[Kinetics and stability of glucooxidase from Penicillium vitale].
The kinetics, thermal stability and ultrasonic resistance of glucosoxidase from Penicillium vitale have been investigated. Its oxidative constant is close to, catalytic constant is 1.7 times less and the reductive constant is 5.4 times more than the respective constants of the enzyme from Aspergillus niger. The relationship between the thermal inactivation constant (k(i)=2.1 pT 15.3. The same relationship is true of the ultrasonic inactivation constant and pH in the pH range of 6.5-8.0. In a more acidic medium the rate of ultrasonic inactivation shows an insignificant dependence on pH. The mechanism of enzyme inactivation is discussed.
[Kinetics and stability of glucooxidase from Penicillium vitale]. The kinetics, thermal stability and ultrasonic resistance of glucosoxidase from Penicillium vitale have been investigated. Its oxidative constant is close to, catalytic constant is 1.7 times less and the reductive constant is 5.4 times more than the respective constants of the enzyme from Aspergillus niger. The relationship between the thermal inactivation constant (k(i)=2.1 pT 15.3. The same relationship is true of the ultrasonic inactivation constant and pH in the pH range of 6.5-8.0. In a more acidic medium the rate of ultrasonic inactivation shows an insignificant dependence on pH. The mechanism of enzyme inactivation is discussed.