Improvement of the alkaline protease properties via immobilization on the TiO2 nanoparticles supported by mesoporous MCM-41

被引:18
|
作者
Sadjadi, M. S. [1 ]
Farhadyar, N. [1 ]
Zare, K. [1 ]
机构
[1] Islamic Azad Univ, Dept Chem Sci & Res Campus, Tehran, Iran
关键词
Titanium oxide nanoparticles; Mesoporous MCM-41; Alkaline Protease immobilization; Biocatalytic materials; GLUCOSE-OXIDASE; ENZYME; PARTICLES; STABILITY;
D O I
10.1016/j.spmi.2008.10.022
中图分类号
O469 [凝聚态物理学];
学科分类号
070205 ;
摘要
Enzymes are able to catalyze the most complex chemical processes under the mildest experimental and environmental conditions. However, in general, enzymes do not fulfill the requirements for industry. Therefore, most enzymes have to be greatly improved before industrial implementation. They may be immobilized by using very different protocols. Nanoparticles have been significantly used for coupling with biomolecules. They are excellent biocompatible surfaces for the immobilization of enzymes. In this work, we demonstrated that the alkaline protease enzyme immobilized on the TiO2 nanoparticles assembled on the porous MCM-41 (Mobile Crystalline Material No. 41) particles could provide an active biocatalyst, stable at different pH and temperature. Absorption of the TiO2 nanoparticles on the MCM-41 was monitored by UV-visible spectroscopy. Scanning Electron Microscopy (SEM), Transmission Electron Microscopy (TEM) and dispersive analysis of X-RAY (EDAX) were used to characterize the size and morphology of the TiO2 nanoparticles on the MCM-41. (c) 2008 Elsevier Ltd. All rights reserved.
引用
收藏
页码:77 / 83
页数:7
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