Notice of RetractionSequence analysis of manganese peroxidase in Phanerochaete sordida

Notice of Retraction

After careful and considered review of the content of this paper by a duly constituted expert committee, this paper has been found to be in violation of IEEE´s Publication Principles.

We hereby retract the content of this paper. Reasonable effort should be made to remove all past references to this paper.

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Manganese peroxidase(MnP) was the most common lignin-modifying peroxidase produced by almost all wood-colonizing basidiomycetes causing white-rot and various soil-colonizing litter-decomposing fungi. MnP could be applied in biotechnological applications, removing of hazardous wastes or in certain organic syntheses. In the present study, some characters of the amino acid sequence of P.sordida manganese peroxidase were predicted and analyzed with the tools of bioinformatics. These results showed that the protein was composed of 19 kinds of amino acid; the theoretical pI of manganese peroxidase was 4.46 and the theoretical molecular weight of manganese peroxidase was 39559.4 Da; total number of atoms was 5485; the extinction coefficient was 6125(280 nm).The N-terminal of the sequence considered was M (Met) and the estimated half-life was 30 hours. The instability index (II) was computed to be 42.17; Aliphatic index was 79.03. There were 8 glycosylation sites, a signal peptide. There were 18 glycosylation sites in P.sordida manganese peroxidase. It was a hydrolyze protein.