Comparative study of ASNase Immobilization on Tannic Acid-Modified Magnetic Fe3O4/SBA-15 Nanoparticles to Enhance Stability and Reusability
In this work, L-asparaginase (ASNase) was immobilized on tannic acid (TA)-modified magnetic mesoporous particles. In brief, Fe3O4/SBA-15/TA magnetic particles were synthesized and fully characterized by using various methods as structural and morphological. The properties of free and immobilized enzyme were examined in terms of pH, temperature, thermal stability, storage stability and reusability. Moreover, the effects of metal ions, inhibitors and organic solvents were investigated on activity of the immobilized enzyme. As compared to the free enzyme, the immobilized enzyme possessed better tolerance to changes in ambient temperature and pH. Additionally, thermal incubation results showed that the free enzyme lost its activity while the immobilized enzyme exhibited the opposite behavior. Most strikingly, the immobilized ASNase exhibited a high degree of activity (70%) after being reused 16 times while also demonstrating 71% and 63% storage stability of the initial activity even after 28 days, at 4 oC and room temperature, respectively. Together with these results, ASNase was successfully immobilized upon Fe3O4/SBA-15/TA magnetic nanoparticles with improved stability properties. This support holds great potential and open up a novel perspective for its growing applications.