Sato T, Mori T, Tosa T, Chibata I, Furui M
Biotechnol Bioeng. 1975 Dec;17(12):1797-1804. doi: 10.1002/bit.260171209.
The reaction mechanism and decay behavior of aspartase activity for immobilized Escherichia coli cells were investigated by using a sectional packed column. Reaction within the immobilized cell column proceeded at zero-order on substrate solutions ranging in concentration from 0.1 to 1.0M, and the initial reaction rate was found to be 1.556 X 10(-2) mol/min/liter of immobilized cells. The effect of temperature on the reaction rate constant was investigated. The Arrhenius plot was a straight line at temperatures below 43 degrees C, and the activation energy for immobilized cells was calculated to be 12.36 kcal/mol. Aspartase activity in the immobilized cell column decayed exponentially and uniformly in all sections of a column. Its half-life was approximately 120 days. The rate of formation of L-aspartic acid was shown to be independent of column dimensions.
采用分段填充柱研究了固定化大肠杆菌细胞中天冬氨酸酶活性的反应机理和衰减行为。固定化细胞柱内的反应在浓度范围为0.1至1.0M的底物溶液上呈零级反应，发现初始反应速率为1.556×10(-2) mol/（min·升固定化细胞）。研究了温度对反应速率常数的影响。在低于43℃的温度下，阿仑尼乌斯图呈直线，计算出固定化细胞的活化能为12.36 kcal/mol。固定化细胞柱中的天冬氨酸酶活性在柱的所有部分呈指数衰减且均匀。其半衰期约为120天。结果表明，L-天冬氨酸的形成速率与柱尺寸无关。
