Imobilization of enzymes in clinical diagnosis using nanotechnology Research Proposal

Imobilization of enzymes in clinical diagnosis using nanotechnology - Research Proposal Example Immobilization can be done either physically or chemically. Physical immobilization involves weak interactions between the existing enzyme and the support whereas chemical immobilization includes formation of covalent bonds with the enzyme. Examples of physical methods of immobilization include adsorbing the enzyme in a water-soluble matrix, microencapsulating the enzyme with a solid membrane. This article looks into an overview of how immobilization was applied in the clinical diagnosis of the above mentioned diseases and new techniques that can be applied in the diagnosis process that reflect on advancements in the preceding methods. Nanotechnology has been applied in immobilization of enzymes via peptide mapping which is achieved through proteolytic digestion with enzymes such as trypsin. This process has been a possibility due to the quick and efficiency in the identification and digestion of unknown protein. Peptide mapping is done with the aid of enzymatic cleavage of the protein. Identification of the peptide fragments is done using either matrix-assisted laser desorption/ionization mass spectrometry or electrospray ionization mass spectrometry and in each case of identification separation of the mixture improves the coverage of the sequence. Peptide mapping is disadvantageous from the manual way of manipulation of samples besides lengthened enzymatic activities during proteolytic digestion. An antibody having a high affinity for a the substance under test is attached to a solid surface for example the human chorionic gonadotropin and a mixture of the purified human chorionic gonadotropin and a fluid test sample are passed through a test system and observations made on the results. Absence of human chorionic gonadotropin in the sample tested in deduced from the binding of the linked enzyme and the less the human