Instituto de Ciências Ambientais, Química e Farmacêuticas, Universidade Federal de São Paulo, Diadema, SP, Brazil.
J Colloid Interface Sci. 2012 May 1;373(1):69-74. doi: 10.1016/j.jcis.2011.07.095. Epub 2011 Aug 16.
Preserving the enzyme structure in solid films is key for producing various bioelectronic devices, including biosensors, which has normally been performed with nanostructured films that allow for control of molecular architectures. In this paper, we investigate the adsorption of uricase onto Langmuir monolayers of stearic acid (SA), and their transfer to solid supports as Langmuir-Blodgett (LB) films. Structuring of the enzyme in β-sheets was preserved in the form of 1-layer LB film, which was corroborated with a higher catalytic activity than for other uricase-containing LB film architectures where the β-sheets structuring was not preserved. The optimized architecture was also used to detect uric acid within a range covering typical concentrations in the human blood. The approach presented here not only allows for an optimized catalytic activity toward uric acid but also permits one to explain why some film architectures exhibit a superior performance.
在固态薄膜中保存酶的结构对于生产各种生物电子设备至关重要,包括生物传感器,通常使用允许控制分子结构的纳米结构薄膜来实现。在本文中,我们研究了尿酸酶在硬脂酸(SA)的Langmuir 单层上的吸附及其作为 Langmuir-Blodgett(LB)薄膜转移到固体载体上。酶在β-折叠结构中的形式在 1 层 LB 薄膜中得到了保留,这得到了比其他未保留β-折叠结构的含有尿酸酶的 LB 薄膜结构更高的催化活性的证实。优化的结构也被用于检测人类血液中典型浓度范围内的尿酸。这里提出的方法不仅允许对尿酸表现出优化的催化活性,而且还可以解释为什么某些薄膜结构表现出更好的性能。