Immobilization of chitosanases onto magnetic nanoparticles to enhance enzyme performance

Abstract

In this study, chitosanase cloning from Streptomyces albolongus was fermented and purified by a Ni-NTA column. Fe3O4-SiO2 magnetite nanoparticles (MNPs) were synthesized by the co-precipitation method coating with silica via a sol-gel reaction and were then amino functioned by treating with 3-aminopropyltriethoxysilane. Chitosanases were immobilized onto the surface of MNPs by covalent bonding (MNPs@chitosanase). Transmission electron microscopy (TEM), Fourier transform infrared spectrometer (FT–IR), and magnetic measurements were used to illustrate the MNPs and immobilized chitosanase. The optimal conditions of immobilization were studied. The thermal, pH, and stabilities of immobilized chitosanase were tested and the results showed that the stabilities were significantly enhanced compared with free chitosanase. After being recycled 10 times, the residual activity of the immobilized chitosanase was 43.7% of the initial activity.