An improved method for the purification of lignin peroxidases from Phanerochaete chrysosporium INA-12: properties of two major isoforms.
1. Phanerochaete chrysosporium INA-12 secretes several lignin peroxidase isoenzymes. This paper reports an improved procedure for the purification of the different isoforms compared to those previously described. 2. Lignin peroxidases are first concentrated and prefractionated on fast-flow ion-exchangers which avoid concentration by ultrafiltration and dialysis. 3. Further purification is achieved by hydrophobic interaction chromatography and anion-exchange FPLC. 4. Two major forms were purified to homogeneity. Kinetic measurements and protein characterization (isoelectric points, phosphate content) suggest that they are similar to those produced by P. chrysosporium BKM strain.
Asther
M
M
Laboratoire de Chimie Biologique, Institut National Agronomique, Centre de Biotechnologie Agro-Industrielle, Thiverval-Grignon, France.
Vilter
H
H
Kurek
B
B
Meunier
J C
JC
D001487:Basidiomycota / Q000201:enzymology*; D002852:Chromatography, Ion Exchange; D007525:Isoelectric Focusing; D007527:Isoenzymes / Q000302:isolation & purification* / Q000378:metabolism; D007700:Kinetics; D010544:Peroxidases / Q000302:isolation & purification* / Q000378:metabolism; D017385:Sequence Homology; D013057:Spectrum Analysis
D007527:Isoenzymes; D010544:Peroxidases; C042858:lignin peroxidase