Abstract
Microperoxidase-11 (MP-11) derived from horse heart cytochrome c was utilized as a peroxidative catalyst. Mn II-oxidation activity of MP-11 was demonstrated for the first time. Although the activity of MP-11 was low compared to manganese peroxidase (MnP) from Phanerochaete chrysosporium in aqueous system, it can be utilized in water-miscible organic solvents if at least 5% water exists. Mn II-oxidation by MP-11 was optimized at higher pH compared to MnP, probably because of the lack of distal His acting as a proton acceptor during the catalytic cycle. Finally, the depolymerization of lignin was also achieved in 90% methanol using MP-11 in the presence of H 2O 2 and Mn II.
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