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Please use this identifier to cite or link to this item: http://hdl.handle.net/2067/1411

Title: Kinetic and redox properties of MnP II, a major manganese peroxidase isoenzyme from Panus tigrinus CBS 577.79.
Authors: Petruccioli, Maurizio
Frascono, Marco
Quaratino, Daniele
Covino, Stefano
Favero, Gabriele
Mazzei, Franco
Federici, Federico
D'Annibale, Alessandro
Keywords: Manganese peroxidase
Purification
Panus tigrinus
Phenols
Direct electron transfer
Issue Date: 2009
Publisher: Springer
Citation: Petruccioli, M. et al. 2009. Kinetic and redox properties of MnP II, a major manganese peroxidase isoenzyme from Panus tigrinus CBS 577.79. "Journal of Biological Inorganic Chemistry" 14(8): 1153-1163
Abstract: A manganese peroxidase (MnP) isoenzyme from Panus tigrinus CBS 577.79 was produced in a benchtop stirred-tank reactor and purified to apparent homogeneity. The purification scheme involving ultrafiltration, affinity chromatography on concanavalin–A Sepharose, and gel filtration led to a purified MnP, termed ‘‘MnP II,’’ with a specific activity of 288 IU mg-1 protein and a final yield of 22%. The enzyme turned out to be a monomeric protein with molecular mass of 50.5 kDa, pI of 4.07, and an exte
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Description: L'articolo è disponibile sul sito dell'editore: http://www.springerlink.com
DOI: 10.1007/s00775-009-0559-8
URI: http://hdl.handle.net/2067/1411
ISSN: 0949-8257
Appears in Collections:DABAC - Archivio della produzione scientifica

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