Applied Microbiology and Biotechnology

, Volume 39, Issue 4, pp 632–636

Stability and activity of a phenol oxidase from the ligninolytic fungus Pleurotus ostreatus

  • G. Palmeiri
  • P. Giardina
  • L. Marzullo
  • B. Desiderio
  • G. Nittii
  • R. Cannio
  • G. Sannia
Environmetal Biotechnology

DOI: 10.1007/BF00205066

Cite this article as:
Palmeiri, G., Giardina, P., Marzullo, L. et al. Appl Microbiol Biotechnol (1993) 39: 632. doi:10.1007/BF00205066

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 forcaused on the most abundantly secreated of these proteins, a copper-e nzyme specific towards ortho-diphenol substrates. This protein was purified to homogeneity and part of its primary structure determined by direct protein sequencing. The ingluence of pH, temperature and presence of water-soluible or water-insoluble organic solvents on the activity and stability of the enzyme were also investigated. These data can be used for applying bioarectors to problems of environmental concern such as waste-water treatment

Copyright information

© Springer-Verlag 1993

Authors and Affiliations

  • G. Palmeiri
    • 1
  • P. Giardina
    • 1
  • L. Marzullo
    • 1
  • B. Desiderio
    • 1
  • G. Nittii
    • 2
  • R. Cannio
    • 1
  • G. Sannia
    • 1
  1. 1.Dipartimento di Chimica Organica e BiologicUniversitá du NaploiNaplesItaly
  2. 2.Farmitalia Carlo ErbaCentro Ricerche BiotecnlogieNervianoItaly