The effects of temperature, pH, concentration of camel chymosin and addition of CaCl2 on the hydrolysis of κ-casein (κ−CN) and the coagulation kinetics of camel milk were investigated. The rate of κ−CN hydrolysis was higher at 40 °C than at 30 °C and with increasing addition of chymosin and decreasing pH. For all samples gelation was initiated at levels of camel milk κ−CN hydrolysis >95%. The gelation time (Tg) of camel milk was significantly reduced (from 717 to 526 s) at 30 °C when the concentration of chymosin was increased, but was independent of chymosin concentration at 40 °C. Reducing pH also reduced Tg. The gel firmness increased at 40 °C (58 Pa) compared with 30 °C (44 Pa) and effect of CaCl2 addition on the gelation properties of camel milk was found to be dependent on pH; a significant improvement was only found at pH 6.3.