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Appl Environ Microbiol, May 1998, p. 1601-1606, Vol. 64, No. 5
Department of Biotechnology, University of
Kaiserslautern, D-67663 Kaiserslautern,
Germany,1 and
Novo Nordisk A/S,
DK-2880 Bagsvaerd, Denmark2
Received 27 August 1997/Accepted 21 January 1998
Panaeolus sphinctrinus, Panaeolus
papilionaceus, and Coprinus friesii are described as
producers of ligninolytic enzymes. P. papilionaceus and
P. sphinctrinus both produced a laccase. In addition,
P. sphinctrinus produced a manganese peroxidase. C. friesii secreted a laccase and two peroxidases similar to the peroxidase of Coprinus cinereus. The purified laccases and
peroxidases were characterized by broad substrate specificities,
significant enzyme activities at alkaline pH values, and remarkably
high pH optima. The two peroxidases of C. friesii remained
active at pH 7.0 and 60°C for up to 60 min of incubation. The
peroxidases were inhibited by sodium azide and ethylene
glycol-bis(
0099-2240/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Characterization of Laccases and Peroxidases
from Wood-Rotting Fungi (Family Coprinaceae)
-aminoethyl ether)-N,N,N',N'-tetraacetic
acid (EGTA), whereas the laccases were inhibited by sodium azide and
N,N-diethyldithiocarbamic acid. As determined
by native polyacrylamide gel electrophoresis and isoelectric focusing,
all three fungi produced laccase isoenzymes.
*
Corresponding author. Mailing address: Department of
Biotechnology, University of Kaiserslautern, Paul-Ehrlich-Str. 23, D-67663 Kaiserslautern, Germany. Phone: (01149) 631/205-2697. Fax:
(01149) 631/205-2999. E-mail: anke{at}rhrk.uni-kl.de.
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