title: A new method for immobilization of acetylcholinesterase.
abstract: A new method for immobilization of acetylcholinesterase (AChE) to alginate gel beads by activating the carbonyl groups of alginate using carbodiimide coupling agent has been successfully developed. Maximum reaction rate (V (max)) and Michaelis-Menten constant (K (m)) were determined for the free and binary immobilized enzyme. The effects of pH, temperature, storage stability, reuse number and thermal stability on the free and immobilized AChE were also investigated. For the free and binary immobilized enzyme on the Ca-alginate gel beads, optimum pH values were found to be 7 and 8, respectively. Optimum temperatures for the free and immobilized enzyme were observed to be 30 and 35 degrees C, respectively. Upon 60 days of storage the preserved activity of free and immobilized enzyme were found as 4 and 68%, respectively. In addition, reuse number, and thermal stability of the free AChE were increased by as a result of binary immobilization.
authors.affiliation: Department of Chemistry, Faculty of Art and Science, Gazi University, Teknikokullar, Ankara, Turkey.
authors.forename: Hayrettin
authors.initials: H
authors.lastname: Tümtürk
authors.forename: Ferat
authors.initials: F
authors.lastname: Sahin
authors.forename: Gökhan
authors.initials: G
authors.lastname: Demirel
mesh_terms: D000110:Acetylcholinesterase / Q000737:chemistry*; D000464:Alginates / Q000737:chemistry*; D015374:Biosensing Techniques / Q000379:methods*; D020099:Coated Materials, Biocompatible / Q000737:chemistry*; D004789:Enzyme Activation; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000737:chemistry; D020723:Glucuronic Acid / Q000737:chemistry; D006603:Hexuronic Acids / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D008422:Materials Testing; D008863:Microspheres; D013696:Temperature
chemical_list: D000464:Alginates; D020099:Coated Materials, Biocompatible; D004800:Enzymes, Immobilized; D006603:Hexuronic Acids; D020723:Glucuronic Acid; D000110:Acetylcholinesterase