IMMOBILIZATION OF LACCASE FROM PHLEBIA-RADIATA ON CONTROLLED POROSITYGLASS

Laccase from the white-rot fungus Phlebia radiata was immobilized on g lass beads which were activated by gamma-aminopropyl-triethoxysilane. 98% of the protein and 96% of the laccase activity were coupled to the support. The final preparation contained ca. 1 mg of protein per gram of glass beads. The activity of the immobilized enzyme retained after two weeks preservation at + 4 degrees C was 100% and at + 25 degrees C over 90%. The activity in the presence of organic solvents was rathe r similar irrespective of the form of the enzyme, free or bound. Howev er, the catalytic activity of the immobilized laccase was less vulnera ble against inhibitors such as Cu-chelators and 2,6-dimethoxy-1,4-benz oquinone.