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Immobilization of Cellulase onto Core-Shell Magnetic Gold Nanoparticles Functionalized by Aspartic Acid and Determination of its Activity.
The Protein Journal ( IF 3 ) Pub Date : 2020-07-15 , DOI: 10.1007/s10930-020-09906-z
Elahe Poorakbar 1, 2 , Ali Akbar Saboury 2, 3 , Behzad Laame Rad 1 , Kamyar Khoshnevisan 4, 5
Affiliation  

New support was fabricated to enhance the enzyme activity of cellulase following immobilization. Functionalized core-shell magnetic gold nanoparticles were prepared and characterized by X-ray diffraction (XRD), vibrating sample magnetometer (VSM), scanning electron microscopy (SEM) and transmission electron microscopy (TEM). Cellulase enzyme was immobilized on support via covalent bonding. The successful binding of the enzyme was chemically confirmed by Fourier-transform infrared spectroscopy (FTIR). The binding efficiency was 84% determined by Bradford assay. Filter Paper Activity (FPase) method was used to measure the enzyme activity at different temperatures (35–75 °C) and pH (2–8). The immobilized cellulase maintained 73% of its initial catalytic activity after 9 h and its activity is 0.78 mmol.ml−1. The newly designed nano-system also enhanced the thermal stability of immobilized cellulase in comparison to free cellulase and facilitated its long term storage.

中文翻译:

将纤维素酶固定在天冬氨酸功能化的核-壳磁性金纳米粒子上,并测定其活性。

制备了新的支持物以增强固定后的纤维素酶的酶活性。制备了功能化的核壳磁性金纳米颗粒,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)和透射电子显微镜(TEM)对其进行了表征。纤维素酶通过共价键固定在支持物上。酶的成功结合通过傅里叶变换红外光谱法(FTIR)在化学上得以证实。通过Bradford测定法测定的结合效率为84%。滤纸活性(FPase)方法用于测量不同温度(35–75°C)和pH(2–8)下的酶活性。固定的纤维素酶在9小时后保持其初始催化活性的73%,其活性为0.78 mmol.ml -1。与游离纤维素酶相比,新设计的纳米系统还增强了固定纤维素酶的热稳定性,并促进了其长期保存。
更新日期:2020-07-15
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