Open AccessCharacteristics of novel lignin peroxidases produced by white‐rot fungus Phanerochaete sordida YK‐624
Author(s) -
Hirai Hirofumi,
Sugiura Mutsumi,
Kawai Shingo,
Nishida Tomoaki
Publication year - 2005
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 - 10.1016/j.femsle.2005.03.032
Subject(s) - phanerochaete , hydrogen peroxide , chemistry , kinetics , lignin , peroxidase , biochemistry , enzyme , organic chemistry , physics , quantum mechanics
We characterized a lignin peroxidase (YK‐LiP2) isolated from shaking culture inoculated with the white‐rot fungus Phanerochaete sordida YK‐624. The YK‐LiP2 enzyme was identified and purified to homogeneity by anion‐exchange chromatography and gel permeation chromatography. The molecular weight of YK‐LiP2 was approximately 45 kDa, and its absorption spectrum was almost the same as that of the LiP (Pc‐LiP) from P. chrysosporium . Steady‐state kinetics of veratryl alcohol (VA) oxidation by YK‐LiP2 revealed an ordered bi‐bi ping‐pong mechanism, although the Pc‐LiP oxidation of ferrocytochrome c obeys peroxidase ping‐pong kinetics rather than ordered bi‐bi ping‐pong kinetics. Degradation of dimeric lignin model compounds by YK‐LiP2 was more effective than that by Pc‐LiP. Moreover, YK‐LiP2 and YK‐LiP1, which was previously isolated from static culture inoculated with P . sordida YK‐624, oxidized VA under a higher concentration of hydrogen peroxide (>2.5 mM) although Pc‐LiP could not oxidize VA in the presence of 2.5 mM hydrogen peroxide.