DUERRE J A, RIBI E
Appl Microbiol. 1963 Nov;11(6):467-71. doi: 10.1128/am.11.6.467-471.1963.
The release and stability of the enzymes S-adenosylhomocysteine nucleosidase, lysine decarboxylase, arginine decarboxylase, glutamic decarboxylase, formic hydrogenlyase, formic oxidase, and glucose oxidase from Escherichia coli during disruption of the organisms in a Servall-Ribi refrigerated cell fractionator were examined. With the possible exception of arginine decarboxylase, maximal activity was retained by all the enzymes reported here when the cell suspensions were processed at pressures necessary for rupture of all the organisms (15,000 to 25,000 psi). Considerable variation in the stability of different enzymes liberated by disruption at higher pressures (45,000 to 55,000 psi) was observed. It is reasonable to assume that mechanical forces rather than effects of temperature are responsible for inactivation of these enzymes.
研究了在Servall-Ribi冷冻细胞分级分离器中破碎大肠杆菌时,S-腺苷同型半胱氨酸核苷酶、赖氨酸脱羧酶、精氨酸脱羧酶、谷氨酸脱羧酶、甲酸氢裂解酶、甲酸氧化酶和葡萄糖氧化酶的释放及稳定性。除精氨酸脱羧酶外,当细胞悬液在所有生物体破裂所需的压力(15,000至25,000磅力/平方英寸)下处理时,此处报道的所有酶均保留了最大活性。在较高压力(45,000至55,000磅力/平方英寸)下破碎释放的不同酶的稳定性存在相当大的差异。可以合理地假设,这些酶失活的原因是机械力而非温度的影响。