Rational surface silane modification for immobilizing glucose oxidase

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• 作者：Feibao Tian ; Yi Guo ; Feifei Lin ; Yumei Zhang ; Qipeng Yuan ; Hao Liang ; ^{lianghao@mail.buct.edu.cn" class="auth_mail" title="E-mail the corresponding author}
• 关键词：Glucose oxidase ; Silica nanoparticles ; Immobilization ; Silane surface modification
• 刊名：International Journal of Biological Macromolecules
• 出版年：2016
• 出版时间：June 2016
• 年：2016
• 卷：87
• 期：Complete
• 页码：191-194
• 全文大小：967 K

文摘

Glucose oxidase (GOx) has many significant applications in biosensor and biocatalysis. In this study, we firstly quantitatively analyzed the binding efficiency of (3-aminopropyl) trimethoxysilane (APTES) modified onto the surface of GOx. It was found that the contents of the grafted silane did not significantly influence the relative activities and tertiary structures of all surface modified GOxs. Immobilization ratio and relative activity of all instances of APTES modified GOx increased, compared with those of native enzyme. However, good stability of immobilized GOx at extreme pH and high temperature could only be obtained when modified protein with low binding silane content. At pH 2.0, the immobilized GOx with low binding content showed a more than 600% activity, compared to the free enzyme. Therefore, rational surface modification would be beneficial to improving the activity and stability of immobilized enzyme as well as increasing loading amount.