Changes in the apparent hydrophobicity of Pseudomonas 31 proteinase after heat treatments

Proteinase from Pseudomonas 31 appeared to be a metalloenzyme. The remainin g activity and the increase in the apparent hydrophobicity after heating th e proteinase at 55 degrees C for 15 min were 10 and 60%, respectively, rela ting to unheated samples. On the other hand, the above parameters after the treatment at 95 degrees C for 15 min were 14 and 140%, respectively, indic ating that different phenomena occur at these 2 temperatures. After heating the proteinase at 55 degrees C for 15 min in the presence of casein, the a bove 2 parameters were 16 and 35%, respectively, indicating the involvement in the inactivation of the proteinase at 55 degrees C.