Immobilization of Lactoperoxidase on Zno Nanoparticles With Improved Stability Publisher Pubmed



Movahedi M¹ ; Samsam Shariat SZA² ; Nazem H¹ ; Movahedi M¹ Show Affiliations
Source: Biotechnology Letters Published:2020

Abstract

Objectives: The study aimed to develop a facile and effectual method to enhance the stability of lactoperoxidase (LPO) by immobilizing it on ZnO Nanoparticles (ZnO NPs). Results: The successful immobilization of LPO on ZnO NPs was confirmed by using Fourier transform infrared spectroscopy (FT-IR) and field emission scanning electron microscopy (FE-SEM). The Km values of free LPO and LPO immobilized on ZnO were 53.19, 89.28 mM and their Vmax values were 0.629, 0.46 µmol/mL min, respectively. The overall results showed that the stability of the immobilized LPO was significantly improved compared to free LPO. The LPO immobilized on ZnO (LPO–ZnO) retained 18% of the initial activity within 30 days at 25 °C whereas the free enzyme lost its activity after 7 days at the same temperature. Moreover, evaluation of the thermal stability of LPO at 75 °C determined the conservation of 12% of the initial activity of LPO in the LPO–ZnO sample after 60 min whereas the free enzyme lost its activity after 5 min. Conclusions: According to the present results, ZnO nanoparticles are suitable for the immobilization of LPO. © 2020, Springer Nature B.V.