title: Stability and activity of a phenol oxidase from the ligninolytic fungus Pleurotus ostreatus.
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 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.
authors.affiliation: Dipartimento di Chimica Organica e Biologica, Università di Napoli, Italy.
authors.forename: G
authors.initials: G
authors.lastname: Palmieri
authors.forename: P
authors.initials: P
authors.lastname: Giardina
authors.forename: L
authors.initials: L
authors.lastname: Marzullo
authors.forename: B
authors.initials: B
authors.lastname: Desiderio
authors.forename: G
authors.initials: G
authors.lastname: Nitti
authors.forename: R
authors.initials: R
authors.lastname: Cannio
authors.forename: G
authors.initials: G
authors.lastname: Sannia
mesh_terms: D000595:Amino Acid Sequence; D001709:Biotechnology; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008969:Molecular Sequence Data; D014442:Monophenol Monooxygenase / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D011124:Polyporaceae / Q000201:enzymology* / Q000235:genetics; D013696:Temperature
chemical_list: D014442:Monophenol Monooxygenase