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介绍了一种新型的酶生物传感器，以具有一定规整结构的γ－氧化铝（γ－Ａｌ２Ｏ３）固定 尿酸氧化酶制备了尿酸传感器，利用傅里叶变换红外光谱研究了γ－Ａｌ２Ｏ３与尿酸氧化酶之 间的相互作用；为了探讨吸附与γ－Ａｌ２Ｏ３间的相互作用，分别用Ｎ２的吸附－脱附等温线和质 量滴定法测定了γ－Ａｌ２Ｏ３的孔分布和等电点，解释了 ｐＨ对吸附的影响，并对电极的制备条 件和工作性能进行了考察，结果表明电极对尿酸在１．０×１０－５～７．５×１０－４ｍｏｌ／Ｌ范围内有着 灵敏快速的响应，检出下限为２．０×１０－６ｍｏｌ／Ｌ。该实验对固定化酶反应机理的研究和应用 提供了理论基础。
A novel enzyme biosensor was introduced to prepare uric acid sensor by immobilizing uric acid oxidase with γ-alumina (γ-Al2O3) with a regular structure. Fourier transform infrared spectroscopy (FTIR) was used to study the relationship between γ-Al2O3 and uric acid oxidase In order to investigate the interaction between adsorption and γ-Al2O3, the pore distribution and isoelectric point of γ-Al2O3 were determined by N2 adsorption-desorption isotherms and mass titration, respectively. The effects of pH on adsorption The results show that the electrode has a sensitive and rapid response to uric acid in the range of 1.0 × 10-5 ~ 7.5 × 10-4mol / L, and the lower limit of detection 2.0 × 10 -6 mol / L. This experiment provides a theoretical basis for the research and application of immobilized enzyme reaction mechanism.