as viscoelasticity, is what gives dough its unique properties, allowing it to hold its shape and trap gas.

The Core Components: Glutenin and Gliadin

At its heart, the process of how is gluten created begins with two specific storage proteins found within grains like wheat, rye, and barley. In dry flour, these proteins, known as glutenin and gliadin, exist separately. They are dormant until they come into contact with a liquid, most commonly water. Their unique properties determine the final structure and characteristics of baked goods.

Gliadin: These are smaller, single-chain proteins that are responsible for the dough's extensibility or stretchiness. They provide the viscous, flowy quality that allows dough to be shaped and spread out.
Glutenin: These are larger, more complex proteins that bond together to form a polymer network, providing elasticity and strength. This is what gives dough its tenacious, rubber-band-like quality, allowing it to hold its shape.

The Catalytic Reaction: Water and Mixing

Gluten does not spontaneously form just by adding water; the process requires mechanical energy. The magic happens in two distinct phases:

Hydration: When water is introduced to flour, the glutenin and gliadin proteins begin to absorb the liquid and emerge from their dormant state. The water allows these proteins to become mobile and interact with one another.
Agitation: The act of mixing, stirring, or kneading provides the mechanical shear needed to bring the hydrated glutenin and gliadin molecules together. This movement encourages them to bond through cross-links, forming long, strong, and intertwined protein chains. This continuous network is the substance we call gluten. The more you work the dough, the more organized and developed this protein matrix becomes, trapping gas and giving the dough its characteristic elasticity and structure.

Key Factors Influencing Gluten Development

The final outcome of gluten formation is not uniform across all baking projects. Several factors influence how the gluten network develops:

Flour Type: The protein content of the flour is the most significant factor. High-protein flours, such as bread flour, contain more glutenin and gliadin, leading to a stronger gluten network suitable for chewy breads. Low-protein flours, like cake or pastry flour, result in weaker gluten, perfect for tender, delicate baked goods.
Water Content: The amount of water, or hydration level, affects how the proteins are able to move and bond. Less water results in a stiffer dough and less gluten development, while higher hydration can soften the gluten strands, allowing for larger gas bubbles and a more open crumb structure.
Mixing Time: Kneading or mixing the dough for longer periods increases gluten development. Techniques like the "autolyse" method, where flour and water rest before adding other ingredients, also promote stronger gluten with less intensive mixing.
Inhibitors: Ingredients like fats, oils, and sugars can interfere with gluten development. Fats coat the flour proteins, preventing them from hydrating and bonding, which results in a more tender crumb. Sugar also competes with the flour proteins for water, further inhibiting gluten formation.
Salt: Unlike inhibitors, salt strengthens the gluten network. It tightens the protein strands and reinforces their structure, contributing to a finer crumb and better volume in bread.

Understanding the Viscoelastic Dough

To grasp the properties of gluten, it is helpful to understand the concept of viscoelasticity, a combination of viscous (extensible) and elastic properties.


Property	Key Protein Contributor	Effect on Dough	Example Application
Elasticity	Glutenin	Allows the dough to snap back to its original shape when stretched, providing structure and resistance.	High-volume, chewy bread crusts.
Extensibility	Gliadin	Allows the dough to be stretched and extended without breaking, giving it a flowy quality.	Rolling out pastry dough or stretching pizza dough.
Viscosity	Gliadin	Provides the adhesive or sticky quality to the wet dough.	Ensures ingredients are held together, like in cake batters.
Tenacity	Glutenin	Measures the force needed to stretch the dough, indicating its strength.	Strong bread doughs that hold their shape well.

Conclusion: The Purpose of Gluten Creation

The journey of how is gluten created is a masterful interplay of chemistry and mechanics. The two key proteins, glutenin and gliadin, are mere potential until they are hydrated and agitated. This process weaves them into the complex, viscoelastic network that gives structure to countless baked goods, from the chewiness of a perfect sourdough to the fluffiness of a delicate cake. By understanding the factors that control this process, bakers can manipulate the gluten to achieve their desired texture, turning a simple mix of flour and water into a culinary masterpiece.

The Windowpane Test: A Simple Indicator

Experienced bakers often use the "windowpane test" to check if the gluten has been sufficiently developed. To perform this, a small piece of dough is stretched between the fingers. If it can be stretched into a thin, translucent sheet without tearing—like a windowpane—the gluten network is well-developed and ready to trap gas during fermentation, leading to a high-volume, airy crumb. If it tears quickly, the dough needs more kneading to strengthen the gluten network.

Outbound Link

For further reading on the functional properties of gluten proteins in various foods, including their use as additives, explore this detailed research article: Gluten formation: Its Sources, composition and health effects.

Frequently Asked Questions

The two primary ingredients needed to create gluten are flour from grains like wheat, rye, or barley and a liquid, most commonly water.

No, dry flour does not contain gluten. It contains the separate proteins, glutenin and gliadin, which combine to form the gluten network only after liquid is added and it is agitated.

If dough is not kneaded enough, the gluten network will be underdeveloped and weak. This can result in a dense, less structured baked good that may crumble easily.

Some baked goods, like cakes and pastries, require less gluten development to achieve a tender and soft texture. Minimizing kneading and using low-protein flours helps prevent the formation of a tough, chewy structure.

Fats and sugars inhibit gluten formation. Fats coat the protein strands, blocking them from interacting with water, while sugars compete for the water needed for hydration, both resulting in a more tender product.

The 'windowpane test' is a method bakers use to check for sufficient gluten development. If a small piece of dough can be stretched until it is thin and translucent without tearing, the gluten is well-developed.

Gluten is specifically formed from the proteins found in wheat and related grains like rye and barley. Flours from other sources, such as rice or almond flour, do not contain the necessary proteins and are therefore naturally gluten-free.