Chymosin, Pepsins and Other Aspartyl Proteinases: Structures, Functions, Catalytic Mechanism and Milk-Clotting Properties

This chapter comprehensively reviews the classification, structure, function, catalytic mechanism, and milk-clotting properties of chymosin, pepsin, and other aspartyl proteinases Hydrolysis of the principal bovine milk proteins (β-, α_s-, and κ-caseins) by calf chymosin is described in detail, as is the hydrolysis of caseins from the milk of other, nonbovine, species. Rennets, other than chymosin, are discussed and their hydrolysis of caseins is described. Interspecies milk coagulation is reviewed and includes detail on the chymosins of several nonbovine species, including, camel, pig, equine, New World monkies, rat, and seal. The milk-clotting ability of aspartyl proteinases from other sources, for example, plants, fish, and crustaceans is discussed.