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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.
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Hirai et al. (2005) studied this question.
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