Open AccessPurification and characterization of peroxidases from the dye‐decolorizing fungus Bjerkandera adusta
Author(s) -
Heinfling Annette,
Martı́nez Marı́a Jesús,
Martı́nez Angel T,
Bergbauer Matthias,
Szewzyk Ulrich
Publication year - 1998
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1998.tb13125.x
Subject(s) - phanerochaete , peroxidase , lignin , manganese peroxidase , lignin peroxidase , biochemistry , chemistry , isoelectric point , isozyme , fungus , enzyme , organic chemistry , biology , botany
A peroxidase oxidizing Mn 2+ (MnP) is described for the first time in Bjerkandera adusta , a fungus efficiently degrading xenobiotic compounds. The MnP appeared as two isoenzymes, which were purified to homogeneity together with two lignin peroxidases (LiP). Their N‐terminal sequences were identical, but the MnP isoenzymes showed more basic isoelectric points and differences in amino acid composition and catalytic properties. The B. adusta LiP is similar to LiP from Phanerochaete chrysosporium . However, the interest of the MnP described here is related to its ability to catalyze Mn 2+ ‐mediated as well as Mn 2+ ‐independent reactions on aromatic compounds, which may be of use for applications in biotechnology and environmental technology.