• Microbiology and Biotechnology Letters
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• v.24 no.5
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• pp.585-590
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• 1996

Peroxidase was purified to homogeneity from cell free extract of Flavobacterium meningosepticum. The molecular weight of the enzyme estimated by gel filtration column chromatography was 220, 000. A identical subunit (54, 000) was detected on SDS-PAGE of the enzyme. From these results, the enzyme was supposed to have four identical subunits. On the basis of the visible absorption spectra of the purified enzyme, the enzyme was a typical hemoprotein. The isoelectric point of the enzyme was 4.1. On using N-ethyl-N-(2-hydroxy-3-sulfopropyl)-m- toluidine (Toos) as a hydrogen donor, the enzyme showed optimum activity at the pH 5.5 and 50$\circ$C. The enzyme activity was inhibited by carbonyl reagent and Hg$^{2+}$ .