論文
子牛小腸アルカリホスファターゼの熱変性機構
2018 年 67 巻 5 号 p. 533-538
詳細
2018 年 67 巻 5 号 p. 533-538
The pressure effects on thermal inactivation of calf intestine alkaline phosphatase (CIAP) have been studied by measuring the rate of hydrolysis of p-nitrophenyl phosphate (pNPP) catalyzed by CIAP in the temperature range of 25～60 ℃ and at the pressures up to 150 MPa. The apparent rate of hydrolysis decreased with time above a certain temperature. The decrease is due to the decrease in CIAP activity. The enthalpy change of the thermal inactivation was 354～478 kJ mol-1, and volume change of this process was 8.8～40 cm3mol-1. The mechanism of the thermal inactivation of CIAP is discussed in terms of each thermodynamic parameters.
