Akulova V F, Vaĭtkiavichius R K, Kurtinaĭtene B S, Kulis Iu I
Prikl Biokhim Mikrobiol. 1978 May-Jun;14(3):377-82.
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.
对来自产黄青霉的葡萄糖氧化酶的动力学、热稳定性和抗超声性进行了研究。其氧化常数相近,催化常数比黑曲霉的相应常数小1.7倍,还原常数比黑曲霉的相应常数大5.4倍。热失活常数(k(i)=2.1 pT 15.3)之间的关系。在pH值6.5 - 8.0范围内,超声失活常数与pH值也存在相同关系。在酸性更强的介质中,超声失活速率对pH值的依赖性不显著。文中讨论了酶失活的机制。