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首页> 外文期刊>Artificial cells, nanomedicine, and biotechnology. >Magnetic FeO@MCM-41 core–shell nanoparticles functionalized with thiol silane for efficient l-asparaginase immobilization functionalized with thiol silane for efficient lasparaginaseimmobilization
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Magnetic FeO@MCM-41 core–shell nanoparticles functionalized with thiol silane for efficient l-asparaginase immobilization functionalized with thiol silane for efficient lasparaginaseimmobilization

机译：磁性FeO @ MCM-41核壳纳米粒子，经巯基硅烷官能化可有效固定L-天冬酰胺酶，经巯基硅烷官能化可有效固定Las天冬酰胺酶。

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l -Asparaginase ( l -ASNase) is a vital enzyme for medical treatment and food industry. Here, we assessed the use of Fe3O4@Mobil Composition of Matter No. 41 (MCM-41) magnetic nanoparticles as carrier matrix for l -ASNase immobilization. In addition, surface of Fe3O4@MCM-41 magnetic nanoparticles was functionalized with 3-mercaptopropyltrimethoxysilane (MPTMS) to enhance stability of l -ASNase. The chemical structure, thermal properties, magnetic profile and morphology of the thiol-functionalized Fe3O4@MCM-41 magnetic nanoparticles were characterized with Fourier transform infrared spectroscopy (FTIR), thermogravimetric analysis (TGA), differential thermal analysis (DTA), differential scanning calorimetry (DSC), vibrating sample magnetometer (VSM), scanning electron microscope (SEM), energy dispersive X-ray (EDX) spectroscopy and zeta-potential measurement. l -ASNase was covalently immobilized onto the thiol-functionalized Fe3O4@MCM-41 magnetic nanoparticles. The properties of the immobilized enzyme, including optimum pH, temperature, kinetic parameters, thermal stability, reusability and storage stability were investigated and compared to free one. Immobilized enzyme was found to be stable over a wide range of pH and temperature range than free enzyme. The immobilized l -ASNase also showed higher thermal stability after 180?min incubation at 50?°C. The immobilized enzyme still retained 63% of its original activity after 16 times of reuse. The Km value for the immobilized enzyme was 1.15-fold lower than the free enzyme, which indicates increased affinity for the substrate. Additionally, the immobilized enzyme was active over 65% and 53% after 30?days of storage at 4?°C and room temperature (～25?°C), respectively. Thereby, the results confirmed that thiol-functionalized Fe3O4@MCM-41 magnetic nanoparticles had high efficiency for l -ASNase immobilization and improved stability of L -ASNase.
机译：l-天冬酰胺酶（l -ASNase）是用于医疗和食品工业的重要酶。在这里，我们评估了Fe3O4 @ Mobil物质第41号（MCM-41）磁性纳米颗粒作为1-ASNase固定化载体基质的用途。另外，用3-巯基丙基三甲氧基硅烷（MPTMS）将Fe 3 O 4 @ MCM-41磁性纳米颗粒的表面官能化以增强1-ASNase的稳定性。通过傅立叶变换红外光谱（FTIR），热重分析（TGA），差示热分析（DTA），差示扫描量热法对巯基官能化的Fe3O4 @ MCM-41磁性纳米粒子的化学结构，热性质，磁特性和形貌进行了表征。 （DSC），振动样品磁力计（VSM），扫描电子显微镜（SEM），能量色散X射线（EDX）光谱和Zeta电位测量。将1-ASNase共价固定在巯基官能化的Fe3O4 @ MCM-41磁性纳米颗粒上。研究了固定化酶的性质，包括最佳pH，温度，动力学参数，热稳定性，可重复使用性和储存稳定性，并将其与游离酶进行了比较。发现固定化酶比游离酶在宽范围的pH和温度范围内稳定。固定化的1-ASNase在50°C下孵育180分钟后也显示出更高的热稳定性。重复使用16次后，固定化酶仍保留其原始活性的63％。固定化酶的Km值比游离酶低1.15倍，表明对底物的亲和力增加。此外，在4℃和室温（〜25℃）下储存30天后，固定化酶的活性分别超过65％和53％。因此，结果证实了硫醇官能化的Fe 3 O 4 @ MCM-41磁性纳米颗粒具有高的1-ASNase固定化效率和改善的L-ASNase稳定性。

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