α-amylase was immobilized covalently on iron oxide magnetic nanoparticles. The synthesis of magnetic nanoparticles was done by the coprecipitation conventional method. The chemical composition and particle size of the synthesized particles was confirmed via X-ray diffraction. Tyrosine, Lucien and chitosan and glutaraldehyde were investigated to make a covalent binding between the iron oxide magnetic core and the immobilized enzyme. Immobilization using chitosan and glutaraldehyde show the best result. Finally the immobilization efficiency was tested by determination of protein concentration in a solution before and after mixing with the magnetic nanoparticles.
Introduction
In the last two decades, new terms with the prefix `nano' have rushed into the scientific vocabulary; nanoparticle, nanostructure, nanotechnology, nanomaterial, nanocluster, nanochemistry, nanocolloids, nanoreactor and so on. Nanoparticles, are defined as particulate dispersions with a size in the range of 10-100nm (Gubin et al, 2005). Magnetic nanoparticles have gained a remarkable interest in the last years both for basic research and applied studies. The use of magnetic nanostructures has been proven in biochemistry, biomedicine, and waste treatment among other fields. This broad range of applications is based on the fact that magnetic particles have very large magnetic moments, which allow them to be transported and driven by external magnetic fields. The magnetic nanostructures have also a great potential in biotechnological processes taking into account that they can be utilized as a carrier for enzymes during different biocatalytic transformations (Dussán et al, 2007). Different types of biomolecules such as proteins, enzymes, antibodies, and anticancer agents can be immobilized on these nanoparticles. Magnetic supports for immobilization purpose are either prepared by incorporating magnetic particles during the synthesis of the supporting polymer or magnetic particles