A novel matrix for the immobilization of acetylcholinesterase.
In this study, a new matrix for immobilization of acetylcholinesterase was investigated by using alginate and kappa-carrageenan. The effects of pH, temperature, storage and thermal stability on the free and immobilized acetylcholinesterase activity were examined. Maximum reaction rate (V(max)) and Michaelis-Menten constant (K(m)) was also investigated for free and immobilized enzymes. For free and immobilized enzymes into Ca-alginate and alginate/kappa-carrageenan polymer blends, optimum pH and temperature was found to be 7 and 30 degrees C, respectively. For free enzyme, maximum reaction rate (V(max)) and Michaelis-Menten constant (K(m)) values were found to be 6.35 mM and 50 mM min(-1), respectively, the same values for immobilized enzymes were determined as 8.68, 12.7 mM and 39.7, 52.9 mM min(-1), respectively. Storage and thermal stability of acetylcholinesterase was increased by as a result of immobilization.
Sahin
Ferat
F
Department of Chemistry, Faculty of Art and Science, Gazi University, Teknikokullar, 06500 Ankara, Turkey.
Demirel
Gökhan
G
Tümtürk
Hayrettin
H
D000110:Acetylcholinesterase / Q000737:chemistry*; D000464:Alginates / Q000737:chemistry; D000818:Animals; D001672:Biocompatible Materials / Q000737:chemistry*; D002351:Carrageenan / Q000737:chemistry; D004593:Electrophorus; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000737:chemistry*; D020723:Glucuronic Acid / Q000737:chemistry; D006603:Hexuronic Acids / Q000737:chemistry; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D011108:Polymers / Q000737:chemistry; D011489:Protein Denaturation; D013048:Specimen Handling; D013696:Temperature; D013997:Time Factors
D000464:Alginates; D001672:Biocompatible Materials; D004800:Enzymes, Immobilized; D006603:Hexuronic Acids; D011108:Polymers; D020723:Glucuronic Acid; D002351:Carrageenan; D000110:Acetylcholinesterase