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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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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
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description 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.
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source Springer Online Journals Archive Complete
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
title Stability and activity of a phenol oxidase from the ligninolytic fungus Pleurotus ostreatus
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