STABILITY AND ACTIVITY OF A PHENOL OXIDASE FROM THE LIGNINOLYTIC FUNGUS PLEUROTUS-OSTREATUS

Three different phenol oxidases produced by the basidiomycete fungus Pleurotus ostreatus have been isolated and their main structural, enzymatic and physicochemical properties characterized. Studies have focused on the most abundantly secreted of these proteins, a copper-enzyme specific towards ortho-diphenol substrates. This protein was purified to homogeneity and part of its primary structure determined by direct protein sequencing. The influence of pH, temperature and presence of water-soluble or water-insoluble organic solvents on the activity and stability of the enzyme were also investigated. These data can be used for applying bioreactors to problems of environmental concern such as waste-water treatment.