This is why sugar is added gradually; why beating needs to be gradually increased; why temperature matters... I wasn’t going to explain it because it's a lot to consume. But since you’re a teacher, I figured you can handle it.
The egg white is about 90% water and 10% protein
Beating egg whites triggers the denaturation of protein: long chain amino acids unfurl from a somewhat spherical shape. This exposes various amino acids that are either hydrophilic (absorbs water on a molecular level) or hydrophobic (repels water on a molecular level).
If whipped correctly, the hydrophilic amino acids will form what are called ionic bonds, created by electrically charged molecules that bind to water molecules. Ionic bonds are the best bonds as they create a voluminous, silky, and moist meringue.
Water molecules easily bond to each other and form a film. But as more and more air is best into the egg whites it stretches the water film; the more air, the farther the water molecules separate from each other. If too much air is whipped into the egg whites, it forces the water molecules out of the network of amino acids (proteins), water, and air bubbles.
Disulfide bonds are bonds between the amino acids that have sulfurs. When too many water molecules are squeezed out of the network and these really tight disulfide bonds form between the sulfur amino acids form the result is dry egg whites with gritty tiny white specks.
So two types of bonds can occur in whipped egg whites:
- ionic bonds (perfectly beaten egg whites)
- disulfide bonds (over beaten egg whites)
The ionic bonds are desirable for meringue, but they are NOT stable.
To stabilize the ionic bond you must do three things:
1. add an acid
2. add sugar at the correct time and slowly
3. gradually beat egg whites from low speed to high speed
Acid: recipes instruct bakers to add an acid, but never explain why. An acid, like cream of tartar is potassium hydrogen tartrate. It’s the hydrogen that is important. A hydrogen atom contains a single positively charged proton and a negatively charged electron. Because it has a negatively charged electron, it can keep protein from binding with other proteins. So disulfide bonds are less likely to occur.
Sugar: Adding the sugar to whipped eggs too soon will interfere with the protein denaturalization process (sugar molecules can get in the way as the hydrophilic amino acids bind with water molecules). The sugar and water molecules also bind, adding more stability to the egg whites by keeping the water molecules from being forced out. If the sugar is dumped in or added too fast it will not disperse the sugar evenly throughout the egg whites to build a good network of water and sugar molecule bonds.
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What happens during the beating of egg whites: The meringue is formed when the amino acids unfurl and bind with water molecules. Then air bubbles are pushed in between the proteins and water molecules. As the water molecules are pushed apart by air it expands the network, creating volume.
Water has surface tension so its surface can stretch; water can dribble down your chin or across the counter. But you can only stretch the surface of water so far. Keep in mind the water in the eggs is no different--it will only stretch so far. As more air bubbles are beaten into the egg whites, the water molecules form a film and stretch out. Beating the egg whites gradually and increasing the speed makes for tiny uniform air bubbles and reduces the risk of forcing in so much air that it forces the water molecules to stretch beyond their tolerance level and eventually forces them out of the network.
So in making a meringue, the timing and rate sugar is added is important as sugar will interfere with protein denaturation (sugar molecules interfere with how the hydrophilic amino acids [protein molecules] bind with water molecules).
If the sugar is added too soon, sugar delays egg coagulation. Water molecules are displaced. The result is a weaker foam with lower volume.
But if the sugar is added at the correct time and gradually, sugar and water molecules bind, adding more stability to the egg whites by keeping the water molecules from being forced out. This creates a stronger foam network with greater volume.
In most Swiss meringue recipes all the sugar is dumped in at the beginning. So there is the issue of delayed protein denaturation.
Heat is a way to denature the protein. It also dissolves the sugar crystals, and that allows the sugar and water molecules to bind. So heat can undo the adverse effects of frontloading the sugar. But you have to heat it to a high enough temperature. The temperatures below 160°F are too low to stabilize the meringue.
Gradually beat in a portion of the sugar after heating to trigger the binding of the sugar and water molecules further enhancing the stability of the meringue.
People who use lower temperatures assume heating is simply to kill the salmonella, nothing else. They don’t understand heating is also to address the delayed protein denaturation and the need to stabilize the egg whites.
Interestingly, pastry Stella Parks found if you heat at higher temperatures the meringue becomes more stable—enough that it will not deflate or weep.
However, I do not care for the texture of the meringue and buttercream at the higher temperature. I find the product to be too dense, stiff, and sticky. It also has less volume.
Meringues for toppings can be stabilized against weeping with cornstarch