Abstract
The partially purified bromoperoxidase of Corallina pilulifera (Corallinaceae, Rhodophyta) was immobilized on the following matrices: Cellulofine (covalent binding), DEAE-Cellulofine (ionic binding), or alkylsilane treated Controlled-Pore Glass (physical adsorption), and entrapped in the soft gels using photo-crosslinkable resin prepolymer (ENT-2000), polyurethane prepolymer (PU-6), or κ-carrageenan. These different forms of immobilized bromoperoxidase were tested for the bromination reactions of monochlorodimedone and uracil. The immobilization techniques using DEAE-Cellulofine and ENT-2000 were found to be suitable for the bromoperoxidase reaction. The immobilized enzyme on DEAE-Cellulofine showed the highest activity and a half-life of 45 days when it was used for the conversion of uracil to 5-bromouracil.
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