Terrés Eduardo, Montiel Mayra, Le Borgne Sylvie, Torres Eduardo
Instituto Mexicano del Petróleo, Eje Central Lázaro Cárdenas 152, 07730,Mexico City, DF, Mexico.
Biotechnol Lett. 2008 Jan;30(1):173-9. doi: 10.1007/s10529-007-9512-5. Epub 2007 Sep 18.
The catalytic potential of chloroperoxidase (CPO) immobilized on mesoporous materials was evaluated for the oxidation of 4,6-dimethyldibenzothiophene in water/acetonitrile mixtures. Two different types of materials were used for the immobilization: a metal containing Al-MCM-41 material with a pore size of 26 A and SBA-16 materials with three different pore sizes: 40, 90 and 117 A. The SBA-16 40 A did not retain any CPO. The nature and the pore size of the material affected the catalytic activity of the enzyme as well as its stability. Compared to the free enzyme, the thermal stability of CPO at 45 degrees C was two and three times higher than when immobilized on Al-MCM-41 and SBA-16 90 A, respectively.
评估了固定在介孔材料上的氯过氧化物酶（CPO）在水/乙腈混合物中氧化4,6-二甲基二苯并噻吩的催化潜力。使用了两种不同类型的材料进行固定：一种孔径为26 Å的含金属Al-MCM-41材料和三种不同孔径（40、90和117 Å）的SBA-16材料。孔径为40 Å的SBA-16没有保留任何CPO。材料的性质和孔径影响了酶的催化活性及其稳定性。与游离酶相比，CPO在45℃时的热稳定性分别比固定在Al-MCM-41和90 Å的SBA-16上时高两倍和三倍。
