Protein is about the blandest thing we treat ourselves to on a daily basis. I’m not even thinking of my roommate’s giant jar of everlasting protein powder (it’s a serious testimony to the willpower of those who can chug that stuff). Natural and unprocessed proteins in forms from quinoa to egg whites are paradigms of blandness—nutritious, but not particularly delicious on their own. That is because proteins are rather bulky hunks of molecules compared to the wily tiny molecules that are best at triggering our taste buds. The salts, sugars, and acids that trigger intense sensory reactions are all molecules that range from one to a few dozen atoms each; they stand in contrast against the most basic proteins that are made up of thousands of atoms. When it comes to taste, bigger is not better. To make protein delicious, we often use the obvious tricks of adding salt, sugar, acids, and spices to pump up the flavor—inventing barbeque, adobo, ceviche, confit, rillettes, and many other amazing dishes along the way. Yet the subtlest ingredient that draws out the exquisite flavors locked in proteins is time, and the flavor that emerges is umami.

The buzz about umami has come and gone by a few thousand years, in the age when humans first began methodically aging everything from meat, fish, and beans to preserve and improve their sources of protein. The aged steak, the smoked fish, and the fermented bean (source of soy sauce and miso paste) all develop the rich depth of umami after time and microorganisms (bacteria and fungi) have broken down the large tangle of proteins into smaller links of amino acids that we can more easily wrap our taste buds around. It’s a matter of surface area, molecular structure, and chemical technicalities that will probably anesthetize most people, but most people will perk up at the smell of a piece of ripe oozing Camembert—either to make for it or make for the door. All that delicious or debilitating odor is the result of the breakdown of proteins by bacteria over time, so as some cheeses age, the stinkier and tastier they get.

In every food culture, meticulously managing the breakdown of food as a way of preserving it and improving the flavor has become an art, appropriately known as curing (from the Latin curare: to take care of). It takes great care, knowledge, and patience to coax a block of mushroomy Camembert into existence from a bucket of milk, a sweet slice of prosciutto from the leg of a pig, and a fruity spoonful of miso from a handful of soybeans. It’s an acquired skill and an acquired taste, but one that humans have had for a long while. We may never master death, but we’ve got decay down pretty well; not only do we make use of decomposition, we can even cheat it.

Cheating brings us back to the beginning, to the egg that bored me enough to make me want to write about it. I could never manage to choke down a hardboiled egg, a solid nugget protein and fat that is pretty near tasteless, and in spite of my admiration for controlled decomp, eggs do not rot gracefully. There are a few ways around this problem, scramble or cheat, to name a couple. Cheating is culinarily more interesting, as it involves breaking down the proteins in eggs to unlock umami through chemical means and without the participation of bacteria. The result is a pidan, also known as the century egg, which is actually cured in an alkaline solution for weeks rather than decades. The high pH of the solution breaks down the proteins of the egg white and transforms it into a translucent obsidian rind, while the yolk becomes a gooey center whose stink rivals your typical aged cheese. The glossy black egg looks like an evil twin from an alternate universe, but it does make for a much tastier breakfast. Taste the breakdown with a drizzle of soy sauce and sesame oil.

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