Notice of RetractionAnalysis of lignin peroxidase in Phanerochaete chrysosporium

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.

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Basidiomycetes white-rot fungi which can secrete several extracellular enzymes, in which lignin peroxidase plays a dominant role in lignin degradation. In the present study, some characters of the amino acid sequence of P. chrysosporium lignin peroxidase were predicted and analysed with the tools of bioinformatics. These results showed that the protein was composed of 19 kinds of amino acid; the theoretical pI of lignin peroxidase was 4.71 and the theoretical molecular weight of lignin peroxidase was 39329.4 Da; the total number of atoms was 5141. It was a hydrolyze and stable protein. There were 8 glhemeycosylation sites, a signal peptide and substrate/inhibitor binding site, heme binding site, manganese binding site and substrate-binding site in this lignin peroxidase.