The Flour Myth: Why There Is Actually No Gluten in Your Bag
- Fabio
- Jul 27
- 4 min read
That’s right: there is no gluten in flour!
While we often hear about high-protein or low-protein flours as if they were pre-packaged gluten containers, wheat flour actually contains only the precursors to gluten—specifically two distinct families of proteins called gliadins and glutenins.
Gluten itself doesn't exist until you, the baker, bring those components together.
Understanding how gluten is formed, and how it eventually degrades, is one of the most useful scientific insights you can bring into your home kitchen. Here is the step-by-step biological and chemical journey of dough formation.
TL;DR - This article in short (click to expand)
Flour contains NO gluten, only two precursor proteins: gliadins are responsible for extensibility and glutenin, which gives elasticity and strength.
Gluten is born when you add water and knead. Hydration activates the proteins; mechanical energy forces them to bond into a 3D elastic network (the gluten matrix) that traps gas and gives bread structure.
Gluten decays during fermentation via:
Enzymes (proteases) that slowly break down protein chains.
Acids produced by yeast/bacteria that weaken bonds.
Over-proofing, where the network collapses and dough can't hold gas.
The baker's job: Balance mixing (to build gluten) with fermentation (to gently relax it) for the best volume, texture, and flavour.
Step 1: The Birth of Gluten (Mixing and Hydration)
In dry flour, gliadins and glutenins sit side by side, completely separate and inactive. To transform these proteins into a complex, elastic network, two critical ingredients are required: water and mechanical energy.
Hydration: When water is introduced, the flour particles absorb it, allowing the dormant proteins to swell and become mobile.
Mechanical Action: As you mix or knead the dough, you physically push and stretch these hydrated proteins into contact with one another.
When gliadins and glutenins collide, they begin forming chemical bonds (nerdy note: they are disulfide bonds).
Gliadins provides extensibility and allow the dough to stretch without immediately snapping back.
Glutenins provides elasticity and strength, giving the dough structure and the ability to bounce back into shape.
Together, they form a cohesive, three-dimensional web known as the gluten matrix. This matrix acts like a microscopic balloon, trapping the carbon dioxide gas produced by yeast during fermentation and giving dough its volume and structure.
Gliadins | Glutenins | |
Type | Monomers (single-chain proteins) | Large polymers (many subunits linked by disulfide bonds) |
Role in dough | Lubricant, they provide extensibility and viscosity. | Form the structural backbone, they provide elasticity and strength |
What that means | They let the dough stretch and expand as gas bubbles form during fermentation, without tearing right away. | They give the dough the ability to snap back to its original shape after being stretched, and they determine the dough's overall tenacity (baking strength, measured as parameter W). |
Step 2: The Decay of Gluten (Fermentation and Degradation)
Once the gluten network is created, it doesn't stay rigid or permanent. Throughout the fermentation process, gluten continuously changes and eventually begins to break down. Many link this process to an improvement in the digestibility of pizza, but the scientific evidence tells it has very little to do with it, like I explained in this article.
This degradation happens through a few key mechanisms overtime:
Enzymatic Activity: Wheat flour naturally contains enzymes called proteases. As fermentation progresses, these enzymes break down the protein chains within the gluten matrix. While excessive protease activity can turn dough into a sticky, unmanageable puddle, a controlled amount of breakdown relaxes the dough, making it more extensible and easier to shape.
Acidity and Fermentation: As yeast and beneficial bacteria metabolize sugars, they produce carbon dioxide along with organic acids (such as lactic and acetic acids). This increase in acidity alters the electrical charge on the protein strands, weakening the bonds over extended proofing times.
Over-Proofing: If dough ferments for too long, the structural web degrades past its tipping point. The gluten network becomes too weak to hold the expanding gas bubbles, causing the dough to collapse in the oven.
Finding the Right Balance
Baking science is all about managing this life cycle of gluten: creating a strong enough network during mixing, and then letting fermentation gently soften that network to achieve optimal volume, texture, and flavour.
By paying attention to your mixing times, hydration levels, and fermentation lengths, you control the creation and breakdown of gluten, turning basic flour and water into a nice pizza.
If you liked this article, you’ll find a few ways to support my work and help me keep nerding out about pizza. And if you have any questions or thoughts just leave a comment, I always enjoy this kind of conversations.
Ciao, see you next time 🍕
Here's how you can support me!
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Sources: Advanced Bread and Pastry: A Professional Approach (Michel Suas); Culture and Cuisine (Jean-François Revel); Treatise on Baking (historic work mentioned by Chrysippus of Tyanus)
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