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一种生物印迹脲酶生物传感器:提高了热稳定性和操作稳定性。

A bio-imprinted urease biosensor: Improved thermal and operational stabilities.

作者信息

Teke Mustafa, Sezgintürk Mustafa Kemal, Dinçkaya Erhan, Telefoncu Azmi

机构信息

Muğla University, Science and Art Faculty, Chemistry Department, 48000 Muğla, Turkiye.

出版信息

Talanta. 2008 Jan 15;74(4):661-5. doi: 10.1016/j.talanta.2007.06.031. Epub 2007 Jul 1.

Abstract

Despite the increasing number of applications of biosensors in many fields, the construction of a steady biosensor remains still challenging. The high stability of molecularly bio-imprinted enzymes for its substrate can make them ideal alternatives as recognition elements for sensors. Urease (urea aminohydrolase, EC 3.5.1.5), which catalysis the hydrolysis of urea to ammonia and carbon dioxide, has been used in immobilized form in artificial kidney for blood detoxification. According to one report approximately half a million patients worldwide are being supported by haemodialysis. In this study, the enzyme of urease was first complexed by using a substrate analogue, thiourea, in aqueous medium and then this enzyme was immobilized on gelatin by crosslinking with glutaraldehyde on a glass electrode surface. Similarly, urease noncomplexed with thiourea was also immobilized on a glass electrode in the same conditions. The aim of the study was to compare the two biosensors in terms of their repeatability, pH stability and thermal stability, and also, linear ranges of two biosensors were compared with each other.

摘要

尽管生物传感器在许多领域的应用越来越多,但构建稳定的生物传感器仍然具有挑战性。分子生物印迹酶对其底物具有高稳定性,这使其成为传感器识别元件的理想替代品。脲酶(尿素氨基水解酶,EC 3.5.1.5)催化尿素水解为氨和二氧化碳,已以固定化形式用于人工肾进行血液解毒。根据一份报告,全球约有50万患者依靠血液透析维持生命。在本研究中,脲酶首先在水介质中与底物类似物硫脲络合,然后通过与戊二醛交联将该酶固定在明胶上,置于玻璃电极表面。同样,未与硫脲络合的脲酶也在相同条件下固定在玻璃电极上。该研究的目的是比较两种生物传感器的重复性、pH稳定性和热稳定性,并且还比较了两种生物传感器的线性范围。

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