Please use this identifier to cite or link to this item:
https://hdl.handle.net/1822/58184
Title: | PEGylation 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 |
Keywords: | laccase polyethylene glycol polymerization template alcohols enzyme catalysis molecular dynamics template synthesis |
Issue date: | 23-Oct-2017 |
Publisher: | Wiley-Blackwell |
Journal: | ChemCatChem |
Citation: | Jing 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. |
Type: | Article |
URI: | https://hdl.handle.net/1822/58184 |
DOI: | 10.1002/cctc.201700849 |
ISSN: | 1867-3880 |
e-ISSN: | 1867-3899 |
Publisher version: | http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1867-3899 |
Peer-Reviewed: | yes |
Access: | Open access |
Appears in Collections: | CEB - Publicações em Revistas/Séries Internacionais / Publications in International Journals/Series |
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document_46915_1.pdf | 1,01 MB | Adobe PDF | View/Open |