Instituto de Investigación, Desarrollo e Innovación en Biotecnología Sanitaria de Elche (IDiBE), Universidad Miguel Hernández de Elche (UMH), 03202 Elche, Spain.
Instituto Regional de Investigación Científica Aplicada (IRICA), Universidad de Castilla-La Mancha, Avda. Camilo José Cela, s/n, 13071 Ciudad Real, Spain.
Int J Mol Sci. 2023 Jan 31;24(3):2672. doi: 10.3390/ijms24032672.
Here, we present a study on the incorporation and characterization of the enzyme alkaline phosphatase (ALP) into a three-dimensional polymeric network through a green protocol to obtain transparent hydrogels (ALP@AETA) that can be stored at room temperature and potentially used as a disposable biosensor platform for the rapid detection of ALP inhibitors. For this purpose, different strategies for the immobilization of ALP in the hydrogel were examined and the properties of the new material, compared to the hydrogel in the absence of enzyme, were studied. The conformation and stability of the immobilized enzyme were characterized by monitoring the changes in its intrinsic fluorescence as a function of temperature, in order to study the unfolding/folding process inside the hydrogel, inherently related to the enzyme activity. The results show that the immobilized enzyme retains its activity, slightly increases its thermal stability and can be stored as a xerogel at room temperature without losing its properties. A small portion of a few millimeters of ALP@AETA xerogel was sufficient to perform enzymatic activity inhibition assays, so as a proof of concept, the device was tested as a portable optical biosensor for the detection of phosphate in water with satisfactory results. Given the good stability of the ALP@AETA xerogel and the interesting applications of ALP, not only in the environmental field but also as a therapeutic enzyme, we believe that this study could be of great use for the development of new devices for sensing and protein delivery.
在这里,我们通过绿色方案研究了将酶碱性磷酸酶(ALP)掺入三维聚合网络中,并将其表征为透明水凝胶(ALP@AETA),该水凝胶可以在室温下储存,并可能用作用于快速检测 ALP 抑制剂的一次性生物传感器平台。为此,研究了在水凝胶中固定 ALP 的不同策略,并研究了新材料的性质,与没有酶的水凝胶相比。通过监测其固有荧光随温度的变化来表征固定化酶的构象和稳定性,以研究水凝胶内部固有地与酶活性相关的展开/折叠过程。结果表明,固定化酶保留其活性,略微提高其热稳定性,并可作为干凝胶在室温下储存而不会失去其性质。几毫米长的一小部分 ALP@AETA 干凝胶就足以进行酶活性抑制测定,因此作为概念验证,该设备被测试为用于检测水中磷酸盐的便携式光学生物传感器,结果令人满意。鉴于 ALP@AETA 干凝胶的良好稳定性以及 ALP 的有趣应用,不仅在环境领域,而且在治疗酶领域,我们相信这项研究对于开发用于传感和蛋白质输送的新设备将非常有用。