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Stability and activity of a phenol oxidase from the ligninolytic fungus Pleurotus ostreatus.
Dipartimento di Chimica Organica e Biologica, Università di Napoli, Italy.
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.
PMID: 7763931 [PubMed - indexed for MEDLINE]
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Cited by 6 PubMed Central articles
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Importance of Laccase in Vegetative Growth of Pleurotus florida.
Das N, Sengupta S, Mukherjee M.
Appl Environ Microbiol. 1997 Oct; 63(10):4120-4122.
[Appl Environ Microbiol. 1997]
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Induction, isolation, and characterization of two laccases from the white rot basidiomycete Coriolopsis rigida.
Saparrat MC, Guillén F, Arambarri AM, Martínez AT, Martínez MJ.
Appl Environ Microbiol. 2002 Apr; 68(4):1534-40.
[Appl Environ Microbiol. 2002]
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Copper induction of laccase isoenzymes in the ligninolytic fungus Pleurotus ostreatus.
Palmieri G, Giardina P, Bianco C, Fontanella B, Sannia G.
Appl Environ Microbiol. 2000 Mar; 66(3):920-4.
[Appl Environ Microbiol. 2000]
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