Department of Marine Biology, Faculty of Marine Science and Technology, University of Hormozgan, P.O. Box 3995, Bandar Abbas, Iran.
Department of Marine Biology, Faculty of Marine Science and Technology, University of Hormozgan, P.O. Box 3995, Bandar Abbas, Iran; Department of Biologyy, Faculty of Sciences, University of Hormozgan, Bandar Abbas, Iran.
Int J Biol Macromol. 2018 Oct 15;118(Pt A):92-98. doi: 10.1016/j.ijbiomac.2018.06.075. Epub 2018 Jun 18.
The activity, stability, and kinetics of immobilized enzymes are influenced by the nature of the support or carrier material. In this research, zinc oxide nanoparticles were synthesized by chemical precipitation, and the purified protease from shrimp Penaeus vanamei was immobilized on the nanoparticles. Size, structure, and morphology of the ZnO nanoparticles, and the immobilization of the protease were studied by transmission electron microscopy (TEM), Fourier transform infrared (FT-IR) spectroscopy, UV-Vis spectroscopy, and dynamic light scattering (DLS). The immobilization of protease on ZnO nanoparticles improved the long-term and thermal stability, plus its stability at extreme pH values, and it increased the optimum functional temperature of the enzyme. The optimum pH value of the immobilized protease was shifted from 7.0 to 8.0 upon immobilization. Additionally, and due to the immobilization an increased K was observed, whereas its catalytic efficiency was estimated a little less as compared to that of free enzyme. These results show that the immobilization of Penaeus vanamei protease on zinc oxide nanoparticles enhanced its appropriateness for a future use in various biotechnological and industrial applications.
固定化酶的活性、稳定性和动力学受到载体材料性质的影响。本研究通过化学沉淀法合成了氧化锌纳米粒子，并将对虾（Penaeus vanamei）来源的纯化蛋白酶固定在纳米粒子上。通过透射电子显微镜（TEM）、傅里叶变换红外（FT-IR）光谱、紫外-可见光谱和动态光散射（DLS）研究了 ZnO 纳米粒子的大小、结构和形态，以及蛋白酶的固定化情况。蛋白酶固定在 ZnO 纳米粒子上提高了酶的长期和热稳定性，以及在极端 pH 值下的稳定性，并提高了酶的最佳功能温度。固定化蛋白酶的最适 pH 值从 7.0 转移到 8.0。此外，由于固定化，观察到 K 值增加，而其催化效率估计略低于游离酶。这些结果表明，将对虾蛋白酶固定在氧化锌纳米粒子上增强了其在未来各种生物技术和工业应用中的适用性。
