What makes bread ryes and shine? Swetha Sivakumar breaks down gluten - Hindustan Times
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What makes bread ryes and shine? Swetha Sivakumar breaks down gluten

BySwetha Sivakumar
Feb 23, 2024 05:29 PM IST

The feisty protein composite is what makes our bread light and airy. How does it do that? And what happens when there’s no gluten? Take a look.

“Gluten” comes to us unchanged, from the Latin word for glue. In English, it is a protein composite found in just three grains: wheat, barley and rye (and triticale, which is a cross between wheat and rye).

Gluten is not found in all grains. The hardy protein composite is only found in cereals such as wheat, barley and rye. (Adobe Stock) PREMIUM
Gluten is not found in all grains. The hardy protein composite is only found in cereals such as wheat, barley and rye. (Adobe Stock)

Why only these? I like to think of this like one of those subplots in Game of Thrones. All cereals belong to the botanical family Poaceae. Within which wheat, barley and rye belong to the subfamily Pooideae, in which gluten-forming proteins are found. The other two subfamilies, Ehrhartoideae (rice) and Panicoideae (millets, maize and sorghum), evolved with proteins that cannot create gluten.

Gluten is formed by the proteins glutenins and gliadins. Look at wheat flour under the microscope and one sees these two tightly coiled around the starch molecules. (I believe this is akin to what goes on in House Targaryen.)

Add liquid to wheat flour and the proteins unwind and let go of the starch molecule, to form a weak sludge. Mix and knead this sludge, and the water, glutenin and gliadin interact chemically to form the compound gluten.

Gluten is approximately one-third protein and two-thirds water. It is very stable and does not break down in heat, cold or water. (Its overall resistance to breaking down completely in the human digestive system is one of the reasons a small percentage of people have gluten intolerance.)

The more one kneads such dough, the more closely the protein and water molecules bond. The protein molecules eventually form sheets of gluten within the dough, making it strong and elastic. Eventually, this will become a dough that can be moulded, filled, or used to trap air bubbles from yeast and leaveners, to make an airy loaf.

Knead it enough and it can be stretched very thin, to near-transparency, as in pizzas or parottas. The delicious chewiness of all these come from the structure provided by gluten.

But getting to this point of deliciousness takes time. When the gluten bonds in dough are at their strongest, they are also tense and liable to break. This is why it is important to let dough rest. As it sits on the counter, the tightest bonds break, making the dough less taut. At this point, it can be easily shaped and given structures and layers that will hold even in intense heat.

What one adds to the dough will change it too. Salt, fats and acids all have an impact on gluten formation. Salt tightens the structure of gluten, making it slightly harder to roll out. Traditionally, salt is not added to rotis for this reason.

Fats such as butter and ghee interfere with gluten formation by coating the protein molecules, preventing them from forming strong bonds with each other. This results in a more tender and crumbly texture, rather than a chewy one.

Acids such as vinegar, lemon juice and buttermilk can weaken gluten by disrupting the bonds between protein molecules. This can result in a softer dough with a finer texture, as in cakes.

Given what gluten brings to the table, it’s no wonder that gluten-free foods often fall short of expectations.

For one thing, it is difficult to get gluten-free dough to trap air and rise. If one simply replaces wheat flour with a non-gluten flour, the results are pretty terrible. The carbon dioxide generated from fermentation in bread, for instance, simply passes through the dough and escapes into the air. To create a structural network in such dough requires a binder, to strengthen the protein webs and increase elasticity. Xanthan gum can do the job in low-moisture foods such as cookies. Psyllium husk works for high-moisture foods such as naans and pizza.

For gluten-free bread, one must add a chemical leavener such as baking powder, even if one already has yeast in the dough. This is because the structure required to trap air is so hard to achieve without gluten, that one must essentially use a mix that will produce more gas.

Another problem that cooks face with gluten-free foods is the lack of browning, due to the low protein content. Wheat flour or atta is typically 14% protein, while gluten-free rice flour is only about 6% protein. One way to get the latter to brown is to add almond flour, which is 21% protein, and then add fat, for a good, crisp Maillard reaction.

Mouthfeel is the final barrier. Plant starches such as tapioca flour and potato flour absorb far more water. If they aren’t fully hydrated, the eventual pizza, roti or fresh loaf can feel gritty on the tongue. This is why most gluten-free blends require one to adjust bake times; to deal with the excess moisture.

There’s a lot of maths and physics that goes into adjusting for the absence of gluten. It is quite a feat to get it all right. Which is why I have the utmost respect for a good gluten-free meal. I won’t choose to eat it, but I will admire it from afar, and offer the chef my heartiest congratulations.

(To reach Swetha Sivakumar with questions or feedback, email upgrademyfood@gmail.com)

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