Changes in the apparent hydrophobicity of Pseudomonas 31 proteinase after heat treatments
(EN)
Triantafyllidou, M.
(EN)
Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας
(EL)
Triantafyllidou, M.
(EN)
Proteinase from Pseudomonas 31 appeared to be a metalloenzyme. The remaining activity and the increase in the apparent hydrophobicity after heating the proteinase at 55 degrees C for 15 min were 10 and 60%, respectively, relating 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, indicating 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 above 2 parameters were 16 and 35%, respectively, indicating the involvement in the inactivation of the proteinase at 55 degrees C.
(EN)
