Enzyme immobilization by radiation-induced polymerization of hydrophobic glass-forming monomers at low temperatures.
Enzyme immobilization was studied by means of radiation-induced polymerization of hydrophobic glass-forming monomers at low temperatures. The polymerized hydrophobic composite was generally obtained in microspheric form. Enzymatic activity showed little decrease with repeated use in these systems. The particle size of the microsphere increased with increasing monomer concentration, and activity yield had a maximum at an optimum monomer concentration. Immobilization by copolymerization of hydrophilic and hydrophobic comonomers was also investigated and a maximum activity yield was found at a certain monomer concentration. A model scheme for immobilization at low temperatures was proposed and discussed.
D002238:Carbohydrate Epimerases / Q000378:metabolism / Q000528:radiation effects; D003080:Cold Temperature; D004800:Enzymes, Immobilized / Q000528:radiation effects*; D005898:Glass / Q000528:radiation effects*; D005947:Glucose; D008689:Methacrylates / Q000528:radiation effects; D010316:Particle Size; D011108:Polymers; D014568:Urokinase-Type Plasminogen Activator / Q000528:radiation effects; D014867:Water
D004800:Enzymes, Immobilized; D008689:Methacrylates; D011108:Polymers; D014867:Water; D014568:Urokinase-Type Plasminogen Activator; D002238:Carbohydrate Epimerases; D005947:Glucose