Spreti N, Bartoletti A, Di Profio P, Germani R, Savelli G
Dipartimento di Chimica, Universitá di L'Aquila, Italy.
Biotechnol Prog. 1995 Jan-Feb;11(1):107-11. doi: 10.1021/bp00031a016.
The activity and stability of beef liver catalase have been investigated in the presence of different ionic and zwitterionic surfactants. All cationic and zwitterionic surfactants used in this work have no effect on the initial activity of catalase, but several of them allow the enzyme to retain a high residual activity for longer periods of time than those observed in the absence of any additives. However, the interactions between surfactants and catalase appear to be very peculiar, and certain zwitterionic surfactants have been found to remarkably slow down enzyme degradation, with the enzyme completely preserving its activity after several weeks at temperatures of up to 30 degrees C. This effect is probably due to an interaction between the surfactant and the intersubunit region of the protein; this interaction could stabilize the quaternary structure of the enzyme.
在不同离子型和两性离子型表面活性剂存在的情况下,对牛肝过氧化氢酶的活性和稳定性进行了研究。本研究中使用的所有阳离子型和两性离子型表面活性剂对过氧化氢酶的初始活性均无影响,但其中几种表面活性剂能使该酶在比无任何添加剂时长的时间内保持较高的残余活性。然而,表面活性剂与过氧化氢酶之间的相互作用似乎非常特殊,并且已发现某些两性离子型表面活性剂能显著减缓酶的降解,在高达30摄氏度的温度下放置数周后,该酶仍能完全保持其活性。这种效应可能是由于表面活性剂与蛋白质亚基间区域的相互作用所致;这种相互作用可稳定酶的四级结构。