A novel matrix for the immobilization of acetylcholinesterase

Int J Biol Macromol. 2005 Nov 15;37(3):148-53; author reply 156-60. doi: 10.1016/j.ijbiomac.2005.10.003. Epub 2005 Nov 7.

Abstract

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.

MeSH terms

  • Acetylcholinesterase / chemistry*
  • Alginates / chemistry
  • Animals
  • Biocompatible Materials / chemistry*
  • Carrageenan / chemistry
  • Electrophorus
  • Enzyme Stability
  • Enzymes, Immobilized / chemistry*
  • Glucuronic Acid / chemistry
  • Hexuronic Acids / chemistry
  • Hot Temperature
  • Hydrogen-Ion Concentration
  • Kinetics
  • Polymers / chemistry
  • Protein Denaturation
  • Specimen Handling
  • Temperature
  • Time Factors

Substances

  • Alginates
  • Biocompatible Materials
  • Enzymes, Immobilized
  • Hexuronic Acids
  • Polymers
  • Glucuronic Acid
  • Carrageenan
  • Acetylcholinesterase