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dc.contributor.authorLundell, Taina
dc.contributor.authorBentley, Elodie
dc.contributor.authorHilden, Kristiina
dc.contributor.authorRytioja, Johanna
dc.contributor.authorKuuskeri, Jaana
dc.contributor.authorUfot, Usenobong F.
dc.contributor.authorNousiainen, Paula
dc.contributor.authorHofrichter, Martin
dc.contributor.authorWahlsten, Matti
dc.contributor.authorDoyle, Wendy
dc.contributor.authorSmith, Andrew T.
dc.date.accessioned2017-05-22T02:50:58Z
dc.date.available2017-05-22T02:50:58Z
dc.date.issued2017
dc.identifier.issn2211-551X
dc.identifier.doi10.2174/2211550105666160520120101
dc.identifier.urihttp://hdl.handle.net/10072/337474
dc.description.abstractBackground: Manganese peroxidases (MnP) and lignin peroxidases (LiP) are haem-including fungal secreted class-II peroxidases, which are interesting oxidoreductases in protein engineering aimed at designing of biocatalysts for lignin and lignocellulose conversion, dye compound degradation, activation of aromatic compounds, and biofuel production. Objective. Recombinant short-type MnP (Pr-MnP3) of the white rot fungus Phlebia radiata, and its manganese- binding site (E40, E44, D186) directed variants were produced and characterized. To allow catalytic applications, enzymatic bleaching of Reactive Blue 5 and conversion of lignin-like compounds by engineered class- II peroxidases were explored. Method: Pr-MnP3 and its variants were expressed in Escherichia coli. The resultant body proteins were lysed, purified and refolded into haem-including enzymes in 6-7% protein recovery, and examined spectroscopically and kinetically. Results: Successful production of active enzymes was attained, with spectral characteristics of high-spin class-II peroxidases. Recombinant Pr-MnP3 demonstrated high affinity to Mn2+, which was noticeably affected by single (D186H/N) and double (E40H+E44H) mutations. Without addition of Mn2+, Pr- MnP3 was able to oxidize ABTS and decolorize Reactive Blue 5. Pc-LiPH8, its Trp-radical site variants, and engineered CiP-LiP demonstrated conversion of veratryl alcohol and dimeric non-phenolic lignin-model compounds (arylglycerol-β-aryl ethers) with production of veratraldehyde, which is evidence for cation radical formation with subsequent Cα-Cβ cleavage. Pc-LiPH8 and CiP variants were able to effectively oxidize and convert the phenolic dimer (guaiacylglycerol-β-guaiacyl ether). Conclusion: Our results demonstrate suitability of engineered MnP and LiP peroxidases for dyedecolorizing, and efficiency of LiP and its variants for activation and degradation of phenolic and nonphenolic lignin-like aryl ether-linked compounds.
dc.description.peerreviewedYes
dc.languageEnglish
dc.language.isoeng
dc.publisherBentham Science
dc.relation.ispartofpagefrom116
dc.relation.ispartofpageto127
dc.relation.ispartofissue2
dc.relation.ispartofjournalCurrent Biotechnology
dc.relation.ispartofvolume6
dc.subject.fieldofresearchMedicinal and Biomolecular Chemistry not elsewhere classified
dc.subject.fieldofresearchBiological Sciences
dc.subject.fieldofresearchTechnology
dc.subject.fieldofresearchcode030499
dc.subject.fieldofresearchcode06
dc.subject.fieldofresearchcode10
dc.titleEngineering Towards Catalytic Use of Fungal Class-II Peroxidases for Dye-Decolorizing and Conversion of Lignin Model Compounds
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.hasfulltextNo Full Text
gro.griffith.authorSmith, Andrew T.


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