Substrate and binding specificity of aspartic proteases with milk clotting properties.

The hydrolysis of whole casein and isolated casein components were investigated with the purpose of obtaining information concerning the kinetic and specifty of aspartic proteases in rennin, pepsin and 4 microbial rennet substitutes. The velocity of hydrolysis decreased rapidly within the first hour. However, the hydrolysis was not completed after 2 days.