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 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.
Palmieri
G
G
Dipartimento di Chimica Organica e Biologica, Università di Napoli, Italy.
Giardina
P
P
Marzullo
L
L
Desiderio
B
B
Nitti
G
G
Cannio
R
R
Sannia
G
G
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
D014442:Monophenol Monooxygenase