Catalytic activity of enzymes immobilized on AlGaN/GaN solution gate field-effect transistors
Catalytic activity of enzymes immobilized on AlGaN/GaN solution gate field-effect transistors
复制标题
AlGaN/GaN溶液栅极场效应晶体管固定化酶的催化活性
DOI：
--
复制
发表时间：
2006
期刊：
影响因子：
--
通讯作者：
M. Eickhoff
中科院分区：
文献类型：
--
作者：
B. Baur;J. Howgate;H. V. Ribbeck;Y. Gawlina;V. Bandalo;G. Steinhoff;M. Stutzmann;M. Eickhoff
将青霉素酶固定在AlGaN ScinGaN溶液栅场效应晶体管上，制备了酶修饰场效应晶体管（EnFET）。通过比较共价固定化和物理吸附固定化，分析了固定化过程对酶功能的影响。共价固定化的氨基丙基三乙氧基硅烷单层改性的GaN表面上的席夫碱形成相对于酶/底物的亲和力表现出高的再现性。将席夫碱键还原胺化为仲胺显著增加了酶层的稳定性。青霉素G的EnFET响应的电子表征表明，共价固定导致形成的酶（子）单层。
Enzyme-modified field-effect transistors (EnFETs) were prepared by immobilization of penicillinase on AlGaN∕GaN solution gate field-effect transistors. The influence of the immobilization process on enzyme functionality was analyzed by comparing covalent immobilization and physisorption. Covalent immobilization by Schiff base formation on GaN surfaces modified with an aminopropyltriethoxysilane monolayer exhibits high reproducibility with respect to the enzyme/substrate affinity. Reductive amination of the Schiff base bonds to secondary amines significantly increases the stability of the enzyme layer. Electronic characterization of the EnFET response to penicillin G indicates that covalent immobilization leads to the formation of an enzyme (sub)monolayer.