4 years ago

PEGylation Greatly Enhances Laccase Polymerase Activity

PEGylation Greatly Enhances Laccase Polymerase Activity
Jiajia Fu, Qiang Wang, Jennifer Noro, Ana Loureiro, Artur Cavaco-Paulo, Madalena Martins, Nuno G. Azoia, Carla Silva, Jing Su
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 3-fold compared with the reaction of the native enzyme, as confirmed by UV/Vis spectroscopy. The polymerization of catechol increased only 1.5-fold if poly(ethylene glycol) (PEG) was added to the medium reaction. Molecular-dynamics 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 polyacrylamide 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. Polymer rules: The role of poly(ethylene glycol) (PEG) as a reaction template is evaluated in the PEG-assisted polymerization of catechol. During the reaction, a miscible complex between PEG and polycatechol is formed by precipitation. The mobility of PEG proves to be crucial for template-assisted reactions.

Publisher URL: http://onlinelibrary.wiley.com/resolve/doi

DOI: 10.1002/cctc.201700849

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