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Synthesis of magnetic gold mesoporous silica nanoparticles core shell for cellulase enzyme immobilization: Improvement of enzymatic activity and thermal stability

机译:固定化纤维素酶的磁性金介孔二氧化硅纳米粒子核壳的合成:提高酶活性和热稳定性

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Magnetic gold mesoporous silica nanoparticle core shells (mAu@PSNs) were fabricated as a support and their size, morphology and structure was further characterized by X-Ray diffraction (XRD), vibrating sample magnetometer (VSM), scanning electron microscopy (SEM), energy dispersive X-ray analysis (EDAX), transmission electron microscopy (TEM), dynamic light scattering (DLS) and thermal gravimetric analysis (TGA). Cellulase (CEL) immobilization on mAu@PSNs was performed via covalent bonding. Fourier transform infrared (FTIR) spectroscopy confirmed the successful binding of enzyme to mAu@PSNs while Bradford assay determined the binding efficiency to be 76%. The enzyme activity was measured at different pHs and temperatures by FPase method using Whatman filter paper as the substrate. The immobilized enzyme maintained 58% of its initial catalytic activity after nine hours. In this research, a new nano-system was designed as a solid support for cellulase immobilization which enhanced its thermal stability and facilitated its long term storage. In addition, the immobilized enzyme can be applied in a broader temperature and pH ranges while enzyme separation can be simply carried out by an external magnet.
机译:制备了磁性金介孔二氧化硅纳米粒子核壳(mAu @ PSNs)作为载体,并通过X射线衍射(XRD),振动样品磁力计(VSM),扫描电子显微镜(SEM)进一步表征了它们的尺寸,形态和结构,能量色散X射线分析(EDAX),透射电子显微镜(TEM),动态光散射(DLS)和热重分析(TGA)。纤维素酶(CEL)通过共价键合固定在mAu @ PSN上。傅里叶变换红外(FTIR)光谱证实了酶与mAu @ PSN的成功结合,而布拉德福德测定法测定的结合效率为76%。使用Whatman滤纸作为底物,通过FPase方法在不同pH和温度下测量酶活性。九小时后,固定化酶保持其初始催化活性的58%。在这项研究中,设计了一种新的纳米系统作为纤维素酶固定化的固体支持物,可增强其热稳定性并促进其长期保存。另外,固定化的酶可以在更宽的温度和pH范围内施用,而酶的分离可以简单地通过外部磁体进行。

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