Sánchez-Montero J M, Sinisterra J V, Ballesteros A
Departamento de Química Orgánica, Universidad de Córdoba, Spain.
Appl Biochem Biotechnol. 1989 Nov;22(2):205-14. doi: 10.1007/BF02921745.
The endonuclease from S. aureus has been immobilized on ground maize cob, previously activated with tosyl chloride. Pretreatment of the support on acid before tosylation yielded the best insoluble enzyme derivatives. The catalytic activity has been evaluated as percent of total hydrolysis attained in a batch reactor using DNA as a model substrate. The derivatives prepared are very resistant to high temperatures under conditions of catalysis (24 h at 45 degrees C). For these long reaction times, the extent of hydrolysis in the presence of small amounts of organic solvent (dimethyl sulfoxide at 2 percent) is larger than in plain buffer (Tris). This type of derivative could be very useful for the removal of nucleic acids from single-cell protein concentrates.
来自金黄色葡萄球菌的核酸内切酶已固定在预先用对甲苯磺酰氯活化的磨碎玉米芯上。在对甲苯磺酰化之前对载体进行酸预处理可得到最佳的不溶性酶衍生物。使用DNA作为模型底物，在间歇反应器中以总水解百分比来评估催化活性。所制备的衍生物在催化条件下（45℃下24小时）对高温具有很强的抗性。对于这些较长的反应时间，在存在少量有机溶剂（2%的二甲基亚砜）的情况下的水解程度大于在普通缓冲液（Tris）中的水解程度。这种类型的衍生物对于从单细胞蛋白质浓缩物中去除核酸可能非常有用。
