1- Department of Biology, Faculty of Sciences, University of Guilan, Rasht, Iran.
2- Department of Biology, Faculty of Sciences, University of Guilan, Rasht, Iran. , Shahangian@guilan.ac.ir
Abstract: (7 Views)
Researchers are currently directing their efforts toward developing new enzyme stabilization and enhancement strategies to broaden their application in various industries. This study utilized a unified platform to stabilize and safeguard proteins in industrial settings. Despite the wide-ranging industrial applications of lipases, their utility in industrial processes is limited by their susceptibility to degradation under harsh environmental conditions. In our study, we used a dual-purpose strategy that involved both enzyme stabilization and the shielding of an organosilica protective layer. After expressing and purifying the recombinant lipase enzyme, we immobilized it onto silica nanoparticles and shielded it with an organosilica nanolayer to protect the enzyme. We meticulously examined the optimal thickness of the protective layer and its influence on enzyme stabilization against environmental stressors. Our research findings demonstrate that the immobilized enzyme exhibited a remarkable level of stability compared to its free enzyme when subjected to various factors, such as fluctuations in temperature and exposure to chemical agents. Furthermore, the immobilized samples displayed optimal activity across a broad range of temperatures, highlighting this approach's adaptability and efficacy. Notably, the organosilica layer significantly bolstered the reactivity recovery of denatured proteins with SDS and urea, highlighting the versatile applications of this method. These findings indicated that our present platform has great potential to improve the efficiency and stability of industrial enzymes against various environmental challenges.
Article Type:
Original Research |
Subject:
Nanotechnology Received: 2024/04/27 | Accepted: 2024/08/24