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 ort...

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Bibliographic Details
Published in:Applied microbiology and biotechnology 1993-07, Vol.39 (4-5), p.632-636
Main Authors: PALMIERI, G, GIARDINA, P, MARZULLO, L, DESIDERIO, B, NITTI, G, CANNIO, R, SANNIA, G
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Biological and medical sciences
Biology of microorganisms of confirmed or potential industrial interest
Biotechnology
Enzyme Stability
Fundamental and applied biological sciences. Psychology
Hydrogen-Ion Concentration
Kinetics
Miscellaneous
Mission oriented research
Molecular Sequence Data
Monophenol Monooxygenase - genetics
Monophenol Monooxygenase - isolation & purification
Monophenol Monooxygenase - metabolism
Pleurotus ostreatus
Polyporaceae - enzymology
Polyporaceae - genetics
Temperature
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Summary: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.
ISSN:0175-7598
1432-0614
DOI:10.1007/bf00205066