Mechanism of Immobilization of Enzymes by Radiation-Induced Polymerization of Glass-Forming Monomers

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Abstract
Immobilization of enzymes by radiation-induced polymerization was studied at low temperatures by use of various hydrophilic and hydrophobic glass-forming monomers such as hydroxyalkyl methacrylate and poly(ethylene glycol diacrylate). Activity yield of the immobilized enzyme [Aspergillus niger glucoamylase] depends on the monomer concentration in polymerization. In the immobilized enzymes with strongly hydrophobic matrices, the activity shows a maximum at an optimum monomer concentration in a certain stage of repeated usage for the enzyme reaction. The decrease of activity with repeated use is very little in strongly hydrophobic systems, particularly in diethylene glycol diacrylate polymer matrices. The hydrophobic polymer-enzyme composite has the microsphere form. In the present method a model scheme for immobilizaton mechanism is proposed which is compared with that formed in the polymerization of a nonglass-forming monomer system and also by the solution polymerization at higher temperatures.