固定在介孔分子筛上的乙酰胆碱酯酶的催化活性。
Catalytic activity of acetylcholinesterase immobilized on mesoporous molecular sieves.
作者信息
Rosales-Hernández M C, Mendieta-Wejebe J E, Correa-Basurto J, Vázquez-Alcántara J I, Terres-Rojas E, Trujillo-Ferrara J
机构信息
Sección de Estudios de Posgrado e Investigación y Departamento de Bioquímica de la Escuela Superior de Medicina del Instituto Politécnico Nacional, Plan de San Luis y Díaz Mirón s/n, 11340 México, D.F., Mexico.
出版信息
Int J Biol Macromol. 2007 Apr 10;40(5):444-8. doi: 10.1016/j.ijbiomac.2006.11.004. Epub 2006 Nov 23.
MCM-41 and FSM-16 were used for enzyme immobilization on account of their good physical and chemical properties. In this work, the catalytic activity of acetylcholinesterase (AChE) immobilized on these materials was investigated, using neostigmina as AChE inhibitor. The results show that AChE was adsorbed on MCM-41 and on FSM-16-TIPB. AChE immobilized on the latter material maintained 70% of its activity and the material did not hydrolyze ACh (as MCM-41) by itself. Therefore, FSM-16-TIPB was the best material, considering also that when neostigmine was applied to AChE immobilized on FSM-16-TIPB, the activity of AChE decreased as occurs in its free from. Hence, this model could be useful in the evaluation of different kinds of AChE inhibitors, allowing the recycling of enzymes and making possible several assays and thereby, lowering cost.
由于MCM-41和FSM-16具有良好的物理和化学性质，它们被用于酶固定化。在这项工作中，以新斯的明作为乙酰胆碱酯酶（AChE）抑制剂，研究了固定在这些材料上的AChE的催化活性。结果表明，AChE吸附在MCM-41和FSM-16-TIPB上。固定在后者材料上的AChE保持了其70%的活性，并且该材料本身不会水解ACh（与MCM-41不同）。因此，考虑到当将新斯的明应用于固定在FSM-16-TIPB上的AChE时，AChE的活性会像其游离形式一样降低，FSM-16-TIPB是最佳材料。因此，该模型可用于评估不同种类的AChE抑制剂，实现酶的循环利用，并使多次测定成为可能，从而降低成本。
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