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首页> 外文期刊>International Journal of Biological Macromolecules: Structure, Function and Interactions >Maltose functionalized magnetic core/shell Fe3O4@Au nanoparticles for an efficient L-asparaginase immobilization
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Maltose functionalized magnetic core/shell Fe3O4@Au nanoparticles for an efficient L-asparaginase immobilization

机译:麦芽糖官能化磁芯/壳Fe3O4 @ Au纳米粒子用于高效的L-天酰胺酶固定化

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In this study, maltose-functionalized magnetic core/shell nanoparticles (Fe3O4@Au NPs) as a promising carrier matrix for a simple and effective immobilization of L-asparaginase (L-ASNase) were prepared and characterized using imaging techniques including atomic force microscopy (AFM) and transmission electron microscopy (TEM), and vibrating sample magnetometry (VSM). The results indicate that the NPs are monodispersed with an average diameter of 10 nm and magnetization of 9.0 emu g(-1). Under the optimal conditions, 77.2 +/- 2.3% of the total L-ASNase was immobilized. It was found that the acid-base tolerance and thermal stability of immobilized L-ASNase were significantly improved in comparison to the free form of the enzyme in solution. For instance, while only 10% of the immobilized enzyme was lost its activity, the free form was lost its activity more than 50% after 3 h incubation at 55 degrees C. After 13 times recycling, the immobilized L-ASNase retained about 50% of its initial activity. Moreover, the free and immobilized L-ASNase maintained their initial activities about 25 and 64% after 28 days storage at 25 degrees C, respectively. Km value of immobilized L-ASNase decreased to 1.59 from 2.95 mM as an indication of increased enzyme affinity for the substrate. The results of this study suggest that the maltose-coated magnetic nanoparticles are excellent nanovehicles to carry enzymes for a range of industrial applications. (C) 2019 Elsevier B.V. All rights reserved.
机译:在这项研究中,麦芽糖官能磁性核/壳纳米颗粒(四氧化三铁@金纳米粒子),作为一个简单的和L-天冬酰胺酶(L-ASNase)的有效固定化制备一个有前途的载体基质和使用成像技术,包括原子力显微镜,其特征在于( AFM)和透射电子显微镜(TEM),和振动样品磁强计(VSM)。结果表明,该纳米颗粒与10纳米的平均直径和磁化的9.0鸸鹋克(-1)单分散的。在此条件下,总的L-ASNase的77.2 +/- 2.3%的固定化。已经发现,酸 - 碱耐受性和固定化的L-ASNase的热稳定性相比,在溶液中的酶的游离形式被显著改善。例如,虽然只有10%的固定化的酶的丢失其活性,游离形式在55℃下失去其活性后超过50%的3小时的温育13次循环后,将固定化的L-ASNase保留约50%的其初始活性。此外,自由和固定化的L-ASNase在25度分别维持其初始活动约28天之后存储器25和64%C,。固定化的L-ASNase的Km值从2.95毫米减小到1.59为增加酶的亲和力为基材的指示。这项研究的结果表明,麦芽糖涂覆磁性纳米颗粒是纳米载体优良携带酶的范围内工业应用。 (c)2019 Elsevier B.v.保留所有权利。

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