Abstract
Three different phenol oxidases produced by the basidiomycete fungus Pleurotus ostreatus have been isolated and their main structural, enzymatic and physico-chemical properties characterized. Studies have forcaused on the most abundantly secreated of these proteins, a copper-e nzyme specific towards ortho-diphenol substrates. This protein was purified to homogeneity and part of its primary structure determined by direct protein sequencing. The ingluence of pH, temperature and presence of water-soluible or water-insoluble organic solvents on the activity and stability of the enzyme were also investigated. These data can be used for applying bioarectors to problems of environmental concern such as waste-water treatment
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Palmeiri, G., Giardina, P., Marzullo, L. et al. Stability and activity of a phenol oxidase from the ligninolytic fungus Pleurotus ostreatus . Appl Microbiol Biotechnol 39, 632–636 (1993). https://doi.org/10.1007/BF00205066
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DOI: https://doi.org/10.1007/BF00205066