Author(s): Wariishi H, Kabuto M, Mikuni J, Oyadomari M, Tanaka H
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Abstract Microperoxidase-11 (MP-11), a heme-containing undecapeptide, derived from horse heart cytochrome c was utilized as a peroxidative catalyst. Catalytic characteristics of MP-11 in hydrophilic organic media were studied using 2,6-dimethoxyphenol as a reducing substrate in a series of organic solvents at various concentrations, indicating that MP-11 was active in water-miscible organic solvents but at least 5\% water was compulsory for the catalytic action. Thus, MP-11 was not active in hydrophobic solvents. The pH of the water portion in the media affected the reaction rate. The optimal pH was found to be 9, where a release of protons from either an oxidizing or reducing substrate to the media was facilitated. The decolorization of water-insoluble synthetic dyes by MP-11 in 90\% methanol was attempted. MP-11 showed effective decolorization activities against either azo or anthraquinone dyes. The degradation pathway for Solvent Orange 7 was investigated in detail, showing that MP-11 catalyzed the oxidative cleavage of the azo linkage to generate 1,2-naphthoquinone and 2,4-dimethylphenol as key intermediates.
This article was published in Biotechnol Prog
and referenced in Journal of Bioremediation & Biodegradation