What Is Protein Coagulation in Beer Making?

You may have heard of protein coagulation in a chemistry class, but probably not as a part of brewing. Or you may be wondering about the clumpy stuff that forms in your wort during the mashing process. Shockingly, these two things are one and the same.

So, now you find yourself asking “what is protein coagulation in beer making?” We’ve got your answers.

Protein Coagulation

Protein coagulation when discussed in chemistry, merely refers to the chemical process undergone when a protein goes from a liquid into a solid form, or at least a thicker liquid. We see this most clearly outlined in cheesemaking. Milk undergoes a chemical process that allows the proteins to coagulate, curdling, and ultimately making cheese.

The primary ingredient essential to protein coagulation is the addition of heat.

As a result, many new brewers won’t recognize protein coagulation as they brew various batches. However, it is always taking place.

The thing is, in various batches, particularly in darker batches, the protein coagulation takes place in the mash tun and is removed from the beer during the sparging process, or it comes out as part of the hot trap. So as a brewer, you might never notice it.

Until one day, perhaps in a lighter brew, you bring your wort to a higher boil, and you notice as the temperature rises that clumps start to form in the top of your liquid, taking on the appearance of egg drop soup.

That is protein coagulation.

The Brewing Process

To understand how it is possible that protein coagulation takes place without you realizing it, it helps to understand in detail the various steps of the brewing process.

First, note that all grains used for brewing – wheat, oats, barley, etc. – contain proteins. Those grains are harvested and roasted.

The roasting process creates a chemical reaction that converts the starches in the grains into sugars.

Those sugary grains are then cracked or ground in order to expose the sugars.

Now you have ideal brewing grains.

For thousands of years, brewers have discovered the perfect temperatures at which to add grains (and sometimes hops) to water and at which to steep those grains in a temperature controlled vessel, called a mash tun. This is called the “mash in” process.

In general, mash in takes about 60 minutes to get all of those fermentable sugars from the grains into the wort.

Next is sparging, during which the grains are filtered out of the wort and rinsed off to completely remove all fermentable sugars and proteins. The sparged liquid can be used for a separate, lighter, batch or added back into the original batch of wort.

Finally, the wort is cooled, yeast is added, and the wort is allowed to ferment.

Depending on the temperatures at which each of these steps is undergone, protein coagulation can occur at various points. Typically, the protein coagulation occurs during the boiling point and those protein conglomerates are filtered out of the wort as hot trub along with tannins and hop residue.

Proteins in Beer

Obviously, not all proteins in beer are filtered out as proteins conglomerates in the brew, which is what keeps our head stable and adds much of the flavor and aroma to the end result.

Indeed, it is the proteins in beer that function as structural components of cells, and the water soluble proteins function as enzymes that catalyze reactions. In the form of enzymes, those proteins are the key, organic catalysts that break down the raw barley and make it compliant for filtration and ready for the yeast to metabolize. Without the proteins, the grains would not break down properly and the yeast would have nothing to ferment.

During the brewing process, the brewer must engage in protein management in order to break down certain proteins and leave others intact. The boiling of the wort is what causes coagulation of the proteins that need to be removed. If left intact, these proteins would cause the end result beer to be opaque, viscous, and unstable.

At the same time, the proteins that remain in the bear are critical to body and mouthfeel. Thus, the brewer must be careful not to go too far in removing proteins, even in the hopes of avoiding protein hazes and sediment.

Hot Break

Hot break is the term used when proteins coagulate about 10 to 30 minutes into the vigorous boiling point of the wort. Proteins will clump together, break off, and fall to the bottom of the kettle.

In order to facilitate this process, some brewers will add about 10% of their total hops during this hot break period. The addition of hops will also help suppress foaming and boilovers.

Other brewers will instead add a seaweed derivative called carrageenan, also commonly referred to as Irish moss. The addition of Irish moss enhances clumping and makes the protein coagulates easier to remove.

Decoction Mashing

Decoction mashing is another way to encourage protein coagulation in order to remove clumps.

Brewers will take a small amount of the mashed grain and wort, bring that small amount to a boil, and then add that boiling wort back into the original batch.

This process allows for a steadier rise in temperature of the wort. It was an early approach to temperature control in beer making, and it is still popular today in many European styles of beer, particularly in Germany and the Czech Republic. The goal is to remove some of the proteins and allow other essential proteins to remain.

Decoction mashing is used to get the most out of malt, extracting full flavor and aroma, and it may involve more than one cycle of separating the decoction, boiling it, and then adding it back into the mash. This allows for multiple temperature rises and rests, which will also maximize on the potential for removing coagulated proteins.

In the end, it’s up to each brewer to decide which method of protein coagulation and removal works best not only for the brewer, but also for the specific type of beer being brewed.

Cheers!

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Sources:

  1. https://beerandbrewing.com/dictionary/aSbC3qutQd/
  2. https://www.homebrewersassociation.org/forum/index.php?topic=6093.0
  3. https://link.springer.com/article/10.1007/s12649-020-01163-6
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