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Build ’Em Up and Break ’Em Down

Proteins are not just interesting and significant in food in their intact or even aggregated or complexed states, but often lend their greatest value to food by their disappearance. For example, in cheese, as we discussed in the last chapter, proteins are critical for the coagulation of milk and conversion into curd, and cheesemakers choose the enzymes they use to cause that coagulation specifically for their lack of other impact on the milk protein casein. However, once the cheese is made, the intactness of the casein abruptly becomes a liability, in a sort of cosmic ingratitude, and indeed the cheese will not be considered fit to eat until it is at least partially gone. The reason for this is immediately apparent if the freshly made cheese (of just about any variety) is tasted. Does it taste like cheese? Only if you like your cheese bland and flavored almost entirely of salt. Does it have the texture of cheese? Only if you think cheese should take quite a while to chew while savoring its boring saltiness. This is the taste and flavor of (salted) intact casein curd. So, no one eats cheese in this state, and almost every variety of cheese, from Accasciato to Zamorano, is held for at least some time after manufacture to undergo what is called ripening, during which it develops the flavor and texture we will expect it to have. In the case of the Parmesan shown in Figure 3.1, the crumbliness we associate so closely with this cheese is achieved by a combination of breakdown of the protein network over very long ripening times (often 12 months to 2 years), and a parallel drying out to low-moisture contents (which also concentrates the wide range of compounds produced during such long ripening to give a very strong and piquant flavor). Interestingly, almost all freshly made cheeses enter the ripening stage with similar flavor, but they leave with a ridiculously wide variety of characteristics.