School of Biotechnology, Institute of Science, Banaras Hindu University, Varanasi 221005, India.
Nanoscience Centre, Department of Physics (Centre of Advanced Studies), Institute of Science, Banaras Hindu University, Varanasi 221005, India.
Food Chem. 2018 Apr 15;245:488-499. doi: 10.1016/j.foodchem.2017.10.092. Epub 2017 Oct 19.
Stability of enzymes is an important parameter for their industrial applicability. Here, we report successful immobilization of β-amylase (bamyl) from peanut (Arachis hypogaea) onto Graphene oxide-carbon nanotube composite (GO-CNT), Graphene oxide nanosheets (GO) and Iron oxide nanoparticles (FeO). The Box-Behnken Design of Response Surface Methodology (RSM) was used which optimized parameters affecting immobilization and gave 90%, 88% and 71% immobilization efficiency, respectively, for the above matrices. β-Amylase immobilization onto GO-CNT (bamyl@GO-CNT) and FeO (bamyl@FeO), resulted into approximately 70% retention of activity at 65 °C after 100 min of exposure. We used atomic force microscopy (AFM), scanning and transmission electron microscopy (SEM and TEM), Fourier transformed infrared (FT-IR) spectroscopy and fluorescence microscopy for characterization of free and enzyme bound nanostructures (NS). Due to the non-toxic nature of immobilization matrices and simple but elegant immobilization procedure, these may have potential utility as industrial biocatalysts for production of maltose.
酶的稳定性是其工业应用的一个重要参数。在这里，我们成功地将来自花生的β-淀粉酶（bamyl）固定在氧化石墨烯-碳纳米管复合材料（GO-CNT）、氧化石墨烯纳米片（GO）和氧化铁纳米颗粒（FeO）上。我们使用响应面法（RSM）的 Box-Behnken 设计来优化影响固定化的参数，分别为上述基质带来了 90%、88%和 71%的固定化效率。β-淀粉酶固定在 GO-CNT（bamyl@GO-CNT）和 FeO（bamyl@FeO）上，在 65°C 下暴露 100 分钟后，活性保留约 70%。我们使用原子力显微镜（AFM）、扫描和透射电子显微镜（SEM 和 TEM）、傅里叶变换红外（FT-IR）光谱和荧光显微镜来表征游离和酶结合的纳米结构（NS）。由于固定化基质的无毒性质和简单但优雅的固定化程序，它们可能具有作为工业生物催化剂生产麦芽糖的潜力。
