Please use this identifier to cite or link to this item: http://hdl.handle.net/1822/58184

TitlePEGylation greatly enhances laccase polymerase activity
Author(s)Su, Jing
Noro, Jennifer Martins
Loureiro, Ana
Martins, Madalena
Azoia, Nuno G.
Fu, Jiajia
Wang, Qiang
Silva, Carla
Cavaco-Paulo, Artur
Keywordslaccase
polyethylene glycol
polymerization
template
alcohols
enzyme catalysis
molecular dynamics
template synthesis
Issue date23-Oct-2017
PublisherWiley-Blackwell
JournalChemCatChem
CitationJing Su; Jennifer Noro; Loureiro, Ana; Martins, Madalena; Fu, Jiajia; Silva, Carla; Cavaco-Paulo, Artur, PEGylation greatly enhances laccase polymerase activity. ChemCatChem, 9(20), 3888-3894, 2017
Abstract(s)Laccase catalyzes the oxidation and polymerization of phenolic compounds in the presence of oxygen. Herein, we report for the first time that a previous pegylation of laccase enhances the polymerase activity by 3-fold comparing with the native enzyme, as confirmed by UV-Vis spectroscopy. The polymerization of catechol increased only 1.5-fold when polyethyleneglycol (PEG) was added to the medium reaction. Molecular dynamic simulations suggest the formation of a miscible complex of polycatechol and PEG, which is responsible to push the reaction forward. In a negative control experiment set, all catalysts were entrapped inside acrylamide gels and here the native laccase showed a relatively higher activity. These results suggest that the mobility of PEG is a key feature for the enhancement of the reaction.
TypeArticle
URIhttp://hdl.handle.net/1822/58184
DOI10.1002/cctc.201700849
ISSN1867-3880
e-ISSN1867-3899
Publisher versionhttp://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1867-3899
Peer-Reviewedyes
AccessOpen access
Appears in Collections:CEB - Publicações em Revistas/Séries Internacionais / Publications in International Journals/Series

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