DocumentCode
527214
Title
Notice of Retraction
Analysis of lignin peroxidase in Phanerochaete chrysosporium
Author
Li he ; Zhou Guoying ; Guo Liang ; Liu Junang
Author_Institution
Biotechnol. Core Facilities, Central South Univ. of Forestry & Technol., Changsha, China
Volume
1
fYear
2010
fDate
17-18 July 2010
Firstpage
21
Lastpage
23
Abstract
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.
The presenting author of this paper has the option to appeal this decision by contacting TPII@ieee.org.
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.
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.
The presenting author of this paper has the option to appeal this decision by contacting TPII@ieee.org.
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.
Keywords
biochemistry; bioinformatics; enzymes; microorganisms; molecular biophysics; Phanerochaete chrysosporium; amino acid; amino acid sequence; basidiomycetes; bioinformatics; extracellular enzymes; glycosylation; heme binding site; lignin peroxidase; manganese binding site; protein; substrate-binding site; substrate/inhibitor binding site; Conferences; Decision support systems; Mercury (metals); P. chrysosporium; lignin degradation; lignin peroxidase;
fLanguage
English
Publisher
ieee
Conference_Titel
Environmental Science and Information Application Technology (ESIAT), 2010 International Conference on
Conference_Location
Wuhan
Print_ISBN
978-1-4244-7387-8
Type
conf
DOI
10.1109/ESIAT.2010.5568484
Filename
5568484
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