ABSTRACT
Glutamate decarboxylase from Escherichia coli was immobilized on inorganic macroporous carriers by the glutaraldehyde, carbodiimide and bromacetyl methods, on silicagel coated with a layer of a glutaraldehyde and m-phenylene diamine copolymer, and by polyacrylamide gel incorporation. The efficiency of the above methods of immobilization was evaluated. The bromacetyl method was found to be the most efficient. The dependence of activity of soluble and immobilized Glu-decarboxylase upon pH, temperature, substrate concentration, and stability was established. The differences in the properties of soluble and immobilized Glu-decarboxylase were due to the substrate diffusion in pores of the carrier. The immobilized Glu-decarboxylase obtained showed high activity and stability.
