High Enzymatic Activity Preservation with Carbon Nanotubes Incorporated in Urease-Lipid Hybrid Langmuir-Blodgett Films

被引:22
作者
Caseli, Luciano [1 ]
Siqueira, Jose Roberto, Jr. [2 ]
机构
[1] Univ Fed Sao Paulo UNIFESP, Inst Ciencias Ambientais Quim & Farmaceut, BR-09972270 Sao Paulo, Brazil
[2] Univ Fed Triangulo Mineiro, Inst Ciencias Exatas Nat & Educ, BR-38025180 Uberaba, MG, Brazil
基金
巴西圣保罗研究基金会;
关键词
PHOSPHOLIPID LANGMUIR; AMIDE-I; MONOLAYERS; IMMOBILIZATION; SPECTROSCOPY; INTERFACES;
D O I
10.1021/la300193m
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
The search for optimized architectures, such as thin films, for the production of biosensors has been challenged in recent decades, and thus, the understanding of molecular interactions that occur at interfaces is essential to improve the construction of nanostructured devices. In this study, we investigated the possibility of using carbon nanotubes in hybrid Langmuir-Blodgett (LB) films of lipids and urease to improve the catalytic performance of the immobilized enzyme. The molecular interactions were first investigated at the air-water interface with the enzyme adsorbed from the aqueous subphase onto Langmuir monolayers of dimyristoylphosphatidic acid (DMPA). The transfer to solid supports as LB films and the subsequent incorporation of carbon nanotubes in the hybrid film permitted us to evaluate how these nanomaterials changed the physical properties of the ultrathin film. Colorimetric measurments indicated that the presence of nanotubes preserved and enhanced the enzyme activity of the film, even after 1 month. These results show that the use of such hybrid films is promising for the development of biosensors with an optimized performance.
引用
收藏
页码:5398 / 5403
页数:6
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