PEGylation Greatly Enhances Laccase Polymerase Activity
2017; Wiley; Volume: 9; Issue: 20 Linguagem: Inglês
10.1002/cctc.201700849
ISSN1867-3899
AutoresJing Su, Jennifer Noro, Ana Loureiro, Madalena Martins, Nuno G. Azóia, Jiajia Fu, Qiang Wang, Carla Silva, Artur Cavaco‐Paulo,
Tópico(s)Electrochemical sensors and biosensors
ResumoAbstract 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.
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