Purification and characterization of a novel lignin peroxidase from white-rot fungus Phanerochaete sordida YK-624.
We characterized kinetics and substrate oxidation of a novel lignin peroxidase (YK-LiP) isolated from white-rot fungus Phanerochaete sordida YK-624. YK-LiP enzyme was identified and purified to homogeneity by anion-exchange chromatography and gel permeation chromatography. The molecular mass of YK-LiP was approximately 50 kDa, and the absorption spectrum of YK-LiP was almost the same as that of the LiP (Pc-LiP) from Phanerochaete chrysosporium. Steady-state kinetics of veratryl alcohol oxidation by YK-LiP (unlike that by Pc-LiP) revealed a bi-reactant sequential mechanism, although reactivity of YK-LiP to various monomeric substituted aromatic compounds was similar to that of Pc-LiP. Degradation of dimeric lignin model compounds was more effective by YK-LiP than by Pc-LiP, and the oxidation rate of sinapyl alcohol oligomer by YK-LiP was much faster than that by Pc-LiP.
Sugiura
Mutsumi
M
Department of Forest Resources Science, Faculty of Agriculture, Shizuoka University, Shizuoka 422-8529, Japan.
Hirai
Hirofumi
H
Nishida
Tomoaki
T
D000171:Acrolein / Q000031:analogs & derivatives* / Q000378:metabolism; D000438:Alcohols / Q000378:metabolism; D002384:Catalysis; D019281:Dimerization; D005656:Fungal Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D007700:Kinetics; D008970:Molecular Weight; D010084:Oxidation-Reduction; D010544:Peroxidases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D020075:Phanerochaete / Q000201:enzymology*
D000438:Alcohols; D005656:Fungal Proteins; C075386:sinapaldehyde; D000171:Acrolein; D010544:Peroxidases; C042858:lignin peroxidase