Immobilization of Amylase on Magnetic Nanoparticles

Topics: Enzyme, Magnetism, Magnetic field Pages: 15 (3925 words) Published: January 19, 2013

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.


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 itself be coated with common support materials such as dextran or agarose. Recently, a new method for the direct binding of proteins on magnetic nanoparticles via carbodiimide activation was proposed (Ren et al, 2011). Immobilization is one of the efficient methods to improve enzyme stability. There are various methods for immobilization of enzymes on many different types of supports. It can be a chemical method in which ionic or covalent bond formations occur between the enzyme and the carrier, or it can be a physical method, such as adsorption or entrapment of the enzyme in or on a solid support material. Magnetic nanoparticles as immobilization materials have advantage based on its property and size that make it desirable for using it in various applications (Mateo et al, 2007). Iron oxide nanoparticles, Fe3O4, are one of the widely used types of magnetic nanoparticles and have great potential for applications in biology and medicine due to their strong magnetic properties and low toxicity (Jalal et al, 2011)

Review of literature

I) Magnetic nanoparticles:

The historical development of nanoparticles starting with Paul Ehrlich and then first attempts by Ursula Scheffel and colleagues and the extensive work by the group of Professor Peter Speiser at the ETH Zürich in the late 1960s and early 1970s (Jörg Kreuter 2007). They are solid particles with a size from 10 to 100nm which can be manipulated using magnetic field. Such particles commonly consist of magnetic elements such as iron, nickel and cobalt.  They have been used in catalysis, biomedicine,  magnetic resonance imaging, magnetic particle imaging,  data storage , environmental remediation and optical filters (Gubin et al, 2005).

Magnetic nanoparticles as immobilization materials have the following advantages: simple and inexpensive production, can be released in controlled manner, stable magnetic properties of complexed nanoparticles and easy isolation steps in short time. Among these...
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