Abstract
After milk has been treated with chymosin or other milk coagulating enzymes, there is little apparent reaction for some time, and then the milk coagulates rapidly. This phenomenon, which is the first step of cheesemaking, results from two processes, the first being the attack on κ-casein, which stabilizes the casein micelles, by the proteolytic enzymes (chymosin, pepsin or microbial proteinases) contained in the rennet, and the second being the subsequent clotting of the micelles which have been destabilized by this enzymatic attack. These processes have been described as the primary and secondary stages of the renneting reaction. This sequential description of the reaction is, however, somewhat oversimplified, since it is not necessary for the enzymatic reaction to be complete before aggregation of partly renneted micelles can occur. Indeed, the milk may begin to clot well before the enzymatic cleavage of the κ-casein is complete.1,2,3
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Dalgleish, D.G. (1993). The Enzymatic Coagulation of Milk. In: Fox, P.F. (eds) Cheese: Chemistry, Physics and Microbiology. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2650-6_3
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